YLPM1_HUMAN
ID YLPM1_HUMAN Reviewed; 2146 AA.
AC P49750; P49752; Q96I64; Q9P1V7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 4.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=YLP motif-containing protein 1;
DE AltName: Full=Nuclear protein ZAP3;
DE AltName: Full=ZAP113;
GN Name=YLPM1; Synonyms=C14orf170, ZAP3;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-628 (ISOFORM 4).
RC TISSUE=Fetal brain;
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 [MRNA] OF 734-1042 AND 1592-2146 (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=7596406; DOI=10.1038/375754a0;
RA Sherrington R., Rogaev E.I., Liang Y., Rogaeva E.A., Levesque G., Ikeda M.,
RA Chi H., Lin C., Li G., Holman K., Tsuda T., Mar L., Foncin J.-F.,
RA Bruni A.C., Montesi M.P., Sorbi S., Rainero I., Pinessi L., Nee L.,
RA Chumakov I., Pollen D., Brookes A., Sanseau P., Polinsky R.J., Wasco W.,
RA da Silva H.A.R., Haines J.L., Pericak-Vance M.A., Tanzi R.E., Roses A.D.,
RA Fraser P.E., Rommens J.M., St George-Hyslop P.H.;
RT "Cloning of a gene bearing missense mutations in early-onset familial
RT Alzheimer's disease.";
RL Nature 375:754-760(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1761-2146 (ISOFORMS 1/4).
RC TISSUE=Skin;
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 [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17890166; DOI=10.1016/j.bbapap.2007.07.015;
RA Ulke-Lemee A., Trinkle-Mulcahy L., Chaulk S., Bernstein N.K., Morrice N.,
RA Glover M., Lamond A.I., Moorhead G.B.G.;
RT "The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside
RT kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-G.";
RL Biochim. Biophys. Acta 1774:1339-1350(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-829, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-829, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-829, 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-829 AND SER-1119, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-756; SER-829; SER-1100;
RP SER-1119 AND SER-1402, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [13]
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 [14]
RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-735; ARG-814 AND ARG-831, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1053, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-983 AND LYS-1053, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1053, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1053, AND IDENTIFICATION BY MASS
RP 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 [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-891; LYS-983; LYS-1053; LYS-1652
RP AND LYS-1710, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
CC -!- FUNCTION: Plays a role in the reduction of telomerase activity during
CC differentiation of embryonic stem cells by binding to the core promoter
CC of TERT and controlling its down-regulation. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PPP1CA and NCOA5. Forms a complex with ILF2,
CC ILF3, KHDRBS1, RBMX, NCOA5 and PPP1CA (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P49750; O00555: CACNA1A; NbExp=2; IntAct=EBI-712871, EBI-766279;
CC P49750; P62136: PPP1CA; NbExp=3; IntAct=EBI-712871, EBI-357253;
CC P49750; Q99816: TSG101; NbExp=2; IntAct=EBI-712871, EBI-346882;
CC P49750; Q93009: USP7; NbExp=2; IntAct=EBI-712871, EBI-302474;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17890166}. Nucleus
CC speckle {ECO:0000250}. Note=Migrates to nucleolar caps upon blockage of
CC transcription.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=4;
CC IsoId=P49750-4; Sequence=Displayed;
CC Name=3;
CC IsoId=P49750-3; Sequence=VSP_059470, VSP_059471, VSP_059472;
CC Name=1;
CC IsoId=P49750-1; Sequence=VSP_059470;
CC -!- TISSUE SPECIFICITY: Expressed in neuronal, neuroblastoma and embryonic
CC kidney cell lines (at protein level). {ECO:0000269|PubMed:17890166}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC42008.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF61275.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007956; AAF61275.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK095760; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; L40403; AAC42008.1; ALT_FRAME; mRNA.
DR EMBL; L40400; AAC42006.1; -; mRNA.
DR EMBL; BC007792; AAH07792.1; -; mRNA.
DR CCDS; CCDS45135.1; -. [P49750-4]
DR RefSeq; NP_062535.2; NM_019589.2. [P49750-4]
DR AlphaFoldDB; P49750; -.
DR SMR; P49750; -.
DR BioGRID; 121117; 119.
DR DIP; DIP-53676N; -.
DR IntAct; P49750; 45.
DR MINT; P49750; -.
DR STRING; 9606.ENSP00000324463; -.
DR GlyGen; P49750; 7 sites, 2 O-linked glycans (7 sites).
DR iPTMnet; P49750; -.
DR PhosphoSitePlus; P49750; -.
DR BioMuta; YLPM1; -.
DR DMDM; 57015374; -.
DR EPD; P49750; -.
DR jPOST; P49750; -.
DR MassIVE; P49750; -.
DR MaxQB; P49750; -.
DR PaxDb; P49750; -.
DR PeptideAtlas; P49750; -.
DR PRIDE; P49750; -.
