ZN451_HUMAN
ID ZN451_HUMAN Reviewed; 1061 AA.
AC Q9Y4E5; Q5VVE9; Q5VVF1; Q86YE4; Q8N380; Q8TD15; Q9C0G1; Q9NQM1;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=E3 SUMO-protein ligase ZNF451 {ECO:0000303|PubMed:26524494};
DE EC=2.3.2.- {ECO:0000269|PubMed:26524493, ECO:0000269|PubMed:26524494};
DE AltName: Full=Coactivator for steroid receptors {ECO:0000303|Ref.1};
DE AltName: Full=E3 SUMO-protein transferase ZNF451 {ECO:0000305};
DE AltName: Full=Zinc finger protein 451;
GN Name=ZNF451; Synonyms=COASTER {ECO:0000303|Ref.1}, KIAA0576, KIAA1702;
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 2).
RA Heldens I.M., Dechering K.J.;
RT "Isolation of a novel coactivator for steroid receptors that alters the
RT intrinsic activity of the estrogen receptor alpha liganded with SERMs.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 63-1061 (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-918 (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 36-1061 (ISOFORM 3).
RC TISSUE=Brain, 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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SUMO1; SUMO2 AND
RP UBIQUITIN, AND MUTAGENESIS OF 48-LEU-VAL-49.
RX PubMed=18656483; DOI=10.1016/j.jmb.2008.07.016;
RA Karvonen U., Jaeaeskelaeinen T., Rytinki M., Kaikkonen S., Palvimo J.J.;
RT "ZNF451 is a novel PML body- and SUMO-associated transcriptional
RT coregulator.";
RL J. Mol. Biol. 382:585-600(2008).
RN [7]
RP IDENTIFICATION 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-432, AND
RP IDENTIFICATION BY 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 [9]
RP FUNCTION, INTERACTION WITH EP300; SMAD2; SMAD3 AND SMAD4, IDENTIFICATION IN
RP A COMPLEX WITH SMAD2; SMAD3 AND SMAD4, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 48-LEU-VAL-49 AND LYS-706.
RX PubMed=24324267; DOI=10.1074/jbc.m113.526905;
RA Feng Y., Wu H., Xu Y., Zhang Z., Liu T., Lin X., Feng X.H.;
RT "Zinc finger protein 451 is a novel Smad corepressor in transforming growth
RT factor-beta signaling.";
RL J. Biol. Chem. 289:2072-2083(2014).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-158, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-75; LYS-77; LYS-106; LYS-288;
RP LYS-423; LYS-434; LYS-464; LYS-706; LYS-779; LYS-817; LYS-827; LYS-832;
RP LYS-843 AND LYS-845, SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-130; LYS-164
RP AND LYS-490 (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP 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-706, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-139; LYS-153; LYS-288; LYS-423;
RP LYS-434; LYS-706; LYS-779; LYS-817; LYS-827; LYS-832; LYS-845; LYS-852 AND
RP LYS-993, SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-130 AND LYS-490 (ISOFORM
RP 3), AND 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 [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-288; LYS-434; LYS-664; LYS-779;
RP LYS-817; LYS-827; LYS-832 AND LYS-845, SUMOYLATION [LARGE SCALE ANALYSIS]
RP AT LYS-130; LYS-490 AND LYS-522 (ISOFORM 3), 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 [15]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INTERACTION WITH UBE2I AND SUMO2,
RP MUTAGENESIS OF 31-ILE--VAL-34; GLY-37; 38-PRO--PRO-41; LEU-39;
RP 46-ILE--VAL-49; GLY-188 AND ARG-192, AND DOMAIN.
