ID BAZ1B_MOUSE Reviewed; 1479 AA. AC Q9Z277; B9EJ99; Q3URP5; Q3USR7; Q3UVM2; Q8CAU9; Q9CU68; DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 2. DT 24-JAN-2024, entry version 180. DE RecName: Full=Tyrosine-protein kinase BAZ1B; DE EC=2.7.10.2 {ECO:0000250|UniProtKB:Q9UIG0}; DE AltName: Full=Bromodomain adjacent to zinc finger domain protein 1B; DE AltName: Full=Williams syndrome transcription factor homolog; DE AltName: Full=Williams-Beuren syndrome chromosomal region 9 protein homolog; GN Name=Baz1b; Synonyms=Wbscr9, Wstf; 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 [MRNA]. RX PubMed=9858827; DOI=10.1159/000015110; RA Peoples R.J., Cisco M.J., Kaplan P., Francke U.; RT "Identification of the WBSCR9 gene, encoding a novel transcriptional RT regulator, in the Williams-Beuren syndrome deletion at 7q11.23."; RL Cytogenet. Cell Genet. 82:238-246(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-810 AND 823-1799 (ISOFORM 1), RP AND NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-786 (ISOFORM 2). RC STRAIN=C57BL/6J; RC TISSUE=Corpora quadrigemina, Thymus, and Urinary bladder; 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 [5] RP FUNCTION, IDENTIFICATION IN THE WICH-5 ISWI CHROMATIN-REMODELING COMPLEX, RP AND INTERACTION WITH SMARCA5. RX PubMed=11980720; DOI=10.1093/emboj/21.9.2231; RA Bozhenok L., Wade P.A., Varga-Weisz P.; RT "WSTF-ISWI chromatin remodeling complex targets heterochromatic replication RT foci."; RL EMBO J. 21:2231-2241(2002). RN [6] RP FUNCTION, AND INTERACTION WITH MYO1C. RX PubMed=16514417; DOI=10.1038/sj.embor.7400657; RA Percipalle P., Fomproix N., Cavellan E., Voit R., Reimer G., Krueger T., RA Thyberg J., Scheer U., Grummt I., Oestlund Farrants A.-K.O.; RT "The chromatin remodelling complex WSTF-SNF2h interacts with nuclear myosin RT 1 and has a role in RNA polymerase I transcription."; RL EMBO Rep. 7:525-530(2006). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361 AND SER-1464, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [9] RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH RP SMARCA5. RX PubMed=19092802; DOI=10.1038/nature07668; RA Xiao A., Li H., Shechter D., Ahn S.H., Fabrizio L.A., Erdjument-Bromage H., RA Ishibe-Murakami S., Wang B., Tempst P., Hofmann K., Patel D.J., RA Elledge S.J., Allis C.D.; RT "WSTF regulates the H2A.X DNA damage response via a novel tyrosine kinase RT activity."; RL Nature 457:57-62(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-158; SER-161; RP SER-325; SER-706; SER-709; SER-1464; SER-1466 AND SER-1468, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, 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 [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1331, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Atypical tyrosine-protein kinase that plays a central role in CC chromatin remodeling and acts as a transcription regulator (By CC similarity). Involved in DNA damage response by phosphorylating 'Tyr- CC 142' of histone H2AX (H2AXY142ph) (PubMed:19092802). H2AXY142ph plays a CC central role in DNA repair and acts as a mark that distinguishes CC between apoptotic and repair responses to genotoxic stress CC (PubMed:19092802). Regulatory subunit of the ATP-dependent WICH-1 and CC WICH-5 ISWI chromatin remodeling complexes, which form ordered CC nucleosome arrays on chromatin and facilitate access to DNA during