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E3 SUMO-protein ligase ZNF451 (EC 2.3.2.-) (Coactivator for steroid receptors) (E3 SUMO-protein transferase ZNF451) (Zinc finger protein 451)

 ZN451_HUMAN             Reviewed;        1061 AA.
Q9Y4E5; Q5VVE9; Q5VVF1; Q86YE4; Q8N380; Q8TD15; Q9C0G1; Q9NQM1;
24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
24-OCT-2003, sequence version 2.
26-FEB-2020, entry version 175.
RecName: Full=E3 SUMO-protein ligase ZNF451 {ECO:0000303|PubMed:26524494};
EC=2.3.2.- {ECO:0000269|PubMed:26524493, ECO:0000269|PubMed:26524494};
AltName: Full=Coactivator for steroid receptors {ECO:0000303|Ref.1};
AltName: Full=E3 SUMO-protein transferase ZNF451 {ECO:0000305};
AltName: Full=Zinc finger protein 451;
Name=ZNF451; Synonyms=COASTER {ECO:0000303|Ref.1}, KIAA0576, KIAA1702;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Heldens I.M., Dechering K.J.;
"Isolation of a novel coactivator for steroid receptors that alters the
intrinsic activity of the estrogen receptor alpha liganded with SERMs.";
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9628581; DOI=10.1093/dnares/5.1.31;
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
Ohara O.;
"Prediction of the coding sequences of unidentified human genes. IX. The
complete sequences of 100 new cDNA clones from brain which can code for
large proteins in vitro.";
DNA Res. 5:31-39(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 63-1061 (ISOFORM 3).
TISSUE=Brain;
PubMed=11214970; DOI=10.1093/dnares/7.6.347;
Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIX. The
complete sequences of 100 new cDNA clones from brain which code for large
proteins in vitro.";
DNA Res. 7:347-355(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-918 (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 36-1061 (ISOFORM 3).
TISSUE=Brain, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SUMO1; SUMO2 AND
UBIQUITIN, AND MUTAGENESIS OF 48-LEU-VAL-49.
PubMed=18656483; DOI=10.1016/j.jmb.2008.07.016;
Karvonen U., Jaeaeskelaeinen T., Rytinki M., Kaikkonen S., Palvimo J.J.;
"ZNF451 is a novel PML body- and SUMO-associated transcriptional
coregulator.";
J. Mol. Biol. 382:585-600(2008).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-432, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[9]
FUNCTION, INTERACTION WITH EP300; SMAD2; SMAD3 AND SMAD4, IDENTIFICATION IN
A COMPLEX WITH SMAD2; SMAD3 AND SMAD4, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF 48-LEU-VAL-49 AND LYS-706.
PubMed=24324267; DOI=10.1074/jbc.m113.526905;
Feng Y., Wu H., Xu Y., Zhang Z., Liu T., Lin X., Feng X.H.;
"Zinc finger protein 451 is a novel Smad corepressor in transforming growth
factor-beta signaling.";
J. Biol. Chem. 289:2072-2083(2014).
[10]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-158, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.o113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[11]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-75; LYS-77; LYS-106; LYS-288;
LYS-423; LYS-434; LYS-464; LYS-706; LYS-779; LYS-817; LYS-827; LYS-832;
LYS-843 AND LYS-845, SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-130; LYS-164
AND LYS-490 (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[12]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-706, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[13]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-139; LYS-153; LYS-288; LYS-423;
LYS-434; LYS-706; LYS-779; LYS-817; LYS-827; LYS-832; LYS-845; LYS-852 AND
LYS-993, SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-130 AND LYS-490 (ISOFORM
3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[14]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-288; LYS-434; LYS-664; LYS-779;
LYS-817; LYS-827; LYS-832 AND LYS-845, SUMOYLATION [LARGE SCALE ANALYSIS]
AT LYS-130; LYS-490 AND LYS-522 (ISOFORM 3), AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.o114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to replication
stress reveals novel small ubiquitin-like modified target proteins and
acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[15]
FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INTERACTION WITH UBE2I AND SUMO2,
MUTAGENESIS OF 31-ILE--VAL-34; GLY-37; 38-PRO--PRO-41; LEU-39;
46-ILE--VAL-49; GLY-188 AND ARG-192, AND DOMAIN.
PubMed=26524493; DOI=10.1038/nsmb.3114;
Eisenhardt N., Chaugule V.K., Koidl S., Droescher M., Dogan E., Rettich J.,
Sutinen P., Imanishi S.Y., Hofmann K., Palvimo J.J., Pichler A.;
"A new vertebrate SUMO enzyme family reveals insights into SUMO-chain
assembly.";
Nat. Struct. Mol. Biol. 22:959-967(2015).
