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Sentrin-specific protease 3 (EC 3.4.22.68) (SUMO-1-specific protease 3) (Sentrin/SUMO-specific protease SENP3)

 SENP3_HUMAN             Reviewed;         574 AA.
Q9H4L4; Q66K15; Q86VS7; Q96PS4; Q9Y3W9;
28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
12-DEC-2006, sequence version 2.
25-OCT-2017, entry version 144.
RecName: Full=Sentrin-specific protease 3;
EC=3.4.22.-;
AltName: Full=SUMO-1-specific protease 3;
AltName: Full=Sentrin/SUMO-specific protease SENP3;
Name=SENP3; Synonyms=SSP3, SUSP3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10806345; DOI=10.1016/S0378-1119(00)00139-6;
Yeh E.T.H., Gong L., Kamitani T.;
"Ubiquitin-like proteins: new wines in new bottles.";
Gene 248:1-14(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Choi S.J., Jeon Y.-J., Kim K.I., Nishimori S., Suzuki T., Uchida S.,
Shimbara N., Tanaka K., Chung C.H.;
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Melanoma, and Uterus;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lymph, and Uterus;
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]
IDENTIFICATION IN THE MLL1/MLL COMPLEX.
PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
"Physical association and coordinate function of the H3 K4
methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
Cell 121:873-885(2005).
[7]
FUNCTION.
PubMed=15743823; DOI=10.1128/MCB.25.6.2273-2287.2005;
Gregoire S., Yang X.-J.;
"Association with class IIa histone deacetylases upregulates the
sumoylation of MEF2 transcription factors.";
Mol. Cell. Biol. 25:2273-2287(2005).
[8]
FUNCTION.
PubMed=16608850; DOI=10.1074/jbc.M511658200;
Gong L., Yeh E.T.H.;
"Characterization of a family of nucleolar SUMO-specific proteases
with preference for SUMO-2 or SUMO-3.";
J. Biol. Chem. 281:15869-15877(2006).
[9]
FUNCTION, MUTAGENESIS OF CYS-532, AND INTERACTION WITH NPM1.
PubMed=18259216; DOI=10.1038/embor.2008.3;
Haindl M., Harasim T., Eick D., Muller S.;
"The nucleolar SUMO-specific protease SENP3 reverses SUMO modification
of nucleophosmin and is required for rRNA processing.";
EMBO Rep. 9:273-279(2008).
[10]
SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH NPM1.
PubMed=19015314; DOI=10.1083/jcb.200807185;
Yun C., Wang Y., Mukhopadhyay D., Backlund P., Kolli N., Yergey A.,
Wilkinson K.D., Dasso M.;
"Nucleolar protein B23/nucleophosmin regulates the vertebrate SUMO
pathway through SENP3 and SENP5 proteases.";
J. Cell Biol. 183:589-595(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[12]
ENZYME REGULATION, SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION
WITH EP300.
PubMed=19680224; DOI=10.1038/emboj.2009.210;
Huang C., Han Y., Wang Y., Sun X., Yan S., Yeh E.T.H., Chen Y.,
Cang H., Li H., Shi G., Cheng J., Tang X., Yi J.;
"SENP3 is responsible for HIF-1 transactivation under mild oxidative
stress via p300 de-SUMOylation.";
EMBO J. 28:2748-2762(2009).
[13]
FUNCTION, AND INTERACTION WITH CDCA8.
PubMed=18946085; DOI=10.1091/mbc.E08-05-0511;
Klein U.R., Haindl M., Nigg E.A., Muller S.;
"RanBP2 and SENP3 function in a mitotic SUMO2/3 conjugation-
deconjugation cycle on Borealin.";
Mol. Biol. Cell 20:410-418(2009).
[14]
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).
[15]
FUNCTION, AND IDENTIFICATION IN THE 5FMC COMPLEX.
PubMed=22872859; DOI=10.1074/mcp.M112.017194;
Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J.,
Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S.,
van Dijk T.B.;
"Five friends of methylated chromatin target of protein-arginine-
methyltransferase[prmt]-1 (chtop), a complex linking arginine
methylation to desumoylation.";
Mol. Cell. Proteomics 11:1263-1273(2012).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[17]
INTERACTION WITH CCAR2.
PubMed=25406032; DOI=10.1038/ncomms6483;
Park J.H., Lee S.W., Yang S.W., Yoo H.M., Park J.M., Seong M.W.,
Ka S.H., Oh K.H., Jeon Y.J., Chung C.H.;
"Modification of DBC1 by SUMO2/3 is crucial for p53-mediated apoptosis
in response to DNA damage.";
Nat. Commun. 5:5483-5483(2014).
-!- FUNCTION: Protease that releases SUMO2 and SUMO3 monomers from
sumoylated substrates, but has only weak activity against SUMO1
conjugates. Deconjugates SUMO2 from MEF2D, which increases its
transcriptional activation capability. Deconjugates SUMO2 and
SUMO3 from CDCA8. Redox sensor that, when redistributed into
nucleoplasm, can act as an effector to enhance HIF1A
transcriptional activity by desumoylating EP300. Required for rRNA
processing through deconjugation of SUMO2 and SUMO3 from
nucleophosmin, NPM1. Plays a role in the regulation of sumoylation
status of ZNF148. Functions as a component of the Five Friends of
Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to
ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and
subsequent transactivation of ZNF148 target genes.
{ECO:0000269|PubMed:15743823, ECO:0000269|PubMed:16608850,
ECO:0000269|PubMed:18259216, ECO:0000269|PubMed:18946085,
ECO:0000269|PubMed:19015314, ECO:0000269|PubMed:19680224,
ECO:0000269|PubMed:22872859}.
-!- ENZYME REGULATION: On oxidative stress, SENP3 degradation is
blocked by inhibition of its ubiquitination, which stabilizes it
as it accumulates in the nucleoplasm.
{ECO:0000269|PubMed:19680224}.
-!- SUBUNIT: Binds to SUMO1 and SUMO3 (By similarity). Component of
some MLL1/MLL complex, at least composed of the core components
KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the
facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1,
LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2,
RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9
and TEX10. Interacts with EP300, NPM1 and CDCA8. Component of the
5FMC complex, at least composed of PELP1, LAS1L, TEX10, WDR18 and
SENP3; the complex interacts with methylated CHTOP and ZNF148.
Interacts with NOL9. Interacts with CCAR2.
{ECO:0000250|UniProtKB:Q9EP97, ECO:0000269|PubMed:15960975,
ECO:0000269|PubMed:18259216, ECO:0000269|PubMed:18946085,
ECO:0000269|PubMed:19015314, ECO:0000269|PubMed:19680224,
ECO:0000269|PubMed:22872859, ECO:0000269|PubMed:25406032}.
-!- INTERACTION:
P06748:NPM1; NbExp=6; IntAct=EBI-2880236, EBI-78579;
Q8IZL8:PELP1; NbExp=5; IntAct=EBI-2880236, EBI-716449;
Q9NXF1:TEX10; NbExp=2; IntAct=EBI-2880236, EBI-2371062;
P0CG48:UBC; NbExp=2; IntAct=EBI-2880236, EBI-3390054;
Q9BV38:WDR18; NbExp=3; IntAct=EBI-2880236, EBI-727429;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:19680224}. Nucleus, nucleoplasm
{ECO:0000269|PubMed:19015314, ECO:0000269|PubMed:19680224}.
Cytoplasm {ECO:0000250|UniProtKB:Q9EP97}. Note=Redistributes
between the nucleolus and the nucleoplasm in response to mild
oxidative stress (PubMed:19680224). Mainly found in the
nucleoplasm, with low levels detected in the cytoplasmic and
chromatin fractions (By similarity).
{ECO:0000250|UniProtKB:Q9EP97, ECO:0000269|PubMed:19680224}.
-!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
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EMBL; AY008763; AAG33252.1; -; mRNA.
EMBL; AF199459; AAL25652.1; -; mRNA.
EMBL; AL050283; CAB43384.2; -; mRNA.
EMBL; AL834294; CAD38967.1; -; mRNA.
EMBL; BC048306; AAH48306.1; -; mRNA.
EMBL; BC080658; AAH80658.1; -; mRNA.
CCDS; CCDS73958.1; -.
PIR; T08759; T08759.
RefSeq; NP_056485.2; NM_015670.5.
UniGene; Hs.513926; -.
UniGene; Hs.733104; -.
ProteinModelPortal; Q9H4L4; -.
SMR; Q9H4L4; -.
BioGrid; 117594; 119.
CORUM; Q9H4L4; -.
DIP; DIP-47511N; -.
IntAct; Q9H4L4; 32.
MINT; MINT-1200849; -.
STRING; 9606.ENSP00000403712; -.
MEROPS; C48.003; -.
iPTMnet; Q9H4L4; -.
PhosphoSitePlus; Q9H4L4; -.
BioMuta; SENP3; -.
DMDM; 119370525; -.
EPD; Q9H4L4; -.
MaxQB; Q9H4L4; -.
PaxDb; Q9H4L4; -.
PeptideAtlas; Q9H4L4; -.
PRIDE; Q9H4L4; -.
DNASU; 26168; -.
Ensembl; ENST00000321337; ENSP00000314029; ENSG00000161956.
Ensembl; ENST00000429205; ENSP00000403712; ENSG00000161956.
GeneID; 26168; -.
KEGG; hsa:26168; -.
UCSC; uc032esp.2; human.
CTD; 26168; -.
DisGeNET; 26168; -.
EuPathDB; HostDB:ENSG00000161956.12; -.
GeneCards; SENP3; -.
H-InvDB; HIX0013501; -.
HGNC; HGNC:17862; SENP3.
HPA; HPA060290; -.
MIM; 612844; gene.
neXtProt; NX_Q9H4L4; -.
OpenTargets; ENSG00000161956; -.
PharmGKB; PA134933213; -.
eggNOG; KOG0778; Eukaryota.
eggNOG; COG5160; LUCA.
GeneTree; ENSGT00530000062941; -.
HOGENOM; HOG000154287; -.
HOVERGEN; HBG059450; -.
InParanoid; Q9H4L4; -.
KO; K08593; -.
OrthoDB; EOG091G092N; -.
PhylomeDB; Q9H4L4; -.
TreeFam; TF316289; -.
BRENDA; 3.4.22.B72; 2681.
Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
ChiTaRS; SENP3; human.
GeneWiki; SENP3; -.
GenomeRNAi; 26168; -.
PRO; PR:Q9H4L4; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000161956; -.
CleanEx; HS_SENP3; -.
ExpressionAtlas; Q9H4L4; baseline and differential.
Genevisible; Q9H4L4; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:LIFEdb.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
GO; GO:0016926; P:protein desumoylation; IBA:GO_Central.
GO; GO:0006364; P:rRNA processing; TAS:Reactome.
InterPro; IPR003653; Peptidase_C48_C.
Pfam; PF02902; Peptidase_C48; 1.
PROSITE; PS50600; ULP_PROTEASE; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Hydrolase; Nucleus; Phosphoprotein;
Polymorphism; Protease; Reference proteome; Thiol protease;
Ubl conjugation pathway.
CHAIN 1 574 Sentrin-specific protease 3.
/FTId=PRO_0000101721.
REGION 386 543 Protease.
MOTIF 125 128 Nuclear localization signal.
{ECO:0000255}.
MOTIF 153 159 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 13 68 Pro-rich.
COMPBIAS 76 92 Glu-rich.
COMPBIAS 192 195 Poly-Pro.
ACT_SITE 465 465 {ECO:0000250}.
ACT_SITE 482 482 {ECO:0000250}.
ACT_SITE 532 532 {ECO:0000250}.
MOD_RES 54 54 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 73 73 Phosphoserine.
{ECO:0000250|UniProtKB:Q9EP97}.
MOD_RES 75 75 Phosphoserine.
{ECO:0000250|UniProtKB:Q9EP97}.
MOD_RES 169 169 Phosphoserine.
{ECO:0000250|UniProtKB:Q9EP97}.
MOD_RES 176 176 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9EP97}.
MOD_RES 181 181 Phosphoserine.
{ECO:0000250|UniProtKB:Q9EP97}.
MOD_RES 188 188 Phosphoserine.
{ECO:0000250|UniProtKB:Q9EP97}.
MOD_RES 212 212 Phosphoserine.
{ECO:0000250|UniProtKB:Q9EP97}.
MOD_RES 232 232 Phosphoserine.
{ECO:0000250|UniProtKB:Q9EP97}.
VARIANT 515 515 W -> R (in dbSNP:rs9972914).
/FTId=VAR_051544.
MUTAGEN 532 532 C->S: Loss of enzymatic activity.
{ECO:0000269|PubMed:18259216}.
CONFLICT 30 31 ER -> DG (in Ref. 1; AAG33252).
{ECO:0000305}.
CONFLICT 60 60 A -> T (in Ref. 1; AAG33252).
{ECO:0000305}.
CONFLICT 65 65 V -> A (in Ref. 1; AAG33252).
{ECO:0000305}.
CONFLICT 113 114 PS -> AL (in Ref. 1; AAG33252).
{ECO:0000305}.
CONFLICT 117 117 T -> S (in Ref. 1; AAG33252).
{ECO:0000305}.
CONFLICT 134 134 R -> Q (in Ref. 1; AAG33252).
{ECO:0000305}.
CONFLICT 161 161 L -> S (in Ref. 5; AAH48306).
{ECO:0000305}.
SEQUENCE 574 AA; 65010 MW; E495137EE7500741 CRC64;
MKETIQGTGS WGPEPPGPGI PPAYSSPRRE RLRWPPPPKP RLKSGGGFGP DPGSGTTVPA
RRLPVPRPSF DASASEEEEE EEEEEDEDEE EEVAAWRLPP RWSQLGTSQR PRPSRPTHRK
TCSQRRRRAM RAFRMLLYSK STSLTFHWKL WGRHRGRRRG LAHPKNHLSP QQGGATPQVP
SPCCRFDSPR GPPPPRLGLL GALMAEDGVR GSPPVPSGPP MEEDGLRWTP KSPLDPDSGL
LSCTLPNGFG GQSGPEGERS LAPPDASILI SNVCSIGDHV AQELFQGSDL GMAEEAERPG
EKAGQHSPLR EEHVTCVQSI LDEFLQTYGS LIPLSTDEVV EKLEDIFQQE FSTPSRKGLV
LQLIQSYQRM PGNAMVRGFR VAYKRHVLTM DDLGTLYGQN WLNDQVMNMY GDLVMDTVPE
KVHFFNSFFY DKLRTKGYDG VKRWTKNVDI FNKELLLIPI HLEVHWSLIS VDVRRRTITY
FDSQRTLNRR CPKHIAKYLQ AEAVKKDRLD FHQGWKGYFK MNVARQNNDS DCGAFVLQYC
KHLALSQPFS FTQQDMPKLR RQIYKELCHC KLTV


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