ID ARI4B_HUMAN Reviewed; 1312 AA. AC Q4LE39; A1L465; Q3MHV4; Q5HY99; Q5T2C2; Q5T2C3; Q5T2C4; Q5T2C5; Q5T2C6; AC Q6P600; Q86UX1; Q86WR4; Q9H915; Q9NYU3; Q9NZB6; Q9NZG4; Q9P2W4; Q9UF62; AC Q9Y6E1; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 2. DT 04-NOV-2026, entry version 173. DE RecName: Full=AT-rich interactive domain-containing protein 4B; DE Short=ARID domain-containing protein 4B; DE AltName: Full=180 kDa Sin3-associated polypeptide; DE Short=Sin3-associated polypeptide p180; DE AltName: Full=Breast cancer-associated antigen BRCAA1; DE AltName: Full=Histone deacetylase complex subunit SAP180; DE AltName: Full=Retinoblastoma-binding protein 1-like 1; GN Name=ARID4B; Synonyms=BRCAA1, RBBP1L1, RBP1L1, SAP180; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=11481388; DOI=10.1093/jnci/93.15.1159; RA Cao J.-N., Gao T.-W., Stanbridge E.J., Irie R.; RT "RBP1L1, a retinoblastoma-binding protein-related gene encoding an RT antigenic epitope abundantly expressed in human carcinomas and normal RT testis."; RL J. Natl. Cancer Inst. 93:1159-1165(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DOMAIN, TISSUE RP SPECIFICITY, AND IDENTIFICATION IN A MSIN3A COREPRESSOR COMPLEX WITH SIN3A; RP SAP130; SUDS3; ARID4B; HDAC1 AND HDAC2. RX PubMed=12724404; DOI=10.1128/mcb.23.10.3456-3467.2003; RA Fleischer T.C., Yun U.J., Ayer D.E.; RT "Identification and characterization of three new components of the mSin3A RT corepressor complex."; RL Mol. Cell. Biol. 23:3456-3467(2003). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=15247124; DOI=10.1158/1055-9965.1136.13.7; RA Cui D., Jin G., Gao T.W., Sun T., Tian F., Estrada G.G., Gao H., Sarai A.; RT "Characterization of BRCAA1 and its novel antigen epitope identification."; RL Cancer Epidemiol. Biomarkers Prev. 13:1136-1145(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4). RC TISSUE=Synovium; RA Tanaka M.; RT "Rheumatoid arthritis antigenic protein similar to retinoblastoma binding RT protein 1 (RBP1)."; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RA Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., RA Okazaki N., Koga H., Nagase T., Ohara O.; RT "Preparation of a set of expression-ready clones of mammalian long cDNAs RT encoding large proteins by the ORF trap cloning method."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 1-651 (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [LARGE RP SCALE MRNA] OF 1-424. RC TISSUE=Hippocampus, Kidney, and Lung; 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1149 (ISOFORM 2), AND RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1147-1312. RC TISSUE=Adipose tissue, 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., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 440-1312 (ISOFORM 1). RA Cao J., Irie R.F., Stanbridge E.J.; RT "Human breast carcinoma-associated antigen isoform I."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 547-1312. RA Liu T., Tao J., Zhang J., Li W., Ye M., Zhou J., Wu J., Shen Y., Yu M., RA Chen S., Mao M., Chen Z.; RT "Human Rb binding protein homolog gene, partial CDS."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 828-1312. 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-717, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [13] RP INTERACTION WITH ARID4A. RX PubMed=17043311; DOI=10.1101/gad.1452206; RA Wu M.Y., Tsai T.F., Beaudet A.L.; RT "Deficiency of Rbbp1/Arid4a and Rbbp1l1/Arid4b alters epigenetic RT modifications and suppresses an imprinting defect in the PWS/AS domain."; RL Genes Dev. 20:2859-2870(2006). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666; SER-675; SER-790; RP THR-793; THR-1150; SER-1152; SER-1153; SER-1155 AND SER-1159, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; 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). