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Reviewed, UniProtKB/Swiss-Prot Q9H4L4 (SENP3_HUMAN)

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

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length574 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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

Nucleusnucleolus By similarity.

Sequence similarities

Belongs to the peptidase C48 family.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   Molecular functionHydrolase
Protease
Thiol protease
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processmodification-dependent protein catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnucleolus

Inferred from direct assay. Source: LIFEdb

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 574574Sentrin-specific protease 3
PRO_0000101721

Regions

Region386 – 543158Protease
Motif125 – 1284Nuclear localization signal Potential
Motif153 – 1597Nuclear localization signal Potential
Compositional bias13 – 6856Pro-rich
Compositional bias76 – 9217Glu-rich
Compositional bias192 – 1954Poly-Pro

Sites

Active site4651 By similarity
Active site4821 By similarity
Active site5321 By similarity

Amino acid modifications

Modified residue731Phosphoserine Ref.11
Modified residue751Phosphoserine Ref.11
Modified residue1691Phosphoserine Ref.11 Ref.7 Ref.10 Ref.12
Modified residue1761Phosphothreonine Ref.12
Modified residue1811Phosphoserine Ref.11 Ref.10 Ref.12
Modified residue1881Phosphoserine Ref.12
Modified residue2121Phosphoserine Ref.11 Ref.12
Modified residue2321Phosphoserine Ref.11 Ref.7
Modified residue3071Phosphoserine Ref.11
Modified residue3531Phosphothreonine Ref.8

Natural variations

Natural variant5151W → R: dbSNP rs9972914.
VAR_051544

Experimental info

Sequence conflict30 – 312ER → DG in AAG33252. Ref.1
Sequence conflict601A → T in AAG33252. Ref.1
Sequence conflict651V → A in AAG33252. Ref.1
Sequence conflict113 – 1142PS → AL in AAG33252. Ref.1
Sequence conflict1171T → S in AAG33252. Ref.1
Sequence conflict1341R → Q in AAG33252. Ref.1
Sequence conflict1611L → S in AAH48306. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9H4L4-1 [UniParc].

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

FASTA57465,010
        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 

« Hide

References

« Hide '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. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., 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.

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.
IPIIPI00171525.
PIRT08759.
RefSeqNP_056485.2.
UniGeneHs.513926

3D structure databases

HSSPHSSP built from PDB template 1EUV based on UniProtKB Q02724.
ModBaseSearch...

Protein family/group databases

MEROPSC48.003.

PTM databases

PhosphoSiteQ9H4L4.

Proteomic databases

PRIDEQ9H4L4.

Genome annotation databases

EnsemblENSG00000161956. Homo sapiens. [Contig view]
GeneID26168.
KEGGhsa:26168.

Organism-specific databases

GeneCardsGC17P007406.
H-InvDBHIX0013501.
HGNCHGNC:17862. SENP3.
PharmGKBPA134933213.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ9H4L4.
HOVERGENQ9H4L4.

Gene expression databases

ArrayExpressQ9H4L4.
BgeeQ9H4L4.
CleanExHS_SENP3.
GermOnlineENSG00000161956. Homo sapiens.

Family and domain databases

InterProIPR003653. Peptidase_C48.
[Graphical view]
PfamPF02902. Peptidase_C48. 1 hit.
[Graphical view]
PROSITEPS50600. ULP_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio48279.

Entry information

Entry nameSENP3_HUMAN
AccessionPrimary (citable) accession number: Q9H4L4
Secondary accession number(s): Q66K15 expand/collapse secondary AC list , Q86VS7, Q96PS4, 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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

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) · Sequences · References · Cross-references · Entry information · Relevant documents