MSL1_HUMAN
ID MSL1_HUMAN Reviewed; 614 AA.
AC Q68DK7; Q0VF46; Q69Z03;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Male-specific lethal 1 homolog;
DE Short=MSL-1;
DE AltName: Full=Male-specific lethal 1-like 1;
DE Short=MSL1-like 1;
DE AltName: Full=Male-specific lethal-1 homolog 1;
GN Name=MSL1; Synonyms=MSL1L1;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Rectum tumor, and Uterus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Rectum tumor;
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 SUMOYLATION WITH SUMO1, AND SUBCELLULAR LOCATION.
RX PubMed=15561718; DOI=10.1074/jbc.m411718200;
RA Gocke C.B., Yu H., Kang J.;
RT "Systematic identification and analysis of mammalian small ubiquitin-like
RT modifier substrates.";
RL J. Biol. Chem. 280:5004-5012(2005).
RN [5]
RP SUBUNIT, INTERACTION WITH MSL2, AND FUNCTION.
RX PubMed=16227571; DOI=10.1128/mcb.25.21.9175-9188.2005;
RA Smith E.R., Cayrou C., Huang R., Lane W.S., Cote J., Lucchesi J.C.;
RT "A human protein complex homologous to the Drosophila MSL complex is
RT responsible for the majority of histone H4 acetylation at lysine 16.";
RL Mol. Cell. Biol. 25:9175-9188(2005).
RN [6]
RP ERRATUM OF PUBMED:16227571.
RA Smith E.R., Cayrou C., Huang R., Lane W.S., Cote J., Lucchesi J.C.;
RL Mol. Cell. Biol. 26:387-387(2006).
RN [7]
RP IDENTIFICATION IN THE MSL COMPLEX.
RX PubMed=16543150; DOI=10.1016/j.molcel.2006.02.007;
RA Mendjan S., Taipale M., Kind J., Holz H., Gebhardt P., Schelder M.,
RA Vermeulen M., Buscaino A., Duncan K., Mueller J., Wilm M.,
RA Stunnenberg H.G., Saumweber H., Akhtar A.;
RT "Nuclear pore components are involved in the transcriptional regulation of
RT dosage compensation in Drosophila.";
RL Mol. Cell 21:811-823(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, AND IDENTIFICATION BY
RP 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 [9]
RP INTERACTION WITH NUPR1 AND TP53BP1, AND INDUCTION BY GAMMA-IRRADIATION.
RX PubMed=19650074; DOI=10.1002/jcp.21889;
RA Gironella M., Malicet C., Cano C., Sandi M.J., Hamidi T., Tauil R.M.,
RA Baston M., Valaco P., Moreno S., Lopez F., Neira J.L., Dagorn J.C.,
RA Iovanna J.L.;
RT "p8/nupr1 regulates DNA-repair activity after double-strand gamma
RT irradiation-induced DNA damage.";
RL J. Cell. Physiol. 221:594-602(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-353, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, AND IDENTIFICATION BY
RP 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 [12]
RP FUNCTION IN H2B UBIQUITINATION.
RX PubMed=21726816; DOI=10.1016/j.molcel.2011.05.015;
RA Wu L., Zee B.M., Wang Y., Garcia B.A., Dou Y.;
RT "The RING finger protein MSL2 in the MOF complex is an E3 ubiquitin ligase
RT for H2B K34 and is involved in crosstalk with H3 K4 and K79 methylation.";
RL Mol. Cell 43:132-144(2011).
RN [13]
RP INTERACTION WITH KAT8 AND MSL3.
RX PubMed=21217699; DOI=10.1038/nsmb.1960;
RA Kadlec J., Hallacli E., Lipp M., Holz H., Sanchez-Weatherby J., Cusack S.,
RA Akhtar A.;
RT "Structural basis for MOF and MSL3 recruitment into the dosage compensation
RT complex by MSL1.";
RL Nat. Struct. Mol. Biol. 18:142-149(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, AND IDENTIFICATION BY
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-205; SER-393 AND
RP THR-396, AND IDENTIFICATION BY MASS SPECTROMETRY [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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126; SER-205 AND SER-442, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-301; LYS-365 AND LYS-378, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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).
RN [18]
RP INTERACTION WITH MSL3.