RX PubMed=26524493; DOI=10.1038/nsmb.3114;
RA Eisenhardt N., Chaugule V.K., Koidl S., Droescher M., Dogan E., Rettich J.,
RA Sutinen P., Imanishi S.Y., Hofmann K., Palvimo J.J., Pichler A.;
RT "A new vertebrate SUMO enzyme family reveals insights into SUMO-chain
RT assembly.";
RL Nat. Struct. Mol. Biol. 22:959-967(2015).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-75; LYS-77; LYS-106; LYS-139;
RP LYS-144; LYS-153; LYS-167; LYS-270; LYS-275; LYS-283; LYS-288; LYS-301;
RP LYS-309; LYS-357; LYS-423; LYS-434; LYS-446; LYS-452; LYS-454; LYS-464;
RP LYS-543; LYS-585; LYS-632; LYS-647; LYS-664; LYS-706; LYS-731; LYS-748;
RP LYS-777; LYS-779; LYS-790; LYS-817; LYS-827; LYS-832; LYS-843; LYS-845;
RP LYS-852; LYS-951; LYS-992 AND LYS-993, SUMOYLATION [LARGE SCALE ANALYSIS]
RP AT LYS-121; LYS-130; LYS-138; LYS-164; LYS-226; LYS-240; LYS-247; LYS-263;
RP LYS-286; LYS-293; LYS-473; LYS-490; LYS-500; LYS-505; LYS-508; LYS-522 AND
RP LYS-532 (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [17]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-56 IN COMPLEX WITH SUMO2 AND
RP UBE2I, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH UBE2I AND SUMO2,
RP SUBUNIT, PATHWAY, DOMAIN, MUTAGENESIS OF 38-PRO--PRO-41 AND ARG-40, AND
RP SUMOYLATION.
RX PubMed=26524494; DOI=10.1038/nsmb.3116;
RA Cappadocia L., Pichler A., Lima C.D.;
RT "Structural basis for catalytic activation by the human ZNF451 SUMO E3
RT ligase.";
RL Nat. Struct. Mol. Biol. 22:968-975(2015).
CC -!- FUNCTION: E3 SUMO-protein ligase; has a preference for SUMO2 and SUMO3
CC and facilitates UBE2I/UBC9-mediated sumoylation of target proteins
CC (PubMed:26524493, PubMed:26524494). Plays a role in protein SUMO2
CC modification in response to stress caused by DNA damage and by
CC proteasome inhibitors (in vitro). Required for MCM4 sumoylation (By
CC similarity). Has no activity with SUMO1 (PubMed:26524493).
CC Preferentially transfers an additional SUMO2 chain onto the SUMO2
CC consensus site 'Lys-11' (PubMed:26524493). Negatively regulates
CC transcriptional activation mediated by the SMAD4 complex in response to
CC TGF-beta signaling. Inhibits EP300-mediated acetylation of histone H3
CC at 'Lys-9' (PubMed:24324267). Plays a role in regulating the
CC transcription of AR targets (PubMed:18656483).
CC {ECO:0000250|UniProtKB:Q8C0P7, ECO:0000269|PubMed:18656483,
CC ECO:0000269|PubMed:24324267, ECO:0000269|PubMed:26524493,
CC ECO:0000269|PubMed:26524494}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000269|PubMed:26524493, ECO:0000269|PubMed:26524494}.
CC -!- SUBUNIT: Homooligomer. Interacts (via N-terminal region) with SUMO1
CC (PubMed:18656483). Interacts (via N-terminal region) with SUMO2
CC (PubMed:18656483, PubMed:26524494). Interacts simultaneously with two
CC SUMO2 chains (PubMed:26524493, PubMed:26524494). Identified in a
CC complex with SUMO2 and UBE2I/UBC9, where one ZNF451 interacts with one
CC UBE2I/UBC9 and two SUMO2 chains, one bound to the UBE2I/UBC9 active
CC site and the other to another region of the same UBE2I/UBC9 molecule
CC (PubMed:26524493, PubMed:26524494). Interacts (via C-terminus) with
CC ubiquitin (PubMed:18656483). Interacts (via N-terminal zinc-finger
CC domains) with SMAD4 (via MH2 domain). Interacts with SMAD2 and SMAD3.
CC Identified in a complex that contains at least ZNF451, SMAD2, SMAD3 and
CC SMAD4. Interacts with EP300. Inhibits interaction between EP300 and the
CC SMAD4 complex (PubMed:24324267). {ECO:0000269|PubMed:18656483,
CC ECO:0000269|PubMed:24324267, ECO:0000269|PubMed:26524493,
CC ECO:0000269|PubMed:26524494}.
CC -!- INTERACTION:
CC Q9Y4E5; P63279: UBE2I; NbExp=4; IntAct=EBI-747230, EBI-80168;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18656483,
CC ECO:0000269|PubMed:24324267}. Nucleus, PML body
CC {ECO:0000269|PubMed:18656483}. Nucleus, nucleoplasm. Note=Colocalizes
CC with UBE2I/UBC9, SUMO1 and SUMO2 in nuclear granules; this probably
CC requires sumoylation. Desumoylation leads to diffuse nucleoplasmic
CC location. {ECO:0000269|PubMed:18656483}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y4E5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y4E5-2; Sequence=VSP_008624;
CC Name=3;
CC IsoId=Q9Y4E5-4; Sequence=VSP_035312;
CC -!- DOMAIN: Binds UBE2I/UBC9 and two SUMO2 molecules via its N-terminus.
CC The most N-terminal region interacts with the SUMO2 chain that is
CC covalently bound to the UBE2I/UBC9 active site, while the second region
CC interacts with another SUMO2 that is non-covalently associated with the
CC same UBE2I/UBC9 chain. {ECO:0000269|PubMed:26524494,
CC ECO:0000305|PubMed:26524493}.
CC -!- PTM: Sumoylated. Predominantly sumoylated on the N-terminal region that
CC is important for interaction with SUMO1 and SUMO2 (PubMed:18656483,
CC PubMed:26524493, PubMed:26524494). Sumoylation is important for
CC localization in nuclear granules; desumoylation leads to diffuse
CC nucleoplasmic location (PubMed:18656483). Autosumoylated (in vitro)
CC (PubMed:26524493, PubMed:26524494). Sumoylation enhances E3 SUMO-
CC protein ligase activity (PubMed:26524494).
CC {ECO:0000269|PubMed:18656483, ECO:0000269|PubMed:26524493,
CC ECO:0000269|PubMed:26524494}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH21712.2; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=AAH42450.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
CC Sequence=AAH58853.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
CC Sequence=BAA25502.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB21793.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY055204; AAL17975.1; -; mRNA.
DR EMBL; AB011148; BAA25502.1; ALT_INIT; mRNA.
DR EMBL; AB051489; BAB21793.1; ALT_INIT; mRNA.
DR EMBL; AL136311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL450489; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021712; AAH21712.2; ALT_SEQ; mRNA.
DR EMBL; BC042450; AAH42450.1; ALT_SEQ; mRNA.
DR EMBL; BC058853; AAH58853.1; ALT_SEQ; mRNA.
DR CCDS; CCDS43477.1; -. [Q9Y4E5-1]
DR CCDS; CCDS4960.1; -. [Q9Y4E5-2]
DR CCDS; CCDS59026.1; -. [Q9Y4E5-4]
DR PIR; T00341; T00341.
DR RefSeq; NP_001026794.1; NM_001031623.2. [Q9Y4E5-1]
DR RefSeq; NP_056370.2; NM_015555.2. [Q9Y4E5-2]
DR PDB; 5D2M; X-ray; 2.40 A; G=2-56.
DR PDBsum; 5D2M; -.
DR AlphaFoldDB; Q9Y4E5; -.
DR SMR; Q9Y4E5; -.
DR BioGRID; 117502; 67.
DR DIP; DIP-51264N; -.
DR ELM; Q9Y4E5; -.
DR IntAct; Q9Y4E5; 33.
DR MINT; Q9Y4E5; -.
DR STRING; 9606.ENSP00000359740; -.
DR iPTMnet; Q9Y4E5; -.
DR PhosphoSitePlus; Q9Y4E5; -.
DR BioMuta; ZNF451; -.
DR DMDM; 37999825; -.
DR EPD; Q9Y4E5; -.
DR jPOST; Q9Y4E5; -.
DR MassIVE; Q9Y4E5; -.
DR MaxQB; Q9Y4E5; -.
DR PaxDb; Q9Y4E5; -.
DR PeptideAtlas; Q9Y4E5; -.
DR PRIDE; Q9Y4E5; -.
DR ProteomicsDB; 86178; -. [Q9Y4E5-1]
DR ProteomicsDB; 86179; -. [Q9Y4E5-2]
DR ProteomicsDB; 86180; -. [Q9Y4E5-4]
DR Antibodypedia; 2845; 88 antibodies from 21 providers.
DR DNASU; 26036; -.
DR Ensembl; ENST00000357489.7; ENSP00000350083.3; ENSG00000112200.17. [Q9Y4E5-2]
DR Ensembl; ENST00000370706.9; ENSP00000359740.4; ENSG00000112200.17. [Q9Y4E5-1]
DR Ensembl; ENST00000370708.8; ENSP00000359742.4; ENSG00000112200.17. [Q9Y4E5-4]
DR GeneID; 26036; -.
DR KEGG; hsa:26036; -.
DR MANE-Select; ENST00000370706.9; ENSP00000359740.4; NM_001031623.3; NP_001026794.1.
DR UCSC; uc003pdm.3; human. [Q9Y4E5-1]
DR CTD; 26036; -.
