GPTC8_HUMAN
ID GPTC8_HUMAN Reviewed; 1502 AA.
AC Q9UKJ3; B9EGP9; O60300; Q8TB99;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=G patch domain-containing protein 8;
GN Name=GPATCH8; Synonyms=GPATC8, KIAA0553;
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=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 998-1502 (ISOFORMS 1/2).
RC TISSUE=Skin, and Testis;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-678 (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 414-1502, AND VARIANT GLY-1259.
RX PubMed=10477733;
RA Thornton M.A., Poncz M., Korostishevsky M., Yakobson E., Usher S.,
RA Seligsohn U., Peretz H.;
RT "The human platelet alphaIIb gene is not closely linked to its integrin
RT partner beta3.";
RL Blood 94:2039-2047(1999).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1014, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-758; SER-1033; SER-1035;
RP SER-1081 AND SER-1107, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-738; SER-740; SER-981;
RP SER-1035 AND SER-1107, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491; SER-653; SER-738;
RP SER-740; SER-1009; SER-1014; SER-1033; SER-1035 AND SER-1107, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-740, AND IDENTIFICATION BY
RP 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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-311; LYS-577 AND LYS-1105, 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 [16]
RP VARIANT PRO-979.
RX PubMed=21594610; DOI=10.1007/s00439-011-1006-9;
RA Kaneko H., Kitoh H., Matsuura T., Masuda A., Ito M., Mottes M., Rauch F.,
RA Ishiguro N., Ohno K.;
RT "Hyperuricemia cosegregating with osteogenesis imperfecta is associated
RT with a mutation in GPATCH8.";
RL Hum. Genet. 130:671-683(2011).
CC -!- INTERACTION:
CC Q9UKJ3; P54253: ATXN1; NbExp=4; IntAct=EBI-948259, EBI-930964;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UKJ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UKJ3-2; Sequence=VSP_037683;
CC Name=3;
CC IsoId=Q9UKJ3-3; Sequence=VSP_037684, VSP_037685;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI36630.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC Sequence=BAA25479.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB011125; BAA25479.2; ALT_INIT; mRNA.
DR EMBL; AC103703; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471178; EAW51593.1; -; Genomic_DNA.
DR EMBL; BC024147; AAH24147.2; -; mRNA.
DR EMBL; BC136629; AAI36630.1; ALT_SEQ; mRNA.
DR EMBL; AK025600; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF160252; AAF03681.1; -; Genomic_DNA.
DR CCDS; CCDS32666.1; -. [Q9UKJ3-1]
DR PIR; T00329; T00329.
DR RefSeq; NP_001002909.1; NM_001002909.3. [Q9UKJ3-1]
DR RefSeq; NP_001291868.1; NM_001304939.1.
DR RefSeq; NP_001291869.1; NM_001304940.1. [Q9UKJ3-2]
DR RefSeq; NP_001291870.1; NM_001304941.1. [Q9UKJ3-2]
DR RefSeq; NP_001291871.1; NM_001304942.1. [Q9UKJ3-2]
DR RefSeq; NP_001291872.1; NM_001304943.1. [Q9UKJ3-2]
DR RefSeq; XP_016879864.1; XM_017024375.1. [Q9UKJ3-2]
DR RefSeq; XP_016879865.1; XM_017024376.1. [Q9UKJ3-2]
DR RefSeq; XP_016879866.1; XM_017024377.1.
DR RefSeq; XP_016879867.1; XM_017024378.1. [Q9UKJ3-2]
DR RefSeq; XP_016879868.1; XM_017024379.1. [Q9UKJ3-2]
DR AlphaFoldDB; Q9UKJ3; -.
DR SMR; Q9UKJ3; -.
DR BioGRID; 116749; 93.
DR IntAct; Q9UKJ3; 41.
DR STRING; 9606.ENSP00000467556; -.
DR ChEMBL; CHEMBL4523489; -.
DR iPTMnet; Q9UKJ3; -.
DR MetOSite; Q9UKJ3; -.
DR PhosphoSitePlus; Q9UKJ3; -.
DR BioMuta; GPATCH8; -.
DR DMDM; 254763309; -.
DR EPD; Q9UKJ3; -.
DR jPOST; Q9UKJ3; -.
DR MassIVE; Q9UKJ3; -.
DR MaxQB; Q9UKJ3; -.