DR ProteomicsDB; 56063; -. [P49750-1]
DR ProteomicsDB; 56064; -. [P49750-3]
DR ProteomicsDB; 56065; -. [P49750-4]
DR Antibodypedia; 62380; 17 antibodies from 7 providers.
DR DNASU; 56252; -.
DR Ensembl; ENST00000325680.12; ENSP00000324463.7; ENSG00000119596.18. [P49750-4]
DR GeneID; 56252; -.
DR KEGG; hsa:56252; -.
DR MANE-Select; ENST00000325680.12; ENSP00000324463.7; NM_019589.3; NP_062535.2.
DR UCSC; uc001xqj.5; human. [P49750-4]
DR CTD; 56252; -.
DR DisGeNET; 56252; -.
DR GeneCards; YLPM1; -.
DR HGNC; HGNC:17798; YLPM1.
DR HPA; ENSG00000119596; Low tissue specificity.
DR MIM; 619766; gene.
DR neXtProt; NX_P49750; -.
DR OpenTargets; ENSG00000119596; -.
DR PharmGKB; PA134962086; -.
DR VEuPathDB; HostDB:ENSG00000119596; -.
DR eggNOG; KOG2400; Eukaryota.
DR GeneTree; ENSGT00440000039837; -.
DR InParanoid; P49750; -.
DR OMA; WDRDRYW; -.
DR PhylomeDB; P49750; -.
DR TreeFam; TF329361; -.
DR PathwayCommons; P49750; -.
DR SignaLink; P49750; -.
DR BioGRID-ORCS; 56252; 50 hits in 1093 CRISPR screens.
DR ChiTaRS; YLPM1; human.
DR GeneWiki; YLPM1; -.
DR GenomeRNAi; 56252; -.
DR Pharos; P49750; Tdark.
DR PRO; PR:P49750; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P49750; protein.
DR Bgee; ENSG00000119596; Expressed in ganglionic eminence and 200 other tissues.
DR ExpressionAtlas; P49750; baseline and differential.
DR Genevisible; P49750; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0032204; P:regulation of telomere maintenance; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR026314; YLP_motif_con_p1.
DR PANTHER; PTHR13413; PTHR13413; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..2146
FT /note="YLP motif-containing protein 1"
FT /id="PRO_0000066298"
FT REGION 1..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..1211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1243..1351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1407..1438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1469..1573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1602..1828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2096..2103
FT /note="Involved in interaction with PPP1CA"
FT /evidence="ECO:0000250"
FT COMPBIAS 13..30
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..115
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..198
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..368
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..650
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..803
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..912
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..940
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..980
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1011
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1087
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1243..1268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1275..1325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1491..1505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1507..1528
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1535..1564
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1604..1635
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1665..1774
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1808..1828
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 735
FT /note="N6-methyllysine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 756
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 814
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 829
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 831
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1402
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 891