[16]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-75; LYS-77; LYS-106; LYS-139;
LYS-144; LYS-153; LYS-167; LYS-270; LYS-275; LYS-283; LYS-288; LYS-301;
LYS-309; LYS-357; LYS-423; LYS-434; LYS-446; LYS-452; LYS-454; LYS-464;
LYS-543; LYS-585; LYS-632; LYS-647; LYS-664; LYS-706; LYS-731; LYS-748;
LYS-777; LYS-779; LYS-790; LYS-817; LYS-827; LYS-832; LYS-843; LYS-845;
LYS-852; LYS-951; LYS-992 AND LYS-993, SUMOYLATION [LARGE SCALE ANALYSIS]
AT LYS-121; LYS-130; LYS-138; LYS-164; LYS-226; LYS-240; LYS-247; LYS-263;
LYS-286; LYS-293; LYS-473; LYS-490; LYS-500; LYS-505; LYS-508; LYS-522 AND
LYS-532 (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-modification
with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[17]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-56 IN COMPLEX WITH SUMO2 AND
UBE2I, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH UBE2I AND SUMO2,
SUBUNIT, PATHWAY, DOMAIN, MUTAGENESIS OF 38-PRO--PRO-41 AND ARG-40, AND
SUMOYLATION.
PubMed=26524494; DOI=10.1038/nsmb.3116;
Cappadocia L., Pichler A., Lima C.D.;
"Structural basis for catalytic activation by the human ZNF451 SUMO E3
ligase.";
Nat. Struct. Mol. Biol. 22:968-975(2015).
-!- FUNCTION: E3 SUMO-protein ligase; has a preference for SUMO2 and SUMO3
and facilitates UBE2I/UBC9-mediated sumoylation of target proteins
(PubMed:26524493, PubMed:26524494). Plays a role in protein SUMO2
modification in response to stress caused by DNA damage and by
proteasome inhibitors (in vitro). Required for MCM4 sumoylation (By
similarity). Has no activity with SUMO1 (PubMed:26524493).
Preferentially transfers an additional SUMO2 chain onto the SUMO2
consensus site 'Lys-11' (PubMed:26524493). Negatively regulates
transcriptional activation mediated by the SMAD4 complex in response to
TGF-beta signaling. Inhibits EP300-mediated acetylation of histone H3
at 'Lys-9' (PubMed:24324267). Plays a role in regulating the
transcription of AR targets (PubMed:18656483).
{ECO:0000250|UniProtKB:Q8C0P7, ECO:0000269|PubMed:18656483,
ECO:0000269|PubMed:24324267, ECO:0000269|PubMed:26524493,
ECO:0000269|PubMed:26524494}.
-!- PATHWAY: Protein modification; protein sumoylation.
{ECO:0000269|PubMed:26524493, ECO:0000269|PubMed:26524494}.
-!- SUBUNIT: Homooligomer. Interacts (via N-terminal region) with SUMO1
(PubMed:18656483). Interacts (via N-terminal region) with SUMO2
(PubMed:18656483, PubMed:26524494). Interacts simultaneously with two
SUMO2 chains (PubMed:26524493, PubMed:26524494). Identified in a
complex with SUMO2 and UBE2I/UBC9, where one ZNF451 interacts with one
UBE2I/UBC9 and two SUMO2 chains, one bound to the UBE2I/UBC9 active
site and the other to another region of the same UBE2I/UBC9 molecule
(PubMed:26524493, PubMed:26524494). Interacts (via C-terminus) with
ubiquitin (PubMed:18656483). Interacts (via N-terminal zinc-finger
domains) with SMAD4 (via MH2 domain). Interacts with SMAD2 and SMAD3.
Identified in a complex that contains at least ZNF451, SMAD2, SMAD3 and
SMAD4. Interacts with EP300. Inhibits interaction between EP300 and the
SMAD4 complex (PubMed:24324267). {ECO:0000269|PubMed:18656483,
ECO:0000269|PubMed:24324267, ECO:0000269|PubMed:26524493,
ECO:0000269|PubMed:26524494}.
-!- INTERACTION:
P63279:UBE2I; NbExp=3; IntAct=EBI-747230, EBI-80168;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18656483,
ECO:0000269|PubMed:24324267}. Nucleus, PML body
{ECO:0000269|PubMed:18656483}. Nucleus, nucleoplasm. Note=Colocalizes
with UBE2I/UBC9, SUMO1 and SUMO2 in nuclear granules; this probably
requires sumoylation. Desumoylation leads to diffuse nucleoplasmic
location. {ECO:0000269|PubMed:18656483}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9Y4E5-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y4E5-2; Sequence=VSP_008624;
Name=3;
IsoId=Q9Y4E5-4; Sequence=VSP_035312;
-!- DOMAIN: Binds UBE2I/UBC9 and two SUMO2 molecules via its N-terminus.
The most N-terminal region interacts with the SUMO2 chain that is
covalently bound to the UBE2I/UBC9 active site, while the second region
interacts with another SUMO2 that is non-covalently associated with the
same UBE2I/UBC9 chain. {ECO:0000269|PubMed:26524494,
ECO:0000305|PubMed:26524493}.
-!- PTM: Sumoylated. Predominantly sumoylated on the N-terminal region that
is important for interaction with SUMO1 and SUMO2 (PubMed:18656483,
PubMed:26524493, PubMed:26524494). Sumoylation is important for
localization in nuclear granules; desumoylation leads to diffuse
nucleoplasmic location (PubMed:18656483). Autosumoylated (in vitro)
(PubMed:26524493, PubMed:26524494). Sumoylation enhances E3 SUMO-
protein ligase activity (PubMed:26524494).
{ECO:0000269|PubMed:18656483, ECO:0000269|PubMed:26524493,
ECO:0000269|PubMed:26524494}.
-!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH21712.2; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
Sequence=AAH42450.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
Sequence=AAH58853.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
Sequence=BAA25502.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAB21793.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AY055204; AAL17975.1; -; mRNA.
EMBL; AB011148; BAA25502.1; ALT_INIT; mRNA.
EMBL; AB051489; BAB21793.1; ALT_INIT; mRNA.
EMBL; AL136311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL450489; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC021712; AAH21712.2; ALT_SEQ; mRNA.
EMBL; BC042450; AAH42450.1; ALT_SEQ; mRNA.
EMBL; BC058853; AAH58853.1; ALT_SEQ; mRNA.
CCDS; CCDS43477.1; -. [Q9Y4E5-1]
CCDS; CCDS4960.1; -. [Q9Y4E5-2]
CCDS; CCDS59026.1; -. [Q9Y4E5-4]
PIR; T00341; T00341.
RefSeq; NP_001026794.1; NM_001031623.2. [Q9Y4E5-1]
RefSeq; NP_056370.2; NM_015555.2. [Q9Y4E5-2]
PDB; 5D2M; X-ray; 2.40 A; G=2-56.
PDBsum; 5D2M; -.
SMR; Q9Y4E5; -.
BioGrid; 117502; 43.
DIP; DIP-51264N; -.
ELM; Q9Y4E5; -.
IntAct; Q9Y4E5; 29.
MINT; Q9Y4E5; -.
STRING; 9606.ENSP00000359740; -.
iPTMnet; Q9Y4E5; -.
PhosphoSitePlus; Q9Y4E5; -.
BioMuta; ZNF451; -.
DMDM; 37999825; -.
EPD; Q9Y4E5; -.
jPOST; Q9Y4E5; -.
MassIVE; Q9Y4E5; -.
PaxDb; Q9Y4E5; -.
PeptideAtlas; Q9Y4E5; -.
PRIDE; Q9Y4E5; -.
ProteomicsDB; 86178; -. [Q9Y4E5-1]
ProteomicsDB; 86179; -. [Q9Y4E5-2]
ProteomicsDB; 86180; -. [Q9Y4E5-4]
DNASU; 26036; -.
Ensembl; ENST00000357489; ENSP00000350083; ENSG00000112200. [Q9Y4E5-2]
Ensembl; ENST00000370708; ENSP00000359742; ENSG00000112200. [Q9Y4E5-4]
Ensembl; ENST00000370706; ENSP00000359740; ENSG00000112200. [Q9Y4E5-1]
GeneID; 26036; -.
KEGG; hsa:26036; -.
UCSC; uc003pdm.3; human. [Q9Y4E5-1]
CTD; 26036; -.
DisGeNET; 26036; -.
GeneCards; ZNF451; -.
HGNC; HGNC:21091; ZNF451.
HPA; HPA028838; -.
MIM; 615708; gene.
neXtProt; NX_Q9Y4E5; -.
OpenTargets; ENSG00000112200; -.
PharmGKB; PA134967635; -.
eggNOG; ENOG410ITHH; Eukaryota.
eggNOG; ENOG41116BX; LUCA.
GeneTree; ENSGT00390000011354; -.
HOGENOM; CLU_010658_0_0_1; -.
InParanoid; Q9Y4E5; -.
OMA; TITIIDH; -.
OrthoDB; 148216at2759; -.
PhylomeDB; Q9Y4E5; -.
TreeFam; TF331947; -.
UniPathway; UPA00886; -.
ChiTaRS; ZNF451; human.
GeneWiki; ZNF451; -.
GenomeRNAi; 26036; -.
Pharos; Q9Y4E5; Tbio.
PRO; PR:Q9Y4E5; -.
Proteomes; UP000005640; Chromosome 6.
RNAct; Q9Y4E5; protein.
Bgee; ENSG00000112200; Expressed in corpus callosum and 235 other tissues.
ExpressionAtlas; Q9Y4E5; baseline and differential.
Genevisible; Q9Y4E5; HS.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0061665; F:SUMO ligase activity; IDA:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB.
GO; GO:2000616; P:negative regulation of histone H3-K9 acetylation; IMP:UniProtKB.
GO; GO:0060633; P:negative regulation of transcription initiation from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
GO; GO:0016925; P:protein sumoylation; IDA:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
GO; GO:0031060; P:regulation of histone methylation; IBA:GO_Central.
InterPro; IPR041192; PIN_11.
InterPro; IPR013087; Znf_C2H2_type.
Pfam; PF18479; PIN_11; 1.
SMART; SM00355; ZnF_C2H2; 12.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
1: Evidence at protein level;
3D-structure; Alternative splicing; Isopeptide bond; Metal-binding;
Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
Transcription; Transcription regulation; Transferase; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1..1061
/note="E3 SUMO-protein ligase ZNF451"
/id="PRO_0000047598"
ZN_FING 169..195
/note="C2H2-type 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
ZN_FING 253..277
/note="C2H2-type 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
ZN_FING 315..337
/note="C2H2-type 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
ZN_FING 362..386
/note="C2H2-type 4"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
ZN_FING 498..521
/note="C2H2-type 5"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
ZN_FING 531..554
/note="C2H2-type 6"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
ZN_FING 606..631
/note="C2H2-type 7; atypical"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
ZN_FING 636..659
/note="C2H2-type 8"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
ZN_FING 667..690
/note="C2H2-type 9"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
ZN_FING 753..776
/note="C2H2-type 10"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
ZN_FING 789..812
/note="C2H2-type 11"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
REGION 1..344
/note="Important for interaction with SUMO1 and SUMO2"
/evidence="ECO:0000269|PubMed:18656483"
REGION 1..246
/note="Sufficient for E3 SUMO-protein ligase activity"
/evidence="ECO:0000269|PubMed:26524493"
REGION 30..37
/note="Interaction with SUMO2 1"
/evidence="ECO:0000269|PubMed:26524494"
REGION 42..50
/note="Interaction with SUMO2 2"
/evidence="ECO:0000269|PubMed:26524494"
REGION 168..525
/note="Important for interaction with SMAD4"
/evidence="ECO:0000269|PubMed:24324267"
REGION 1050..1061
/note="Important for ubiquitin binding"
/evidence="ECO:0000269|PubMed:18656483"
MOTIF 38..41
/note="PLRP"
/evidence="ECO:0000305"
MOD_RES 155
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 158
/note="Omega-N-methylarginine"
/evidence="ECO:0000244|PubMed:24129315"
MOD_RES 432
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
CROSSLNK 75
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733"
CROSSLNK 77
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733"
CROSSLNK 106
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733"
CROSSLNK 139
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733"
CROSSLNK 144
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 153
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733"
CROSSLNK 167
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 270
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 275
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 283
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 288
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297, ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733"
CROSSLNK 301
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 309
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 357
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 423
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364, ECO:0000244|PubMed:28112733"
CROSSLNK 434
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297, ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733"
CROSSLNK 446
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 452
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 454
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 464
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733"
CROSSLNK 543
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 585
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 632
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 647
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 664
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733"
CROSSLNK 706
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO1); alternate"
/evidence="ECO:0000244|PubMed:25114211"
CROSSLNK 706
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447, ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733"
CROSSLNK 731
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 748
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 777
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 779
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297, ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733"
CROSSLNK 790
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 817
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297, ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733"
CROSSLNK 827
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297, ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733"
CROSSLNK 832
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297, ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733"
CROSSLNK 843
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733"
CROSSLNK 845
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297, ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733"
CROSSLNK 852
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733"
CROSSLNK 951
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 992
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 993
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733"
VAR_SEQ 63..1061
/note="ENIKRKDHIDYQKDKVALTLARLARHVEVEKQQKEEKNRAFREKIDFQHAHG
LQELEFIRGHSDTEAARLCVDQWLKMPGLKTGTINCGTKSSFRRGGHTWVSGKPILCPI
MHCNKEFDNGHLLLGHLKRFDHSPCDPTITLHGPFFSSFACVVCYKKFVTQQQYRDHLF
DKEATDDGHNNNLLPQIIQCFACPNCFLLFSRKEECSKHMSGKNHFHQSFKLGDNKGIA
HPISFPSFAKKLLISLCKDVPFQVKCVACHKTLRSHMELTAHFRVHCRNAGPVAVAEKS
ITQVAEKFILRGYCPDCNQVFVDETSTQNHKQNSGHKVRVINSVEESVLLYCHSSEGNK
DPSSDLHLLLDQSKFSSLKRTMSIKESSSLECIAIPKKKMNLKDKSHEGVACVQKEKSV
VKTWFCECNQRFPSEDAVEKHVFSANTMGYKCVVCGKVCDDSGVIRLHMSRIHGGAHLN
NFLFWCRTCKKELTRKDTIMAHVTEFHNGHRYFYEMDEVEGETLPSSSTTLDNLTANKP
SSAITVIDHSPANSSPRGKWQCRICEDMFDSQEYVKQHCMSLASHKFHRYSCAHCRKPF
HKIETLYRHCQDEHDNEIKIKYFCGLCDLIFNVEEAFLSHYEEHHSIDYVFVSEKTETS
IKTEDDFPVIETSNQLTCGCRESYICKVNRKEDYSRCLQIMLDKGKLWFRCSLCSATAQ
NLTDMNTHIHQVHKEKSDEEEQQYVIKCGTCTKAFHDPESAQQHFHRKHCFLQKPSVAH
FGSEKSNLYKFTASASHTERKLKQAINYSKSLDMEKGVENDLSYQNIEEEIVELPDLDY
LRTMTHIVFVDFDNWSNFFGHLPGHLNQGTFIWGFQGGNTNWKPPLNCKIYNYLNRIGC
FFLHPRCSKRKDAADFAICMHAGRLDEQLPKQIPFTILSGDQGFLELENQFKKTQRPAH
ILNPHHLEGDMMCALLNSISDTTKECDSDDNMGAKNTSIGEEFISTEDVELEEAIRRSL
EEM -> RMPESKVPSSENHRPEMCSSCNVPLPIGDSSSFSGSCSSSPERIVSQTSSVE
NPLENQKNDQNNSDTKISETETLKSSQNFQTLPSSPLLVPQESLASSEVKENLRIDSSS
ASQHGRDAILYLQTQVAEMSRVIRDLQSRSCFRFHHSRPSENSSVPWDISTSKEENLST
VEEETDYKSPSADDKGQPSDPSQSSFTGLLKRMEQRGVIKRVTLQSEAESCEGKPDCVT
SKKRLVPPLHPLLRIATTEVFKDPADCHPSSFMGHRVYPVAKDTSPFQPNPPAEGPIVE
ALEHSKRGNTTSPLDSTSKEMEVMGCRFYHAASIAARAASYMAYMTQYQRKLWEDMEDL
VHDPEFDRGKARCIISDGMDAGLWQLCTTRDIMDSVVRVMAMAIDYRRQAWLRLTSLTK
KTQEKISHLPFDGTSLFGQDVKAVVAEDNNIKENDYKDHKYYNQHRYFYSHDQKAHYHN
RGYSKGDWYKPRNHPYRYRKKGDSPERHGYKN (in isoform 3)"
/evidence="ECO:0000303|PubMed:11214970,
ECO:0000303|PubMed:15489334"
/id="VSP_035312"
VAR_SEQ 870..917
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|Ref.1"
/id="VSP_008624"
MUTAGEN 31..34
/note="IQFV->AQAA: Nearly abolishes E3 SUMO-protein ligase
activity (in vitro)."
/evidence="ECO:0000269|PubMed:26524493"
MUTAGEN 37
/note="G->GGSGG: Nearly abolishes E3 SUMO-protein ligase
activity (in vitro)."
/evidence="ECO:0000269|PubMed:26524493"
MUTAGEN 38..41
/note="PLRP->ALRA: Reduces E3 SUMO-protein ligase activity
by 97% (in vitro)."
/evidence="ECO:0000269|PubMed:26524494"
MUTAGEN 38..41
/note="PLRP->GLRG: Nearly abolishes E3 SUMO-protein ligase
activity (in vitro)."
/evidence="ECO:0000269|PubMed:26524493"
MUTAGEN 39
/note="L->LGSGG: Nearly abolishes E3 SUMO-protein ligase
activity (in vitro)."
/evidence="ECO:0000269|PubMed:26524493"
MUTAGEN 40
/note="R->A: Reduces E3 SUMO-protein ligase activity by 96%
(in vitro)."
/evidence="ECO:0000269|PubMed:26524494"
MUTAGEN 46..49
/note="IDLV->ADAA: Nearly abolishes E3 SUMO-protein ligase
activity (in vitro)."
/evidence="ECO:0000269|PubMed:26524493"
MUTAGEN 48..49
/note="LV->AA: Impairs interaction with SUMO1. No effect on
negative regulation of SMAD4-mediated transcription
activation."
/evidence="ECO:0000269|PubMed:18656483,
ECO:0000269|PubMed:24324267"
MUTAGEN 188
/note="G->E: Mildly reduces E3 SUMO-protein ligase
activity."
/evidence="ECO:0000269|PubMed:26524493"
MUTAGEN 192
/note="R->E: Mildly reduces E3 SUMO-protein ligase
activity."
/evidence="ECO:0000269|PubMed:26524493"
MUTAGEN 706
/note="K->R: No effect on negative regulation of SMAD4-
mediated transcription activation."