DNA- CC templated processes such as DNA replication, transcription, and repair CC (PubMed:11980720). Both complexes regulate the spacing of nucleosomes CC along the chromatin and have the ability to slide mononucleosomes to CC the center of a DNA template (PubMed:16514417). The WICH-1 ISWI CC chromatin remodeling complex has a lower ATP hydrolysis rate than the CC WICH-5 ISWI chromatin remodeling complex (By similarity). The WICH-5 CC ISWI chromatin remodeling complex regulates the transcription of CC various genes, has a role in RNA polymerase I transcription CC (PubMed:16514417). Within the B-WICH complex has a role in RNA CC polymerase III transcription (By similarity). Mediates the recruitment CC of the WICH-5 ISWI chromatin remodeling complex to replication foci CC during DNA replication (By similarity). {ECO:0000250|UniProtKB:Q9UIG0, CC ECO:0000269|PubMed:11980720, ECO:0000269|PubMed:16514417, CC ECO:0000269|PubMed:19092802}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; CC Evidence={ECO:0000250|UniProtKB:Q9UIG0}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000250|UniProtKB:Q9UIG0}; CC -!- SUBUNIT: Component of the WICH-1 ISWI chromatin remodeling complex, at CC least composed of SMARCA1 and BAZ1B/WSTF, which regulates the spacing CC of histone octamers on the DNA template to facilitate access to DNA (By CC similarity). Within the WICH-1 ISWI chromatin remodeling complex CC interacts with SMARCA1; the interaction is direct (By similarity). CC Component of the WICH-5 ISWI chromatin remodeling complex (also called CC the WICH complex), at least composed of SMARCA5/SNF2H and BAZ1B/WSTF, CC which regulates the spacing of histone octamers on the DNA template to CC facilitate access to DNA (PubMed:16514417). Within the WICH-5 ISWI CC chromatin remodeling complex interacts with SMARCA5/SNF2H; the CC interaction is direct (PubMed:16514417, PubMed:19092802). Component of CC the B-WICH chromatin remodeling complex, at least composed of CC SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21 CC (By similarity). Within the B-WICH chromatin remodeling complex, CC interacts with SMARCA5/SNF2H, DDX21, DEK, MYBBP1A, SF3B1 and ERCC6 (By CC similarity). Interacts with MYO1C (PubMed:16514417). Interacts with CC PCNA; the interaction is direct and is required for BAZ1B/WSTF binding CC to replication foci during S phase (By similarity). Interacts with CDT1 CC (By similarity). {ECO:0000250|UniProtKB:Q9UIG0, CC ECO:0000269|PubMed:16514417, ECO:0000269|PubMed:19092802}. CC -!- INTERACTION: CC Q9Z277; Q91ZW3: Smarca5; NbExp=2; IntAct=EBI-927576, EBI-927547; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00063, CC ECO:0000255|PROSITE-ProRule:PRU00475}. Note=Accumulates in CC pericentromeric heterochromatin during replication. Targeted to CC replication foci throughout S phase via its association with PCNA (By CC similarity). Localizes to sites of DNA damage (By similarity). CC {ECO:0000250|UniProtKB:Q9UIG0}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9Z277-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Z277-2; Sequence=VSP_037470; CC -!- DEVELOPMENTAL STAGE: Expressed as early as day 7 and in equal amounts CC during gestation. CC -!