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MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
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Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7

DescriptionRecName: Full=Zinc finger protein with KRAB and SCAN domains 1; AltName: Full=Zinc finger protein 139; AltName: Full=Zinc finger protein 36; AltName: Full=Zinc finger protein KOX18;
MyHits logo
MyHits synonymsZKSC1_HUMAN , P17029 , A4D294 , P52745 , Q2M1U1 , Q8TBW5 , Q8TEK7 , 9960C9E320554352
match map segment
iprf:ZINC_FINGER_C2H2_2 iprf:ZINC_FINGER_C2H2_2 iprf:ZINC_FINGER_C2H2_2 ismart:ZnF_C2H2 ipat:ZINC_FINGER_C2H2_1 ismart:ZnF_C2H2 iprf:SCAN_BOX ismart:SCAN ipat:ZINC_FINGER_C2H2_1 ipat:ZINC_FINGER_C2H2_1 iprf:ZINC_FINGER_C2H2_2 iprf:ZINC_FINGER_C2H2_2 ismart:ZnF_C2H2 ismart:ZnF_C2H2 ismart:ZnF_C2H2 ipfam:SCAN ipat:ZINC_FINGER_C2H2_1 ismart:ZnF_C2H2 iprf:KRAB ipat:ZINC_FINGER_C2H2_1 ipat:ZINC_FINGER_C2H2_1 ismart:KRAB iprf:ZINC_FINGER_C2H2_2 ipfam:KRAB  
Legends: 1, Phosphoserine. {ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:18691976, ECO:0000244|PubMed:19369195, ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569}; 2, Phosphoserine. {ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569}; 3, CROSSLNK Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2). {ECO:0000244|PubMed:25218447}; 4, CROSSLNK Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2). {ECO:0000244|PubMed:25218447, ECO:0000244|PubMed:25772364}; 5, CROSSLNK Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2). {ECO:0000244|PubMed:25772364}; 6, VARIANT V -> A (in dbSNP:rs17851996). {ECO:0000269|PubMed:15489334}; 7, SCAN box. {ECO:0000255|PROSITE- ProRule:PRU00187}; 8, KRAB. {ECO:0000255|PROSITE- ProRule:PRU00119}; 9, ZN_FING C2H2-type 1. {ECO:0000255|PROSITE- ProRule:PRU00042}; 10, ZN_FING C2H2-type 2. {ECO:0000255|PROSITE- ProRule:PRU00042}; 11, ZN_FING C2H2-type 3. {ECO:0000255|PROSITE- ProRule:PRU00042}; 12, ZN_FING C2H2-type 4. {ECO:0000255|PROSITE- ProRule:PRU00042}; 13, ZN_FING C2H2-type 5. {ECO:0000255|PROSITE- ProRule:PRU00042}; 14, ZN_FING C2H2-type 6. {ECO:0000255|PROSITE- ProRule:PRU00042}; 15, iprf:ZINC_FINGER_C2H2_2 [T]; 16, ismart:ZnF_C2H2 [T]; 17, ipat:ZINC_FINGER_C2H2_1 [T]; 18, iprf:SCAN_BOX [T]; 19, ismart:KRAB [T]; 20, ipfam:KRAB [T].
ID   ZKSC1_HUMAN             Reviewed;         563 AA.
AC   P17029; A4D294; P52745; Q2M1U1; Q8TBW5; Q8TEK7;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 3.
DT   10-MAY-2017, entry version 169.
DE   RecName: Full=Zinc finger protein with KRAB and SCAN domains 1;
DE   AltName: Full=Zinc finger protein 139;
DE   AltName: Full=Zinc finger protein 36;
DE   AltName: Full=Zinc finger protein KOX18;
GN   Name=ZKSCAN1; Synonyms=KOX18, ZNF139, ZNF36;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
RX   PubMed=12693554; DOI=10.1093/dnares/10.1.49;
RA   Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N.,
RA   Ohara O.;
RT   "Characterization of long cDNA clones from human adult spleen. II. The
RT   complete sequences of 81 cDNA clones.";
RL   DNA Res. 10:49-57(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
RA   Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA   Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA   Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA   Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA   Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA   Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA   Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA   Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA   Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA   Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA   Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA   Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
RA   Mural R.J., Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-26.
RC   TISSUE=Brain, 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 240-563.
RC   TISSUE=Insulinoma;
RX   PubMed=7557990; DOI=10.1006/geno.1995.1040;
RA   Tommerup N., Vissing H.;
RT   "Isolation and fine mapping of 16 novel human zinc finger-encoding
RT   cDNAs identify putative candidate genes for developmental and
RT   malignant disorders.";
RL   Genomics 27:259-264(1995).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 405-460.
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION
RP   BY 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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION
RP   BY 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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION
RP   BY 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.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-208, 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-13 AND SER-208, AND
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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [15]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-280 AND LYS-339, 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   [16]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-339 AND LYS-560, 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).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- INTERACTION:
CC       I3L3J2:ZSCAN32; NbExp=3; IntAct=EBI-10199654, EBI-10178206;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00187}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC50264.1; Type=Frameshift; Positions=241; Evidence={ECO:0000305};
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DR   EMBL; AK074116; BAB84942.1; -; mRNA.
DR   EMBL; BX640646; CAE45792.1; -; mRNA.
DR   EMBL; CH236956; EAL23861.1; -; Genomic_DNA.
DR   EMBL; CH471091; EAW76613.1; -; Genomic_DNA.
DR   EMBL; BC022378; AAH22378.1; -; mRNA.
DR   EMBL; BC112224; AAI12225.1; -; mRNA.
DR   EMBL; BC113697; AAI13698.1; -; mRNA.
DR   EMBL; U09848; AAC50264.1; ALT_FRAME; mRNA.
DR   EMBL; X52349; CAA36575.1; -; mRNA.
DR   CCDS; CCDS34698.1; -.
DR   PIR; I38616; I38616.
DR   RefSeq; NP_001333510.1; NM_001346581.1.
DR   RefSeq; NP_003430.1; NM_003439.3.
DR   RefSeq; XP_011514861.1; XM_011516559.2.
DR   UniGene; Hs.615360; -.
DR   UniGene; Hs.633338; -.
DR   UniGene; Hs.743424; -.
DR   ProteinModelPortal; P17029; -.
DR   SMR; P17029; -.
DR   BioGrid; 113414; 27.
DR   IntAct; P17029; 2.
DR   STRING; 9606.ENSP00000323148; -.
DR   iPTMnet; P17029; -.
DR   PhosphoSitePlus; P17029; -.
DR   DMDM; 85681856; -.
DR   EPD; P17029; -.
DR   MaxQB; P17029; -.
DR   PaxDb; P17029; -.
DR   PeptideAtlas; P17029; -.
DR   PRIDE; P17029; -.
DR   DNASU; 7586; -.
DR   Ensembl; ENST00000324306; ENSP00000323148; ENSG00000106261.
DR   GeneID; 7586; -.
DR   KEGG; hsa:7586; -.
DR   UCSC; uc003usk.3; human.
DR   CTD; 7586; -.
DR   DisGeNET; 7586; -.
DR   GeneCards; ZKSCAN1; -.
DR   HGNC; HGNC:13101; ZKSCAN1.
DR   HPA; HPA006672; -.
DR   MIM; 601260; gene.
DR   neXtProt; NX_P17029; -.
DR   OpenTargets; ENSG00000106261; -.
DR   PharmGKB; PA37676; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00760000118881; -.
DR   HOGENOM; HOG000234619; -.
DR   HOVERGEN; HBG018163; -.
DR   InParanoid; P17029; -.
DR   KO; K09229; -.
DR   OMA; EKREQQG; -.
DR   OrthoDB; EOG091G046Q; -.
DR   PhylomeDB; P17029; -.
DR   TreeFam; TF350830; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   ChiTaRS; ZKSCAN1; human.
DR   GeneWiki; ZKSCAN1; -.
DR   GenomeRNAi; 7586; -.
DR   PRO; PR:P17029; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   Bgee; ENSG00000106261; -.