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-790; THR-793; SER-1014 AND RP THR-1026, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675; SER-778; SER-790 AND RP THR-793, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276; SER-778; SER-790 AND RP THR-793, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483; SER-666; SER-675; RP SER-778; SER-1029 AND SER-1153, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [21] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-429, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [22] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-429, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [23] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-429 AND LYS-440, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [24] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-429; LYS-440; LYS-462; LYS-517 RP AND LYS-751, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). CC -!- FUNCTION: Acts as a transcriptional repressor (PubMed:12724404). May CC function in the assembly and/or enzymatic activity of the Sin3A CC corepressor complex or in mediating interactions between the complex CC and other regulatory complexes (PubMed:12724404). Plays a role in the CC regulation of epigenetic modifications at the PWS/AS imprinting center CC near the SNRPN promoter, where it might function as part of a complex CC with RB1 and ARID4A. Involved in spermatogenesis, together with ARID4A, CC where it functions as a transcriptional coactivator for AR (androgen CC receptor) and enhances expression of genes required for sperm CC maturation. Regulates expression of the tight junction protein CLDN3 in CC the testis, which is important for integrity of the blood-testis CC barrier. Plays a role in myeloid homeostasis where it regulates the CC histone methylation state of bone marrow cells and expression of CC various genes involved in hematopoiesis. May function as a leukemia CC suppressor (By similarity). {ECO:0000250|UniProtKB:A2CG63, CC ECO:0000269|PubMed:12724404}. CC -!- SUBUNIT: Component of a Sin3A corepressor complex consisting of SIN3A, CC SAP130, SUDS3/SAP45, SAP180, HDAC1 and HDAC2 (PubMed:12724404). CC Interacts with ARID4A (PubMed:17043311). Interacts with AR (By CC similarity). {ECO:0000250|UniProtKB:A2CG63, CC ECO:0000269|PubMed:12724404, ECO:0000269|PubMed:17043311}. CC -!- INTERACTION: CC Q4LE39; P14921: ETS1; NbExp=2; IntAct=EBI-2680990, EBI-913209; CC Q4LE39-3; Q9BTE6-2: AARSD1; NbExp=3; IntAct=EBI-11957452, EBI-9357295; CC Q4LE39-3; Q9NQM4: DNAAF6; NbExp=3; IntAct=EBI-11957452, EBI-10239299; CC Q4LE39-3; P63172: DYNLT1; NbExp=3; IntAct=EBI-11957452, EBI-1176455; CC Q4LE39-3; Q96JC9: EAF1; NbExp=3; IntAct=EBI-11957452, EBI-769261; CC Q4LE39-3; I6L957: HNRNPA2B1; NbExp=3; IntAct=EBI-11957452, EBI-1642515; CC Q4LE39-3; Q5HYW2: NHSL2; NbExp=3; IntAct=EBI-11957452, EBI-2859639; CC Q4LE39-3; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-11957452, EBI-741158; CC Q4LE39-3; Q92569: PIK3R3; NbExp=3; IntAct=EBI-11957452, EBI-79893; CC Q4LE39-3; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-11957452, EBI-742388; CC Q4LE39-3; Q6ZRT6: PRR23B; NbExp=3; IntAct=EBI-11957452, EBI-12845180; CC Q4LE39-3; Q9NS25: SPANXB1; NbExp=3; IntAct=EBI-11957452, EBI-17197485; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355}. CC Cytoplasm {ECO:0000269|PubMed:11481388, ECO:0000269|PubMed:15247124}. CC Note=Cytoplasmic in breast cancer cells. {ECO:0000269|PubMed:15247124}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q4LE39-1; Sequence=Displayed; CC Name=2; CC IsoId=Q4LE39-2; Sequence=VSP_024231; CC Name=3; CC IsoId=Q4LE39-3; Sequence=VSP_024234, VSP_024235; CC Name=4; CC IsoId=Q4LE39-4; Sequence=VSP_024230, VSP_024232, VSP_024233; CC -!- TISSUE SPECIFICITY: Highly expressed in the testis and in breast, lung, CC colon, pancreatic and ovarian cancers. Expressed at low levels in the CC thymus, prostate and ovary. {ECO:0000269|PubMed:11481388, CC ECO:0000269|PubMed:12724404, ECO:0000269|PubMed:15247124}. CC -!