RX PubMed=30224647; DOI=10.1038/s41588-018-0220-y;
RG DDD Study;
RA Basilicata M.F., Bruel A.L., Semplicio G., Valsecchi C.I.K., Aktas T.,
RA Duffourd Y., Rumpf T., Morton J., Bache I., Szymanski W.G., Gilissen C.,
RA Vanakker O., Ounap K., Mittler G., van der Burgt I., El Chehadeh S.,
RA Cho M.T., Pfundt R., Tan T.Y., Kirchhoff M., Menten B., Vergult S.,
RA Lindstrom K., Reis A., Johnson D.S., Fryer A., McKay V., Fisher R.B.,
RA Thauvin-Robinet C., Francis D., Roscioli T., Pajusalu S., Radtke K.,
RA Ganesh J., Brunner H.G., Wilson M., Faivre L., Kalscheuer V.M.,
RA Thevenon J., Akhtar A.;
RT "De novo mutations in MSL3 cause an X-linked syndrome marked by impaired
RT histone H4 lysine 16 acetylation.";
RL Nat. Genet. 50:1442-1451(2018).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 473-520 IN COMPLEX WITH KAT8,
RP FUNCTION IN MSL COMPLEX, AND INTERACTION WITH KAT8 AND MSL3.
RX PubMed=22547026; DOI=10.1038/cr.2012.72;
RA Huang J., Wan B., Wu L., Yang Y., Dou Y., Lei M.;
RT "Structural insight into the regulation of MOF in the male-specific lethal
RT complex and the non-specific lethal complex.";
RL Cell Res. 22:1078-1081(2012).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 212-267 IN COMPLEX WITH MSL2,
RP COILED COIL, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, AND INTERACTION
RP WITH MSL2.
RX PubMed=23084835; DOI=10.1016/j.molcel.2012.09.014;
RA Hallacli E., Lipp M., Georgiev P., Spielman C., Cusack S., Akhtar A.,
RA Kadlec J.;
RT "Msl1-mediated dimerization of the dosage compensation complex is essential
RT for male X-chromosome regulation in Drosophila.";
RL Mol. Cell 48:587-600(2012).
CC -!- FUNCTION: Component of histone acetyltransferase complex responsible
CC for the majority of histone H4 acetylation at 'Lys-16' (H4K16ac) which
CC is implicated in the formation of higher-order chromatin structure
CC (PubMed:16227571). Greatly enhances MSL2 E3 ubiquitin ligase activity,
CC promoting monoubiquitination of histone H2B at 'Lys-34' (H2BK34Ub)
CC (PubMed:21726816). This modification in turn stimulates histone H3
CC methylation at 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) and leads to
CC gene activation, including that of HOXA9 and MEIS1 (PubMed:21726816).
CC In the MSL complex, acts as a scaffold to tether MSL3 and KAT8 together
CC for enzymatic activity regulation (PubMed:22547026).
CC {ECO:0000269|PubMed:16227571, ECO:0000269|PubMed:21726816,
CC ECO:0000269|PubMed:22547026}.
CC -!- SUBUNIT: Component of a multisubunit histone acetyltransferase complex
CC (MSL) at least composed of the KAT8/MOF/MYST1, MSL1/hampin, MSL2 and
CC MSL3 (PubMed:16227571, PubMed:16543150). Forms a MSL heterotetrameric
CC core with MSL2 (PubMed:16227571). Interacts with KAT8 and MSL3; both
CC interactions are direct (PubMed:22547026, PubMed:21217699,
CC PubMed:30224647). Directly interacts with NUPR1 (PubMed:19650074).
CC Interacts with TP53BP1; this interaction may be required for MSL1 DNA
CC repair activity, but not for histone acetyltransferase activity
CC (PubMed:19650074). Interacts with TTC4, ECM2 and PIHD1 (By similarity).
CC {ECO:0000250|UniProtKB:Q6PDM1, ECO:0000269|PubMed:16227571,
CC ECO:0000269|PubMed:16543150, ECO:0000269|PubMed:19650074,
CC ECO:0000269|PubMed:21217699, ECO:0000269|PubMed:22547026,
CC ECO:0000269|PubMed:30224647}.