/evidence="ECO:0000269|PubMed:24324267"
CONFLICT 169
/note="I -> T (in Ref. 1; AAL17975)"
/evidence="ECO:0000305"
STRAND 32..40
/evidence="ECO:0000244|PDB:5D2M"
STRAND 42..47
/evidence="ECO:0000244|PDB:5D2M"
CROSSLNK Q9Y4E5-4:121
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK Q9Y4E5-4:130
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297, ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733"
CROSSLNK Q9Y4E5-4:138
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK Q9Y4E5-4:164
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733"
CROSSLNK Q9Y4E5-4:226
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK Q9Y4E5-4:240
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK Q9Y4E5-4:247
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK Q9Y4E5-4:263
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK Q9Y4E5-4:286
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK Q9Y4E5-4:293
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK Q9Y4E5-4:473
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK Q9Y4E5-4:490
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297, ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733"
CROSSLNK Q9Y4E5-4:500
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK Q9Y4E5-4:505
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK Q9Y4E5-4:508
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK Q9Y4E5-4:522
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733"
CROSSLNK Q9Y4E5-4:532
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
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


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CSB-EL026763HU Human zinc finger protein 451 (ZNF451) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL026763MO Mouse zinc finger protein 451 (ZNF451) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
10-663-45613 SUMO-I_Sentrin-I Human - SUMO-1; Ubiquitin-like protein SMT3C; SMT3 homolog 3; Ubiquitin-homology domain protein PIC1; Ubiquitin-like protein UBL1; GAP-modifying protein 1; GMP1; Sentrin N_A 0.05 mg
10-663-45613 SUMO-I_Sentrin-I Human - SUMO-1; Ubiquitin-like protein SMT3C; SMT3 homolog 3; Ubiquitin-homology domain protein PIC1; Ubiquitin-like protein UBL1; GAP-modifying protein 1; GMP1; Sentrin N_A 1 mg
10-663-45613 SUMO-I_Sentrin-I Human - SUMO-1; Ubiquitin-like protein SMT3C; SMT3 homolog 3; Ubiquitin-homology domain protein PIC1; Ubiquitin-like protein UBL1; GAP-modifying protein 1; GMP1; Sentrin N_A 0.01 mg
18-003-44309 SUMO-conjugating enzyme UBC9 - EC 6.3.2.-; SUMO-protein ligase; Ubiquitin-conjugating enzyme E2 I; Ubiquitin-protein ligase I; Ubiquitin carrier protein I; Ubiquitin carrier protein 9; p18 Polyclonal 0.1 mg Protein A
EIAAB44876 Homo sapiens,Human,p18,SUMO-conjugating enzyme UBC9,SUMO-protein ligase,UBC9,UBCE9,UBE2I,Ubiquitin carrier protein 9,Ubiquitin carrier protein I,Ubiquitin-conjugating enzyme E2 I,Ubiquitin-protein lig
EIAAB44874 Rat,Rattus norvegicus,SUMO-conjugating enzyme UBC9,SUMO-protein ligase,Ubce9,Ube2i,Ubiquitin carrier protein 9,Ubiquitin carrier protein I,Ubiquitin-conjugating enzyme E2 I,Ubiquitin-conjugating enzym
EIAAB44873 Mouse,mUBC9,Mus musculus,SUMO-conjugating enzyme UBC9,SUMO-protein ligase,Ubc9,Ubce2i,Ubce9,Ube2i,Ubiquitin carrier protein 9,Ubiquitin carrier protein I,Ubiquitin-conjugating enzyme E2 I,Ubiquitin-pr
18-783-75567 RABBIT ANTI SUMO-1 (N-TERMINAL) - SMALL UBIQUITIN-RELATED MODIFIER-1; SUMO-1; Sentrin; Ubiquitin-like protein SMT3C; SMT3 homolog 3; Ubiquitin-homology domain protein PIC1; Ubiquitin-like protein UBL1 0.1 mg
EIAAB31030 Ddxbp1,DEAD_H box-binding protein 1,E3 SUMO-protein ligase PIAS1,Mouse,Mus musculus,Pias1,Protein inhibitor of activated STAT protein 1
Pathways :
WP2199: Seed Development
WP1678: Nucleotide excision repair
WP1672: Mismatch repair
WP1714: Tyrosine metabolism
WP1625: Base excision repair
WP1676: Non-homologous end-joining
WP1624: Bacterial secretion system
WP1888: Post-translational protein modification
WP525: Mitochondrial Unfolded-Protein Response
WP1675: Nitrogen metabolism
WP2292: Chemokine signaling pathway
WP1685: Peptidoglycan biosynthesis
WP1644: DNA replication
WP1654: gamma-Hexachlorocyclohexane degradation
WP2032: TSH signaling pathway
WP731: Sterol regulatory element binding protein related
WP1690: Propanoate metabolism
WP1502: Mitochondrial biogenesis
WP1694: Pyrimidine metabolism
WP346: Protein Modifications
WP1659: Glycine, serine and threonine metabolism
WP1665: Limonene and pinene degradation
WP2218: sGC
WP1673: Naphthalene and anthracene degradation
WP2272: Pathogenic Escherichia coli infection

Related Genes :
[PIAS2 PIASX] E3 SUMO-protein ligase PIAS2 (EC 2.3.2.-) (Androgen receptor-interacting protein 3) (ARIP3) (DAB2-interacting protein) (DIP) (E3 SUMO-protein transferase PIAS2) (Msx-interacting zinc finger protein) (Miz1) (PIAS-NY protein) (Protein inhibitor of activated STAT x) (Protein inhibitor of activated STAT2)
[Pias2 Miz1 Piasx] E3 SUMO-protein ligase PIAS2 (EC 2.3.2.-) (Androgen receptor-interacting protein 3) (ARIP3) (DAB2-interacting protein) (DIP) (E3 SUMO-protein transferase PIAS2) (Msx-interacting-zinc finger protein) (Protein inhibitor of activated STAT x) (Protein inhibitor of activated STAT2)
[Pias2 Miz1 Piasx] E3 SUMO-protein ligase PIAS2 (EC 2.3.2.27) (Androgen receptor-interacting protein 3) (ARIP3) (DAB2-interacting protein) (DIP) (Msx-interacting zinc finger protein) (Protein inhibitor of activated STAT x) (Protein inhibitor of activated STAT2) (RING-type E3 ubiquitin transferase PIAS2)
[EGR2 KROX20] E3 SUMO-protein ligase EGR2 (EC 2.3.2.-) (AT591) (E3 SUMO-protein transferase ERG2) (Early growth response protein 2) (EGR-2) (Zinc finger protein Krox-20)
[Egr2 Egr-2 Krox-20 Zfp-25] E3 SUMO-protein ligase EGR2 (EC 2.3.2.-) (E3 SUMO-protein transferase ERG2) (Early growth response protein 2) (EGR-2) (Zinc finger protein Krox-20)
[Egr2 Egr-2 Krox-20 Krox20] E3 SUMO-protein ligase EGR2 (EC 2.3.2.-) (E3 SUMO-protein transferase ERG2) (Early growth response protein 2) (EGR-2) (Zinc finger protein Krox-20)
[Pias3] E3 SUMO-protein ligase PIAS3 (EC 2.3.2.-) (E3 SUMO-protein transferase PIAS3) (Protein inhibitor of activated STAT protein 3)
[PIAS1 DDXBP1] E3 SUMO-protein ligase PIAS1 (EC 2.3.2.-) (DEAD/H box-binding protein 1) (E3 SUMO-protein transferase PIAS1) (Gu-binding protein) (GBP) (Protein inhibitor of activated STAT protein 1) (RNA helicase II-binding protein)
[TRIM28 KAP1 RNF96 TIF1B] Transcription intermediary factor 1-beta (TIF1-beta) (E3 SUMO-protein ligase TRIM28) (EC 2.3.2.27) (KRAB-associated protein 1) (KAP-1) (KRAB-interacting protein 1) (KRIP-1) (Nuclear corepressor KAP-1) (RING finger protein 96) (RING-type E3 ubiquitin transferase TIF1-beta) (Tripartite motif-containing protein 28)
[gei-17 W10D5.3] E3 SUMO-protein ligase gei-17 (EC 2.3.2.-) (E3 SUMO-protein transferase gei-17) (Gex-3-interacting protein 17)
[Pias1 Ddxbp1] E3 SUMO-protein ligase PIAS1 (EC 2.3.2.27) (DEAD/H box-binding protein 1) (Protein inhibitor of activated STAT protein 1) (RING-type E3 ubiquitin transferase PIAS1)
[Pias3] E3 SUMO-protein ligase PIAS3 (EC 2.3.2.-) (E3 SUMO-protein transferase PIAS3) (KChAP) (Potassium channel-associated protein) (Protein inhibitor of activated STAT protein 3)
[PIAS3] E3 SUMO-protein ligase PIAS3 (EC 2.3.2.-) (E3 SUMO-protein transferase PIAS3) (Protein inhibitor of activated STAT protein 3)
