M18BP_HUMAN
ID M18BP_HUMAN Reviewed; 1132 AA.
AC Q6P0N0; D3DSA7; Q86V14; Q96PY4; Q9NUR5; Q9Y4X9;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Mis18-binding protein 1;
DE AltName: Full=Kinetochore-associated protein KNL-2 homolog {ECO:0000303|PubMed:17339379};
DE Short=HsKNL-2 {ECO:0000303|PubMed:17339379};
DE AltName: Full=P243;
GN Name=MIS18BP1; Synonyms=C14orf106, KIAA1903, KNL2, M18BP1;
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 1).
RC TISSUE=Brain;
RX PubMed=11572484; DOI=10.1093/dnares/8.4.179;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXI. The
RT complete sequences of 60 new cDNA clones from brain which code for large
RT proteins.";
RL DNA Res. 8:179-187(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis, and Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 523-760, AND INTERACTION WITH SP1.
RC TISSUE=Colon carcinoma;
RX PubMed=10976766; DOI=10.1023/a:1007177623283;
RA Gunther M., Laithier M., Brison O.;
RT "A set of proteins interacting with transcription factor Sp1 identified in
RT a two-hybrid screening.";
RL Mol. Cell. Biochem. 210:131-142(2000).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY,
RP INTERACTION WITH MIS18A, AND IDENTIFICATION IN A COMPLEX CONTAINING MIS18A;
RP OIP5; MIS18BP1; RBBP7 AND RBBP4.
RX PubMed=17199038; DOI=10.1016/j.devcel.2006.11.002;
RA Fujita Y., Hayashi T., Kiyomitsu T., Toyoda Y., Kokubu A., Obuse C.,
RA Yanagida M.;
RT "Priming of centromere for CENP-A recruitment by human hMis18alpha,
RT hMis18beta, and M18BP1.";
RL Dev. Cell 12:17-30(2007).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17339379; DOI=10.1083/jcb.200701065;
RA Maddox P.S., Hyndman F., Monen J., Oegema K., Desai A.;
RT "Functional genomics identifies a Myb domain-containing protein family
RT required for assembly of CENP-A chromatin.";
RL J. Cell Biol. 176:757-763(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; THR-653; THR-821;
RP SER-824; SER-1008; SER-1086; THR-1087; THR-1089 AND SER-1104, 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1008 AND SER-1104, AND
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-653; SER-860; SER-1008;
RP SER-1104 AND SER-1116, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135; SER-172; SER-299;
RP THR-653; SER-772; SER-773; SER-1008; SER-1104 AND SER-1116, AND
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-131; SER-135; SER-192;
RP SER-299; SER-365; THR-653; SER-860; SER-1104 AND SER-1116, AND
RP 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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-639; LYS-742 AND LYS-899, 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 [16]
RP INTERACTION WITH KAT7.
RX PubMed=27270040; DOI=10.1016/j.devcel.2016.05.006;
RA Ohzeki J., Shono N., Otake K., Martins N.M., Kugou K., Kimura H.,
RA Nagase T., Larionov V., Earnshaw W.C., Masumoto H.;
RT "KAT7/HBO1/MYST2 regulates CENP-A chromatin assembly by antagonizing
RT Suv39h1-mediated centromere inactivation.";
RL Dev. Cell 37:413-427(2016).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-7; LYS-65; LYS-211; LYS-262;
RP LYS-534; LYS-612; LYS-639; LYS-647; LYS-727; LYS-742; LYS-840; LYS-899;
RP LYS-956; LYS-964; LYS-983 AND LYS-1079, AND IDENTIFICATION BY MASS
RP 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 STRUCTURE BY NMR OF 877-936.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-022, a Myb DNA-binding domain in human
RT cDNA.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Required for recruitment of CENPA to centromeres and normal
CC chromosome segregation during mitosis. {ECO:0000269|PubMed:17199038,
CC ECO:0000269|PubMed:17339379}.
CC -!- SUBUNIT: Interacts with SP1 (PubMed:10976766). Interacts with MIS18A.
CC Identified in a complex containing MIS18A, OIP5/MIS18B, MIS18BP1, RBBP7
CC and RBBP4 (PubMed:17199038). Interacts with KAT7/HBO1
CC (PubMed:27270040). Interacts (via N-terminus) with FLNA (via N-
CC terminus) (By similarity). {ECO:0000250|UniProtKB:Q80WQ8,
CC ECO:0000269|PubMed:10976766, ECO:0000269|PubMed:17199038,
CC ECO:0000269|PubMed:27270040}.
CC -!- INTERACTION:
CC Q6P0N0; O43482: OIP5; NbExp=4; IntAct=EBI-9870821, EBI-536879;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17199038}.
