Z280D_HUMAN
ID Z280D_HUMAN Reviewed; 979 AA.
AC Q6N043; A1L495; B2RMT6; Q6MZM6; Q6N085; Q6P2R6; Q7Z6J5; Q9H0U5; Q9HCI8;
AC Q9NXS0;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Zinc finger protein 280D;
DE AltName: Full=Suppressor of hairy wing homolog 4;
DE AltName: Full=Zinc finger protein 634;
GN Name=ZNF280D; Synonyms=KIAA1584, SUHW4, ZNF634;
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), AND VARIANT ILE-568.
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT ILE-568.
RC TISSUE=Colon;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT
RP ILE-568.
RC TISSUE=Colon endothelium, Liver, and Uterine endothelium;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6), AND VARIANT
RP ILE-568.
RC TISSUE=Brain, Liver, Skin, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-34; LYS-74; LYS-126; LYS-210 AND
RP LYS-292, AND IDENTIFICATION BY MASS 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 [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-34; LYS-126 AND LYS-210, AND
RP IDENTIFICATION BY MASS 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 [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-740, 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 [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-32; LYS-34; LYS-74; LYS-87;
RP LYS-126; LYS-140; LYS-189; LYS-210; LYS-223; LYS-233; LYS-275; LYS-284;
RP LYS-550; LYS-740 AND LYS-976, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
CC -!- FUNCTION: May function as a transcription factor.
CC -!- INTERACTION:
CC Q6N043-2; Q13185: CBX3; NbExp=3; IntAct=EBI-12027202, EBI-78176;
CC Q6N043-2; P45973: CBX5; NbExp=3; IntAct=EBI-12027202, EBI-78219;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q6N043-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6N043-2; Sequence=VSP_017624;
CC Name=3;
CC IsoId=Q6N043-3; Sequence=VSP_017625, VSP_017626;
CC Name=4;
CC IsoId=Q6N043-4; Sequence=VSP_017623, VSP_017627, VSP_017628;
CC Name=5;
CC IsoId=Q6N043-5; Sequence=VSP_017622;
CC Name=6;
CC IsoId=Q6N043-6; Sequence=VSP_054317, VSP_054318;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13410.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAE46003.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB046804; BAB13410.1; ALT_INIT; mRNA.
DR EMBL; AK000093; BAA90940.1; -; mRNA.
DR EMBL; AL136634; CAB66569.1; -; mRNA.
DR EMBL; BX640637; CAE45785.1; -; mRNA.
DR EMBL; BX640707; CAE45827.1; -; mRNA.
DR EMBL; BX641000; CAE46003.1; ALT_INIT; mRNA.
DR EMBL; AC010999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015382; AAH15382.2; -; mRNA.
DR EMBL; BC053649; AAH53649.2; -; mRNA.
DR EMBL; BC064359; AAH64359.1; -; mRNA.
DR EMBL; BC130451; AAI30452.1; -; mRNA.
DR EMBL; BC136412; AAI36413.1; -; mRNA.
DR CCDS; CCDS32245.1; -. [Q6N043-1]
DR CCDS; CCDS42041.1; -. [Q6N043-2]
DR CCDS; CCDS58364.1; -. [Q6N043-6]
DR RefSeq; NP_001002843.1; NM_001002843.2. [Q6N043-2]
DR RefSeq; NP_001002844.1; NM_001002844.2. [Q6N043-6]
DR RefSeq; NP_001275517.1; NM_001288588.1. [Q6N043-1]
DR RefSeq; NP_001275518.1; NM_001288589.1. [Q6N043-6]
DR RefSeq; NP_060131.2; NM_017661.3. [Q6N043-1]
DR RefSeq; XP_011520004.1; XM_011521702.1. [Q6N043-1]
DR RefSeq; XP_016877833.1; XM_017022344.1. [Q6N043-1]
DR RefSeq; XP_016877834.1; XM_017022345.1. [Q6N043-1]
DR AlphaFoldDB; Q6N043; -.
DR BioGRID; 120173; 15.
DR IntAct; Q6N043; 4.
DR MINT; Q6N043; -.