DR PaxDb; Q9UKJ3; -.
DR PeptideAtlas; Q9UKJ3; -.
DR PRIDE; Q9UKJ3; -.
DR ProteomicsDB; 84806; -. [Q9UKJ3-1]
DR ProteomicsDB; 84807; -. [Q9UKJ3-2]
DR ProteomicsDB; 84808; -. [Q9UKJ3-3]
DR Antibodypedia; 52434; 35 antibodies from 14 providers.
DR Ensembl; ENST00000587228.5; ENSP00000468719.1; ENSG00000186566.13. [Q9UKJ3-3]
DR Ensembl; ENST00000591680.6; ENSP00000467556.1; ENSG00000186566.13. [Q9UKJ3-1]
DR GeneID; 23131; -.
DR KEGG; hsa:23131; -.
DR MANE-Select; ENST00000591680.6; ENSP00000467556.1; NM_001002909.4; NP_001002909.1.
DR UCSC; uc002igw.3; human. [Q9UKJ3-1]
DR CTD; 23131; -.
DR DisGeNET; 23131; -.
DR GeneCards; GPATCH8; -.
DR HGNC; HGNC:29066; GPATCH8.
DR HPA; ENSG00000186566; Low tissue specificity.
DR MIM; 614396; gene.
DR neXtProt; NX_Q9UKJ3; -.
DR OpenTargets; ENSG00000186566; -.
DR PharmGKB; PA162390105; -.
DR VEuPathDB; HostDB:ENSG00000186566; -.
DR eggNOG; KOG2184; Eukaryota.
DR GeneTree; ENSGT00940000159523; -.
DR HOGENOM; CLU_006418_0_0_1; -.
DR InParanoid; Q9UKJ3; -.
DR OMA; AEPEYYH; -.
DR OrthoDB; 332880at2759; -.
DR PhylomeDB; Q9UKJ3; -.
DR PathwayCommons; Q9UKJ3; -.
DR SignaLink; Q9UKJ3; -.
DR BioGRID-ORCS; 23131; 29 hits in 1082 CRISPR screens.
DR ChiTaRS; GPATCH8; human.
DR GeneWiki; GPATCH8; -.
DR GenomeRNAi; 23131; -.
DR Pharos; Q9UKJ3; Tdark.
DR PRO; PR:Q9UKJ3; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9UKJ3; protein.
DR Bgee; ENSG00000186566; Expressed in sural nerve and 207 other tissues.
DR ExpressionAtlas; Q9UKJ3; baseline and differential.
DR Genevisible; Q9UKJ3; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR022755; Znf_C2H2_jaz.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01585; G-patch; 1.
DR Pfam; PF12171; zf-C2H2_jaz; 1.
DR SMART; SM00443; G_patch; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Isopeptide bond;
KW Metal-binding; Phosphoprotein; Reference proteome; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1502
FT /note="G patch domain-containing protein 8"
FT /id="PRO_0000050761"
FT DOMAIN 40..86
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT ZN_FING 136..160
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 172..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..1301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 89..124
FT /evidence="ECO:0000255"
FT COMPBIAS 172..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..689
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..769
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..932
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..979
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1030
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1058
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1075
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1252..1266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 479
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:A2A6A1"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 740
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 758
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 911
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2A6A1"
FT MOD_RES 914
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2A6A1"
FT MOD_RES 981
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1009
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1014
