ZNF12_HUMAN
ID ZNF12_HUMAN Reviewed; 697 AA.
AC P17014; A8MYC4; A8WFQ8; B2RNQ7; B4DF45; Q6N016; Q8NHZ0; Q9H9P0; Q9ULZ6;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Zinc finger protein 12;
DE AltName: Full=Gonadotropin-inducible ovary transcription repressor 3;
DE Short=GIOT-3;
DE AltName: Full=Zinc finger protein 325;
DE AltName: Full=Zinc finger protein KOX3;
GN Name=ZNF12; Synonyms=GIOT3, KOX3, ZNF325;
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 [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16806083; DOI=10.1016/j.bbrc.2006.06.031;
RA Zhao Y., Zhou L., Liu B., Deng Y., Wang Y., Wang Y., Huang W., Yuan W.,
RA Wang Z., Zhu C., Liu M., Wu X., Li Y.;
RT "ZNF325, a novel human zinc finger protein with a RBaK-like RB-binding
RT domain, inhibits AP-1- and SRE-mediated transcriptional activity.";
RL Biochem. Biophys. Res. Commun. 346:1191-1199(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Ovary;
RA Okada T., Mizutani T., Miyamoto K.;
RT "Identification and characterization of novel zinc finger proteins in the
RT human ovary.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
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] (ISOFORM 4).
RC TISSUE=Fetal kidney;
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=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC TISSUE=Leiomyosarcoma, and Lung;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 409-464.
RC TISSUE=Lymphoid tissue;
RX PubMed=2288909;
RA Thiesen H.-J.;
RT "Multiple genes encoding zinc finger domains are expressed in human T
RT cells.";
RL New Biol. 2:363-374(1990).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-179, 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 [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-179, 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 [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-98 AND LYS-239, 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 [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-3; LYS-98; LYS-179; LYS-182;
RP LYS-209; LYS-215; LYS-224; LYS-239; LYS-309 AND LYS-337, AND IDENTIFICATION
RP 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).
CC -!- FUNCTION: Transcriptional repressor which suppresses activation protein
CC 1 (AP-1)- and serum response element (SRE)-mediated transcriptional
CC activity. {ECO:0000269|PubMed:16806083}.
CC -!- INTERACTION:
CC P17014; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-11278550, EBI-3866279;
CC P17014; P23508: MCC; NbExp=3; IntAct=EBI-11278550, EBI-307531;
CC P17014; Q99750: MDFI; NbExp=3; IntAct=EBI-11278550, EBI-724076;
CC P17014; Q9GZM8: NDEL1; NbExp=3; IntAct=EBI-11278550, EBI-928842;
CC P17014; Q16623: STX1A; NbExp=3; IntAct=EBI-11278550, EBI-712466;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16806083}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=P17014-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P17014-2; Sequence=VSP_040335;
CC Name=3;
CC IsoId=P17014-3; Sequence=VSP_040334;
CC Name=4;
CC IsoId=P17014-4; Sequence=VSP_040738, VSP_040739;
CC Name=5;
CC IsoId=P17014-5; Sequence=VSP_040739;
CC -!- TISSUE SPECIFICITY: Widely expressed in various adult tissues and
CC embryonic developmental stages (isoform 3).
CC {ECO:0000269|PubMed:16806083}.
CC -!- DEVELOPMENTAL STAGE: Shows a relatively higher expression level in the
CC fetal brain and a lower level in adult. The expression level in liver
CC is highest at 16 weeks of development and declines from 16 to 24 weeks
CC and is lower in adult. Expressed strongly in fetal heart on 18 and 24
CC weeks, but relatively weakly on the other development stage of embryo,
CC and then reaches a higher level in adult (isoform 3).
CC {ECO:0000269|PubMed:16806083}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14183.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG57306.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF505656; AAM28195.1; -; mRNA.
DR EMBL; AB021643; BAA86989.1; -; mRNA.
DR EMBL; AK022691; BAB14183.1; ALT_INIT; mRNA.
DR EMBL; AK293925; BAG57306.1; ALT_INIT; mRNA.
DR EMBL; BX640749; CAE45857.1; -; mRNA.
DR EMBL; AC073343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH878731; EAW55016.1; -; Genomic_DNA.
DR EMBL; BC051892; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC137068; AAI37069.1; -; mRNA.
DR EMBL; BC137069; AAI37070.1; -; mRNA.
DR EMBL; BC154414; AAI54415.1; -; mRNA.
DR EMBL; X52334; CAA36560.1; -; mRNA.
DR CCDS; CCDS47538.1; -. [P17014-1]
DR CCDS; CCDS47539.1; -. [P17014-5]
DR PIR; I37970; I37970.
DR RefSeq; NP_008887.2; NM_006956.2. [P17014-5]
DR RefSeq; NP_057349.2; NM_016265.3. [P17014-1]
DR AlphaFoldDB; P17014; -.
DR SMR; P17014; -.
DR BioGRID; 113391; 16.
DR IntAct; P17014; 8.
DR STRING; 9606.ENSP00000385939; -.
DR iPTMnet; P17014; -.
DR PhosphoSitePlus; P17014; -.
DR BioMuta; ZNF12; -.
DR DMDM; 317373491; -.
DR EPD; P17014; -.
DR jPOST; P17014; -.
DR MassIVE; P17014; -.
DR MaxQB; P17014; -.
DR PaxDb; P17014; -.
DR PeptideAtlas; P17014; -.