CC -!- INTERACTION:
CC Q68DK7; Q9HCI7: MSL2; NbExp=2; IntAct=EBI-2560816, EBI-2560775;
CC Q68DK7-1; Q9H7Z6-1: KAT8; NbExp=2; IntAct=EBI-26435399, EBI-26435386;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15561718}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:Q6PDM1}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q6PDM1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q68DK7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q68DK7-2; Sequence=VSP_035237;
CC Name=3;
CC IsoId=Q68DK7-3; Sequence=VSP_035236;
CC -!- INDUCTION: Up-regulated by gamma-irradiation.
CC {ECO:0000269|PubMed:19650074}.
CC -!- DOMAIN: The coiled coil is formed by helices from two subunits in the
CC MSL1 homodimer. {ECO:0000269|PubMed:23084835}.
CC -!- PTM: Sumoylated with SUMO1. {ECO:0000269|PubMed:15561718}.
CC -!- SIMILARITY: Belongs to the msl-1 family. {ECO:0000305}.
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DR EMBL; AL049450; CAH10734.1; -; mRNA.
DR EMBL; CR749360; CAH18213.1; -; mRNA.
DR EMBL; AC068669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC118997; AAI18998.1; -; mRNA.
DR EMBL; BC122543; AAI22544.1; -; mRNA.
DR CCDS; CCDS45670.1; -. [Q68DK7-3]
DR RefSeq; NP_001012241.1; NM_001012241.1. [Q68DK7-3]
DR RefSeq; XP_005257355.1; XM_005257298.4.
DR PDB; 4B7Y; X-ray; 3.25 A; A/B=212-252.
DR PDB; 4B86; X-ray; 3.50 A; A/B/E/F/I/J=212-267.
DR PDB; 4DNC; X-ray; 2.05 A; D/E=473-520.
DR PDBsum; 4B7Y; -.
DR PDBsum; 4B86; -.
DR PDBsum; 4DNC; -.
DR AlphaFoldDB; Q68DK7; -.
DR SMR; Q68DK7; -.
DR BioGRID; 130859; 54.
DR ComplexPortal; CPX-815; MSL histone acetyltransferase complex.
DR CORUM; Q68DK7; -.
DR DIP; DIP-56862N; -.
DR IntAct; Q68DK7; 23.
DR MINT; Q68DK7; -.
DR STRING; 9606.ENSP00000462945; -.
DR iPTMnet; Q68DK7; -.
DR PhosphoSitePlus; Q68DK7; -.
DR BioMuta; MSL1; -.
DR DMDM; 322510113; -.
DR EPD; Q68DK7; -.
DR jPOST; Q68DK7; -.
DR MassIVE; Q68DK7; -.
DR MaxQB; Q68DK7; -.
DR PaxDb; Q68DK7; -.
DR PeptideAtlas; Q68DK7; -.
DR PRIDE; Q68DK7; -.
DR ProteomicsDB; 66086; -. [Q68DK7-1]
DR ProteomicsDB; 66087; -. [Q68DK7-2]
DR ProteomicsDB; 66088; -. [Q68DK7-3]
DR TopDownProteomics; Q68DK7-2; -. [Q68DK7-2]
DR Antibodypedia; 7890; 93 antibodies from 20 providers.
DR DNASU; 339287; -.
DR Ensembl; ENST00000398532.9; ENSP00000381543.3; ENSG00000188895.12. [Q68DK7-1]
DR Ensembl; ENST00000579565.5; ENSP00000462945.1; ENSG00000188895.12. [Q68DK7-3]
DR GeneID; 339287; -.
DR KEGG; hsa:339287; -.
DR MANE-Select; ENST00000398532.9; ENSP00000381543.3; NM_001365919.1; NP_001352848.1.
DR UCSC; uc002hua.6; human. [Q68DK7-1]
DR CTD; 339287; -.
DR DisGeNET; 339287; -.
DR GeneCards; MSL1; -.
DR HGNC; HGNC:27905; MSL1.
DR HPA; ENSG00000188895; Low tissue specificity.
DR MIM; 614801; gene.
DR neXtProt; NX_Q68DK7; -.
DR OpenTargets; ENSG00000188895; -.
DR PharmGKB; PA164723127; -.
DR VEuPathDB; HostDB:ENSG00000188895; -.
DR eggNOG; ENOG502QQ0S; Eukaryota.
DR GeneTree; ENSGT00390000018292; -.