[Trim28 Kap1 Krip1 Tif1b] Transcription intermediary factor 1-beta (TIF1-beta) (E3 SUMO-protein ligase TRIM28) (EC 2.3.2.27) (KRAB-A-interacting protein) (KRIP-1) (RING-type E3 ubiquitin transferase TIF1-beta) (Tripartite motif-containing protein 28)
[PIAS4 PIASG] E3 SUMO-protein ligase PIAS4 (EC 2.3.2.27) (PIASy) (Protein inhibitor of activated STAT protein 4) (Protein inhibitor of activated STAT protein gamma) (PIAS-gamma) (RING-type E3 ubiquitin transferase PIAS4)
[Pias4 Piasg] E3 SUMO-protein ligase PIAS4 (EC 2.3.2.27) (PIASy) (Protein inhibitor of activated STAT protein 4) (Protein inhibitor of activated STAT protein gamma) (PIAS-gamma) (RING-type E3 ubiquitin transferase PIAS4)
[ubc-9 F29B9.6] SUMO-conjugating enzyme UBC9 (EC 2.3.2.-) (RING-type E3 SUMO transferase UBC9) (SUMO-protein ligase) (Ubiquitin carrier protein 9) (Ubiquitin-conjugating enzyme E2 9) (Ubiquitin-protein ligase 9)
[Trim28 Kap1 Tif1b] Transcription intermediary factor 1-beta (TIF1-beta) (E3 SUMO-protein ligase TRIM28) (EC 2.3.2.27) (KRAB-associated protein 1) (Nuclear corepressor KAP-1) (RING-type E3 ubiquitin transferase TIF1-beta) (Tripartite motif-containing protein 28)
[UBE2I UBC9 UBCE9] SUMO-conjugating enzyme UBC9 (EC 2.3.2.-) (RING-type E3 SUMO transferase UBC9) (SUMO-protein ligase) (Ubiquitin carrier protein 9) (Ubiquitin carrier protein I) (Ubiquitin-conjugating enzyme E2 I) (Ubiquitin-protein ligase I)
[NSMCE2 C8orf36 MMS21] E3 SUMO-protein ligase NSE2 (EC 2.3.2.-) (E3 SUMO-protein transferase NSE2) (MMS21 homolog) (hMMS21) (Non-structural maintenance of chromosomes element 2 homolog) (Non-SMC element 2 homolog)
[SUMO2 SMT3B SMT3H2] Small ubiquitin-related modifier 2 (SUMO-2) (HSMT3) (SMT3 homolog 2) (SUMO-3) (Sentrin-2) (Ubiquitin-like protein SMT3B) (Smt3B)
[Uhrf1 Np95] E3 ubiquitin-protein ligase UHRF1 (EC 2.3.2.27) (Nuclear protein 95) (Nuclear zinc finger protein Np95) (RING-type E3 ubiquitin transferase UHRF1) (Ubiquitin-like PHD and RING finger domain-containing protein 1) (mUhrf1) (Ubiquitin-like-containing PHD and RING finger domains protein 1)
[TRIM63 IRF MURF1 RNF28 SMRZ] E3 ubiquitin-protein ligase TRIM63 (EC 2.3.2.27) (Iris RING finger protein) (Muscle-specific RING finger protein 1) (MuRF-1) (MuRF1) (RING finger protein 28) (RING-type E3 ubiquitin transferase TRIM63) (Striated muscle RING zinc finger protein) (Tripartite motif-containing protein 63)
[RNF4 SNURF RES4-26] E3 ubiquitin-protein ligase RNF4 (EC 2.3.2.27) (RING finger protein 4) (RING-type E3 ubiquitin transferase RNF4) (Small nuclear ring finger protein) (Protein SNURF)
[TRIM24 RNF82 TIF1 TIF1A] Transcription intermediary factor 1-alpha (TIF1-alpha) (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRIM24) (RING finger protein 82) (RING-type E3 ubiquitin transferase TIF1-alpha) (Tripartite motif-containing protein 24)
[ube2ia ubc9a ube2i] SUMO-conjugating enzyme UBC9-A (EC 2.3.2.-) (RING-type E3 SUMO transferase UBC9-A) (SUMO-protein ligase A) (Ubiquitin carrier protein 9-A) (Ubiquitin carrier protein I-A) (Ubiquitin-conjugating enzyme E2 I-A) (Ubiquitin-protein ligase I-A)
[Rnf212] Probable E3 SUMO-protein ligase RNF212 (EC 2.3.2.-) (Probable E3 SUMO-protein transferase RNF212) (RING finger protein 212)
[RANBP2 NUP358] E3 SUMO-protein ligase RanBP2 (EC 2.3.2.-) (358 kDa nucleoporin) (Nuclear pore complex protein Nup358) (Nucleoporin Nup358) (Ran-binding protein 2) (RanBP2) (p270)
[Rnf2 DinG Ring1b] E3 ubiquitin-protein ligase RING2 (EC 2.3.2.27) (RING finger protein 1B) (RING1b) (RING finger protein 2) (RING-type E3 ubiquitin transferase RING2)
[Rnf4 Snurf] E3 ubiquitin-protein ligase RNF4 (EC 2.3.2.27) (RING finger protein 4) (RING-type E3 ubiquitin transferase RNF4) (Small nuclear ring finger protein) (Protein SNURF)

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