Sentrin-specific protease 3 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot Q9H4L4 (SENP3_HUMAN)

Last modified May 5, 2009. Version 61. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Sentrin-specific protease 3
    EC=3.4.22.-
Alternative name(s):
    Sentrin/SUMO-specific protease SENP3
    SUMO-1-specific protease 3

Gene names

Name:	SENP3
Synonyms:	SSP3, SUSP3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	574 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

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. Ref.6 Ref.9
Subunit structure	Binds to UBL1 and SMT3H1 By similarity.
Subcellular location	Nucleus › nucleolus By similarity.
Sequence similarities	Belongs to the peptidase C48 family.

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Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleolus Inferred from direct assay. Source: LIFEdb
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 574

574

Sentrin-specific protease 3

PRO_0000101721

Regions

Region

386 – 543

158

Protease

Motif

125 – 128

Nuclear localization signal Potential

Motif

153 – 159

Nuclear localization signal Potential

Compositional bias

13 – 68

Pro-rich

Compositional bias

76 – 92

Glu-rich

Compositional bias

192 – 195

Poly-Pro

Sites

Active site

465

By similarity

Active site

482

By similarity

Active site

532

By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.11

Modified residue

Phosphoserine Ref.11

Modified residue

169

Phosphoserine Ref.11 Ref.7 Ref.10 Ref.12

Modified residue

176

Phosphothreonine Ref.12

Modified residue

181

Phosphoserine Ref.11 Ref.10 Ref.12

Modified residue

188

Phosphoserine Ref.12

Modified residue

212

Phosphoserine Ref.11 Ref.12

Modified residue

232

Phosphoserine Ref.11 Ref.7

Modified residue

307

Phosphoserine Ref.11

Modified residue

353

Phosphothreonine Ref.8

Natural variations

Natural variant

515

W → R: dbSNP rs9972914.

VAR_051544

Experimental info

Sequence conflict

30 – 31

ER → DG in AAG33252. Ref.1

Sequence conflict

A → T in AAG33252. Ref.1

Sequence conflict

V → A in AAG33252. Ref.1

Sequence conflict

113 – 114

PS → AL in AAG33252. Ref.1

Sequence conflict

117

T → S in AAG33252. Ref.1

Sequence conflict

134

R → Q in AAG33252. Ref.1

Sequence conflict

161

L → S in AAH48306. Ref.4

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9H4L4-1 [UniParc].

Last modified December 12, 2006. Version 2.
Checksum: E495137EE7500741
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FASTA

574

65,010

        10         20         30         40         50         60 
MKETIQGTGS WGPEPPGPGI PPAYSSPRRE RLRWPPPPKP RLKSGGGFGP DPGSGTTVPA 

        70         80         90        100        110        120 
RRLPVPRPSF DASASEEEEE EEEEEDEDEE EEVAAWRLPP RWSQLGTSQR PRPSRPTHRK 

       130        140        150        160        170        180 
TCSQRRRRAM RAFRMLLYSK STSLTFHWKL WGRHRGRRRG LAHPKNHLSP QQGGATPQVP 

       190        200        210        220        230        240 
SPCCRFDSPR GPPPPRLGLL GALMAEDGVR GSPPVPSGPP MEEDGLRWTP KSPLDPDSGL 

       250        260        270        280        290        300 
LSCTLPNGFG GQSGPEGERS LAPPDASILI SNVCSIGDHV AQELFQGSDL GMAEEAERPG 

       310        320        330        340        350        360 
EKAGQHSPLR EEHVTCVQSI LDEFLQTYGS LIPLSTDEVV EKLEDIFQQE FSTPSRKGLV 

       370        380        390        400        410        420 
LQLIQSYQRM PGNAMVRGFR VAYKRHVLTM DDLGTLYGQN WLNDQVMNMY GDLVMDTVPE 

       430        440        450        460        470        480 
KVHFFNSFFY DKLRTKGYDG VKRWTKNVDI FNKELLLIPI HLEVHWSLIS VDVRRRTITY 

       490        500        510        520        530        540 
FDSQRTLNRR CPKHIAKYLQ AEAVKKDRLD FHQGWKGYFK MNVARQNNDS DCGAFVLQYC 

       550        560        570 
KHLALSQPFS FTQQDMPKLR RQIYKELCHC KLTV

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Ubiquitin-like proteins: new wines in new bottles." Yeh E.T.H., Gong L., Kamitani T. Gene 248:1-14(2000) [PubMed: 10806345] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	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 Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." 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. Poustka A. Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Melanoma and Uterus.
[4]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lymph and Uterus.
[6]	"Association with class IIa histone deacetylases upregulates the sumoylation of MEF2 transcription factors." Gregoire S., Yang X.-J. Mol. Cell. Biol. 25:2273-2287(2005) [PubMed: 15743823] [Abstract] Cited for: FUNCTION.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169 AND SER-232, MASS SPECTROMETRY. Tissue: Epithelium.
[8]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-353, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	"Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3." Gong L., Yeh E.T.H. J. Biol. Chem. 281:15869-15877(2006) [PubMed: 16608850] [Abstract] Cited for: FUNCTION.
[10]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169 AND SER-181, MASS SPECTROMETRY.
[11]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-75; SER-169; SER-181; SER-212; SER-232 AND SER-307, MASS SPECTROMETRY.
[12]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; THR-176; SER-181; SER-188 AND SER-212, MASS SPECTROMETRY.
[13]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	AY008763 mRNA. Translation: AAG33252.1. AF199459 mRNA. Translation: AAL25652.1. AL050283 mRNA. Translation: CAB43384.2. AL834294 mRNA. Translation: CAD38967.1. BC048306 mRNA. Translation: AAH48306.1. BC080658 mRNA. Translation: AAH80658.1.
IPI	IPI00171525.
PIR	T08759.
RefSeq	NP_056485.2.
UniGene	Hs.513926
3D structure databases
HSSP	HSSP built from PDB template 1EUV based on UniProtKB Q02724.
ModBase	Search...
Protein family/group databases
MEROPS	C48.003.
PTM databases
PhosphoSite	Q9H4L4.
Proteomic databases
PRIDE	Q9H4L4.
Genome annotation databases
Ensembl	ENSG00000161956. Homo sapiens. [Contig view]
GeneID	26168.
KEGG	hsa:26168.
Organism-specific databases
GeneCards	GC17P007406.
H-InvDB	HIX0013501.
HGNC	HGNC:17862. SENP3.
PharmGKB	PA134933213.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q9H4L4.
HOVERGEN	Q9H4L4.
Gene expression databases
ArrayExpress	Q9H4L4.
Bgee	Q9H4L4.
CleanEx	HS_SENP3.
GermOnline	ENSG00000161956. Homo sapiens.
Family and domain databases
InterPro	IPR003653. Peptidase_C48. [Graphical view]
Pfam	PF02902. Peptidase_C48. 1 hit. [Graphical view]
PROSITE	PS50600. ULP_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	48279.

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Entry information

Entry name

SENP3_HUMAN

Accession

Primary (citable) accession number: Q9H4L4
Secondary accession number(s): Q66K15

Q9Y3W9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2002
Last sequence update:	December 12, 2006
Last modified:	May 5, 2009
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents