ZN646_HUMAN
ID ZN646_HUMAN Reviewed; 1832 AA.
AC O15015; Q8IVD8;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-JUN-2019, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Zinc finger protein 646 {ECO:0000305};
GN Name=ZNF646 {ECO:0000312|HGNC:HGNC:29004};
GN Synonyms=KIAA0296 {ECO:0000303|PubMed:9205841};
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=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-327.
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLY-327.
RC TISSUE=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 [5]
RP IDENTIFICATION BY 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1157; LYS-1168 AND LYS-1178, AND
RP 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 [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1157 AND LYS-1168, 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 [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1157 AND LYS-1168, 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 [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-451; LYS-534; LYS-557; LYS-688;
RP LYS-1157; LYS-1168 AND LYS-1178, 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).
RN [11]
RP VARIANT [LARGE SCALE ANALYSIS] ILE-1337.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- INTERACTION:
CC O15015; Q7Z589: EMSY; NbExp=3; IntAct=EBI-745608, EBI-6598631;
CC O15015; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-745608, EBI-17490413;
CC O15015; Q99750: MDFI; NbExp=3; IntAct=EBI-745608, EBI-724076;
CC O15015; Q13976: PRKG1; NbExp=4; IntAct=EBI-745608, EBI-3952014;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=O15015-2; Sequence=Displayed;
CC Name=1;
CC IsoId=O15015-1; Sequence=VSP_060189;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20756.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB002294; BAA20756.2; ALT_INIT; mRNA.
DR EMBL; AC135050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471192; EAW52170.1; -; Genomic_DNA.
DR EMBL; BC035589; AAH35589.1; -; mRNA.
DR CCDS; CCDS10702.1; -. [O15015-2]
DR RefSeq; NP_055514.3; NM_014699.3. [O15015-2]
DR RefSeq; XP_005255767.1; XM_005255710.3. [O15015-2]
DR RefSeq; XP_005255768.1; XM_005255711.3. [O15015-2]
DR RefSeq; XP_011544292.1; XM_011545990.2. [O15015-2]
DR AlphaFoldDB; O15015; -.
DR BioGRID; 115075; 38.
DR IntAct; O15015; 19.
DR STRING; 9606.ENSP00000300850; -.
DR iPTMnet; O15015; -.
DR PhosphoSitePlus; O15015; -.
DR SwissPalm; O15015; -.
DR BioMuta; ZNF646; -.
DR EPD; O15015; -.
DR jPOST; O15015; -.
DR MassIVE; O15015; -.
DR MaxQB; O15015; -.
DR PaxDb; O15015; -.
DR PeptideAtlas; O15015; -.
DR PRIDE; O15015; -.
DR ProteomicsDB; 48370; -. [O15015-1]
DR ProteomicsDB; 48371; -. [O15015-2]
DR Antibodypedia; 27569; 27 antibodies from 12 providers.
DR DNASU; 9726; -.
DR Ensembl; ENST00000300850.5; ENSP00000300850.5; ENSG00000167395.10. [O15015-2]
DR Ensembl; ENST00000394979.2; ENSP00000378429.2; ENSG00000167395.10. [O15015-1]
DR GeneID; 9726; -.
DR KEGG; hsa:9726; -.
DR MANE-Select; ENST00000300850.5; ENSP00000300850.5; NM_014699.4; NP_055514.3.
DR UCSC; uc002eap.4; human. [O15015-2]
DR CTD; 9726; -.
DR DisGeNET; 9726; -.
DR GeneCards; ZNF646; -.
DR HGNC; HGNC:29004; ZNF646.
DR HPA; ENSG00000167395; Tissue enhanced (testis).
DR MIM; 619299; gene.
DR neXtProt; NX_O15015; -.
DR OpenTargets; ENSG00000167395; -.
DR PharmGKB; PA134955953; -.
DR VEuPathDB; HostDB:ENSG00000167395; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161588; -.
DR HOGENOM; CLU_002678_44_18_1; -.
DR InParanoid; O15015; -.
