ARI4B_MOUSE
ID ARI4B_MOUSE Reviewed; 1314 AA.
AC A2CG63; A2CG61; A2CG62; A2CG64; B2RQ67; Q8BMI8; Q8BYA5;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=Histone deacetylase complex subunit SAP180;
GN Name=Arid4b; Synonyms=Sap180;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-531.
RC STRAIN=C57BL/6J; TISSUE=Forelimb, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP FUNCTION, INTERACTION WITH ARID4A, AND DISRUPTION PHENOTYPE.
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18728284; DOI=10.1093/jnci/djn253;
RA Wu M.Y., Eldin K.W., Beaudet A.L.;
RT "Identification of chromatin remodeling genes Arid4a and Arid4b as leukemia
RT suppressor genes.";
RL J. Natl. Cancer Inst. 100:1247-1259(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668; SER-675; SER-790 AND
RP THR-793, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, INTERACTION WITH AR, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23487765; DOI=10.1073/pnas.1218318110;
RA Wu R.C., Jiang M., Beaudet A.L., Wu M.Y.;
RT "ARID4A and ARID4B regulate male fertility, a functional link to the AR and
RT RB pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:4616-4621(2013).
CC -!- FUNCTION: Acts as a transcriptional repressor. May function in the
CC assembly and/or enzymatic activity of the Sin3A corepressor complex or
CC in mediating interactions between the complex and other regulatory
CC complexes (By similarity). Plays a role in the regulation of epigenetic
CC modifications at the PWS/AS imprinting center near the SNRPN promoter,
CC where it might function as part of a complex with RB1 and ARID4A
CC (PubMed:17043311). 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 (PubMed:23487765). Plays a role in myeloid homeostasis where it
CC regulates the histone methylation state of bone marrow cells and
CC expression of various genes involved in hematopoiesis. May function as
CC a leukemia suppressor (PubMed:18728284). {ECO:0000250|UniProtKB:Q4LE39,
CC ECO:0000269|PubMed:17043311, ECO:0000269|PubMed:18728284,
CC ECO:0000269|PubMed:23487765}.
CC -!- SUBUNIT: Component of a Sin3A corepressor complex consisting of SIN3A,
CC SAP130, SUDS3/SAP45, SAP180, HDAC1 and HDAC2 (By similarity). Interacts
CC with ARID4A (PubMed:17043311). Interacts with AR (PubMed:23487765).
CC {ECO:0000250|UniProtKB:Q4LE39, ECO:0000269|PubMed:17043311,
CC ECO:0000269|PubMed:23487765}.
CC -!- INTERACTION:
CC A2CG63; P70278: Stra8; NbExp=4; IntAct=EBI-6394082, EBI-6394115;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2CG63-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2CG63-2; Sequence=VSP_024236;
CC -!- TISSUE SPECIFICITY: Expressed in Sertoli cells of the testis.
CC {ECO:0000269|PubMed:23487765}.
CC -!- DOMAIN: The C-terminus mediates interaction with mSin3A corepressor
CC complex. {ECO:0000250|UniProtKB:Q4LE39}.
CC -!- DOMAIN: The N-terminus is involved in transcriptional repression by
CC HDAC-independent mechanisms. {ECO:0000250|UniProtKB:Q4LE39}.
CC -!- DOMAIN: The ARID domain is involved in stabilizing the mSin3A
CC corepressor complex on DNA. {ECO:0000250|UniProtKB:Q4LE39}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal. Lethality occurs between
CC embryonic day E3.5 and E7.5 (PubMed:17043311). Heterozygous males are
CC fully fertile (PubMed:23487765). Double knockouts of ARID4B
CC heterozygotes with ARID4A homozygotes show various hematological
CC abnormalities, which are more severe than the ARID4A phenotype alone.
CC Hematopoietic stem cell (HSC) and common myeloid progenitor (CMP)
CC counts in bone marrow and spleen are increased. Lymphocyte numbers in
CC spleen are significantly reduced. In peripheral blood, red blood cell
CC counts and lymphocyte counts are reduced. Approximately 83% of animals
CC develop acute myeloid leukemia (AML) and/or myeloid sarcoma. In bone
CC marrow cells, expression of FOXP3 is significantly reduced
CC (PubMed:18728284). Expression of HOXB3, HOXB5, HOXB6, HOXB8 and PITX2
CC in bone marrow cells is reduced (PubMed:17043311). Males show
CC progressive reduction in fertility from 2 months of age onwards, with
CC reduced testis size and variable defects in seminal vesicle formation.
