ID SWA_DROME Reviewed; 548 AA. AC P40688; Q9W400; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 05-MAY-2009, entry version 65. DE RecName: Full=Protein swallow; GN Name=swa; ORFNames=CG3429; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND RP DEVELOPMENTAL STAGE. RC STRAIN=Canton-S; RX MEDLINE=92217243; PubMed=1806330; RA Chao Y.-C., Donahue K.M., Pokrywka N.J., Stephenson E.C.; RT "Sequence of swallow, a gene required for the localization of bicoid RT message in Drosophila eggs."; RL Dev. Genet. 12:333-341(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP SUBCELLULAR LOCATION. RX MEDLINE=94116446; PubMed=7507030; RA Hegde J., Stephenson E.C.; RT "Distribution of swallow protein in egg chambers and embryos of RT Drosophila melanogaster."; RL Development 119:457-470(1993). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; SER-368; SER-463; RP SER-471; SER-475; SER-483; SER-485 AND SER-487, AND MASS SPECTROMETRY. RC TISSUE=Embryo; RX PubMed=18327897; DOI=10.1021/pr700696a; RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.; RT "Phosphoproteome analysis of Drosophila melanogaster embryos."; RL J. Proteome Res. 7:1675-1682(2008). CC -!- FUNCTION: Has a role in localizing bicoid mRNA at the anterior CC margin of the oocyte during oogenesis, and a poorly characterized CC role in nuclear divisions in early embryogenesis. CC -!- SUBUNIT: May be a homo- or heterodimer. CC -!- INTERACTION: CC Q9VTL4:-; NbExp=1; IntAct=EBI-173220, EBI-182056; CC O96860:Cdlc2; NbExp=1; IntAct=EBI-173220, EBI-146410; CC Q9VL70:yip2; NbExp=1; IntAct=EBI-173220, EBI-132221; CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Uniformly distributed in eggs, CC becomes localized to the nuclei during early mitotic divisions in CC early embryogenesis. Enters each nucleus at the beginning of CC mitosis, occupies a position complementary to that of condensed CC chromatin, and leaves each nucleus at the end of mitosis. CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X56023; CAA39500.1; -; Genomic_DNA. DR EMBL; AE014298; AAF46160.3; -; Genomic_DNA. DR EMBL; AY069487; AAL39632.1; -; mRNA. DR PIR; S20806; S20806. DR RefSeq; NP_511060.2; -. DR UniGene; Dm.7242; -. DR PDB; 3BRL; X-ray; 1.90 A; C=287-296. DR PDB; 3E2B; X-ray; 2.00 A; C=281-296. DR PDBsum; 3BRL; -. DR PDBsum; 3E2B; -. DR DIP; DIP:17669N; -. DR IntAct; P40688; 10. DR PRIDE; P40688; -. DR GeneID; 31580; -. DR KEGG; dme:Dmel_CG3429; -. DR NMPDR; fig|7227.3.peg.16720; -. DR FlyBase; FBgn0003655; swa. DR HOGENOM; P40688; -. DR OMA; P40688; NDSAIEV. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-000818-MON; -. DR NextBio; 774289; -. DR ArrayExpress; P40688; -. DR GermOnline; CG3429; Drosophila melanogaster. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW. DR GO; GO:0045502; F:dynein binding; TAS:FlyBase. DR GO; GO:0003729; F:mRNA binding; TAS:FlyBase. DR GO; GO:0045450; P:bicoid mRNA localization; TAS:FlyBase. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0008595; P:determination of anterior/posterior axis, e...; IGI:FlyBase. DR GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW. DR GO; GO:0007317; P:regulation of pole plasm oskar mRNA localiz...; IGI:FlyBase. PE 1: Evidence at protein level; KW 3D-structure; Cell cycle; Cell division; Complete proteome; KW Developmental protein; Mitosis; Nucleus; Phosphoprotein. FT CHAIN 1 548 Protein swallow. FT /FTId=PRO_0000072342. FT MOD_RES 362 362 Phosphoserine. FT MOD_RES 368 368 Phosphoserine. FT MOD_RES 463 463 Phosphoserine. FT MOD_RES 471 471 Phosphoserine. FT MOD_RES 475 475 Phosphoserine. FT MOD_RES 483 483 Phosphoserine. FT MOD_RES 485 485 Phosphoserine. FT MOD_RES 487 487 Phosphoserine. SQ SEQUENCE 548 AA; 62070 MW; B8E0351C7B005159 CRC64; MSLQDESFPT DELFDQLNNL SSSGARNTWF AEHHKPAVFE RDTAPFLEIC YADPDFDADG DVANKSAKTC VSDPVGRDQE DEDDYDEDVD GDDHKLGCEK APLGSGRSSK AVSYQDIHSA YTKRRFQHVT SKVGQYIAEI QAQDQKRRNV KFAGFQRVNS MPESLTPTLQ QVYVHDGDFK VDKNCQTHSN SDSNYNSNSN NSSSSFDRLL AENESLQQKI NSLRVEAKRL QGFNEYVQER LDRKTDDFVK MKCNFETLRT ELSECQQKLR RQQDNSQHHF MYHIRSATSA KATQTDFLVD TIPASGNVLV TPHPLGDLTY NSSKGSIELA LLSVAPSARV AQNPVQVQRA IHPQSLDFSS VSTEADGSGS GEHRVETSSR ALVRRTPAPN NSETSQPSSN DSAIEVEAHE EERPSSRRQW EQQGELISPR QWGQHEGMYY FDKRNNRVIE VMGFNISQGR NQSHDTIHNQ SINDSQTRLL VHSMSMSHLE AHDHFRSKRT TLGSRMLRFL GPCVRCRNGD PLNRSNVTYK DGLPAMPEEE FVDQRNQR // ID DYIN_DROME Reviewed; 663 AA. AC Q24246; O96508; O96510; O96511; O96512; O96513; O96514; O96515; AC O96516; Q5U0Z1; Q86BQ5; Q9NG49; Q9TZR7; Q9TZR8; Q9TZR9; Q9TZS0; AC Q9VR78; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 03-JUL-2003, sequence version 3. DT 05-MAY-2009, entry version 99. DE RecName: Full=Dynein intermediate chain, cytosolic; DE Short=DH IC; DE AltName: Full=Cytoplasmic dynein intermediate chain; DE AltName: Full=Protein short wing; GN Name=sw; Synonyms=Cdic, Dic19B; ORFNames=CG18000; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1A; 1B; 1C; 2A; 2B; RP 2C; 3A; 3B; 4; 5A AND 5B), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP AND DEVELOPMENTAL STAGE. RC TISSUE=Ovary; RX MEDLINE=98449968; PubMed=9774695; RA Nurminsky D.I., Nurminskaya M.V., Benevolenskaya E.V., Shevelyov Y.Y., RA Hartl D.L., Gvozdev V.A.; RT "Cytoplasmic dynein intermediate-chain isoforms with different RT targeting properties created by tissue-specific alternative RT splicing."; RL Mol. Cell. Biol. 18:6816-6825(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2B), FUNCTION, AND TISSUE RP SPECIFICITY. RC TISSUE=Ovary; RX MEDLINE=20525500; PubMed=11071907; RA Boylan K., Serr M., Hays T.S.; RT "A molecular genetic analysis of the interaction between the RT cytoplasmic dynein intermediate chain and the glued (Dynactin) RT complex."; RL Mol. Biol. Cell 11:3791-3803(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1B). RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., RA Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 101-663 (ISOFORM 4). RC STRAIN=GT WA; RA Benevolenskaya E.V., Gvozdev V.A.; RT "Cluster of tandem repeats in Drosophila genome comprising putative RT genes encoding cytoplasmic dynein intermediate chain and 3'-part of RT annexin X."; RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The intermediate chains seem to help dynein bind to CC dynactin 150 kDa component. CC -!