DR STRING; 9606.ENSP00000267807; -.
DR GlyGen; Q6N043; 1 site.
DR iPTMnet; Q6N043; -.
DR PhosphoSitePlus; Q6N043; -.
DR BioMuta; ZNF280D; -.
DR DMDM; 223634726; -.
DR EPD; Q6N043; -.
DR jPOST; Q6N043; -.
DR MassIVE; Q6N043; -.
DR MaxQB; Q6N043; -.
DR PaxDb; Q6N043; -.
DR PeptideAtlas; Q6N043; -.
DR PRIDE; Q6N043; -.
DR ProteomicsDB; 66603; -. [Q6N043-1]
DR ProteomicsDB; 66604; -. [Q6N043-2]
DR ProteomicsDB; 66605; -. [Q6N043-3]
DR ProteomicsDB; 66606; -. [Q6N043-4]
DR ProteomicsDB; 66607; -. [Q6N043-5]
DR ProteomicsDB; 69425; -.
DR Antibodypedia; 25170; 73 antibodies from 21 providers.
DR DNASU; 54816; -.
DR Ensembl; ENST00000267807.12; ENSP00000267807.7; ENSG00000137871.21. [Q6N043-1]
DR Ensembl; ENST00000558067.5; ENSP00000454173.1; ENSG00000137871.21. [Q6N043-4]
DR Ensembl; ENST00000558320.5; ENSP00000453706.1; ENSG00000137871.21. [Q6N043-6]
DR Ensembl; ENST00000559237.5; ENSP00000454111.1; ENSG00000137871.21. [Q6N043-2]
DR Ensembl; ENST00000560002.5; ENSP00000453636.1; ENSG00000137871.21. [Q6N043-3]
DR GeneID; 54816; -.
DR KEGG; hsa:54816; -.
DR MANE-Select; ENST00000267807.12; ENSP00000267807.7; NM_017661.4; NP_060131.2.
DR UCSC; uc002adu.5; human. [Q6N043-1]
DR CTD; 54816; -.
DR GeneCards; ZNF280D; -.
DR HGNC; HGNC:25953; ZNF280D.
DR HPA; ENSG00000137871; Low tissue specificity.
DR neXtProt; NX_Q6N043; -.
DR OpenTargets; ENSG00000137871; -.
DR PharmGKB; PA162410004; -.
DR VEuPathDB; HostDB:ENSG00000137871; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158889; -.
DR HOGENOM; CLU_010097_2_0_1; -.
DR InParanoid; Q6N043; -.
DR OMA; PNCQEEI; -.
DR OrthoDB; 105829at2759; -.
DR PhylomeDB; Q6N043; -.
DR TreeFam; TF331707; -.
DR PathwayCommons; Q6N043; -.
DR SignaLink; Q6N043; -.
DR BioGRID-ORCS; 54816; 7 hits in 1103 CRISPR screens.
DR ChiTaRS; ZNF280D; human.
DR GeneWiki; SUHW4; -.
DR GenomeRNAi; 54816; -.
DR Pharos; Q6N043; Tdark.
DR PRO; PR:Q6N043; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q6N043; protein.
DR Bgee; ENSG00000137871; Expressed in calcaneal tendon and 194 other tissues.
DR ExpressionAtlas; Q6N043; baseline and differential.