CC Spermatogenesis is partially blocked from the meiosis II stage onwards
CC leading to reduced numbers of mature spermatozoa. Expression in testis
CC of CLDN3, an androgen receptor-regulated gene, is significantly
CC reduced. Expression of PTGDS is also reduced, whereas expression of
CC INHA and EMB is moderately increased (PubMed:23487765).
CC {ECO:0000269|PubMed:17043311, ECO:0000269|PubMed:18728284,
CC ECO:0000269|PubMed:23487765}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM21242.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CT025604; CAM21242.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CT025604; CAM21243.1; -; Genomic_DNA.
DR EMBL; CT025604; CAM21244.1; -; Genomic_DNA.
DR EMBL; CT025604; CAM21245.1; -; Genomic_DNA.
DR EMBL; BC137783; AAI37784.1; -; mRNA.
DR EMBL; AK031062; BAC27233.1; -; mRNA.
DR EMBL; AK041414; BAC30936.1; -; mRNA.
DR CCDS; CCDS36599.1; -. [A2CG63-1]
DR CCDS; CCDS36600.1; -. [A2CG63-2]
DR RefSeq; NP_919238.1; NM_194262.2. [A2CG63-1]
DR RefSeq; NP_937755.1; NM_198122.2. [A2CG63-2]
DR RefSeq; XP_006516869.1; XM_006516806.2. [A2CG63-1]
DR RefSeq; XP_006516870.1; XM_006516807.2. [A2CG63-1]
DR RefSeq; XP_017171137.1; XM_017315648.1. [A2CG63-1]
DR AlphaFoldDB; A2CG63; -.
DR SMR; A2CG63; -.
DR BioGRID; 220492; 9.
DR ComplexPortal; CPX-3441; SIN3A histone deacetylase complex, ES cell-specific variant.
DR ComplexPortal; CPX-3443; SIN3A histone deacetylase complex.
DR ComplexPortal; CPX-3444; SIN3B histone deacetylase complex.
DR IntAct; A2CG63; 3.
DR MINT; A2CG63; -.
DR STRING; 10090.ENSMUSP00000106163; -.
DR iPTMnet; A2CG63; -.
DR PhosphoSitePlus; A2CG63; -.
DR EPD; A2CG63; -.
DR jPOST; A2CG63; -.
DR MaxQB; A2CG63; -.
DR PaxDb; A2CG63; -.
DR PeptideAtlas; A2CG63; -.
DR PRIDE; A2CG63; -.
DR ProteomicsDB; 265094; -. [A2CG63-1]
DR ProteomicsDB; 265095; -. [A2CG63-2]
DR Antibodypedia; 20807; 170 antibodies from 31 providers.
DR DNASU; 94246; -.
DR Ensembl; ENSMUST00000039538; ENSMUSP00000043889; ENSMUSG00000039219. [A2CG63-2]
DR Ensembl; ENSMUST00000110534; ENSMUSP00000106163; ENSMUSG00000039219. [A2CG63-1]
DR Ensembl; ENSMUST00000110536; ENSMUSP00000106165; ENSMUSG00000039219. [A2CG63-2]
DR GeneID; 94246; -.
DR KEGG; mmu:94246; -.
DR UCSC; uc007pmz.2; mouse. [A2CG63-1]
DR UCSC; uc007pna.2; mouse. [A2CG63-2]
DR CTD; 51742; -.
DR MGI; MGI:2137512; Arid4b.
DR VEuPathDB; HostDB:ENSMUSG00000039219; -.
DR eggNOG; KOG2744; Eukaryota.
DR eggNOG; KOG3001; Eukaryota.
DR GeneTree; ENSGT00940000158149; -.
DR HOGENOM; CLU_007419_0_0_1; -.
DR InParanoid; A2CG63; -.
DR OMA; XCTGQKR; -.
DR OrthoDB; 329541at2759; -.
DR PhylomeDB; A2CG63; -.
DR TreeFam; TF106427; -.
DR Reactome; R-MMU-3214815; HDACs deacetylate histones.
DR BioGRID-ORCS; 94246; 7 hits in 75 CRISPR screens.
DR ChiTaRS; Arid4b; mouse.
DR PRO; PR:A2CG63; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; A2CG63; protein.
DR Bgee; ENSMUSG00000039219; Expressed in metanephric cortical collecting duct and 251 other tissues.
DR ExpressionAtlas; A2CG63; baseline and differential.