- DOMAIN: The C-terminus mediates interaction with mSin3A corepressor CC complex. {ECO:0000269|PubMed:12724404}. CC -!- DOMAIN: The N-terminus is involved in transcriptional repression by CC HDAC-independent mechanisms. {ECO:0000269|PubMed:12724404}. CC -!- DOMAIN: The ARID domain is involved in stabilizing the mSin3A CC corepressor complex on DNA. {ECO:0000269|PubMed:12724404}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD41239.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAF23433.3; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAB14428.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAE06114.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF214114; AAF28341.2; -; mRNA. DR EMBL; AY220790; AAO63590.1; -; mRNA. DR EMBL; AF208045; AAF23433.3; ALT_FRAME; mRNA. DR EMBL; AB030181; BAA89794.1; -; mRNA. DR EMBL; AB210032; BAE06114.1; ALT_INIT; mRNA. DR EMBL; AL133418; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL391994; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC048959; AAH48959.1; ALT_TERM; mRNA. DR EMBL; BC062536; AAH62536.1; ALT_TERM; mRNA. DR EMBL; BC104632; AAI04633.1; ALT_TERM; mRNA. DR EMBL; BC130418; AAI30419.1; -; mRNA. DR EMBL; BX648820; CAI46047.1; -; mRNA. DR EMBL; AL133594; CAB63731.1; -; mRNA. DR EMBL; AF227899; AAF36964.1; -; mRNA. DR EMBL; AF083249; AAD41239.1; ALT_FRAME; mRNA. DR EMBL; AK023144; BAB14428.1; ALT_INIT; mRNA. DR CCDS; CCDS31060.1; -. [Q4LE39-2] DR CCDS; CCDS31061.1; -. [Q4LE39-1] DR PIR; T43497; T43497. DR RefSeq; NP_001193723.1; NM_001206794.2. [Q4LE39-1] DR RefSeq; NP_057458.4; NM_016374.6. [Q4LE39-1] DR RefSeq; NP_112739.2; NM_031371.4. [Q4LE39-2] DR RefSeq; XP_011542514.1; XM_011544212.4. [Q4LE39-1] DR RefSeq; XP_024303394.1; XM_024447626.2. [Q4LE39-2] DR RefSeq; XP_054192975.1; XM_054337000.1. [Q4LE39-1] DR RefSeq; XP_054192978.1; XM_054337003.1. [Q4LE39-2] DR PDB; 7DM4; NMR; -; A=1-151. DR AlphaFoldDB; Q4LE39; -. DR SMR; Q4LE39; -. DR BioGRID; 119708; 206. DR ComplexPortal; CPX-3321; SIN3A histone deacetylase complex. DR ComplexPortal; CPX-3322; SIN3B histone deacetylase complex. DR ComplexPortal; CPX-3323; SIN3A histone deacetylase complex, ES cell-specific variant. DR CORUM; Q4LE39; -. DR FunCoup; Q4LE39; 4909. DR IntAct; Q4LE39; 114. DR NDEx; IQUERY-CP-ARID4B; 1 NDEx IQuery Curated Pathway. DR STRING; 9606.ENSP00000264183; -. DR GlyGen; Q4LE39; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q4LE39; -. DR PhosphoSitePlus; Q4LE39; -. DR BioMuta; ARID4B; -. DR DMDM; 143955276; -. DR CPTAC; CPTAC-1754; -. DR jPOST; Q4LE39; -. DR MassIVE; Q4LE39; -. DR PaxDb; 9606-ENSP00000264183; -. DR PeptideAtlas; Q4LE39; -. DR ProteomicsDB; 62238; -. [Q4LE39-1] DR ProteomicsDB; 62239; -. [Q4LE39-2] DR ProteomicsDB; 62240; -. [Q4LE39-3] DR ProteomicsDB; 62241; -. [Q4LE39-4] DR Pumba; Q4LE39; -. DR ABCD; Q4LE39; 1 sequenced antibody. DR Antibodypedia; 20807; 192 antibodies from 33 providers. DR DNASU; 51742; -. DR Ensembl; ENST00000264183.9; ENSP00000264183.3; ENSG00000054267.23. [Q4LE39-1] DR Ensembl; ENST00000349213.7; ENSP00000264184.4; ENSG00000054267.23. [Q4LE39-2] DR Ensembl; ENST00000366603.6; ENSP00000355562.2; ENSG00000054267.23. [Q4LE39-1] DR Ensembl; ENST00000421364.5; ENSP00000394663.1; ENSG00000054267.23. [Q4LE39-3] DR GeneID; 51742; -. DR KEGG; hsa:51742; -. DR MANE-Select; ENST00000264183.9; ENSP00000264183.3; NM_016374.6; NP_057458.4. DR UCSC; uc001hwq.3; human. [Q4LE39-1] DR AGR; HGNC:15550; -. DR ClinPGx; PA134940494; -. DR CTD; 51742; -. DR DisGeNET; 51742; -. DR GeneCards; ARID4B; -. DR HGNC; HGNC:15550; ARID4B. DR HPA; ENSG00000054267; Low tissue specificity. DR MIM; 609696; gene. DR OpenTargets; ENSG00000054267; -. DR VEuPathDB; HostDB:ENSG00000054267; -. DR eggNOG; KOG2744; Eukaryota. DR