CC Chromosome, centromere {ECO:0000269|PubMed:17199038}. Note=Associated
CC with centromeres in interphase cells, from late anaphase to the G1
CC phase. Not detected on centromeres during earlier phases of mitosis.
CC Associated with chromatin. {ECO:0000269|PubMed:17199038}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P0N0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P0N0-2; Sequence=VSP_014105;
CC -!- SEQUENCE CAUTION:
CC Sequence=AK002048; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB67796.1; Type=Frameshift; Evidence={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; AB067490; BAB67796.1; ALT_FRAME; mRNA.
DR EMBL; AK002048; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL121809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW65778.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65779.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65780.1; -; Genomic_DNA.
DR EMBL; BC051885; AAH51885.1; -; mRNA.
DR EMBL; BC065544; AAH65544.1; -; mRNA.
DR EMBL; AJ242977; CAB45134.1; -; mRNA.
DR CCDS; CCDS9684.1; -. [Q6P0N0-1]
DR RefSeq; NP_060823.3; NM_018353.4. [Q6P0N0-1]
DR RefSeq; XP_005267890.1; XM_005267833.4. [Q6P0N0-1]
DR RefSeq; XP_016876914.1; XM_017021425.1. [Q6P0N0-1]
DR PDB; 1WGX; NMR; -; A=877-936.
DR PDBsum; 1WGX; -.
DR AlphaFoldDB; Q6P0N0; -.
DR SMR; Q6P0N0; -.
DR BioGRID; 120601; 51.
DR ComplexPortal; CPX-3272; Mis18 complex.
DR CORUM; Q6P0N0; -.
DR IntAct; Q6P0N0; 18.
DR MINT; Q6P0N0; -.
DR STRING; 9606.ENSP00000309790; -.
DR iPTMnet; Q6P0N0; -.
DR PhosphoSitePlus; Q6P0N0; -.
DR BioMuta; MIS18BP1; -.
DR DMDM; 68052324; -.
DR EPD; Q6P0N0; -.
DR jPOST; Q6P0N0; -.
DR MassIVE; Q6P0N0; -.
DR MaxQB; Q6P0N0; -.
DR PaxDb; Q6P0N0; -.
DR PeptideAtlas; Q6P0N0; -.
DR PRIDE; Q6P0N0; -.
DR ProteomicsDB; 66813; -. [Q6P0N0-1]
DR ProteomicsDB; 66814; -. [Q6P0N0-2]
DR Antibodypedia; 12; 60 antibodies from 14 providers.
DR DNASU; 55320; -.
DR Ensembl; ENST00000310806.9; ENSP00000309790.4; ENSG00000129534.14. [Q6P0N0-1]
DR GeneID; 55320; -.
DR KEGG; hsa:55320; -.
DR MANE-Select; ENST00000310806.9; ENSP00000309790.4; NM_018353.5; NP_060823.3.
DR UCSC; uc001wwf.3; human. [Q6P0N0-1]
DR CTD; 55320; -.
DR GeneCards; MIS18BP1; -.
DR HGNC; HGNC:20190; MIS18BP1.
DR HPA; ENSG00000129534; Tissue enhanced (bone).
DR MIM; 618139; gene.
DR neXtProt; NX_Q6P0N0; -.
DR OpenTargets; ENSG00000129534; -.
DR PharmGKB; PA134927557; -.
DR VEuPathDB; HostDB:ENSG00000129534; -.
DR eggNOG; ENOG502QRUS; Eukaryota.
DR GeneTree; ENSGT00390000007395; -.
DR HOGENOM; CLU_009019_1_0_1; -.
DR InParanoid; Q6P0N0; -.
DR OMA; MCHSNCQ; -.
DR OrthoDB; 815579at2759; -.
DR PhylomeDB; Q6P0N0; -.
DR TreeFam; TF106401; -.
DR PathwayCommons; Q6P0N0; -.
DR Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR SignaLink; Q6P0N0; -.
DR BioGRID-ORCS; 55320; 564 hits in 1088 CRISPR screens.
DR ChiTaRS; MIS18BP1; human.
DR EvolutionaryTrace; Q6P0N0; -.
DR GeneWiki; C14orf106; -.
DR GenomeRNAi; 55320; -.
DR Pharos; Q6P0N0; Tbio.
DR PRO; PR:Q6P0N0; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q6P0N0; protein.
DR Bgee; ENSG00000129534; Expressed in monocyte and 155 other tissues.
DR ExpressionAtlas; Q6P0N0; baseline and differential.
DR Genevisible; Q6P0N0; HS.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd00167; SANT; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR039110; KNL2-like.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR015216; SANTA.