- SIMILARITY: Belongs to the WAL family. BAZ1B subfamily. {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; AF084480; AAD08676.1; -; mRNA. DR EMBL; CH466529; EDL19376.1; -; Genomic_DNA. DR EMBL; BC141399; AAI41400.1; -; mRNA. DR EMBL; AK017894; BAB30992.1; -; mRNA. DR EMBL; AK037737; BAC29862.1; -; mRNA. DR EMBL; AK137139; BAE23247.1; -; mRNA. DR EMBL; AK140172; BAE24264.1; -; mRNA. DR EMBL; AK141305; BAE24643.1; -; mRNA. DR CCDS; CCDS19736.1; -. [Q9Z277-1] DR PIR; T17401; T17401. DR RefSeq; NP_035844.2; NM_011714.2. [Q9Z277-1] DR RefSeq; XP_011239182.1; XM_011240880.2. [Q9Z277-2] DR AlphaFoldDB; Q9Z277; -. DR SMR; Q9Z277; -. DR BioGRID; 204552; 15. DR ComplexPortal; CPX-1133; B-WICH chromatin remodelling complex. DR ComplexPortal; CPX-841; WICH chromatin remodelling complex. DR CORUM; Q9Z277; -. DR DIP; DIP-36072N; -. DR IntAct; Q9Z277; 2. DR STRING; 10090.ENSMUSP00000002825; -. DR GlyGen; Q9Z277; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9Z277; -. DR PhosphoSitePlus; Q9Z277; -. DR SwissPalm; Q9Z277; -. DR EPD; Q9Z277; -. DR jPOST; Q9Z277; -. DR MaxQB; Q9Z277; -. DR PaxDb; 10090-ENSMUSP00000002825; -. DR PeptideAtlas; Q9Z277; -. DR ProteomicsDB; 277180; -. [Q9Z277-1] DR ProteomicsDB; 277181; -. [Q9Z277-2] DR Pumba; Q9Z277; -. DR Antibodypedia; 14309; 327 antibodies from 32 providers. DR DNASU; 22385; -. DR Ensembl; ENSMUST00000002825.6; ENSMUSP00000002825.6; ENSMUSG00000002748.8. [Q9Z277-1] DR GeneID; 22385; -. DR KEGG; mmu:22385; -. DR UCSC; uc008zxz.2; mouse. [Q9Z277-1] DR AGR; MGI:1353499; -. DR CTD; 9031; -. DR MGI; MGI:1353499; Baz1b. DR VEuPathDB; HostDB:ENSMUSG00000002748; -. DR eggNOG; KOG1245; Eukaryota. DR GeneTree; ENSGT00940000156831; -. DR HOGENOM; CLU_004410_0_0_1; -. DR InParanoid; Q9Z277; -. DR OMA; RFNHRKD; -. DR OrthoDB; 5490909at2759; -. DR PhylomeDB; Q9Z277; -. DR TreeFam; TF106397; -. DR Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression. DR BioGRID-ORCS; 22385; 16 hits in 118 CRISPR screens. DR ChiTaRS; Baz1b; mouse. DR PRO; PR:Q9Z277; -. DR Proteomes; UP000000589; Chromosome 5. DR RNAct; Q9Z277; Protein. DR Bgee; ENSMUSG00000002748; Expressed in ileal epithelium and 263 other cell types or tissues. DR GO; GO:0110016; C:B-WICH complex; ISO:MGI. DR GO; GO:0000793; C:condensed chromosome; IDA:MGI. DR GO; GO:0043596; C:nuclear replication fork; IEA:Ensembl. DR GO; GO:0005730; C:nucleolus; NAS:ComplexPortal. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal. DR GO; GO:0005721; C:pericentric heterochromatin; IDA:ComplexPortal. DR GO; GO:0090535; C:WICH complex; ISO:MGI. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0042393; F:histone binding; IPI:UniProtKB. DR GO; GO:0140801; F:histone H2AXY142 kinase activity; ISS:UniProtKB. DR GO; GO:0035173; F:histone kinase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0006325; P:chromatin organization; IDA:MGI. DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal. DR GO; GO:0006974; P:DNA damage response; ISS:UniProtKB. DR GO; GO:1905213; P:negative regulation of mitotic chromosome condensation; ISO:MGI. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0035066; P:positive regulation of histone acetylation; NAS:ComplexPortal. DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; NAS:ComplexPortal. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; NAS:ComplexPortal. DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; ISO:MGI. DR GO; GO:0043687; P:post-translational protein modification; ISS:UniProtKB. DR CDD; cd05505; Bromo_WSTF_like; 1. DR CDD; cd15628; PHD_BAZ1B; 1. DR Gene3D; 1.20.920.10; Bromodomain-like; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR047174; BAZ1B. DR InterPro; IPR037375; BAZ1B_Bromo. DR InterPro; IPR047256; BAZ1B_PHD. DR InterPro; IPR001487; Bromodomain. DR InterPro; IPR036427; Bromodomain-like_sf. DR InterPro; IPR018359; Bromodomain_CS. DR InterPro; IPR018501; DDT_dom. DR InterPro; IPR028942; WHIM1_dom. DR InterPro; IPR028941; WHIM2_dom. DR InterPro; IPR013136; WSTF_Acf1_Cbp146. DR InterPro; IPR019786; Zinc_finger_PHD-type_CS. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR019787; Znf_PHD-finger. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR46802; TYROSINE-PROTEIN KINASE BAZ1B; 1. DR PANTHER; PTHR46802:SF1; TYROSINE-PROTEIN KINASE BAZ1B; 1. DR Pfam; PF00439; Bromodomain; 1. DR Pfam; PF00628; PHD; 1. DR Pfam; PF10537; WAC_Acf1_DNA_bd; 1. DR Pfam; PF15612; WHIM1; 1. DR Pfam; PF15613; WSD; 1. DR PRINTS; PR00503; BROMODOMAIN. DR SMART; SM00297; BROMO; 1. DR SMART; SM00571; DDT; 1. DR SMART; SM00249; PHD; 1. DR SUPFAM; SSF47370; Bromodomain; 1. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1. DR PROSITE; PS00633; BROMODOMAIN_1; 1. DR PROSITE; PS50014; BROMODOMAIN_2; 1. DR PROSITE; PS50827; DDT; 1. DR PROSITE; PS51136; WAC; 1. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 1. DR Genevisible; Q9Z277; MM. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; ATP-binding; Bromodomain; Coiled coil; KW DNA damage; Isopeptide bond; Kinase; Metal-binding; Nucleotide-binding; KW Nucleus; Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation; Transferase; Tyrosine-protein kinase; KW Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..1479 FT /note="Tyrosine-protein kinase BAZ1B" FT /id="PRO_0000211171" FT DOMAIN 20..126 FT /note="WAC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00475" FT DOMAIN 605..669 FT /note="DDT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00063" FT DOMAIN 1352..1422 FT /note="Bromo" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT ZN_FING 1184..1234 FT /note="PHD-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT REGION 146..212 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 302..333 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 376..433 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 448..472 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 789..813 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1231..1324 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1451..1479 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 537..587 FT /evidence="ECO:0000255" FT COILED 774..809 FT /evidence="ECO:0000255" FT COILED 854..890 FT /evidence="ECO:0000255" FT COILED 1257..1284 FT /evidence="ECO:0000255" FT MOTIF 207..213 FT /note="C motif" FT COMPBIAS 159..174 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 175..212 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 309..323 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 414..433 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1251..1276 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 152 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 158 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 161 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 266 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9UIG0" FT MOD_RES 325 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 330 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9UIG0" FT