eggNOG; KOG3001; Eukaryota. DR GeneTree; ENSGT00940000158149; -. DR HOGENOM; CLU_007419_0_0_1; -. DR InParanoid; Q4LE39; -. DR OMA; AAFCGWS; -. DR OrthoDB; 10068428at2759; -. DR PAN-GO; Q4LE39; 3 GO annotations based on evolutionary models. DR PhylomeDB; Q4LE39; -. DR PathwayCommons; Q4LE39; -. DR Reactome; R-HSA-3214815; HDACs deacetylate histones. DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression. DR Reactome; R-HSA-9679191; Potential therapeutics for SARS. DR SignaLink; Q4LE39; -. DR Agora; ENSG00000054267; -. DR BioGRID-ORCS; 51742; 96 hits in 1172 CRISPR screens. DR ChiTaRS; ARID4B; human. DR GeneWiki; ARID4B; -. DR GenomeRNAi; 51742; -. DR Pharos; Q4LE39; Tbio. DR PRO; PR:Q4LE39; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q4LE39; protein. DR Bgee; ENSG00000054267; Expressed in choroid plexus epithelium and 200 other cell types or tissues. DR ExpressionAtlas; Q4LE39; baseline and differential. DR GO; GO:0005737; C:cytoplasm; EXP:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0070822; C:Sin3-type complex; NAS:ComplexPortal. DR GO; GO:0003677; F:DNA binding; IMP:DisProt. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central. DR GO; GO:0030336; P:negative regulation of cell migration; NAS:ComplexPortal. DR GO; GO:1902455; P:negative regulation of stem cell population maintenance; NAS:ComplexPortal. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; NAS:ComplexPortal. DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; NAS:ComplexPortal. DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; NAS:ComplexPortal. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd16883; ARID_ARID4B; 1. DR CDD; cd20460; Tudor_ARID4B_rpt1; 1. DR CDD; cd20462; Tudor_ARID4B_rpt2; 1. DR DisProt; DP03669; -. DR FunFam; 2.30.30.140:FF:000012; AT-rich interactive domain-containing protein 4A; 1. DR FunFam; 2.30.30.140:FF:000009; AT-rich interactive domain-containing protein 4B; 1. DR FunFam; 2.30.30.140:FF:000044; AT-rich interactive domain-containing protein 4B isoform X1; 1. DR Gene3D; 2.30.30.140; -; 3. DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1. DR InterPro; IPR012603; ARID4A/B_PWWP. DR InterPro; IPR028853; ARID4B_ARID/BRIGHT. DR InterPro; IPR001606; ARID_dom. DR InterPro; IPR036431; ARID_dom_sf. DR InterPro; IPR016197; Chromo-like_dom_sf. DR InterPro; IPR002999; Tudor. DR InterPro; IPR025995; Tudor-knot. DR InterPro; IPR047476; Tudor_ARID4B_rpt1. DR InterPro; IPR047474; Tudor_ARID4B_rpt2. DR PANTHER; PTHR13964:SF24; AT-RICH INTERACTIVE DOMAIN-CONTAINING PROTEIN 4B; 1. DR PANTHER; PTHR13964; RBP-RELATED; 1. DR Pfam; PF01388; ARID; 1. DR Pfam; PF08169; RBB1NT; 1. DR Pfam; PF11717; Tudor-knot; 1. DR SMART; SM01014; ARID; 1. DR SMART; SM00501; BRIGHT; 1. DR SMART; SM00333; TUDOR; 2. DR SUPFAM; SSF46774; ARID-like; 1. DR SUPFAM; SSF54160; Chromo domain-like; 1. DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2. DR PROSITE; PS51011; ARID; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chromatin regulator; Coiled coil; KW Cytoplasm; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; KW Proteomics identification; Reference proteome; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..1312 FT /note="AT-rich interactive domain-containing protein 4B" FT /id="PRO_0000282863" FT DOMAIN 306..398 FT /note="ARID" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355" FT DOMAIN 572..624 FT /note="Tudor-knot" FT /evidence="ECO:0000255" FT REGION 124..166 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 266..306 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 458..577 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 465..473 FT /note="Antigenic epitope" FT REGION 635..680 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 708..894 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 909..1212 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1130..1137 