DR OMA; GWESQPD; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; O15015; -.
DR TreeFam; TF350868; -.
DR PathwayCommons; O15015; -.
DR SignaLink; O15015; -.
DR BioGRID-ORCS; 9726; 13 hits in 1101 CRISPR screens.
DR ChiTaRS; ZNF646; human.
DR GenomeRNAi; 9726; -.
DR Pharos; O15015; Tdark.
DR PRO; PR:O15015; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; O15015; protein.
DR Bgee; ENSG00000167395; Expressed in right testis and 128 other tissues.
DR ExpressionAtlas; O15015; baseline and differential.
DR Genevisible; O15015; 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; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 12.
DR SMART; SM00355; ZnF_C2H2; 32.
DR SUPFAM; SSF57667; SSF57667; 16.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 30.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 29.
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..1832
FT /note="Zinc finger protein 646"
FT /id="PRO_0000047699"
FT ZN_FING 8..31
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 48..70
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 75..97
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 239..261
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 266..288
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 294..316
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 374..396
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 401..424
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 465..487
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 492..514
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 575..597
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 617..639
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 644..666
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 821..843
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 848..870
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 881..904
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 958..980
FT /note="C2H2-type 17; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1052..1074
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1079..1101
FT /note="C2H2-type 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1203..1225
FT /note="C2H2-type 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1230..1252
FT /note="C2H2-type 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1258..1280
FT /note="C2H2-type 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1299..1321
FT /note="C2H2-type 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1326..1348
FT /note="C2H2-type 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1364..1386
FT /note="C2H2-type 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1557..1579
FT /note="C2H2-type 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1585..1607
FT /note="C2H2-type 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1677..1699
FT /note="C2H2-type 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1704..1726
FT /note="C2H2-type 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1732..1754
FT /note="C2H2-type 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1761..1783
FT /note="C2H2-type 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 26..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1274..1294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1377..1481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1509..1529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1606..1672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1781..1832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..679
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..771