DR PANTHER; PTHR16124; PTHR16124; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF09133; SANTA; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51293; SANT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Centromere;
KW Chromosome; DNA-binding; Isopeptide bond; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..1132
FT /note="Mis18-binding protein 1"
FT /id="PRO_0000197140"
FT DOMAIN 383..469
FT /note="SANTA"
FT DOMAIN 875..930
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 123..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 653
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 772
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 773
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 821
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 824
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 860
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1008
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 1086
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1087
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1089
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 65
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 211
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 262
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 534
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 612
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 639
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 647
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 727
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 742
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 840
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 899
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 956
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 964
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 983
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1079
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 391..1132
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014105"
FT VARIANT 164
FT /note="C -> R (in dbSNP:rs1269008)"
FT /id="VAR_050184"
FT VARIANT 347
FT /note="P -> R (in dbSNP:rs34168608)"
FT /id="VAR_050185"
FT VARIANT 583
FT /note="E -> D (in dbSNP:rs34101857)"
FT /id="VAR_050186"
FT VARIANT 851
FT /note="E -> Q (in dbSNP:rs34402741)"
FT /id="VAR_050187"
FT CONFLICT 510
FT /note="R -> Q (in Ref. 1; BAB67796)"
FT /evidence="ECO:0000305"
FT HELIX 882..894
FT /evidence="ECO:0007829|PDB:1WGX"
FT STRAND 897..901
FT /evidence="ECO:0007829|PDB:1WGX"
FT HELIX 902..909
FT /evidence="ECO:0007829|PDB:1WGX"
FT TURN 910..912
FT /evidence="ECO:0007829|PDB:1WGX"
FT HELIX 915..924
FT /evidence="ECO:0007829|PDB:1WGX"
FT STRAND 925..929
FT /evidence="ECO:0007829|PDB:1WGX"
FT STRAND 934..936
FT /evidence="ECO:0007829|PDB:1WGX"
SQ SEQUENCE 1132 AA; 129085 MW; 92F2787CD4687059 CRC64;
MIATPLKHSR IYLPPEASSQ RRNLPMDAIF FDSIPSGTLT PVKDLVKYQN SSLKLNDHKK
NQFLKMTTFN NKNIFQSTML TEATTSNSSL DISAIKPNKD GLKNKANYES PGKIFLRMKE
KVLRDKQEQP SRNSSLLEPQ KSGNNETFTP NRVEKKKLQH TYLCEEKENN KSFQSDDSSL
RASVQGVPLE SSNNDIFLPV KQKIQCQQEK KAPLHNLTYE LPTLNQEQEN FLAVEARNKT
LTRAQLAKQI FHSKESIVAT TKSKKDTFVL ESVDSADEQF QNTNAETLST NCIPIKNGSL
LMVSDSERTT EGTSQQKVKE GNGKTVPGET GLPGSMKDTC KIVLATPRLH ITIPRRSKRN
ISKLSPPRIF QTVTNGLKKN QVVQLQEWMI KSINNNTAIC VEGKLIDVTN IYWHSNVIIE
RIEHNKLRTI SGNVYILKGM IDQISMKEAG YPNYLIRKFM FGFPENWKEH IDNFLEQLRA
GEKNREKTKQ KQKTGRSVRD IRKSMKNDAR ENQTDTAQRA TTTYDFDCDN LELKSNKHSE
SPGATELNMC HSNCQNKPTL RFPDDQVNNT IQNGGGDDLS NQELIGKKEY KMSSKKLKIG
ERTNERIIKS QKQETTEELD VSIDILTSRE QFFSDEERKY MAINQKKAYI LVTPLKSRKV
IEQRCMRYNL SAGTIKAVTD FVIPECQKKS PISKSMGTLE NTFEGHKSKN KEDCDERDLL
TVNRKIKISN LEKEQMLTSD FKKNTRLLPK LKKIENQVAM SFYKHQSSPD LSSEESETEK
EIKRKAEVKK TKAGNTKEAV VHLRKSTRNT SNIPVILEPE TEESENEFYI KQKKARPSVK
ETLQKSGVRK EFPITEAVGS DKTNRHPLEC LPGLIQDKEW NEKELQKLHC AFASLPKHKP
GFWSEVAAAV GSRSPEECQR KYMENPRGKG SQKHVTKKKP ANSKGQNGKR GDADQKQTIK
ITAKVGTLKR KQQMREFLEQ LPKDDHDDFF STTPLQHQRI LLPSFQDSED DDDILPNMDK
NPTTPSSVIF PLVKTPQCQH VSPGMLGSIN RNDCDKYVFR MQKYHKSNGG IVWGNIKKKL
VETDFSTPTP RRKTPFNTDL GENSGIGKLF TNAVESLDEE EKDYYFSNSD SA