- SUBUNIT: Consists of at least two heavy chains and a number of CC intermediate and light chains. CC -!- INTERACTION: CC Q9V8S1:CG7229; NbExp=1; IntAct=EBI-213425, EBI-182982; CC -!- SUBCELLULAR LOCATION: Isoform 2c: Lysosome membrane; Peripheral CC membrane protein; Cytoplasmic side. Note=Aggregates in cytoplasm CC around lysosomes. CC -!- SUBCELLULAR LOCATION: Isoform 2a: Nucleus membrane; Peripheral CC membrane protein; Cytoplasmic side. Note=Aggregates in cytoplasm CC around the nucleus. CC -!- SUBCELLULAR LOCATION: Isoform 2b: Nucleus membrane; Peripheral CC membrane protein; Cytoplasmic side. Note=Aggregates in cytoplasm CC around the nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=11; CC Name=5a; Synonyms=J; CC IsoId=Q24246-11; Sequence=Displayed; CC Name=1a; Synonyms=A; CC IsoId=Q24246-2; Sequence=VSP_001345; CC Name=1b; Synonyms=B; CC IsoId=Q24246-3; Sequence=VSP_001346; CC Name=1c; Synonyms=C; CC IsoId=Q24246-4; Sequence=VSP_001347; CC Name=2a; Synonyms=D; CC IsoId=Q24246-5; Sequence=VSP_007686, VSP_001348; CC Name=2b; Synonyms=E; CC IsoId=Q24246-6; Sequence=VSP_007686; CC Name=2c; Synonyms=F; CC IsoId=Q24246-7; Sequence=VSP_007686, VSP_007687; CC Name=3a; Synonyms=G; CC IsoId=Q24246-8; Sequence=VSP_001342, VSP_001348; CC Name=3b; Synonyms=H; CC IsoId=Q24246-9; Sequence=VSP_001342; CC Name=4; Synonyms=I; CC IsoId=Q24246-10; Sequence=VSP_001343; CC Name=5b; Synonyms=K; CC IsoId=Q24246-12; Sequence=VSP_007685; CC -!- TISSUE SPECIFICITY: High levels of isoform 1b, isoform 1c, isoform CC 3a and isoform 4 accumulate in early egg chambers and at stage 9 CC become concentrated at the posterior of the oocyte. Isoform 5a and CC isoform 5b are highly expressed in adult head and to a lesser CC extent in adult torso. Isoform 1a, isoform 2a and isoform 2b are CC found in all tissues examined, including ovaries, midgut, torso CC and head. CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. CC Abundant in embryos and adults, low levels in larva and pupae. CC Isoform 1a, isoform 2a and isoform 2b are constitutively expressed CC at high levels and isoform 2c at low levels in embryos and adults. CC -!- SIMILARITY: Belongs to the dynein intermediate chain family. CC -!- SIMILARITY: Contains 7 WD repeats. CC -!- SEQUENCE CAUTION: CC Sequence=AAC70942.1; Type=Erroneous gene model prediction; CC Sequence=AAC78306.1; Type=Erroneous gene model prediction; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF070687; AAC78306.1; ALT_SEQ; Genomic_DNA. DR EMBL; AF070689; AAC70933.1; -; mRNA. DR EMBL; AF070690; AAC70934.1; -; mRNA. DR EMBL; AF070691; AAC70935.1; -; mRNA. DR EMBL; AF070692; AAC70936.1; -; mRNA. DR EMBL; AF070693; AAC70937.1; -; mRNA. DR EMBL; AF070694; AAC70938.1; -; mRNA. DR EMBL; AF070695; AAC70939.1; -; mRNA. DR EMBL; AF070696; AAC70940.1; -; mRNA. DR EMBL; AF070697; AAC70941.1; -; mRNA. DR EMBL; AF070698; AAC70942.1; ALT_SEQ; mRNA. DR EMBL; AF070699; AAC70943.1; -; mRNA. DR EMBL; AF263371; AAF73046.1; -; mRNA. DR EMBL; AE014298; AAF50928.2; -; Genomic_DNA. DR EMBL; AE014298; AAN09553.1; -; Genomic_DNA. DR EMBL; AE014298; AAN09554.1; -; Genomic_DNA. DR EMBL; AE014298; AAN09555.1; -; Genomic_DNA. DR EMBL; AE014298; AAN09556.1; -; Genomic_DNA. DR EMBL; AE014298; AAN09557.1; -; Genomic_DNA. DR EMBL; AE014298; AAN09558.1; -; Genomic_DNA. DR EMBL; AE014298; AAN09559.1; -; Genomic_DNA. DR EMBL; AE014298; AAN09560.1; -; Genomic_DNA. DR EMBL; AE014298; AAN09561.1; -; Genomic_DNA. DR EMBL; AE014298; AAN09562.1; -; Genomic_DNA. DR EMBL; BT016101; AAV36986.1; -; mRNA. DR EMBL; L41945; AAB51185.1; -; Genomic_DNA. DR RefSeq; NP_477069.1; -. DR RefSeq; NP_477070.1; -. DR RefSeq; NP_477071.1; -. DR RefSeq; NP_477072.1; -. DR RefSeq; NP_477073.1; -. DR RefSeq; NP_477074.1; -. DR RefSeq; NP_477075.2; -. DR RefSeq; NP_477076.1; -. DR RefSeq; NP_477077.1; -. DR RefSeq; NP_477078.1; -. DR RefSeq; NP_477079.1; -. DR UniGene; Dm.20780; -. DR DIP; DIP:19664N; -. DR IntAct; Q24246; 2. DR GeneID; 44160; -. DR KEGG; dme:Dmel_CG18000; -. DR FlyBase; FBgn0003654; sw. DR OMA; Q24246; GGHERDV. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-002729-MON; -. DR NextBio; 836907; -. DR ArrayExpress; Q24246; -. DR GermOnline; CG18000; Drosophila melanogaster. DR GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW. DR GO; GO:0045503; F:dynein light chain binding; IPI:FlyBase. DR GO; GO:0003774; F:motor activity; IEA:UniProtKB-KW. DR GO; GO:0051642; P:centrosome localization; IMP:FlyBase. DR GO; GO:0016482; P:cytoplasmic transport; IMP:FlyBase. DR GO; GO:0001754; P:eye photoreceptor cell differentiation; IGI:FlyBase. DR GO; GO:0007291; P:sperm individualization; IMP:FlyBase. DR GO; GO:0007051; P:spindle organization; IMP:FlyBase. DR InterPro; IPR015943; WD40/YVTN_repeat-like. DR InterPro; IPR001680; WD40_repeat. DR InterPro; IPR019782; WD40_repeat_2. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR017986; WD40_repeat_region. DR Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1. DR SMART; SM00320; WD40; 6. DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG. DR PROSITE; PS50082; WD_REPEATS_2; 1. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Dynein; Lysosome; Membrane; KW Microtubule; Motor protein; Nucleus; Repeat; WD repeat. FT CHAIN 1 663 Dynein intermediate chain, cytosolic. FT /FTId=PRO_0000114661. FT REPEAT 311 360 WD 1. FT REPEAT 364 404 WD 2. FT REPEAT 413 454 WD 3. FT REPEAT 463 503 WD 4. FT REPEAT 508 553 WD 5. FT REPEAT 556 596 WD 6. FT REPEAT 602 641 WD 7. FT VAR_SEQ 144 187 VLSCHSSPLSGYMEDWWRPRKAHATDYYDEYNLNPGLEWED FT EFT -> AHATDYYVLAFDAQG (in isoform 1a). FT /FTId=VSP_001345. FT VAR_SEQ 144 187 VLSCHSSPLSGYMEDWWRPRKAHATDYYDEYNLNPGLEWED FT EFT -> AHATDYYG (in isoform 1b). FT /FTId=VSP_001346. FT VAR_SEQ 144 187 VLSCHSSPLSGYMEDWWRPRKAHATDYYDEYNLNPGLEWED FT EFT -> AHATDYY (in isoform 1c). FT /FTId=VSP_001347. FT VAR_SEQ 144 171 Missing (in isoform 3a and isoform 3b). FT /FTId=VSP_001342. FT VAR_SEQ 144 164 Missing (in isoform 2a, isoform 2b and FT isoform 2c). FT /FTId=VSP_007686. FT VAR_SEQ 144 153 Missing (in isoform 5b). FT /FTId=VSP_007685. FT VAR_SEQ 146 187 SCHSSPLSGYMEDWWRPRKAHATDYYDEYNLNPGLEWEDEF FT T -> AFDAQG (in isoform 4). FT /FTId=VSP_001343. FT VAR_SEQ 187 187 T -> TG (in isoform 2a and isoform 3a). FT /FTId=VSP_001348. FT VAR_SEQ 187 187 T -> TVLAFDAQG (in isoform 2c). FT /FTId=VSP_007687. FT CONFLICT 47 47 D -> G (in Ref. 1; AAC78306/AAC70933/ FT AAC70934/AAC70935/AAC70936/AAC70937/ FT AAC70938/AAC70939/AAC70940/AAC70941/ FT AAC70942/AAC70943). FT CONFLICT 139 145 GGNGDVL -> AETAMV (in Ref. 6; AAB51185). FT CONFLICT 235 235 V -> L (in Ref. 6; AAB51185). FT CONFLICT 296 297 HA -> SM (in Ref. 6; AAB51185). FT CONFLICT 521 522 NQ -> KP (in Ref. 6; AAB51185). FT CONFLICT 537 548 DWTIKLWSLKDT -> KIWSLKLPISSCQFSVVSGINSN FT (in Ref. 6; AAB51185). FT CONFLICT 579 579 G -> A (in Ref. 6; AAB51185). FT CONFLICT 593 593 E -> K (in Ref. 6; AAB51185). FT CONFLICT 628 628 L -> Q (in Ref. 6; AAB51185). FT CONFLICT 645 663 WSRFNTHLSEIKMNQSDEV -> IKMNQSVRSRTI (in FT Ref. 6; AAB51185). SQ SEQUENCE 663 AA; 73917 MW; 4C726D4C5F47FAF7 CRC64; MDRKAELERK KAKLAALREE KDRRRREKEI KDMEEAAGRI GGGAGIDKDQ RKDLDEMLSS LGVAPVSEVL SSLSSVNSMT SDNSNTQTPD ASLQATVNGQ SGGKKQPLNL SVYNVQATNI PPKETLVYTK QTQTTSTGGG NGDVLSCHSS PLSGYMEDWW RPRKAHATDY YDEYNLNPGL EWEDEFTDDE ESSLQNLGNG FTSKLPPGYL THGLPTVKDV APAITPLEIK KETEVKKEVN ELSEEQKQMI ILSENFQRFV VRAGRVIERA LSENVDIYTD YIGGGDSEEA NDERSHARLS LNRVFYDERW SKNRCITSMD WSTHFPELVV GSYHNNEESP NEPDGVVMVW NTKFKKSTPE DVFHCQSAVM STCFAKFNPN LILGGTYSGQ IVLWDNRVQK RTPIQRTPLS AAAHTHPVYC LQMVGTQNAH NVISISSDGK LCSWSLDMLS QPQDTLELQQ RQSKAIAITS MAFPANEINS LVMGSEDGYV YSASRHGLRS GVNEVYERHL GPITGISTHY NQLSPDFGHL FLTSSIDWTI KLWSLKDTKP LYSFEDNSDY VMDVAWSPVH PALFAAVDGS GRLDLWNLNQ DTEVPTASIV VAGAPALNRV SWTPSGLHVC IGDEAGKLYV YDVAENLAQP SRDEWSRFNT HLSEIKMNQS DEV // ID DC1I1_MOUSE Reviewed; 628 AA. AC O88485; O88486; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 05-MAY-2009, entry version 67. DE RecName: Full=Cytoplasmic dynein 1 intermediate chain 1; DE AltName: Full=Cytoplasmic dynein intermediate chain 1; DE AltName: Full=Dynein intermediate chain 1, cytosolic; DE AltName: Full=DH IC-1; GN Name=Dync1i1; Synonyms=Dnci1, Dncic1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A AND 1B). RX MEDLINE=99168894; PubMed=10049579; DOI=10.1006/geno.1998.5665; RA Crackower M.A., Sinasac D.S., Xia J., Motoyama J., Prochazka M., RA Rommens J.M., Scherer S.W., Tsui L.-C.; RT "Cloning and characterization of two cytoplasmic dynein intermediate RT chain genes in mouse and human."; RL Genomics 55:257-267(1999). RN [2] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-618, AND MASS RP SPECTROMETRY. RC TISSUE=Brain; RX PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200; RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., RA Burlingame A.L.; RT "Comprehensive identification of phosphorylation sites in postsynaptic RT density preparations."; RL Mol. Cell. Proteomics 5:914-922(2006). CC -!- FUNCTION: The intermediate chains seem to help dynein bind to CC dynactin 150 kDa component. May play a role in mediating the CC interaction of cytoplasmic dynein with membranous organelles and CC kinetochores. CC -!- SUBUNIT: Consists of at least two heavy chains and a number of CC intermediate and light chains. CC -!- INTERACTION: CC P06537:Nr3c1; NbExp=2; IntAct=EBI-492834, EBI-492753; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=Additional isoforms seem to exist; CC Name=1A; CC IsoId=O88485-1; Sequence=Displayed; CC Name=1B; CC IsoId=O88485-2; Sequence=VSP_001334; CC -!- SIMILARITY: Belongs to the dynein intermediate chain family. CC -!- SIMILARITY: Contains 7 WD repeats. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF063229; AAC33444.1; -; mRNA. DR EMBL; AF063230; AAC33445.1; -; mRNA. DR IPI; IPI00131084; -. DR IPI; IPI00226946; -. DR UniGene; Mm.20893; -. DR IntAct; O88485; 2. DR PhosphoSite; O88485; -. DR PRIDE; O88485; -. DR Ensembl; ENSMUSG00000029757; Mus musculus. DR MGI; MGI:107743; Dync1i1. DR HOGENOM; O88485; -. DR HOVERGEN; O88485; -. DR ArrayExpress; O88485; -. DR Bgee; O88485; -. DR CleanEx; MM_DYNC1I1; -. DR GermOnline; ENSMUSG00000029757; Mus musculus. DR GO; GO:0030286; C:dynein complex; TAS:MGI. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:HGNC. DR GO; GO:0008017; F:microtubule binding; ISS:HGNC. DR GO; GO:0003777; F:microtubule motor activity; ISS:HGNC. DR GO; GO:0047496; P:vesicle transport along microtubule; ISS:HGNC. DR InterPro; IPR015943; WD40/YVTN_repeat-like. DR InterPro; IPR001680; WD40_repeat. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR017986; WD40_repeat_region. DR Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1. DR SMART; SM00320; WD40; 5. DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. PE 1: Evidence at protein level; KW Alternative splicing; Dynein; Microtubule; Motor protein; KW Phosphoprotein; Repeat; WD repeat. FT CHAIN 1 628 Cytoplasmic dynein 1 intermediate chain FT 1. FT /FTId=PRO_0000114653. FT REPEAT 268 317 WD 1. FT REPEAT 321 361 WD 2. FT REPEAT 370 411 WD 3. FT REPEAT 420 460 WD 4. FT REPEAT 465 510 WD 5. FT REPEAT 513 553 WD 6. FT REPEAT 559 598 WD 7. FT MOD_RES 618 618 Phosphoserine. FT VAR_SEQ 106 125 Missing (in isoform 1B). FT /FTId=VSP_001334. SQ SEQUENCE 628 AA; 70679 MW; 3C29AF6DA3467FD6 CRC64; MSDKSDLKAE LERKKQRLAQ IREEKKRKEE ERKKKEADMQ QKKEPVQDDS DLDRKRRETE ALLQSIGISP EPPLVPTPMS PSSKSVSTPS DAGSQDSGDL GPLTRTLQWD TDPSVLQLQS DSELGRRLHK LGVSKVTQVD FLPREVVSYS KETQTPLATH QSEEDEEDEE MVEPKIGHDS ELENQEKKQE TKEAPPRELT EEEKQQILHS EEFLIFFDRT IRVIERALAE DSDIFFDYSG RELEEKDGDV QAGANLSFNR QFYDEHWSKH RVVTCMDWSL QYPELMVASY SNNEDAPHEP DGVALVWNMK FKKTTPEYVF HCQSSVMSVC FARFHPNLVV GGTYSGQIVL WDNRSHRRTP VQRTPLSAAA HTHPVYCVNV VGTHNARNLI TVSTDGKMCS WSLDMLSTPQ ESMELVYNKS KPVAVTGMAF PTGDVNNFVV GSEEGTVYTA CRHGSKAGIG EVFEGHQGPV TGINCHMAVG PIDFSHLFVT SSFDWTVKLW TTKHNKPVYS SEDNADYVYD VMWSPVHPAL FACVDGMGRL DLWNLNSDTE VPTASVAIEG ASALNRVRWA QGGKEVAVGD SEGRIWIYDV GELAVPHNDE WTRFARTLVE IRANRADSEE EGAVELAA // ID ZMY11_HUMAN Reviewed; 562 AA. AC Q15326; B2R6G8; Q5VUI1; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 05-MAY-2009, entry version 75. DE RecName: Full=Zinc finger MYND domain-containing protein 11; DE AltName: Full=Adenovirus 5 E1A-binding protein; DE AltName: Full=Protein BS69; GN Name=ZMYND11; Synonyms=BS69; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Colon carcinoma; RX MEDLINE=95347342; PubMed=7621829; RA Hateboer G., Gennissen A., Ramos Y.F.M., Kerkhoven R.M., RA Sonntag-Buck V., Stunnenberg H.G., Bernards R.; RT "BS69, a novel adenovirus E1A-associated protein that inhibits E1A RT transactivation."; RL EMBO J. 14:3159-3169(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, AND MASS RP SPECTROMETRY. RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, AND MASS RP SPECTROMETRY. RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). CC -!- FUNCTION: Binds to the transactivation domain of the adenovirus CC type 5 E1A 32 kDa protein (289R) and inhibits its transactivating CC activity. May act as tumor suppressor through suppression of CC adenovirus replication. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. CC -!- SIMILARITY: Contains 1 bromo domain. CC -!- SIMILARITY: Contains 1 MYND-type zinc finger. CC -!- SIMILARITY: Contains 1 PHD-type zinc finger. CC -!- SIMILARITY: Contains 1 PWWP domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X86098; CAA60052.1; -; mRNA. DR EMBL; AK312570; BAG35465.1; -; mRNA. DR EMBL; AL589988; CAH69845.1; -; Genomic_DNA. DR EMBL; AL603831; CAH69845.1; JOINED; Genomic_DNA. DR EMBL; AL603831; CAI40899.1; -; Genomic_DNA. DR EMBL; AL589988; CAI40899.1; JOINED; Genomic_DNA. DR IPI; IPI00873394; -. DR PIR; S56145; S56145. DR RefSeq; NP_006615.1; -. DR UniGene; Hs.292265; -. DR PhosphoSite; Q15326; -. DR PRIDE; Q15326; -. DR Ensembl; ENSG00000015171; Homo sapiens. DR GeneID; 10771; -. DR KEGG; hsa:10771; -. DR GeneCards; GC10P000170; -. DR H-InvDB; HIX0025946; -. DR HGNC; HGNC:16966; ZMYND11. DR HPA; HPA015816; -. DR MIM; 608668; gene. DR PharmGKB; PA128394578; -. DR HOVERGEN; Q15326; -. DR OMA; Q15326; ARPDNWF. DR NextBio; 40897; -. DR ArrayExpress; Q15326; -. DR Bgee; Q15326; -. DR CleanEx; HS_ZMYND11; -. DR GermOnline; ENSG00000015171; Homo sapiens. DR GO; GO:0005634; C:nucleus; TAS:ProtInc. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0005515; F:protein binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc. DR GO; GO:0045786; P:negative regulation of cell cycle; IEA:UniProtKB-KW. DR GO; GO:0000122; P:negative regulation of transcription from R...; TAS:ProtInc. DR InterPro; IPR001487; Bromodomain. DR InterPro; IPR000313; PWWP. DR InterPro; IPR002893; Znf_MYND. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR001841; Znf_RING. DR Gene3D; G3DSA:1.20.920.10; Bromodomain; 1. DR Pfam; PF00439; Bromodomain; 1. DR Pfam; PF00855; PWWP; 1. DR Pfam; PF01753; zf-MYND; 1. DR SMART; SM00297; BROMO; 1. DR SMART; SM00249; PHD; 1. DR SMART; SM00293; PWWP; 1. DR SMART; SM00184; RING; 1. DR PROSITE; PS50014; BROMODOMAIN_2; 1. DR PROSITE; PS50812; PWWP; 1. DR PROSITE; PS01360; ZF_MYND_1; 1. DR PROSITE; PS50865; ZF_MYND_2; 1. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 1. PE 1: Evidence at protein level; KW Anti-oncogene; Bromodomain; Cell cycle; DNA-binding; Metal-binding; KW Nucleus; Phosphoprotein; Repressor; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1 562 Zinc finger MYND domain-containing FT protein 11. FT /FTId=PRO_0000211218. FT DOMAIN 128 198 Bromo. FT DOMAIN 240 291 PWWP. FT ZN_FING 60 108 PHD-type. FT ZN_FING 523 558 MYND-type. FT REGION 412 532 Required for binding to E1A. FT MOTIF 354 360 Nuclear localization signal (Potential). FT MOD_RES 381 381 Phosphoserine. SQ SEQUENCE 562 AA; 66203 MW; E4280C54505B0894 CRC64; MSRVHGMHPK ETTRQLSLAV KDGLIVETLT VGCKGSKAGI EQEGYWLPGD EIDWETENHD WYCFECHLPG EVLICDLCFR VYHSKCLSDE FRLRDSSSPW QCPVCRSIKK KNTNKQEMGT YLRFIVSRMK ERAIDLNKKG KDNKHPMYRR LVHSAVDVPT IQEKVNEGKY RSYEEFKADA QLLLHNTVIF YGADSEQADI ARMLYKDTCH ELDELQLCKN CFYLSNARPD NWFCYPCIPN HELVWAKMKG FGFWPAKVMQ KEDNQVDVRF FGHHHQRAWI PSENIQDITV NIHRLHVKRS MGWKKACDEL ELHQRFLREG RFWKSKNEDR GEEEAESSIS STSNEQLKVT QEPRAKKGRR NQSVEPKKEE PEPETEAVSS SQEIPTMPQP IEKVSVSTQT KKLSASSPRM LHRSTQTTND GVCQSMCHDK YTKIFNDFKD RMKSDHKRET ERVVREALEK LRSEMEEEKR QAVNKAVANM QGEMDRKCKQ VKEKCKEEFV EEIKKLATQH KQLISQTKKK QWCYNCEEEA MYHCCWNTSY CSIKCQQEHW HAEHKRTCRR KR // ID DC1I2_HUMAN Reviewed; 638 AA. AC Q13409; Q32LY9; Q53S84; Q5BJF8; Q7Z4X1; Q96NG7; Q96S87; Q9BXZ5; AC Q9NT58; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 19-SEP-2002, sequence version 3. DT 05-MAY-2009, entry version 94. DE RecName: Full=Cytoplasmic dynein 1 intermediate chain 2; DE AltName: Full=Cytoplasmic dynein intermediate chain 2; DE AltName: Full=Dynein intermediate chain 2, cytosolic; DE AltName: Full=DH IC-2; GN Name=DYNC1I2; Synonyms=DNCI2, DNCIC2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2C). RA Huang J., Yu L., Zhao S.Y.; RT "Cloning of a new human cDNA homologous to Rattus norvegicus RT cytoplasmic dynein intermediate chain 2C."; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2C AND 2F). RA Li N., Wan T., Zhang M., Zhang W., Cao X.; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2C). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2A). RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2C). RC TISSUE=Endometrium, and Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., RA Ottenwalder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2C). RC TISSUE=Kidney, Skin, and Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 82-448 (ISOFORM 2A). RX MEDLINE=96101929; PubMed=8522607; DOI=10.1083/jcb.131.6.1507; RA Vaughan K.T., Vallee R.B.; RT "Cytoplasmic dynein binds dynactin through a direct interaction RT between the intermediate chains and p150Glued."; RL J. Cell Biol. 131:1507-1516(1995). RN [10] RP PROTEIN SEQUENCE OF 236-250, AND MASS SPECTROMETRY. RC TISSUE=Brain, and Cajal-Retzius cell; RA Lubec G., Afjehi-Sadat L.; RL Submitted (MAR-2007) to UniProtKB. RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND MASS RP SPECTROMETRY. RC TISSUE=Epithelium; RX PubMed=15302935; DOI=10.1073/pnas.0404720101; RA Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., RA Li J., Cohn M.A., Cantley L.C., Gygi S.P.; RT "Large-scale characterization of HeLa cell nuclear phosphoproteins."; RL Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND MASS RP SPECTROMETRY. RX PubMed=17287340; DOI=10.1073/pnas.0611217104; RA Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; RT "Global proteomic profiling of phosphopeptides using electron transfer RT dissociation tandem mass spectrometry."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND SER-101, AND MASS RP SPECTROMETRY. RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94 AND SER-97, AND MASS RP SPECTROMETRY. RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). CC -!- FUNCTION: The intermediate chains seem to help dynein bind to CC dynactin 150 kDa component. CC -!- SUBUNIT: Consists of at least two heavy chains and a number of CC intermediate and light chains. CC -!- INTERACTION: CC P63167:DYNLL1; NbExp=1; IntAct=EBI-742998, EBI-349105; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=2A; CC IsoId=Q13409-1; Sequence=Displayed; CC Name=2B; CC IsoId=Q13409-2; Sequence=VSP_001336; CC Name=2C; CC IsoId=Q13409-3; Sequence=VSP_001336, VSP_001337; CC Name=2E; CC IsoId=Q13409-5; Sequence=VSP_023011; CC Name=2F; CC IsoId=Q13409-6; Sequence=VSP_001336, VSP_001337, VSP_023011; CC -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. CC -!- SIMILARITY: Belongs to the dynein intermediate chain family. CC -!- SIMILARITY: Contains 7 WD repeats. CC -!- SEQUENCE CAUTION: CC Sequence=AAA89166.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Several sequence problems; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF134477; AAP97254.1; -; mRNA. DR EMBL; AF250307; AAK37426.1; -; mRNA. DR EMBL; AY037160; AAK67638.1; -; mRNA. DR EMBL; BT007130; AAP35794.1; -; mRNA. DR EMBL; AK055491; BAB70932.1; -; mRNA. DR EMBL; AL137519; CAB70785.1; -; mRNA. DR EMBL; BX537412; CAD97654.1; -; mRNA. DR EMBL; AC064826; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC068039; AAY24133.1; -; Genomic_DNA. DR EMBL; CH471058; EAX11202.1; -; Genomic_DNA. DR EMBL; BC091498; AAH91498.1; -; mRNA. DR EMBL; BC109375; AAI09376.1; -; mRNA. DR EMBL; BC015038; AAH15038.1; -; mRNA. DR EMBL; U39575; AAA89166.1; ALT_SEQ; mRNA. DR IPI; IPI00216348; -. DR IPI; IPI00302712; -. DR IPI; IPI00744015; -. DR IPI; IPI00827813; -. DR IPI; IPI00827859; -. DR PIR; T46365; T46365. DR RefSeq; NP_001369.1; -. DR UniGene; Hs.546250; -. DR IntAct; Q13409; 2. DR PhosphoSite; Q13409; -. DR REPRODUCTION-2DPAGE; IPI00827813; -. DR PRIDE; Q13409; -. DR Ensembl; ENSG00000077380; Homo sapiens. DR GeneID; 1781; -. DR KEGG; hsa:1781; -. DR GeneCards; GC02P172252; -. DR H-InvDB; HIX0002589; -. DR HGNC; HGNC:2964; DYNC1I2. DR MIM; 603331; gene. DR PharmGKB; PA27435; -. DR HOGENOM; Q13409; -. DR HOVERGEN; Q13409; -. DR LinkHub; Q13409; -. DR NextBio; 7247; -. DR ArrayExpress; Q13409; -. DR Bgee; Q13409; -. DR GermOnline; ENSG00000077380; Homo sapiens. DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB. DR GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0003777; F:microtubule motor activity; NAS:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0007018; P:microtubule-based movement; NAS:UniProtKB. DR InterPro; IPR015943; WD40/YVTN_repeat-like. DR InterPro; IPR001680; WD40_repeat. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR017986; WD40_repeat_region. DR Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1. DR SMART; SM00320; WD40; 5. DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG. DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. PE 1: Evidence at protein level; KW Alternative splicing; Direct protein sequencing; Dynein; Microtubule; KW Motor protein; Phosphoprotein; Repeat; WD repeat. FT CHAIN 1 638 Cytoplasmic dynein 1 intermediate chain FT 2. FT /FTId=PRO_0000114655. FT REPEAT 277 326 WD 1. FT REPEAT 330 370 WD 2. FT REPEAT 379 420 WD 3. FT REPEAT 429 469 WD 4. FT REPEAT 474 519 WD 5. FT REPEAT 522 562 WD 6. FT REPEAT 568 607 WD 7. FT MOD_RES 87 87 Phosphoserine. FT MOD_RES 94 94 Phosphoserine. FT MOD_RES 97 97 Phosphoserine. FT MOD_RES 101 101 Phosphoserine. FT VAR_SEQ 77 82 Missing (in isoform 2B, isoform 2C and FT isoform 2F). FT /FTId=VSP_001336. FT VAR_SEQ 113 132 Missing (in isoform 2C and isoform 2F). FT /FTId=VSP_001337. FT VAR_SEQ 602 602 Missing (in isoform 2E and isoform 2F). FT /FTId=VSP_023011. FT CONFLICT 510 510 T -> S (in Ref. 1; AAP97254). FT CONFLICT 525 525 D -> G (in Ref. 1; AAP97254). FT CONFLICT 572 572 A -> G (in Ref. 8; AAI09376). SQ SEQUENCE 638 AA; 71457 MW; 2F868EC9556C47F2 CRC64; MSDKSELKAE LERKKQRLAQ IREEKKRKEE ERKKKETDQK KEAVAPVQEE SDLEKKRREA EALLQSMGLT PESPIVFSEY