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1275..1294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1377..1394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1402..1418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1802..1820
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 451
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 557
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 688
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1157
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1168
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1178
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 VAR_SEQ 1794..1832
FT /note="APVAPVTGRGDLPLPPPPTPTTPLLDPSPQWPADLSFSL -> RGHEGSQEE
FT VGTQWRGKSSPKVGGGARSERREPRGF (in isoform 1)"
FT /id="VSP_060189"
FT VARIANT 98
FT /note="A -> V (in dbSNP:rs28407985)"
FT /id="VAR_057430"
FT VARIANT 327
FT /note="E -> G (in dbSNP:rs749670)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT /id="VAR_057431"
FT VARIANT 774
FT /note="I -> M (in dbSNP:rs17641067)"
FT /id="VAR_057432"
FT VARIANT 921
FT /note="G -> A (in dbSNP:rs35713203)"
FT /id="VAR_057433"
FT VARIANT 1249
FT /note="R -> W (in dbSNP:rs35376811)"
FT /id="VAR_057434"
FT VARIANT 1318
FT /note="R -> Q (in dbSNP:rs3751856)"
FT /id="VAR_057435"
FT VARIANT 1337
FT /note="N -> I (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035594"
FT VARIANT 1477
FT /note="G -> D (in dbSNP:rs7196726)"
FT /id="VAR_057436"
FT VARIANT 1788
FT /note="T -> M (in dbSNP:rs34259949)"
FT /id="VAR_057437"
SQ SEQUENCE 1832 AA; 200825 MW; A93549B71745C803 CRC64;
MEDTPPSLSC SDCQRHFPSL PELSRHRELL HPSPNQDSEE ADSIPRPYRC QQCGRGYRHP
GSLVNHRRTH ETGLFPCTTC GKDFSNPMAL KSHMRTHAPE GRRRHRPPRP KEATPHLQGE
TVSTDSWGQR LGSSEGWENQ TKHTEETPDC ESVPDPRAAS GTWEDLPTRQ REGLASHPGP
EDGADGWGPS TNSARAPPLP IPASSLLSNL EQYLAESVVN FTGGQEPTQS PPAEEERRYK
CSQCGKTYKH AGSLTNHRQS HTLGIYPCAI CFKEFSNLMA LKNHSRLHAQ YRPYHCPHCP
RVFRLPRELL EHQQSHEGER QEPRWEEKGM PTTNGHTDES SQDQLPSAQM LNGSAELSTS
GELEDSGLEE YRPFRCGDCG RTYRHAGSLI NHRKSHQTGV YPCSLCSKQL FNAAALKNHV
RAHHRPRQGV GENGQPSVPP APLLLAETTH KEEEDPTTTL DHRPYKCSEC GRAYRHRGSL
VNHRHSHRTG EYQCSLCPRK YPNLMALRNH VRVHCKAARR SADIGAEGAP SHLKVELPPD
PVEAEAAPHT DQDHVCKHEE EATDITPAAD KTAAHICSIC GLLFEDAESL ERHGLTHGAG
EKENSRTETT MSPPRAFACR DCGKSYRHSG SLINHRQTHQ TGDFSCGACA KHFHTMAAMK
NHLRRHSRRR SRRHRKRAGG ASGGREAKLL AAESWTRELE DNEGLESPQD PSGESPHGAE
GNLESDGDCL QAESEGDKCG LERDETHFQG DKESGGTGEG LERKDASLLD NLDIPGEEGG
GTHFCDSLTG VDEDQKPATG QPNSSSHSAN AVTGWQAGAA HTCSDCGHSF PHATGLLSHR
PCHPPGIYQC SLCPKEFDSL PALRSHFQNH RPGEATSAQP FLCCLCGMIF PGRAGYRLHR
RQAHSSSGMT EGSEEEGEEE GVAEAAPARS PPLQLSEAEL LNQLQREVEA LDSAGYGHIC
GCCGQTYDDL GSLERHHQSQ SSGTTADKAP SPLGVAGDAM EMVVDSVLED IVNSVSGEGG
DAKSQEGAGT PLGDSLCIQG GESLLEAQPR PFRCNQCGKT YRHGGSLVNH RKIHQTGDFL
CPVCSRCYPN LAAYRNHLRN HPRCKGSEPQ VGPIPEAAGS SELQVGPIPE GGSNKPQHMA
EEGPGQAEVE KLQEELKVEP LEEVARVKEE VWEETTVKGE EIEPRLETAE KGCQTEASSE
RPFSCEVCGR SYKHAGSLIN HRQSHQTGHF GCQACSKGFS NLMSLKNHRR IHADPRRFRC
SECGKAFRLR KQLASHQRVH MERRGGGGTR KATREDRPFR CGQCGRTYRH AGSLLNHRRS
HETGQYSCPT CPKTYSNRMA LKDHQRLHSE NRRRRAGRSR RTAVRCALCG RSFPGRGSLE
RHLREHEETE REPANGQGGL DGTAASEANL TGSQGLETQL GGAEPVPHLE DGVPRPGERS
QSPIRAASSE APEPLSWGAG KAGGWPVGGG LGNHSGGWVP QFLTRSEEPE DSVHRSPCHA
GDCQLNGPTL SHMDSWDNRD NSSQLQPGSH SSCSQCGKTY CQSGSLLNHN TNKTDRHYCL
LCSKEFLNPV ATKSHSHNHI DAQTFACPDC GKAFESHQEL ASHLQAHARG HSQVPAQMEE
ARDPKAGTGE DQVVLPGQGK AQEAPSETPR GPGESVERAR GGQAVTSMAA EDKERPFRCT
QCGRSYRHAG SLLNHQKAHT TGLYPCSLCP KLLPNLLSLK NHSRTHTDPK RHCCSICGKA
FRTAARLEGH GRVHAPREGP FTCPHCPRHF RRRISFVQHQ QQHQEEWTVA GSGAPVAPVT
GRGDLPLPPP PTPTTPLLDP SPQWPADLSF SL
