ARI4B_HUMAN
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 03-AUG-2022, entry version 153.
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;
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};
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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_001206794.1. [Q4LE39-1]
DR RefSeq; NP_057458.4; NM_016374.5. [Q4LE39-1]
DR RefSeq; NP_112739.2; NM_031371.3. [Q4LE39-2]
DR RefSeq; XP_011542514.1; XM_011544212.2. [Q4LE39-1]
DR PDB; 7DM4; NMR; -; A=1-151.
DR PDBsum; 7DM4; -.
DR AlphaFoldDB; Q4LE39; -.
DR SMR; Q4LE39; -.
DR BioGRID; 119708; 160.
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 IntAct; Q4LE39; 95.
DR MINT; Q4LE39; -.
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 EPD; Q4LE39; -.
DR jPOST; Q4LE39; -.
DR MassIVE; Q4LE39; -.
DR MaxQB; Q4LE39; -.
DR PaxDb; Q4LE39; -.
DR PeptideAtlas; Q4LE39; -.
DR PRIDE; Q4LE39; -.
DR ProteomicsDB; 62238; -. [Q4LE39-1]
DR ProteomicsDB; 62239; -. [Q4LE39-2]
DR ProteomicsDB; 62240; -. [Q4LE39-3]
DR ProteomicsDB; 62241; -. [Q4LE39-4]
DR ABCD; Q4LE39; 1 sequenced antibody.
DR Antibodypedia; 20807; 170 antibodies from 31 providers.
DR DNASU; 51742; -.
DR Ensembl; ENST00000264183.9; ENSP00000264183.3; ENSG00000054267.22. [Q4LE39-1]
DR Ensembl; ENST00000349213.7; ENSP00000264184.4; ENSG00000054267.22. [Q4LE39-2]
DR Ensembl; ENST00000366603.6; ENSP00000355562.2; ENSG00000054267.22. [Q4LE39-1]
DR Ensembl; ENST00000421364.5; ENSP00000394663.1; ENSG00000054267.22. [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 CTD; 51742; -.
DR DisGeNET; 51742; -.
DR GeneCards; ARID4B; -.
DR HGNC; HGNC:15550; ARID4B.
DR HPA; ENSG00000054267; Low tissue specificity.
DR MIM; 609696; gene.
DR neXtProt; NX_Q4LE39; -.
DR OpenTargets; ENSG00000054267; -.
DR PharmGKB; PA134940494; -.
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; XCTGQKR; -.
DR PhylomeDB; Q4LE39; -.
DR TreeFam; TF106427; -.
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 BioGRID-ORCS; 51742; 91 hits in 1091 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 198 other tissues.
DR ExpressionAtlas; Q4LE39; baseline and differential.
DR Genevisible; Q4LE39; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016580; C:Sin3 complex; IC:ComplexPortal.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0097368; P:establishment of Sertoli cell barrier; IEA:Ensembl.
DR GO; GO:0036124; P:histone H3-K9 trimethylation; IEA:Ensembl.
DR GO; GO:0034773; P:histone H4-K20 trimethylation; IEA:Ensembl.
DR GO; GO:0030336; P:negative regulation of cell migration; IC:ComplexPortal.
DR GO; GO:1902455; P:negative regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR Gene3D; 1.10.150.60; -; 1.
DR InterPro; IPR028853; ARID4B.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR012603; RBB1NT.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR025995; Tudor-knot.
DR PANTHER; PTHR13964:SF24; PTHR13964:SF24; 1.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF08169; RBB1NT; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00333; TUDOR; 2.
DR SUPFAM; SSF46774; SSF46774; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
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 Reference proteome; Transcription; Transcription regulation;
KW 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 144..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..306
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..566
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..747
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..890
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 992..1007
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1288
FT /note="Polar residues"
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