DR Genevisible; A2CG63; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; IGI:MGI.
DR GO; GO:0036124; P:histone H3-K9 trimethylation; IGI:MGI.
DR GO; GO:0034773; P:histone H4-K20 trimethylation; IGI:MGI.
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; IGI:MGI.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; IGI:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IGI:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IGI:MGI.
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 Alternative splicing; Chromatin regulator; Coiled coil; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1314
FT /note="AT-rich interactive domain-containing protein 4B"
FT /id="PRO_0000282864"
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 123..169
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 439..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1256..1290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1227..1272
FT /evidence="ECO:0000255"
FT COMPBIAS 144..169
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 439..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..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..750
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..830
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..852
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..888
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1009
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1055
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1275..1290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
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 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 717
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT MOD_RES 778
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT MOD_RES 790
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 793
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1016
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT MOD_RES 1028
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT MOD_RES 1031
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT MOD_RES 1152
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT MOD_RES 1154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT MOD_RES 1155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT MOD_RES 1157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT MOD_RES 1161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT CROSSLNK 428
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT CROSSLNK 461
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT CROSSLNK 751
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q4LE39"
FT VAR_SEQ 528..614
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_024236"
SQ SEQUENCE 1314 AA; 147643 MW; DE5E69DAA208A200 CRC64;
MKALDEPPYL TVGTDVSAKY RGAFCEAKIK TAKRLVKVKV TFRHDSSTVE VQDDHIKGPL
KVGAIVEVKN LDGAYQEAVI NKLTDASWYT VVFDDGDEKT LRRSSLCLKG ERHFAESETL
DQLPLTNPEH FGTPVIGKKT NRGRRSNHIP EEESSSSSSD DDEEERKQTD ELLGKVVCVD
YVSLEKKKAM WFPALVVCPD CSDEIAVKKD NILVRSFKDG KFTSVPRKDV HEITSDTVPK
PDAVLKQAFD QALEFHKSRA IPANWKTELK EDSSSSEAEE EEEEEDDEKE KEDNSSEEEE
EIEPFPEERE NFLQQLYKFM EDRGTPINKR PVLGYRNLNL FKLFRLVHKL GGFDNIESGA
VWKQVYQDLG IPVLNSAAGY NVKCAYKKYL YGFEEYCRSA NIDFQMALPE KVLNKPCKDC
ENKEVKVKEE SETEIKEVNV EDSKNVMPKE ETPAEDESER KENIKPSLGS KKSLLECIPA
QSDEEKEAHI TKLEENENLE DKDGGRARTE EAFSTEVDGE EEQARSGDET NKEEDEDDEE
IEEEEEEDEE EDEDEDDDDN NEEEEFECYP PGMKVQVRYG RGKNQKMYEA SIKDSDVEGG
EALYLVHYCG WNVRYDEWIK ADKIVRPADK NVPKIKHRKK IKNKLDKEKD RDEKYSPKNC
KLRRLSKSPF QSNPSPEMVS KLDLADAKNS DTAHIKSIEI TSILNGLQAS ESSAEDSEQE
DERCTQDVDN IGKDESKVEH STHSRNELIS KEEQSSPSLL EENKVHTDLV IAKTVSKSPE
RLRKDMEAIS EDTDFEEEDE ITKKRKDVKK DTTDKALKPQ TKRGKRRYCS ADECLQTGSP
GKKEDRTKSK EPLCTENSSN SSSDEDEEEK SKAKMTPTKK YNGLEEKRKS LRTTSFYSGF
SEVAEKRIKL LNNSDERLQN NRAKDRKDVW SSIQGQWPKK TLKELFSDSD TEAAASPPHP
APDEGAVEES LQTVAEEESC SPIMELEKPL PASVDNKPIE EKPLEVSDRK TEFPSSGSNS
VLNTPPTTPE SPSSVTITEA SQQQSSVTVS VPLPPNQEEV RSIKSETDST IEVDSVVGEL
QDLQSEGNSS PAGFDASVSS SSSNQPEPDN PEKACTGQKR VKDTQGVGSS SKKQKRSHKA
TVVNNKKKGK GTNSSDSEEL SAGESVTKTQ TIKSVPTGMK THNSKSPARV QSPGKGGRNG
DKDPDLKEPS NRLPKVYKWS FQTSDLENMT SAERISILQE KLQEIRKHYL SLKSEVASID
RRRKRLKKKE RESAATSSSS SSPSSSSITA AVMLTLAEPS MSSASQNGMS VECR