WVPPPMSPSS KSVSTPSEAG SQDSGDGAVG SRTLHWDTDP SVLQLHSDSD LGRGPIKLGM AKITQVDFPP REIVTYTKET QTPVMAQPKE DEEEDDDVVA PKPPIEPEEE KTLKKDEEND SKAPPHELTE EEKQQILHSE EFLSFFDHST RIVERALSEQ INIFFDYSGR DLEDKEGEIQ AGAKLSLNRQ FFDERWSKHR VVSCLDWSSQ YPELLVASYN NNEDAPHEPD GVALVWNMKY KKTTPEYVFH CQSAVMSATF AKFHPNLVVG GTYSGQIVLW DNRSNKRTPV QRTPLSAAAH THPVYCVNVV GTQNAHNLIS ISTDGKICSW SLDMLSHPQD SMELVHKQSK AVAVTSMSFP VGDVNNFVVG SEEGSVYTAC RHGSKAGISE MFEGHQGPIT GIHCHAAVGA VDFSHLFVTS SFDWTVKLWT TKNNKPLYSF EDNADYVYDV MWSPTHPALF ACVDGMGRLD LWNLNNDTEV PTASISVEGN PALNRVRWTH SGREIAVGDS EGQIVIYDVG EQIAVPRNDE WARFGRTLAE INANRADAEE EAATRIPA // ID SWA_DROPS Reviewed; 537 AA. AC Q9U9I5; Q29JJ4; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 3. DT 03-MAR-2009, entry version 40. DE RecName: Full=Protein swallow; GN Name=swa; ORFNames=GA17446; OS Drosophila pseudoobscura pseudoobscura (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=46245; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=21110505; PubMed=11180817; DOI=10.1007/s004270050023; RA Huang Z., Pokrywka N.J., Yoder J.H., Stephenson E.C.; RT "Analysis of a swallow homologue from Drosophila pseudoobscura."; RL Dev. Genes Evol. 210:157-161(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MV2-25; RX PubMed=15632085; DOI=10.1101/gr.3059305; RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S., RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., RA Couronne O., Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., RA van Batenburg M.F., Howells S.L., Scherer S.E., Sodergren E., RA Matthews B.B., Crosby M.A., Schroeder A.J., Ortiz-Barrientos D., RA Rives C.M., Metzker M.L., Muzny D.M., Scott G., Steffen D., RA Wheeler D.A., Worley K.C., Havlak P., Durbin K.J., Egan A., Gill R., RA Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y., Waldron L., RA Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F., RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M., RA Weinstock G.M., Gibbs R.A.; RT "Comparative genome sequencing of Drosophila pseudoobscura: RT chromosomal, gene, and cis-element evolution."; RL Genome Res. 15:1-18(2005). CC -!- FUNCTION: Has a role in localizing bicoid mRNA at the anterior CC margin of the oocyte during oogenesis, and a poorly characterized CC role in nuclear divisions in early embryogenesis (By similarity). CC -!- SUBUNIT: May be constituted of an homo- or heterodimer (By CC similarity). CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Uniformly distributed in eggs, CC becomes localized to the nuclei during early mitotic divisions in CC early embryogenesis. Swallow enters each nucleus at the beginning CC of mitosis, occupies a position complementary to that of condensed CC chromatin, and leaves each nucleus at the end of mitosis (By CC similarity). CC -!- SEQUENCE CAUTION: CC Sequence=AAD49350.1; Type=Erroneous gene model prediction; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF169634; AAD49350.1; ALT_SEQ; Genomic_DNA. DR EMBL; CH379063; EAL32307.2; -; Genomic_DNA. DR RefSeq; XP_001355250.2; -. DR GeneID; 4815687; -. DR KEGG; dpo:Dpse_GA17446; -. DR FlyBase; FBgn0027807; Dpse\swa. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW. DR GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW. PE 3: Inferred from homology; KW Cell cycle; Cell division; Complete proteome; Developmental protein; KW Mitosis; Nucleus. FT CHAIN 1 537 Protein swallow. FT /FTId=PRO_0000072343. FT CONFLICT 350 350 P -> L (in Ref. 1; AAD49350). FT CONFLICT 390 391 RG -> A (in Ref. 1; AAD49350). SQ SEQUENCE 537 AA; 59641 MW; BC0715A31691CCE7 CRC64; MSLEDESFPA DELFEQLNSA SIGASRQFKS QFGEHDQPEA FERNPAPFLT SDCSDESSFI DAANKSAKTC VSDPVGLDQC EEEEEVDKDF EDSALANGNS ELQIKSARSS KSVSYQDIHS AHTKRRYKHV TSKVAKYIAD IHAQDQQRRN ATKKFQRHSS MPEYLTPTAR ERGAHFSVDE LHNLDESLDN SSAGNITDAK TPNDSYERLL SENERLQNDK EDLKSYSDYL QTKLDEKAME NMQLRRNFDV LRTDLTDCKE KLKRNQSYSL RSLNFCPPAS VPKATQTDHE LLSHAPNISR LSNMVAIADS GTPLPGSNTN NLTYDSSAGS IEVALLSVAP AARQPNAGKP KKNIQPHSLD FSNDSTEAEP NGNGTTSTGH SSSRAITSRR GAAPNNSESS HPSSNDSAIE VEALDLRSPY HRQPQGSIYP PMQDWGHSDG IYFFDKRNSR VIEVRSINVS QSSNPEQNSG TSETNLLNQS HVQFRHKRTS MGTRMLRLLG PCVRCTDTNQ SVNASSATYT IGLPLLREEY GGRHTDR // ID B2L11_HUMAN Reviewed; 198 AA. AC O43521; A8K2W2; O43522; Q0MSE7; Q0MSE8; Q0MSE9; Q53R28; Q6JTU6; AC Q6T851; Q6TE14; Q6TE15; Q6TE16; Q6V402; Q8WYL6; Q8WYL7; Q8WYL8; AC Q8WYL9; Q8WYM0; Q8WYM1; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 05-MAY-2009, entry version 79. DE RecName: Full=Bcl-2-like protein 11; DE Short=Bcl2-L-11; DE AltName: Full=Bcl2-interacting mediator of cell death; GN Name=BCL2L11; Synonyms=BIM; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BIMEL AND BIML), AND FUNCTION. RC TISSUE=Peripheral blood, and Spleen; RX MEDLINE=98094360; PubMed=9430630; DOI=10.1093/emboj/17.2.384; RA O'Connor L., Strasser A., O'Reilly L.A., Hausmann G., Adams J.M., RA Cory S., Huang D.C.S.; RT "Bim: a novel member of the Bcl-2 family that promotes apoptosis."; RL EMBO J. 17:384-395(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BIM-ALPHA1; BIM-ALPHA2; RP BIM-BETA1; BIM-BETA2; BIM-BETA3 AND BIM-BETA4), FUNCTION (ISOFORMS RP BIM-ALPHA1 AND BIM-ALPHA2), AND SUBCELLULAR LOCATION. RX MEDLINE=21592301; PubMed=11734221; DOI=10.1016/S0014-5793(01)03145-3; RA Mami U., Miyashita T., Shikama Y., Tadokoro K., Yamada M.; RT "Molecular cloning and characterization of six novel isoforms of human RT Bim, a member of the proapoptotic Bcl-2 family."; RL FEBS Lett. 509:135-141(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BIM-GAMMA), FUNCTION (ISOFORM RP BIM-GAMMA), SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX MEDLINE=22013778; PubMed=12019181; RA Liu J.-W., Chandra D., Tang S.H., Chopra D., Tang D.G.; RT "Identification and characterization of Bimgamma, a novel proapoptotic RT BH3-only splice variant of Bim."; RL Cancer Res. 62:2976-2981(2002). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BIMS AND BIM-ALPHA3), AND RP FUNCTION (ISOFORM BIM-ALPHA3). RX PubMed=15147734; RA Chen J.Z., Ji C.N., Gu S.H., Li J.X., Zhao E.P., Huang Y., Huang L., RA Ying K., Xie Y., Mao Y.M.; RT "Over-expression of Bim alpha3, a novel isoform of human Bim, result RT in cell apoptosis."; RL Int. J. Biochem. Cell Biol. 36:1554-1561(2004). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] ((ISOFORMS BIM-ALPHA3; BIM-ALPHA4; RP BIM-ALPHA5; BIM-ALPHA6; BIM-BETA5; BIM-BETA6; BIM-BETA7). RX PubMed=17503221; DOI=10.1007/s10495-007-0093-5; RA Miao J., Chen G.G., Yun J.P., Chun S.Y., Zheng Z.Z., Ho R.L.K., RA Chak E.C., Xia N.S., Lai P.B.; RT "Identification and characterization of BH3 domain protein Bim and its RT isoforms in human hepatocellular carcinomas."; RL Apoptosis 12:1691-1701(2007). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS BIMEL AND BIML). RC TISSUE=Teratocarcinoma, and Tongue; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BIMEL). RC TISSUE=Blood; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND MASS RP SPECTROMETRY. RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., RA Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for RT efficient phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND MASS RP SPECTROMETRY. RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [12] RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 141-166 IN COMPLEX WITH RP MCL1. RX PubMed=17389404; DOI=10.1073/pnas.0701297104; RA Czabotar P.E., Lee E.F., van Delft M.F., Day C.L., Smith B.J., RA Huang D.C.S., Fairlie W.D., Hinds M.G., Colman P.M.; RT "Structural insights into the degradation of Mcl-1 induced by BH3 RT domains."; RL Proc. Natl. Acad. Sci. U.S.A. 104:6217-6222(2007). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 141-165 IN COMPLEX WITH RP BCL2A1. RG Structural genomics consortium (SGC); RT "Human BCL-2A1 in complex with BIM."; RL Submitted (FEB-2008) to the PDB data bank. CC -!- FUNCTION: Induces apoptosis. Isoform BimL is more potent than CC isoform BimEL. Isoform Bim-alpha1, isoform Bim-alpha2 and isoform CC Bim-alpha3 induce apoptosis, although less potent than the CC isoforms BimEL, BimL and BimS. Isoform Bim-gamma induces CC apoptosis. CC -!- SUBUNIT: Forms heterodimers with a number of antiapoptotic Bcl-2 CC proteins including MCL1, BCL2, BCL2L1 isoform Bcl-X(L), CC BCL2A1/BFL-1, and BHRF1. Does not heterodimerize with proapoptotic CC proteins such as BAD, BOK, BAX or BAK (By similarity). CC -!- INTERACTION: CC P31749:AKT1; NbExp=1; IntAct=EBI-526416, EBI-296087; CC P10415:BCL2; NbExp=2; IntAct=EBI-526406, EBI-77694; CC P10415:BCL2; NbExp=1; IntAct=EBI-526416, EBI-77694; CC P10415:BCL2; NbExp=2; IntAct=EBI-526420, EBI-77694; CC Q16548:BCL2A1; NbExp=1; IntAct=EBI-526406, EBI-1003550; CC Q07440:Bcl2a1 (xeno); NbExp=1; IntAct=EBI-526406, EBI-707754; CC Q07817:BCL2L1; NbExp=1; IntAct=EBI-526406, EBI-78035; CC Q07817-1:BCL2L1; NbExp=4; IntAct=EBI-526406, EBI-287195; CC Q07817-1:BCL2L1; NbExp=1; IntAct=EBI-526416, EBI-287195; CC Q92843:BCL2L2; NbExp=2; IntAct=EBI-526406, EBI-707714; CC Q9NP97:DYNLRB1; NbExp=1; IntAct=EBI-526406, EBI-372128; CC P63244:GNB2L1; NbExp=2; IntAct=EBI-526406, EBI-296739; CC P63085:Mapk1 (xeno); NbExp=1; IntAct=EBI-526416, EBI-397697; CC Q07820:MCL1; NbExp=1; IntAct=EBI-526406, EBI-1003422; CC P97287:Mcl1 (xeno); NbExp=3; IntAct=EBI-526406, EBI-707292; CC P14174:MIF; NbExp=1; IntAct=EBI-2123748, EBI-372712; CC P14174:MIF; NbExp=1; IntAct=EBI-526416, EBI-372712; CC P14174:MIF; NbExp=5; IntAct=EBI-526420, EBI-372712; CC P31946:YWHAB; NbExp=1; IntAct=EBI-526406, EBI-359815; CC -!- SUBCELLULAR LOCATION: Intracytoplasmic membrane; Peripheral CC membrane protein (By similarity). Note=Associated with CC intracytoplasmic membranes (By similarity). CC -!- SUBCELLULAR LOCATION: Isoform BimEL: Mitochondrion. CC -!- SUBCELLULAR LOCATION: Isoform BimL: Mitochondrion. CC -!- SUBCELLULAR LOCATION: Isoform BimS: Mitochondrion. CC -!- SUBCELLULAR LOCATION: Isoform Bim-alpha1: Mitochondrion. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=17; CC Name=BimEL; Synonyms=Bim(EL); CC IsoId=O43521-1; Sequence=Displayed; CC Name=BimL; Synonyms=Bim(L); CC IsoId=O43521-2; Sequence=VSP_000535; CC Name=BimS; Synonyms=BCL2-like 11 transcript variant 9, Bim(S); CC IsoId=O43521-3; Sequence=VSP_035608; CC Name=Bim-alpha1; CC IsoId=O43521-4; Sequence=VSP_035620; CC Name=Bim-alpha2; CC IsoId=O43521-5; Sequence=VSP_000535, VSP_035620; CC Name=Bim-alpha3; Synonyms=BCL2-like 11 transcript variant 10; CC IsoId=O43521-6; Sequence=VSP_035608, VSP_035620; CC Name=Bim-alpha4; CC IsoId=O43521-7; Sequence=VSP_035608, VSP_035618; CC Name=Bim-alpha5; CC IsoId=O43521-8; Sequence=VSP_035619; CC Name=Bim-alpha6; CC IsoId=O43521-9; Sequence=VSP_035608, VSP_035619; CC Name=Bim-beta1; CC IsoId=O43521-10; Sequence=VSP_035615, VSP_035616; CC Name=Bim-beta2; CC IsoId=O43521-11; Sequence=VSP_035614, VSP_035616; CC Name=Bim-beta3; CC IsoId=O43521-12; Sequence=VSP_035609; CC Name=Bim-beta4; CC IsoId=O43521-13; Sequence=VSP_035610, VSP_035611; CC Name=Bim-beta5; CC IsoId=O43521-14; Sequence=VSP_035613, VSP_035617; CC Name=Bim-beta6; CC IsoId=O43521-15; Sequence=VSP_000535, VSP_035614, VSP_035616; CC Name=Bim-beta7; CC IsoId=O43521-16; Sequence=VSP_000535, VSP_035613, VSP_035617; CC Name=Bim-gamma; CC IsoId=O43521-17; Sequence=VSP_000535, VSP_035612; CC -!- TISSUE SPECIFICITY: Isoform BimEL, isoform BimL and isoform BimS CC are the predominant isoforms and are ubiquitously expressed with a CC tissue-specific variation. Isoform Bim-gamma is most abundantly CC expressed in small intestine and colon, and in lower levels in CC spleen, prostate, testis, heart, liver and kidney. CC -!- DOMAIN: The BH3 motif is required for Bcl-2 binding and CC cytotoxicity. CC -!