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1033
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1035
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1081
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1107
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 1175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2A6A1"
FT CROSSLNK 311
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 577
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1105
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..78
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9628581"
FT /id="VSP_037683"
FT VAR_SEQ 41..43
FT /note="DNI -> PSF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037684"
FT VAR_SEQ 44..1502
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037685"
FT VARIANT 979
FT /note="A -> P (in dbSNP:rs727502862)"
FT /evidence="ECO:0000269|PubMed:21594610"
FT /id="VAR_067000"
FT VARIANT 1012
FT /note="H -> Q (in dbSNP:rs3744427)"
FT /id="VAR_067001"
FT VARIANT 1043
FT /note="R -> Q (in dbSNP:rs741902)"
FT /id="VAR_059658"
FT VARIANT 1161
FT /note="C -> W (in dbSNP:rs936018)"
FT /id="VAR_059659"
FT VARIANT 1259
FT /note="S -> G (in dbSNP:rs760339)"
FT /evidence="ECO:0000269|PubMed:10477733"
FT /id="VAR_067002"
FT CONFLICT 193
FT /note="L -> V (in Ref. 5; AK025600)"
FT /evidence="ECO:0000305"
FT CONFLICT 620
FT /note="E -> K (in Ref. 6; AAF03681)"
FT /evidence="ECO:0000305"
FT CONFLICT 680
FT /note="K -> E (in Ref. 6; AAF03681)"
FT /evidence="ECO:0000305"
FT CONFLICT 691
FT /note="H -> P (in Ref. 6; AAF03681)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1502 AA; 164197 MW; 9A0FA14F3FE7A85C CRC64;
MADRFSRFNE DRDFQGNHFD QYEEGHLEIE QASLDKPIES DNIGHRLLQK HGWKLGQGLG
KSLQGRTDPI PIVVKYDVMG MGRMEMELDY AEDATERRRV LEVEKEDTEE LRQKYKDYVD
KEKAIAKALE DLRANFYCEL CDKQYQKHQE FDNHINSYDH AHKQRLKDLK QREFARNVSS
RSRKDEKKQE KALRRLHELA EQRKQAECAP GSGPMFKPTT VAVDEEGGED DKDESATNSG
TGATASCGLG SEFSTDKGGP FTAVQITNTT GLAQAPGLAS QGISFGIKNN LGTPLQKLGV
SFSFAKKAPV KLESIASVFK DHAEEGTSED GTKPDEKSSD QGLQKVGDSD GSSNLDGKKE
DEDPQDGGSL ASTLSKLKRM KREEGAGATE PEYYHYIPPA HCKVKPNFPF LLFMRASEQM
DGDNTTHPKN APESKKGSSP KPKSCIKAAA SQGAEKTVSE VSEQPKETSM TEPSEPGSKA
EAKKALGGDV SDQSLESHSQ KVSETQMCES NSSKETSLAT PAGKESQEGP KHPTGPFFPV
LSKDESTALQ WPSELLIFTK AEPSISYSCN PLYFDFKLSR NKDARTKGTE KPKDIGSSSK
DHLQGLDPGE PNKSKEVGGE KIVRSSGGRM DAPASGSACS GLNKQEPGGS HGSETEDTGR
SLPSKKERSG KSHRHKKKKK HKKSSKHKRK HKADTEEKSS KAESGEKSKK RKKRKRKKNK
SSAPADSERG PKPEPPGSGS PAPPRRRRRA QDDSQRRSLP AEEGSSGKKD EGGGGSSSQD
HGGRKHKGEL PPSSCQRRAG TKRSSRSSHR SQPSSGDEDS DDASSHRLHQ KSPSQYSEEE
EEEDSGSEHS RSRSRSGRRH SSHRSSRRSY SSSSDASSDQ SCYSRQRSYS DDSYSDYSDR
SRRHSKRSHD SDDSDYASSK HRSKRHKYSS SDDDYSLSCS QSRSRSRSHT RERSRSRGRS
RSSSCSRSRS KRRSRSTTAH SWQRSRSYSR DRSRSTRSPS QRSGSRKRSW GHESPEERHS
GRRDFIRSKI YRSQSPHYFR SGRGEGPGKK DDGRGDDSKA TGPPSQNSNI GTGRGSEGDC
SPEDKNSVTA KLLLEKIQSR KVERKPSVSE EVQATPNKAG PKLKDPPQGY FGPKLPPSLG
NKPVLPLIGK LPATRKPNKK CEESGLERGE EQEQSETEEG PPGSSDALFG HQFPSEETTG
PLLDPPPEES KSGEATADHP VAPLGTPAHS DCYPGDPTIS HNYLPDPSDG DTLESLDSSS
QPGPVESSLL PIAPDLEHFP SYAPPSGDPS IESTDGAEDA SLAPLESQPI TFTPEEMEKY
SKLQQAAQQH IQQQLLAKQV KAFPASAALA PATPALQPIH IQQPATASAT SITTVQHAIL
QHHAAAAAAA IGIHPHPHPQ PLAQVHHIPQ PHLTPISLSH LTHSIIPGHP ATFLASHPIH
IIPASAIHPG PFTFHPVPHA ALYPTLLAPR PAAAAATALH LHPLLHPIFS GQDLQHPPSH
GT