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 SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 983
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1053
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 1053
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1652
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1710
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 431..627
FT /note="TMSVDMQLRHYEMQQQQFQHLYQEWEREFQLWEEQLHSYPHKDQLQEYEKQW
FT KTWQGHMKATQSYLQEKVNSFQNMKNQYMGNMSMPPPFVPYSQMPPPLPTMPPPVLPPS
FT LPPPVMPPALPATVPPPGMPPPVMPPSLPTSVPPPGMPPSLSSAGPPPVLPPPSLSSAG
FT PPPVLPPPSLSSTAPPPVMPLPPLSSA -> AT (in isoform 1 and isoform
FT 3)"
FT /id="VSP_059470"
FT VAR_SEQ 2038..2057
FT /note="GYIPKSKWEMDTSEAKLDKL -> VGDRPTTLNSVSLLKFLKKV (in
FT isoform 3)"
FT /id="VSP_059471"
FT VAR_SEQ 2058..2146
FT /note="Missing (in isoform 3)"
FT /id="VSP_059472"
FT CONFLICT 421
FT /note="Q -> R (in Ref. 2; AK095760)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="S -> P (in Ref. 2; AK095760)"
FT /evidence="ECO:0000305"
FT CONFLICT 816
FT /note="P -> S (in Ref. 3; AAC42006)"
FT /evidence="ECO:0000305"
FT CONFLICT 1599
FT /note="T -> I (in Ref. 3; AAC42008)"
FT /evidence="ECO:0000305"
FT CONFLICT P49750-3:1861
FT /note="K -> E (in Ref. 3; AAC42008)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2146 AA; 241645 MW; 2C8F694D43061047 CRC64;
MYPNWGRYGG SSHYPPPPVP PPPPVALPEA SPGPGYSSST TPAAPSSSGF MSFREQHLAQ
LQQLQQMHQK QMQCVLQPHH LPPPPLPPPP VMPGGGYGDW QPPPPPMPPP PGPALSYQKQ
QQYKHQMLHH QRDGPPGLVP MELESPPESP PVPPGSYMPP SQSYMPPPQP PPSYYPPTSS
QPYLPPAQPS PSQSPPSQSY LAPTPSYSSS SSSSQSYLSH SQSYLPSSQA SPSRPSQGHS
KSQLLAPPPP SAPPGNKTTV QQEPLESGAK NKSTEQQQAA PEPDPSTMTP QEQQQYWYRQ
HLLSLQQRTK VHLPGHKKGP VVAKDTPEPV KEEVTVPATS QVPESPSSEE PPLPPPNEEV
PPPLPPEEPQ SEDPEEDARL KQLQAAAAHW QQHQQHRVGF QYQGIMQKHT QLQQILQQYQ
QIIQPPPHIQ TMSVDMQLRH YEMQQQQFQH LYQEWEREFQ LWEEQLHSYP HKDQLQEYEK
QWKTWQGHMK ATQSYLQEKV NSFQNMKNQY MGNMSMPPPF VPYSQMPPPL PTMPPPVLPP
SLPPPVMPPA LPATVPPPGM PPPVMPPSLP TSVPPPGMPP SLSSAGPPPV LPPPSLSSAG
PPPVLPPPSL SSTAPPPVMP LPPLSSATPP PGIPPPGVPQ GIPPQLTAAP VPPASSSQSS
QVPEKPRPAL LPTPVSFGSA PPTTYHPPLQ SAGPSEQVNS KAPLSKSALP YSSFSSDQGL
GESSAAPSQP ITAVKDMPVR SGGLLPDPPR SSYLESPRGP RFDGPRRFED LGSRCEGPRP
KGPRFEGNRP DGPRPRYEGH PAEGTKSKWG MIPRGPASQF YITPSTSLSP RQSGPQWKGP
KPAFGQQHQQ QPKSQAEPLS GNKEPLADTS SNQQKNFKMQ SAAFSIAADV KDVKAAQSNE
NLSDSQQEPP KSEVSEGPVE PSNWDQNVQS METQIDKAQA VTQPVPLANK PVPAQSTFPS
KTGGMEGGTA VATSSLTADN DFKPVGIGLP HSENNQDKGL PRPDNRDNRL EGNRGNSSSY
RGPGQSRMED TRDKGLVNRG RGQAISRGPG LVKQEDFRDK MMGRREDSRE KMNRGEGSRD
RGLVRPGSSR EKVPGGLQGS QDRGAAGSRE RGPPRRAGSQ ERGPLRRAGS RERIPPRRAG
SRERGPPRGP GSRERGLGRS DFGRDRGPFR PEPGDGGEKM YPYHRDEPPR APWNHGEERG
HEEFPLDGRN APMERERLDD WDRERYWREC ERDYQDDTLE LYNREDRFSA PPSRSHDGDR
RGPWWDDWER DQDMDEDYNR EMERDMDRDV DRISRPMDMY DRSLDNEWDR DYGRPLDEQE
SQFRERDIPS LPPLPPLPPL PPLDRYRDDR WREERNREHG YDRDFRDRGE LRIREYPERG
DTWREKRDYV PDRMDWERER LSDRWYPSDV DRHSPMAEHM PSSHHSSEMM GSDASLDSDQ
GLGGVMVLSQ RQHEIILKAA QELKMLREQK EQLQKMKDFG SEPQMADHLP PQESRLQNTS
SRPGMYPPPG SYRPPPPMGK PPGSIVRPSA PPARSSVPVT RPPVPIPPPP PPPPLPPPPP
VIKPQTSAVE QERWDEDSFY GLWDTNDEQG LNSEFKSETA AIPSAPVLPP PPVHSSIPPP
GPVPMGMPPM SKPPPVQQTV DYGHGRDIST NKVEQIPYGE RITLRPDPLP ERSTFETEHA
GQRDRYDRER DREPYFDRQS NVIADHRDFK RDRETHRDRD RDRGVIDYDR DRFDRERRPR
DDRAQSYRDK KDHSSSRRGG FDRPSYDRKS DRPVYEGPSM FGGERRTYPE ERMPLPAPSL
SHQPPPAPRV EKKPESKNVD DILKPPGRES RPERIVVIMR GLPGSGKTHV AKLIRDKEVE
FGGPAPRVLS LDDYFITEVE KEEKDPDSGK KVKKKVMEYE YEAEMEETYR TSMFKTFKKT
LDDGFFPFII LDAINDRVRH FDQFWSAAKT KGFEVYLAEM SADNQTCGKR NIHGRKLKEI
NKMADHWETA PRHMMRLDIR SLLQDAAIEE VEMEDFDANI EEQKEEKKDA EEEESELGYI
PKSKWEMDTS EAKLDKLDGL RTGTKRKRDW EAIASRMEDY LQLPDDYDTR ASEPGKKRVR
WADLEEKKDA DRKRAIGFVV GQTDWEKITD ESGHLAEKAL NRTKYI
