BAZ1B_MOUSE
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 03-AUG-2022, entry version 172.
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; 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, Pancreas,
RC 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). {ECO:0000250}.
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}.
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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; 14.
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 iPTMnet; Q9Z277; -.
DR PhosphoSitePlus; Q9Z277; -.
DR SwissPalm; Q9Z277; -.
DR EPD; Q9Z277; -.
DR jPOST; Q9Z277; -.
DR MaxQB; Q9Z277; -.
DR PaxDb; Q9Z277; -.
DR PeptideAtlas; Q9Z277; -.
DR PRIDE; Q9Z277; -.
DR ProteomicsDB; 277180; -. [Q9Z277-1]
DR ProteomicsDB; 277181; -. [Q9Z277-2]
DR Antibodypedia; 14309; 286 antibodies from 32 providers.
DR DNASU; 22385; -.
DR Ensembl; ENSMUST00000002825; ENSMUSP00000002825; ENSMUSG00000002748. [Q9Z277-1]
DR GeneID; 22385; -.
DR KEGG; mmu:22385; -.
DR UCSC; uc008zxz.2; mouse. [Q9Z277-1]
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; 858930at2759; -.
DR PhylomeDB; Q9Z277; -.
DR TreeFam; TF106397; -.
DR Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR BioGRID-ORCS; 22385; 16 hits in 112 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 259 other tissues.
DR Genevisible; Q9Z277; MM.
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; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IC: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:0035173; F:histone kinase activity; ISO:MGI.
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:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IDA:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:1990164; P:histone H2A phosphorylation; ISO:MGI.
DR GO; GO:0016572; P:histone phosphorylation; ISO:MGI.
DR GO; GO:1905213; P:negative regulation of mitotic chromosome condensation; ISO:MGI.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IC:ComplexPortal.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC: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 GO; GO:2001020; P:regulation of response to DNA damage stimulus; IC:ComplexPortal.
DR CDD; cd05505; Bromo_WSTF_like; 1.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR037375; BAZ1B_Bromo.
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 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; SSF47370; 1.
DR SUPFAM; SSF57903; SSF57903; 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.
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