FT /note="Antigenic epitope" FT REGION 1252..1288 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 728..754 FT /evidence="ECO:0000255" FT COILED 1231..1270 FT /evidence="ECO:0000255" FT COMPBIAS 277..305 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 483..496 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 532..567 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 643..656 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 722..754 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 778..787 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 788..799 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 807..816 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 828..852 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 909..927 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 995..1010 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1028..1037 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1038..1047 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1056..1065 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1087..1101 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1130..1148 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1162..1191 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1196..1208 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1272..1288 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 276 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 295 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JKB5" FT MOD_RES 296 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JKB5" FT MOD_RES 483 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 666 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 675 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 717 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983" FT MOD_RES 778 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 790 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 793 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 1014 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 1026 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 1029 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1150 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1152 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1153 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1155 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1159 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT CROSSLNK 429 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 440 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 462 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 517 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 751 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..319 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_024230" FT VAR_SEQ 529..614 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11481388, FT ECO:0000303|PubMed:15247124, ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:17974005" FT /id="VSP_024231" FT VAR_SEQ 1112..1122 FT /note="ACTGQKRVKDA -> GEKENVYVDLF (in isoform 4)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_024232" FT VAR_SEQ 1123..1312 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_024233" FT VAR_SEQ 1150..1153 FT /note="TNSS -> SAPH (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_024234" FT VAR_SEQ 1154..1312 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_024235" FT CONFLICT 15 FT /note="D -> G (in Ref. 2; AAO63590)" FT /evidence="ECO:0000305" FT CONFLICT 79 FT /note="V -> A (in Ref. 2; AAO63590)" FT /evidence="ECO:0000305" FT CONFLICT 330 FT /note="R -> Q (in Ref. 1; AAF28341 and 3; AAF23433)" FT /evidence="ECO:0000305" FT CONFLICT 400 FT /note="A -> P (in Ref. 4; BAA89794)" FT /evidence="ECO:0000305" FT CONFLICT 436 