DR PRIDE; P17014; -.
DR ProteomicsDB; 53409; -. [P17014-1]
DR ProteomicsDB; 53410; -. [P17014-2]
DR ProteomicsDB; 53411; -. [P17014-3]
DR ProteomicsDB; 53412; -. [P17014-4]
DR ProteomicsDB; 53413; -. [P17014-5]
DR Antibodypedia; 6020; 93 antibodies from 20 providers.
DR DNASU; 7559; -.
DR Ensembl; ENST00000342651.9; ENSP00000344745.5; ENSG00000164631.19. [P17014-5]
DR Ensembl; ENST00000404360.5; ENSP00000384405.1; ENSG00000164631.19. [P17014-4]
DR Ensembl; ENST00000405858.6; ENSP00000385939.1; ENSG00000164631.19. [P17014-1]
DR GeneID; 7559; -.
DR KEGG; hsa:7559; -.
DR MANE-Select; ENST00000405858.6; ENSP00000385939.1; NM_016265.4; NP_057349.2.
DR UCSC; uc003sqs.3; human. [P17014-1]
DR CTD; 7559; -.
DR DisGeNET; 7559; -.
DR GeneCards; ZNF12; -.
DR HGNC; HGNC:12902; ZNF12.
DR HPA; ENSG00000164631; Low tissue specificity.
DR MIM; 194536; gene.
DR neXtProt; NX_P17014; -.
DR OpenTargets; ENSG00000164631; -.
DR PharmGKB; PA134931984; -.
DR PharmGKB; PA37491; -.
DR VEuPathDB; HostDB:ENSG00000164631; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000154303; -.
DR HOGENOM; CLU_002678_44_5_1; -.
DR InParanoid; P17014; -.
DR OMA; DYHCYQM; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P17014; -.
DR TreeFam; TF350803; -.
DR PathwayCommons; P17014; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; P17014; -.
DR BioGRID-ORCS; 7559; 9 hits in 1103 CRISPR screens.
DR ChiTaRS; ZNF12; human.
DR GenomeRNAi; 7559; -.
DR Pharos; P17014; Tbio.
DR PRO; PR:P17014; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P17014; protein.
DR Bgee; ENSG00000164631; Expressed in cauda epididymis and 206 other tissues.
DR ExpressionAtlas; P17014; baseline and differential.
DR Genevisible; P17014; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 15.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 15.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 10.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 15.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 15.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..697
FT /note="Zinc finger protein 12"
FT /id="PRO_0000047335"
FT DOMAIN 8..79
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 269..291
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 297..319
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 325..347
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 353..375
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 381..403
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 409..431
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 437..459
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 465..487
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 493..515
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 521..543
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 549..571
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 577..599
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 605..627
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 633..655
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 661..683
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 3
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 98
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 179
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 182
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 209
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 215
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 224
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 239
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 267
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYW8"
FT CROSSLNK 309
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 323
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYW8"
FT CROSSLNK 337
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 365
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYW8"
FT CROSSLNK 544
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYW8"
FT CROSSLNK 547
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYW8"
FT VAR_SEQ 1..235
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16806083"
FT /id="VSP_040334"
FT VAR_SEQ 1..36
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_040738"
FT VAR_SEQ 114..151
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_040739"
FT VAR_SEQ 458..653
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_040335"
FT CONFLICT 86
FT /note="D -> E (in Ref. 7; AAI54415)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="L -> P (in Ref. 4; CAE45857)"
FT /evidence="ECO:0000305"
FT CONFLICT 525
FT /note="E -> G (in Ref. 3; BAB14183)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="C -> Y (in Ref. 4; CAE45857)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 697 AA; 81202 MW; 3D12F61C265D6BE3 CRC64;
MNKSLGPVSF KDVAVDFTQE EWQQLDPEQK ITYRDVMLEN YSNLVSVGYH IIKPDVISKL
EQGEEPWIVE GEFLLQSYPD EVWQTDDLIE RIQEEENKPS RQTVFIETLI EERGNVPGKT
FDVETNPVPS RKIAYKNSLC DSCEKCLTSV SEYISSDGSY ARMKADECSG CGKSLLHIKL
EKTHPGDQAY EFNQNGEPYT LNEESLYQKI RILEKPFEYI ECQKAFQKDT VFVNHMEEKP
YKWNGSEIAF LQMSDLTVHQ TSHMEMKPYE CSECGKSFCK KSKFIIHQRT HTGEKPYECN
QCGKSFCQKG TLTVHQRTHT GEKPYECNEC GKNFYQKLHL IQHQRTHSGE KPYECSYCGK
SFCQKTHLTQ HQRTHSGERP YVCHDCGKTF SQKSALNDHQ KIHTGVKLYK CSECGKCFCR
KSTLTTHLRT HTGEKPYECN ECGKFFSRLS YLTVHYRTHS GEKPYECNEC GKTFYLNSAL
MRHQRVHTGE KPYECNECGK LFSQLSYLTI HHRTHSGVKP YECSECGKTF YQNSALCRHR
RIHKGEKPYE CYICGKFFSQ MSYLTIHHRI HSGEKPYECS ECGKTFCQNS ALNRHQRTHT
GEKAYECYEC GKCFSQMSYL TIHHRIHSGE KPFECNECGK AFSRMSYLTV HYRTHSGEKP
YECTECGKKF YHKSAFNSHQ RIHRRGNMNV IDVGRLL