DR DisGeNET; 26036; -.
DR GeneCards; ZNF451; -.
DR HGNC; HGNC:21091; ZNF451.
DR HPA; ENSG00000112200; Tissue enhanced (bone).
DR MIM; 615708; gene.
DR neXtProt; NX_Q9Y4E5; -.
DR OpenTargets; ENSG00000112200; -.
DR PharmGKB; PA134967635; -.
DR VEuPathDB; HostDB:ENSG00000112200; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00390000011354; -.
DR HOGENOM; CLU_010658_0_0_1; -.
DR InParanoid; Q9Y4E5; -.
DR OMA; FACPACF; -.
DR PhylomeDB; Q9Y4E5; -.
DR TreeFam; TF331947; -.
DR PathwayCommons; Q9Y4E5; -.
DR SignaLink; Q9Y4E5; -.
DR UniPathway; UPA00886; -.
DR BioGRID-ORCS; 26036; 15 hits in 1083 CRISPR screens.
DR ChiTaRS; ZNF451; human.
DR GeneWiki; ZNF451; -.
DR GenomeRNAi; 26036; -.
DR Pharos; Q9Y4E5; Tbio.
DR PRO; PR:Q9Y4E5; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9Y4E5; protein.
DR Bgee; ENSG00000112200; Expressed in corpus callosum and 208 other tissues.
DR ExpressionAtlas; Q9Y4E5; baseline and differential.
DR Genevisible; Q9Y4E5; HS.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061665; F:SUMO ligase activity; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB.
DR GO; GO:2000616; P:negative regulation of histone H3-K9 acetylation; IMP:UniProtKB.
DR GO; GO:0060633; P:negative regulation of transcription initiation from RNA polymerase II promoter; IMP:UniProtKB.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0016925; P:protein sumoylation; IDA:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR InterPro; IPR041192; PIN_11.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF18479; PIN_11; 1.
DR SMART; SM00355; ZnF_C2H2; 12.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Isopeptide bond; Metal-binding;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1061
FT /note="E3 SUMO-protein ligase ZNF451"
FT /id="PRO_0000047598"
FT ZN_FING 169..195
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 253..277
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 315..337
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 362..386
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 498..521
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 531..554
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 606..631
FT /note="C2H2-type 7; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 636..659
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 667..690
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 753..776
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 789..812
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..344
FT /note="Important for interaction with SUMO1 and SUMO2"
FT /evidence="ECO:0000269|PubMed:18656483"
FT REGION 1..246
FT /note="Sufficient for E3 SUMO-protein ligase activity"
FT /evidence="ECO:0000269|PubMed:26524493"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 30..37
FT /note="Interaction with SUMO2 1"
FT /evidence="ECO:0000269|PubMed:26524494"
FT REGION 42..50
FT /note="Interaction with SUMO2 2"
FT /evidence="ECO:0000269|PubMed:26524494"
FT REGION 168..525
FT /note="Important for interaction with SMAD4"
FT /evidence="ECO:0000269|PubMed:24324267"
FT REGION 1050..1061
FT /note="Important for ubiquitin binding"
FT /evidence="ECO:0000269|PubMed:18656483"
FT MOTIF 38..41
FT /note="PLRP"
FT /evidence="ECO:0000305"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 158
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 75
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 77
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 106
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 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 144
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 153
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 167
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 270
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 283
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 288
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 301
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
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 357
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 423
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 434
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 446