DR Genevisible; Q6N043; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR025243; DUF4195.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF13836; DUF4195; 1.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..979
FT /note="Zinc finger protein 280D"
FT /id="PRO_0000227977"
FT ZN_FING 321..343
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 358..381
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 388..412
FT /note="C2H2-type 3; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 418..441
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 449..469
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 89..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..780
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 908
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FE8"
FT MOD_RES 911
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FE8"
FT CROSSLNK 32
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 34
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 74
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 87
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 126
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 140
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 189
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 210
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 223
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 233
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 275
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 284
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 292
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT CROSSLNK 550
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 740
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 976
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..759
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_017622"
FT VAR_SEQ 1..296
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_017623"
FT VAR_SEQ 1..13
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10997877,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_017624"
FT VAR_SEQ 128..158
FT /note="GYITNSSRVVSNKSSELLFDLTQDTGLSHYQ -> VSVSKTIRPAQGSIGCC
FT LSISTVPSYNSGLS (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054317"
FT VAR_SEQ 159..979
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054318"
FT VAR_SEQ 579..592
FT /note="KPNGSKSKYKPKIS -> IVGAFTNALSVVPK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_017625"
FT VAR_SEQ 593..979
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_017626"
FT VAR_SEQ 687..717
FT /note="GITLVCLNCDFLSDVSGLDNMATHLSQHKTH -> CVGGQIECDLPKLHKLV
FT VEPRLTLGLLTPNF (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_017627"
FT VAR_SEQ 718..979
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_017628"
FT VARIANT 568
FT /note="V -> I (in dbSNP:rs28620278)"
FT /evidence="ECO:0000269|PubMed:10997877,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_054314"
FT VARIANT 778
FT /note="A -> V (in dbSNP:rs12900993)"
FT /id="VAR_054315"
FT VARIANT 781
FT /note="K -> I (in dbSNP:rs12901843)"
FT /id="VAR_054316"
FT VARIANT 785
FT /note="G -> A (in dbSNP:rs12900729)"
FT /id="VAR_054317"
FT CONFLICT 229
FT /note="S -> P (in Ref. 4; CAE46003)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="L -> W (in Ref. 4; CAE45785)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="A -> T (in Ref. 4; CAE45785)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="L -> P (in Ref. 3; BAA90940)"
FT /evidence="ECO:0000305"
FT CONFLICT 742
FT /note="E -> R (in Ref. 4; CAE45827)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 979 AA; 109285 MW; 9B11A04F21298503 CRC64;
MGDNPFQPKS NSKMAELFME CEEEELEPWQ KKVKEVEDDD DDEPIFVGEI SSSKPAISNI
LNRVNPSSYS RGLKNGALSR GITAAFKPTS QHYTNPTSNP VPASPINFHP ESRSSDSSVI
VQPFSKPGYI TNSSRVVSNK SSELLFDLTQ DTGLSHYQGG PTLSMAGMSE SSFLSKRPST
SEVNNVNPKK PKPSESVSGA NSSAVLPSVK SPSVTSSQAM LAKGTNTSSN QSKNGTPFPR
ACPKCNIHFN LLDPLKNHMK YCCPDMINNF LGLAKTEFSS TVNKNTTIDS EKGKLIMLVN
DFYYGKHEGD VQEEQKTHTT FKCFSCLKIL KNNIRFMNHM KHHLELEKQS SESWENHTTC
QHCYRQFPTP FQLQCHIEST HTPHEFSTIC KICELSFETE HVLLQHMKDN HKPGEMPYVC
QVCNYRSSSF SDVETHFRTS HENTKNLLCP FCLKVIKIAT PYMHHYMKHQ KKGIHRCTKC
RLQFLTCKEK MDHKTQHHRT FIKPKQLEGL PPGTKVTIRA SVGPLQSGAS PTPSISASAS
TLQLSPPRTK NITAKNPAKS NTSKPNTVKS NASKPNTSKP NGSKSKYKPK ISNMQKKQST
LASSNKKSKV NTALRNLRYR RGIHKCIECC SEIKDFANHF PTYVHCSFCR YNTSCSKAYV
NHMMSFHSNR PSKRFCIFKK HSENLRGITL VCLNCDFLSD VSGLDNMATH LSQHKTHTCQ
VVMQKVSVCI PTSEHLSELK KEAPAKEQEP VSKEIARPNM AERETETSNS ESKQDKAASS
KEKNGCNANS FEGSSTTKSE ESITVSDKEN ETCLADQETG SKNIVSCDSN IGADKVEKKK
QIQHVCQEME LKMCQSSENI ILSDQIKDHN SSEARFSSKN IKDLRLASDN VSIDQFLRKR
HEPESVSSDV SEQGSIHLEP LTPSEVLEYE ATEILQKGSG DPSAKTDEVV SDQTDDIPGG
NNPSTTEATV DLEDEKERS