DR HOGENOM; CLU_030878_1_0_1; -.
DR InParanoid; Q68DK7; -.
DR OMA; HAQANCL; -.
DR OrthoDB; 560559at2759; -.
DR PhylomeDB; Q68DK7; -.
DR TreeFam; TF330735; -.
DR PathwayCommons; Q68DK7; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q68DK7; -.
DR SIGNOR; Q68DK7; -.
DR BioGRID-ORCS; 339287; 147 hits in 1089 CRISPR screens.
DR ChiTaRS; MSL1; human.
DR GenomeRNAi; 339287; -.
DR Pharos; Q68DK7; Tbio.
DR PRO; PR:Q68DK7; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q68DK7; protein.
DR Bgee; ENSG00000188895; Expressed in ventricular zone and 206 other tissues.
DR ExpressionAtlas; Q68DK7; baseline and differential.
DR Genevisible; Q68DK7; HS.
DR GO; GO:0072487; C:MSL complex; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0043984; P:histone H4-K16 acetylation; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:1900095; P:regulation of dosage compensation by inactivation of X chromosome; IEA:Ensembl.
DR DisProt; DP01278; -.
DR InterPro; IPR026711; Msl-1.
DR InterPro; IPR031840; MSL1_dimer.
DR InterPro; IPR029332; PEHE_dom.
DR PANTHER; PTHR21656; PTHR21656; 1.
DR Pfam; PF16801; MSL1_dimer; 1.
DR Pfam; PF15275; PEHE; 1.
DR SMART; SM01300; PEHE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chromatin regulator;
KW Coiled coil; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..614
FT /note="Male-specific lethal 1 homolog"
FT /id="PRO_0000349236"
FT REGION 1..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..237
FT /note="Interaction with MSL2"
FT REGION 272..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..518
FT /note="Interaction with KAT8"
FT REGION 550..591
FT /note="Sufficient for interaction with MSL3 MRG domain"
FT COILED 213..282
FT /evidence="ECO:0000269|PubMed:23084835"
FT MOTIF 317..346
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q6PDM1"
FT MOTIF 505..519
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q6PDM1"
FT COMPBIAS 41..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..185
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 353
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 396
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CROSSLNK 301
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 365
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 378
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..263
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035236"
FT VAR_SEQ 1..201
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_035237"
FT CONFLICT 427
FT /note="S -> P (in Ref. 1; CAH18213)"
FT /evidence="ECO:0000305"
FT HELIX 215..250
FT /evidence="ECO:0007829|PDB:4B7Y"
FT STRAND 478..480
FT /evidence="ECO:0007829|PDB:4DNC"
FT HELIX 500..518
FT /evidence="ECO:0007829|PDB:4DNC"
SQ SEQUENCE 614 AA; 67128 MW; D48D845C1C2ABF45 CRC64;
MTMRSAVFKA AAAPAGGNPE QRLDYERAAA LGGPEDEPGA AEAHFLPRHR KLKEPGPPLA
SSQGGSPAPS PAGCGGKGRG LLLPAGAAPG QQEESWGGSV PLPCPPPATK QAGIGGEPAA
AGAGCSPRPK YQAVLPIQTG SLVAAAKEPT PWAGDKGGAA SPAATASDPA GPPPLPLPGP
PPLAPTATAG TLAASEGRWK SMRKSPLGGG GGSGASSQAA CLKQILLLQL DLIEQQQQQL
QAKEKEIEEL KSERDTLLAR IERMERRMQL VKKDNEKERH KLFQGYETEE REETELSEKI
KLECQPELSE TSQTLPPKPF SCGRSGKGHK RKSPFGSTER KTPVKKLAPE FSKVKTKTPK
HSPIKEEPCG SLSETVCKRE LRSQETPEKP RSSVDTPPRL STPQKGPSTH PKEKAFSSEI
EDLPYLSTTE MYLCRWHQPP PSPLPLRESS PKKEETVARC LMPSSVAGET SVLAVPSWRD
HSVEPLRDPN PSDLLENLDD SVFSKRHAKL ELDEKRRKRW DIQRIREQRI LQRLQLRMYK
KKGIQESEPE VTSFFPEPDD VESLMITPFL PVVAFGRPLP KLTPQNFELP WLDERSRCRL
EIQKKQTPHR TCRK
