Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9EQE1 (SENP2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sentrin-specific protease 2

EC=3.4.22.-
Alternative name(s):
Axin-associating molecule
Short name=Axam
Sentrin/SUMO-specific protease SENP2
Gene names
Name:Senp2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length588 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO1, SUMO2 and SUMO3 to their mature forms and deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins. May down-regulate CTNNB1 levels and thereby modulate the Wnt pathway. Ref.2

Subunit structure

Binds to SUMO2 and SUMO3. Interacts with the C-terminal domain of NUP153 via its N-terminus By similarity. Binds to axin.

Subcellular location

Nucleusnuclear pore complex. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side By similarity. Cytoplasm. Cytoplasmic vesicle. Note: Cytoplasmic and in cytoplasmic vesicles, together with axin. May shuttle between the nucleus and the cytoplasm.

Tissue specificity

Ubiquitous. Highly expressed in brain, lung and testis.

Post-translational modification

Polyubiquitinated; which leads to proteasomal degradation By similarity.

Sequence similarities

Belongs to the peptidase C48 family.

Ontologies

Keywords
   Biological processProtein transport
Translocation
Transport
Ubl conjugation pathway
Wnt signaling pathway
mRNA transport
   Cellular componentCytoplasm
Cytoplasmic vesicle
Membrane
Nuclear pore complex
Nucleus
   Molecular functionHydrolase
Protease
Thiol protease
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processWnt receptor signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

dorsal/ventral axis specification

Inferred from direct assay Ref.1. Source: RGD

mRNA transport

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of protein binding

Inferred from direct assay Ref.1. Source: RGD

positive regulation of protein phosphorylation

Inferred from direct assay Ref.1. Source: RGD

protein desumoylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear pore

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functionSUMO-specific protease activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein domain specific binding

Inferred from physical interaction Ref.1. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 588588Sentrin-specific protease 2
PRO_0000101720

Regions

Region72 – 381310Axin-binding
Region394 – 558165Protease
Motif28 – 314Nuclear localization signal Potential
Motif47 – 526Nuclear localization signal Potential
Motif316 – 33116Nuclear export signal By similarity

Sites

Active site4771 By similarity
Active site4941 By similarity
Active site5471Nucleophile By similarity

Amino acid modifications

Modified residue2171Phosphotyrosine By similarity
Modified residue3321Phosphoserine By similarity

Experimental info

Mutagenesis5471C → S: Abolishes protease activity. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9EQE1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: BEC186367D8284C4

FASTA58867,252
        10         20         30         40         50         60 
MYRWLTKVLG TILRLCERPA PGARALLKRR RSSSSLFSTA VDTDEIPAKR PRLDCFIHQV 

        70         80         90        100        110        120 
KNSLYNAASL FGFPFQLTTK PMVSSACNGT RNVAPSGEVF SNSPSCELTT SGSCSSMLKL 

       130        140        150        160        170        180 
GNKSPNGISD YPKIRVTVAR DQPRRVLPSF GFTLKSEGYN RRPSGRRHSK SNPESSLPWK 

       190        200        210        220        230        240 
PQEQGVTEMI SEEGGKGARR PHCTVEEGVQ KDEREKYLKL LERLKEGAHG STFPPAVSHH 

       250        260        270        280        290        300 
SSQRTQMDTL KTKGWMEEQN HGVRTTHLVP KQYRVVETRG PLCSVRSEKR YSKGKADTEK 

       310        320        330        340        350        360 
VVGLRFEKDG TRGHQLEPDL SEEVSARLRL GSGSNGLLRR KISVLEAKEK NFPSKEKDRR 

       370        380        390        400        410        420 
TEDLFELTED MEKEISNALG HGPPDEILSS AFKLRITRGD IQTLKNYHWL NDEVINFYMN 

       430        440        450        460        470        480 
LLVERSKKQG YPALHALSTF FYPKLKSGGY QAVKRWTKGV NLFDQELVLV PIHRKVHWSL 

       490        500        510        520        530        540 
VVMDLRKKCL KYLDSMGQKG HRICEILLQY LQDESKTKRN TDLNLLEWTH YSMKPHEIPQ 

       550        560        570        580 
QLNGSDCGMF TCKYADYISR DKPITFTQHQ MPLFRKKMVW EILHQQLL 

« Hide

References

[1]"Inhibition of Wnt signaling pathway by a novel Axin-binding protein."
Kadoya T., Kishida S., Fukui A., Hinoi T., Michiue T., Asashima M., Kikuchi A.
J. Biol. Chem. 275:37030-37037(2000) [PubMed: 10944533] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Desumoylation activity of Axam, a novel Axin-binding protein, is involved in downregulation of beta-catenin."
Kadoya T., Yamamoto H., Suzuki T., Yukita A., Fukui A., Michiue T., Asahara T., Tanaka K., Asashima M., Kikuchi A.
Mol. Cell. Biol. 22:3803-3819(2002) [PubMed: 11997515] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-547.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF260129 mRNA. Translation: AAG34653.1.
IPIIPI00189898.
RefSeqNP_076479.1. NM_023989.1.
UniGeneRn.9367.

3D structure databases

ProteinModelPortalQ9EQE1.
SMRQ9EQE1. Positions 363-588.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9EQE1.

Protein family/group databases

MEROPSC48.007.

PTM databases

PhosphoSiteQ9EQE1.

Proteomic databases

PRIDEQ9EQE1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000002425; ENSRNOP00000002425; ENSRNOG00000001773.
GeneID78973.
KEGGrno:78973.
UCSCNM_023989. rat.

Organism-specific databases

CTD59343.
RGD708378. Senp2.

Phylogenomic databases

eggNOGroNOG06700.
GeneTreeENSGT00530000062941.
HOVERGENHBG054228.
InParanoidQ9EQE1.
OMAQYRVVET.
OrthoDBEOG4MSCXT.

Gene expression databases

ArrayExpressQ9EQE1.
GenevestigatorQ9EQE1.
GermOnlineENSRNOG00000001773. Rattus norvegicus.

Family and domain databases

InterProIPR003653. Peptidase_C48.
[Graphical view]
KOK03345.
PfamPF02902. Peptidase_C48. 1 hit.
[Graphical view]
PROSITEPS50600. ULP_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio614440.

Entry information

Entry nameSENP2_RAT
AccessionPrimary (citable) accession number: Q9EQE1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: March 1, 2001
Last modified: November 16, 2011
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families