DR   CleanEx; HS_ZKSCAN1; -.
DR   ExpressionAtlas; P17029; baseline and differential.
DR   Genevisible; P17029; HS.
DR   GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; NAS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   CDD; cd07765; KRAB_A-box; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR008916; Retrov_capsid_C.
DR   InterPro; IPR003309; SCAN_dom.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF02023; SCAN; 1.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00431; SCAN; 1.
DR   SMART; SM00355; ZnF_C2H2; 6.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF47353; SSF47353; 1.
DR   SUPFAM; SSF57667; SSF57667; 4.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS50804; SCAN_BOX; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE   1: Evidence at protein level;
KW   Complete proteome; DNA-binding; Isopeptide bond; Metal-binding;
KW   Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    563       Zinc finger protein with KRAB and SCAN
FT                                domains 1.
FT                                /FTId=PRO_0000047753.
FT   DOMAIN       56    138       SCAN box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00187}.
FT   DOMAIN      227    300       KRAB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00119}.
FT   ZN_FING     377    399       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     405    427       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     433    455       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     461    483       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     489    511       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     517    539       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   MOD_RES      13     13       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:18691976,
FT                                ECO:0000244|PubMed:19369195,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES     208    208       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163,
FT                                ECO:0000244|PubMed:24275569}.
FT   CROSSLNK    280    280       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    339    339       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447,
FT                                ECO:0000244|PubMed:25772364}.
FT   CROSSLNK    560    560       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25772364}.
FT   VARIANT      26     26       V -> A (in dbSNP:rs17851996).
FT                                {ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_024839.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       405    432       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       489    516       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       377    404       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       405    427       ismart:ZnF_C2H2 [T]
FT   MYHIT       379    399       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       461    483       ismart:ZnF_C2H2 [T]
FT   MYHIT        56    138       iprf:SCAN_BOX [T]
FT   MYHIT        52    162       ismart:SCAN [T]
FT   MYHIT       491    511       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       435    455       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       433    460       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       517    544       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       517    539       ismart:ZnF_C2H2 [T]
FT   MYHIT       489    511       ismart:ZnF_C2H2 [T]
FT   MYHIT       377    399       ismart:ZnF_C2H2 [T]
FT   MYHIT        52    138       ipfam:SCAN [T]
FT   MYHIT       407    427       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       433    455       ismart:ZnF_C2H2 [T]
FT   MYHIT       227    300       iprf:KRAB [T]
FT   MYHIT       519    539       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       463    483       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       227    287       ismart:KRAB [T]
FT   MYHIT       461    488       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       227    262       ipfam:KRAB [T]
SQ   SEQUENCE   563 AA;  63630 MW;  9960C9E320554352 CRC64;
     MMTAESREAT GLSPQAAQEK DGIVIVKVEE EDEEDHMWGQ DSTLQDTPPP DPEIFRQRFR
     RFCYQNTFGP REALSRLKEL CHQWLRPEIN TKEQILELLV LEQFLSILPK ELQVWLQEYR
     PDSGEEAVTL LEDLELDLSG QQVPGQVHGP EMLARGMVPL DPVQESSSFD LHHEATQSHF
     KHSSRKPRLL QSRALPAAHI PAPPHEGSPR DQAMASALFT ADSQAMVKIE DMAVSLILEE
     WGCQNLARRN LSRDNRQENY GSAFPQGGEN RNENEESTSK AETSEDSASR GETTGRSQKE
     FGEKRDQEGK TGERQQKNPE EKTRKEKRDS GPAIGKDKKT ITGERGPREK GKGLGRSFSL
     SSNFTTPEEV PTGTKSHRCD ECGKCFTRSS SLIRHKIIHT GEKPYECSEC GKAFSLNSNL
     VLHQRIHTGE KPHECNECGK AFSHSSNLIL HQRIHSGEKP YECNECGKAF SQSSDLTKHQ
     RIHTGEKPYE CSECGKAFNR NSYLILHRRI HTREKPYKCT KCGKAFTRSS TLTLHHRIHA
     RERASEYSPA SLDAFGAFLK SCV
//