FT /note="I -> IEFCGR (in Ref. 3; AAF23433)" FT /evidence="ECO:0000305" FT CONFLICT 437 FT /note="K -> Q (in Ref. 4; BAA89794)" FT /evidence="ECO:0000305" FT CONFLICT 559..561 FT /note="DNN -> ATI (in Ref. 4; BAA89794)" FT /evidence="ECO:0000305" FT CONFLICT 568 FT /note="C -> S (in Ref. 4; BAA89794)" FT /evidence="ECO:0000305" FT CONFLICT 575 FT /note="V -> A (in Ref. 4; BAA89794)" FT /evidence="ECO:0000305" FT CONFLICT 584 FT /note="N -> H (in Ref. 4; BAA89794)" FT /evidence="ECO:0000305" FT CONFLICT 605 FT /note="L -> S (in Ref. 9; AAF36964)" FT /evidence="ECO:0000305" FT CONFLICT 616 FT /note="D -> G (in Ref. 9; AAF36964)" FT /evidence="ECO:0000305" FT CONFLICT 813 FT /note="D -> G (in Ref. 2; AAO63590)" FT /evidence="ECO:0000305" FT CONFLICT 915..917 FT /note="RLQ -> LP (in Ref. 3; AAF23433)" FT /evidence="ECO:0000305" FT CONFLICT 940 FT /note="L -> R (in Ref. 3; AAF23433)" FT /evidence="ECO:0000305" FT CONFLICT 1000 FT /note="K -> E (in Ref. 1; AAF28341 and 9; AAF36964)" FT /evidence="ECO:0000305" FT CONFLICT 1001 FT /note="T -> Q (in Ref. 3; AAF23433)" FT /evidence="ECO:0000305" FT CONFLICT 1032 FT /note="S -> P (in Ref. 2; AAO63590)" FT /evidence="ECO:0000305" FT CONFLICT 1087 FT /note="S -> N (in Ref. 2; AAO63590)" FT /evidence="ECO:0000305" FT CONFLICT 1118 FT /note="R -> G (in Ref. 8; CAI46047)" FT /evidence="ECO:0000305" FT CONFLICT 1144 FT /note="K -> T (in Ref. 3; AAF23433 and 10; AAD41239)" FT /evidence="ECO:0000305" FT CONFLICT 1243..1244 FT /note="IR -> NQ (in Ref. 3; AAF23433 and 10; AAD41239)" FT /evidence="ECO:0000305" FT CONFLICT 1290 FT /note="V -> A (in Ref. 1; AAF28341 and 9; AAF36964)" FT /evidence="ECO:0000305" FT STRAND 15..20 FT /evidence="ECO:0007829|PDB:7DM4" FT STRAND 23..42 FT /evidence="ECO:0007829|PDB:7DM4" FT TURN 43..45 FT /evidence="ECO:0007829|PDB:7DM4" FT STRAND 48..52 FT /evidence="ECO:0007829|PDB:7DM4" FT HELIX 53..55 FT /evidence="ECO:0007829|PDB:7DM4" FT STRAND 56..58 FT /evidence="ECO:0007829|PDB:7DM4" FT STRAND 65..69 FT /evidence="ECO:0007829|PDB:7DM4" FT STRAND 75..92 FT /evidence="ECO:0007829|PDB:7DM4" FT STRAND 98..102 FT /evidence="ECO:0007829|PDB:7DM4" FT HELIX 103..105 FT /evidence="ECO:0007829|PDB:7DM4" FT STRAND 106..111 FT /evidence="ECO:0007829|PDB:7DM4" FT STRAND 133..136 FT /evidence="ECO:0007829|PDB:7DM4" FT TURN 146..148 FT /evidence="ECO:0007829|PDB:7DM4" SQ SEQUENCE 1312 AA; 147809 MW; E4175FF80F5217EE CRC64; MKALDEPPYL TVGTDVSAKY RGAFCEAKIK TAKRLVKVKV TFRHDSSTVE VQDDHIKGPL KVGAIVEVKN LDGAYQEAVI NKLTDASWYT VVFDDGDEKT LRRSSLCLKG ERHFAESETL DQLPLTNPEH FGTPVIGKKT NRGRRSNHIP EEESSSSSSD EDEDDRKQID ELLGKVVCVD YISLDKKKAL WFPALVVCPD CSDEIAVKKD NILVRSFKDG KFTSVPRKDV HEITSDTAPK PDAVLKQAFE QALEFHKSRT IPANWKTELK EDSSSSEAEE EEEEEDDEKE KEDNSSEEEE EIEPFPEERE NFLQQLYKFM EDRGTPINKR PVLGYRNLNL FKLFRLVHKL GGFDNIESGA VWKQVYQDLG IPVLNSAAGY NVKCAYKKYL YGFEEYCRSA NIEFQMALPE KVVNKQCKEC ENVKEIKVKE ENETEIKEIK MEEERNIIPR EEKPIEDEIE RKENIKPSLG SKKNLLESIP THSDQEKEVN IKKPEDNENL DDKDDDTTRV DESLNIKVEA EEEKAKSGDE TNKEEDEDDE EAEEEEEEEE EEEDEDDDDN NEEEEFECYP PGMKVQVRYG RGKNQKMYEA SIKDSDVEGG EVLYLVHYCG WNVRYDEWIK ADKIVRPADK NVPKIKHRKK IKNKLDKEKD KDEKYSPKNC KLRRLSKPPF QTNPSPEMVS KLDLTDAKNS DTAHIKSIEI TSILNGLQAS ESSAEDSEQE DERGAQDMDN NGKEESKIDH LTNNRNDLIS KEEQNSSSLL EENKVHADLV ISKPVSKSPE RLRKDIEVLS EDTDYEEDEV TKKRKDVKKD TTDKSSKPQI KRGKRRYCNT EECLKTGSPG KKEEKAKNKE SLCMENSSNS SSDEDEEETK AKMTPTKKYN GLEEKRKSLR TTGFYSGFSE VAEKRIKLLN NSDERLQNSR AKDRKDVWSS IQGQWPKKTL KELFSDSDTE AAASPPHPAP EEGVAEESLQ TVAEEESCSP SVELEKPPPV NVDSKPIEEK TVEVNDRKAE FPSSGSNSVL NTPPTTPESP SSVTVTEGSR QQSSVTVSEP LAPNQEEVRS IKSETDSTIE VDSVAGELQD LQSEGNSSPA GFDASVSSSS SNQPEPEHPE KACTGQKRVK DAQGGGSSSK KQKRSHKATV VNNKKKGKGT NSSDSEELSA GESITKSQPV KSVSTGMKSH STKSPARTQS PGKCGKNGDK DPDLKEPSNR LPKVYKWSFQ MSDLENMTSA ERITILQEKL QEIRKHYLSL KSEVASIDRR RKRLKKKERE SAATSSSSSS PSSSSITAAV MLTLAEPSMS SASQNGMSVE CR //