MOD_RES 345 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9UIG0" FT MOD_RES 361 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319" FT MOD_RES 374 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9UIG0" FT MOD_RES 706 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 709 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 717 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9UIG0" FT MOD_RES 1315 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9UIG0" FT MOD_RES 1331 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 1338 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9UIG0" FT MOD_RES 1464 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319, FT ECO:0007744|PubMed:21183079" FT MOD_RES 1466 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1468 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT CROSSLNK 827 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0000250|UniProtKB:Q9UIG0" FT CROSSLNK 827 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:Q9UIG0" FT CROSSLNK 854 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9UIG0" FT CROSSLNK 1043 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9UIG0" FT CROSSLNK 1089 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9UIG0" FT CROSSLNK 1107 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9UIG0" FT VAR_SEQ 1..298 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_037470" FT CONFLICT 957 FT /note="S -> R (in Ref. 1; AAD08676)" FT /evidence="ECO:0000305" FT CONFLICT 1017 FT /note="L -> F (in Ref. 1; AAD08676)" FT /evidence="ECO:0000305" FT CONFLICT 1031..1034 FT /note="SIYL -> CNYM (in Ref. 1; AAD08676)" FT /evidence="ECO:0000305" SQ SEQUENCE 1479 AA; 170651 MW; 6EFBF3913EA93AF0 CRC64; MAPLLGRKPF PLVKPLPGEE PLFTIPHTQE AFRTREEYEA RLERYSERIW TCKSTGSSQL THKEAWEEEQ EVAELLKEEF PNWYEKLVLE MVHHNTASLE KLVDSAWLEI MTKYAVGEEC DFEVGKEKML KVKIVKIHPL EKVDEEAVEK KSDGACDSPS SDKENSSQMA QDLQKKETVV KEDEGRRESI NDRARRSPRK LPTSLKKGER KWAPPKFLPH KYDVKLQNED KIISNVPADS LIRTERPPNK EILRYFIRHN ALRAGTGENA PWVVEDELVK KYSLPSKFSD FLLDPYKYMT LNPSTKRRNT GSPDRKPSKK PKRDSSSLSS PLNPKLWCHV HLEKSLNGPP LKVKNSKNSK SPEEHLEGVM KIMSPNNNKL HSFHIPKKGP AAKKPGKHSD KPLKAKGRGK GILNGQKSTG NSKSPSKCVK TPKTKMKQMT LLDMAKGTQK MTRTPRSSGG VPRSSGKPHK HLPPAALHLI AYYKENKDKE DKKSALSCVI SKTARLLSNE DRARLPEELR ALVQKRYELL EHKKRWASMS EEQRKEYLKK KRQELKERLR EKAKERRERE MLERLEKQKR FEDQELGGRN LPAFRLVDTP EGLPNTLFGD VALVVEFLSC YSGLLLPDAQ YPITAVSLME ALSADKGGFL YLNRVLVILL QTLLQDEIAE DYGELGMKLS EIPLTLHSVS ELVRLCLRRC DVQEDSEGSE TDDNKDSTPF EDNEVQDEFL EKLETSEFFE LTSEEKLRIL TALCHRILMT YSVQDHMETR QQVSAELWKE RLAVLKEEND KKRAEKQKRK EMEARNKENG KEENVLGKVD RKKEIVKIEQ QVEVEADDMI SAVKSRRLLS MQAKRKREIQ ERETKVRLER EAEEERMRKH KAAAEKAFQE GIAKAKLVLR RTPIGTDRNH NRYWLFSNEV PGLFIEKGWV HNSIDYRFKH HRKDHSNLPD DDYCPRSKKA NLGKNASVNA HHGPALEAVE TTVPKQGQNL WFLCDSQKEL DELLSCLHPQ GIRESQLKER LEKRYQEITH SIYLARKPNL GLKSCDGNQE LLNFLRSDLI EVATRLQKGG LGYMEGTSEF EARVISLEKL KDFGECVIAL QASVIKKFLQ GFMAPKQKKR KLQSEDSTKS EEVDEEKKMV EEAKVASALE KWKTAIREAQ TFSRMHVLLG MLDACIKWDM SAENARCKVC RKKGEDDKLI LCDECNKAFH LFCLRPALYE VPDGEWQCPA CQPPTARRNS RGRNYTEEST SEGSEGDESG EEEEEEEEEE EEEEDYEVAG LRLRPRKTIR GKQSVIPAAR PGRPPGKKSH PARRSRPKDD PEVDDLVLQT KRISRRQSLE LQKCEDILHK LVKYRFSWPF REPVTRDEAE DYYDVIEHPM DFQTIQNKCS CGNYRSVQEF LTDMKQVFAN AELYNCRGSH VLSCMEKTEQ CLLALLQKHL PGHPYVRRKR RKFPDRLADD EGDSDSESVG QSRGRRQKK //