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 452
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 454
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 464
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 543
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 585
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 632
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 647
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 664
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 706
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 706
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 731
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 748
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 777
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 779
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 790
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 817
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 827
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 832
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 843
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 845
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 852
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 951
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 992
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 993
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 63..1061
FT /note="ENIKRKDHIDYQKDKVALTLARLARHVEVEKQQKEEKNRAFREKIDFQHAHG
FT LQELEFIRGHSDTEAARLCVDQWLKMPGLKTGTINCGTKSSFRRGGHTWVSGKPILCPI
FT MHCNKEFDNGHLLLGHLKRFDHSPCDPTITLHGPFFSSFACVVCYKKFVTQQQYRDHLF
FT DKEATDDGHNNNLLPQIIQCFACPNCFLLFSRKEECSKHMSGKNHFHQSFKLGDNKGIA
FT HPISFPSFAKKLLISLCKDVPFQVKCVACHKTLRSHMELTAHFRVHCRNAGPVAVAEKS
FT ITQVAEKFILRGYCPDCNQVFVDETSTQNHKQNSGHKVRVINSVEESVLLYCHSSEGNK
FT DPSSDLHLLLDQSKFSSLKRTMSIKESSSLECIAIPKKKMNLKDKSHEGVACVQKEKSV
FT VKTWFCECNQRFPSEDAVEKHVFSANTMGYKCVVCGKVCDDSGVIRLHMSRIHGGAHLN
FT NFLFWCRTCKKELTRKDTIMAHVTEFHNGHRYFYEMDEVEGETLPSSSTTLDNLTANKP
FT SSAITVIDHSPANSSPRGKWQCRICEDMFDSQEYVKQHCMSLASHKFHRYSCAHCRKPF
FT HKIETLYRHCQDEHDNEIKIKYFCGLCDLIFNVEEAFLSHYEEHHSIDYVFVSEKTETS
FT IKTEDDFPVIETSNQLTCGCRESYICKVNRKEDYSRCLQIMLDKGKLWFRCSLCSATAQ
FT NLTDMNTHIHQVHKEKSDEEEQQYVIKCGTCTKAFHDPESAQQHFHRKHCFLQKPSVAH
FT FGSEKSNLYKFTASASHTERKLKQAINYSKSLDMEKGVENDLSYQNIEEEIVELPDLDY
FT LRTMTHIVFVDFDNWSNFFGHLPGHLNQGTFIWGFQGGNTNWKPPLNCKIYNYLNRIGC
FT FFLHPRCSKRKDAADFAICMHAGRLDEQLPKQIPFTILSGDQGFLELENQFKKTQRPAH
FT ILNPHHLEGDMMCALLNSISDTTKECDSDDNMGAKNTSIGEEFISTEDVELEEAIRRSL
FT EEM -> RMPESKVPSSENHRPEMCSSCNVPLPIGDSSSFSGSCSSSPERIVSQTSSVE
FT NPLENQKNDQNNSDTKISETETLKSSQNFQTLPSSPLLVPQESLASSEVKENLRIDSSS
FT ASQHGRDAILYLQTQVAEMSRVIRDLQSRSCFRFHHSRPSENSSVPWDISTSKEENLST
FT VEEETDYKSPSADDKGQPSDPSQSSFTGLLKRMEQRGVIKRVTLQSEAESCEGKPDCVT
FT SKKRLVPPLHPLLRIATTEVFKDPADCHPSSFMGHRVYPVAKDTSPFQPNPPAEGPIVE
FT ALEHSKRGNTTSPLDSTSKEMEVMGCRFYHAASIAARAASYMAYMTQYQRKLWEDMEDL
FT VHDPEFDRGKARCIISDGMDAGLWQLCTTRDIMDSVVRVMAMAIDYRRQAWLRLTSLTK
FT KTQEKISHLPFDGTSLFGQDVKAVVAEDNNIKENDYKDHKYYNQHRYFYSHDQKAHYHN
FT RGYSKGDWYKPRNHPYRYRKKGDSPERHGYKN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11214970,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_035312"
FT VAR_SEQ 870..917
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_008624"
FT MUTAGEN 31..34
FT /note="IQFV->AQAA: Nearly abolishes E3 SUMO-protein ligase
FT activity (in vitro)."
FT /evidence="ECO:0000269|PubMed:26524493"
FT MUTAGEN 37
FT /note="G->GGSGG: Nearly abolishes E3 SUMO-protein ligase
FT activity (in vitro)."
FT /evidence="ECO:0000269|PubMed:26524493"
FT MUTAGEN 38..41
FT /note="PLRP->ALRA: Reduces E3 SUMO-protein ligase activity
FT by 97% (in vitro)."
FT /evidence="ECO:0000269|PubMed:26524494"
FT MUTAGEN 38..41
FT /note="PLRP->GLRG: Nearly abolishes E3 SUMO-protein ligase
FT activity (in vitro)."
FT /evidence="ECO:0000269|PubMed:26524493"
FT MUTAGEN 39
FT /note="L->LGSGG: Nearly abolishes E3 SUMO-protein ligase
FT activity (in vitro)."
FT /evidence="ECO:0000269|PubMed:26524493"
FT MUTAGEN 40
FT /note="R->A: Reduces E3 SUMO-protein ligase activity by 96%
FT (in vitro)."
FT /evidence="ECO:0000269|PubMed:26524494"
FT MUTAGEN 46..49
FT /note="IDLV->ADAA: Nearly abolishes E3 SUMO-protein ligase
FT activity (in vitro)."