- SIMILARITY: Belongs to the Bcl-2 family. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/BCL2L11ID772ch2q13.html"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF032457; AAC39593.1; -; mRNA. DR EMBL; AF032458; AAC39594.1; -; mRNA. DR EMBL; AB071195; BAB78589.1; -; mRNA. DR EMBL; AB071196; BAB78590.1; -; mRNA. DR EMBL; AB071197; BAB78591.1; -; mRNA. DR EMBL; AB071198; BAB78592.1; -; mRNA. DR EMBL; AB071199; BAB78593.1; -; mRNA. DR EMBL; AB071200; BAB78594.1; -; mRNA. DR EMBL; AY352518; AAQ62569.1; -; mRNA. DR EMBL; AY305714; AAQ82546.1; -; mRNA. DR EMBL; AY305715; AAQ82547.1; -; mRNA. DR EMBL; AY423441; AAQ99148.1; -; mRNA. DR EMBL; AY423442; AAQ99149.1; -; mRNA. DR EMBL; AY423443; AAQ99150.1; -; mRNA. DR EMBL; AY428962; AAR06908.1; -; mRNA. DR EMBL; DQ849200; ABI13589.1; -; mRNA. DR EMBL; DQ849201; ABI13590.1; -; mRNA. DR EMBL; DQ849202; ABI13591.1; -; mRNA. DR EMBL; AK290377; BAF83066.1; -; mRNA. DR EMBL; AK291269; BAF83958.1; -; mRNA. DR EMBL; AC096670; AAY14797.1; -; Genomic_DNA. DR EMBL; CH471237; EAW50365.1; -; Genomic_DNA. DR EMBL; CH471237; EAW50367.1; -; Genomic_DNA. DR EMBL; CH471237; EAW50369.1; -; Genomic_DNA. DR EMBL; CH471237; EAW50370.1; -; Genomic_DNA. DR EMBL; CH471237; EAW50371.1; -; Genomic_DNA. DR EMBL; CH471237; EAW50372.1; -; Genomic_DNA. DR EMBL; CH471237; EAW50373.1; -; Genomic_DNA. DR EMBL; CH471237; EAW50374.1; -; Genomic_DNA. DR EMBL; BC033694; AAH33694.1; -; mRNA. DR IPI; IPI00012853; -. DR IPI; IPI00103743; -. DR IPI; IPI00216585; -. DR IPI; IPI00410159; -. DR IPI; IPI00428840; -. DR IPI; IPI00451139; -. DR IPI; IPI00514401; -. DR IPI; IPI00873921; -. DR IPI; IPI00878323; -. DR IPI; IPI00914559; -. DR IPI; IPI00914560; -. DR IPI; IPI00914563; -. DR IPI; IPI00914586; -. DR IPI; IPI00914592; -. DR IPI; IPI00914600; -. DR IPI; IPI00914670; -. DR IPI; IPI00914677; -. DR RefSeq; NP_006529.1; -. DR RefSeq; NP_619527.1; -. DR RefSeq; NP_996885.1; -. DR UniGene; Hs.469658; -. DR PDB; 2NL9; X-ray; 1.55 A; B=141-166. DR PDB; 2V6Q; X-ray; 2.70 A; B=141-166. DR PDB; 2VM6; X-ray; 2.20 A; B=141-165. DR PDBsum; 2NL9; -. DR PDBsum; 2V6Q; -. DR PDBsum; 2VM6; -. DR DIP; DIP:29185N; -. DR IntAct; O43521; 24. DR PhosphoSite; O43521; -. DR PRIDE; O43521; -. DR Ensembl; ENSG00000153094; Homo sapiens. DR GeneID; 10018; -. DR KEGG; hsa:10018; -. DR GeneCards; GC02P111597; -. DR HGNC; HGNC:994; BCL2L11. DR HPA; CAB002616; -. DR MIM; 603827; gene. DR PharmGKB; PA25305; -. DR HOGENOM; O43521; -. DR HOVERGEN; O43521; -. DR OMA; O43521; PRMVILR. DR Pathway_Interaction_DB; foxopathway; FoxO family signaling. DR Pathway_Interaction_DB; p75ntrpathway; p75(NTR)-mediated signaling. DR Reactome; REACT_11061; Signalling by NGF. DR Reactome; REACT_578; Apoptosis. DR LinkHub; O43521; -. DR NextBio; 37849; -. DR ArrayExpress; O43521; -. DR Bgee; O43521; -. DR GermOnline; ENSG00000153094; Homo sapiens. DR GO; GO:0005829; C:cytosol; EXP:Reactome. DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell. DR GO; GO:0005741; C:mitochondrial outer membrane; EXP:Reactome. DR GO; GO:0005886; C:plasma membrane; EXP:Reactome. DR GO; GO:0008633; P:activation of pro-apoptotic gene products; EXP:Reactome. DR GO; GO:0006917; P:induction of apoptosis; TAS:UniProtKB. DR InterPro; IPR017288; Apoptosis_Bcl-2-like_11. DR InterPro; IPR014771; Apoptosis_Bim_N. DR InterPro; IPR015040; Bcl-x_interacting. DR InterPro; IPR000712; Bcl2_BH. DR Pfam; PF08945; Bclx_interact; 1. DR Pfam; PF06773; Bim_N; 1. DR PIRSF; PIRSF037827; Bcl-2-like_p11; 1. DR PROSITE; PS01259; BH3; FALSE_NEG. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Apoptosis; Membrane; KW Mitochondrion; Phosphoprotein. FT CHAIN 1 198 Bcl-2-like protein 11. FT /FTId=PRO_0000143109. FT MOTIF 148 162 BH3. FT MOD_RES 77 77 Phosphoserine. FT VAR_SEQ 42 131 Missing (in isoform BimS, isoform Bim- FT alpha3, isoform Bim-alpha6 and isoform FT Bim-alpha4). FT /FTId=VSP_035608. FT VAR_SEQ 42 101 Missing (in isoform BimL, isoform Bim- FT alpha2, isoform Bim-gamma, isoform Bim- FT beta6 and isoform Bim-beta7). FT /FTId=VSP_000535. FT VAR_SEQ 42 75 GNPEGNHGGEGDSCPHGSPQGPLAPPASPGPFAT -> VSL FT CHPGWSALVRSWLTATSNSQVQAVLLPQPPK (in FT isoform Bim-beta3). FT /FTId=VSP_035609. FT VAR_SEQ 43 44 NP -> IF (in isoform Bim-beta4). FT /FTId=VSP_035610. FT VAR_SEQ 45 198 Missing (in isoform Bim-beta4). FT /FTId=VSP_035611. FT VAR_SEQ 132 198 ASMRQAEPADMRPEIWIAQELRRIGDEFNAYYARRVFLNNY FT QAAEDHPRMVILRLLRYIVRLVWRMH -> VVILEDIGDLS FT LCFGFIFTGLDLYGHHHSQDTEQLNHKDFS (in FT isoform Bim-gamma). FT /FTId=VSP_035612. FT VAR_SEQ 132 140 ASMRQAEPA -> VREIEEVVV (in isoform Bim- FT beta5 and isoform Bim-beta7). FT /FTId=VSP_035613. FT VAR_SEQ 132 135 ASMR -> GIFE (in isoform Bim-beta2 and FT isoform Bim-beta6). FT /FTId=VSP_035614. FT VAR_SEQ 133 135 SMR -> NWD (in isoform Bim-beta1). FT /FTId=VSP_035615. FT VAR_SEQ 136 198 Missing (in isoform Bim-beta1, isoform FT Bim-beta2 and isoform Bim-beta6). FT /FTId=VSP_035616. FT VAR_SEQ 141 198 Missing (in isoform Bim-beta5 and isoform FT Bim-beta7). FT /FTId=VSP_035617. FT VAR_SEQ 167 198 VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH -> LEK FT (in isoform Bim-alpha1, isoform Bim- FT alpha2 and isoform Bim-alpha3). FT /FTId=VSP_035620. FT VAR_SEQ 167 198 VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH -> LAKLL FT ASST (in isoform Bim-alpha4). FT /FTId=VSP_035618. FT VAR_SEQ 167 198 VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH -> MPLPP FT D (in isoform Bim-alpha5 and isoform Bim- FT alpha6). FT /FTId=VSP_035619. FT CONFLICT 33 33 P -> L (in Ref. 6; BAF83066). FT HELIX 144 164 SQ SEQUENCE 198 AA; 22171 MW; D75735E469CA6997 CRC64; MAKQPSDVSS ECDREGRQLQ PAERPPQLRP GAPTSLQTEP QGNPEGNHGG EGDSCPHGSP QGPLAPPASP GPFATRSPLF IFMRRSSLLS RSSSGYFSFD TDRSPAPMSC DKSTQTPSPP CQAFNHYLSA MASMRQAEPA DMRPEIWIAQ ELRRIGDEFN AYYARRVFLN NYQAAEDHPR MVILRLLRYI VRLVWRMH //