FT /evidence="ECO:0000269|PubMed:26524493"
FT MUTAGEN 48..49
FT /note="LV->AA: Impairs interaction with SUMO1. No effect on
FT negative regulation of SMAD4-mediated transcription
FT activation."
FT /evidence="ECO:0000269|PubMed:18656483,
FT ECO:0000269|PubMed:24324267"
FT MUTAGEN 188
FT /note="G->E: Mildly reduces E3 SUMO-protein ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:26524493"
FT MUTAGEN 192
FT /note="R->E: Mildly reduces E3 SUMO-protein ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:26524493"
FT MUTAGEN 706
FT /note="K->R: No effect on negative regulation of SMAD4-
FT mediated transcription activation."
FT /evidence="ECO:0000269|PubMed:24324267"
FT CONFLICT 169
FT /note="I -> T (in Ref. 1; AAL17975)"
FT /evidence="ECO:0000305"
FT STRAND 32..40
FT /evidence="ECO:0007829|PDB:5D2M"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:5D2M"
FT CROSSLNK Q9Y4E5-4:121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK Q9Y4E5-4:130
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 Q9Y4E5-4:138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK Q9Y4E5-4:164
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 Q9Y4E5-4:226
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK Q9Y4E5-4:240
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK Q9Y4E5-4:247
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK Q9Y4E5-4:263
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK Q9Y4E5-4:286
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK Q9Y4E5-4:293
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK Q9Y4E5-4:473
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK Q9Y4E5-4:490
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 Q9Y4E5-4:500
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK Q9Y4E5-4:505
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK Q9Y4E5-4:508
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK Q9Y4E5-4:522
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 Q9Y4E5-4:532
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ SEQUENCE 1061 AA; 121484 MW; 8F0446B9FBFF28FA CRC64;
MGDPGSEIIE SVPPAGPEAS ESTTDENEDD IQFVSEGPLR PVLEYIDLVS SDDEEPSTSY
TDENIKRKDH IDYQKDKVAL TLARLARHVE VEKQQKEEKN RAFREKIDFQ HAHGLQELEF
IRGHSDTEAA RLCVDQWLKM PGLKTGTINC GTKSSFRRGG HTWVSGKPIL CPIMHCNKEF
DNGHLLLGHL KRFDHSPCDP TITLHGPFFS SFACVVCYKK FVTQQQYRDH LFDKEATDDG
HNNNLLPQII QCFACPNCFL LFSRKEECSK HMSGKNHFHQ SFKLGDNKGI AHPISFPSFA
KKLLISLCKD VPFQVKCVAC HKTLRSHMEL TAHFRVHCRN AGPVAVAEKS ITQVAEKFIL
RGYCPDCNQV FVDETSTQNH KQNSGHKVRV INSVEESVLL YCHSSEGNKD PSSDLHLLLD
QSKFSSLKRT MSIKESSSLE CIAIPKKKMN LKDKSHEGVA CVQKEKSVVK TWFCECNQRF
PSEDAVEKHV FSANTMGYKC VVCGKVCDDS GVIRLHMSRI HGGAHLNNFL FWCRTCKKEL
TRKDTIMAHV TEFHNGHRYF YEMDEVEGET LPSSSTTLDN LTANKPSSAI TVIDHSPANS
SPRGKWQCRI CEDMFDSQEY VKQHCMSLAS HKFHRYSCAH CRKPFHKIET LYRHCQDEHD
NEIKIKYFCG LCDLIFNVEE AFLSHYEEHH SIDYVFVSEK TETSIKTEDD FPVIETSNQL
TCGCRESYIC KVNRKEDYSR CLQIMLDKGK LWFRCSLCSA TAQNLTDMNT HIHQVHKEKS
DEEEQQYVIK CGTCTKAFHD PESAQQHFHR KHCFLQKPSV AHFGSEKSNL YKFTASASHT
ERKLKQAINY SKSLDMEKGV ENDLSYQNIE EEIVELPDLD YLRTMTHIVF VDFDNWSNFF
GHLPGHLNQG TFIWGFQGGN TNWKPPLNCK IYNYLNRIGC FFLHPRCSKR KDAADFAICM
HAGRLDEQLP KQIPFTILSG DQGFLELENQ FKKTQRPAHI LNPHHLEGDM MCALLNSISD
TTKECDSDDN MGAKNTSIGE EFISTEDVEL EEAIRRSLEE M
