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Protein

Sentrin-specific protease 2

Gene

Senp2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Deconjugates SUMO2 from MTA1. Plays a dynamic role in adipogenesis by desumoylating and promoting the stabilization of CEBPB (By similarity).By similarity1 Publication

Catalytic activityi

Hydrolysis of the alpha-linked peptide bond in the sequence Gly-Gly-|-Ala-Thr-Tyr at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptide, Smt3, leading to the mature form of the protein. A second reaction involves the cleavage of an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei477 – 4771By similarity
Active sitei494 – 4941By similarity
Active sitei547 – 5471NucleophileBy similarity

GO - Molecular functioni

  • protein domain specific binding Source: RGD
  • SUMO-specific protease activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport, Ubl conjugation pathway, Wnt signaling pathway

Enzyme and pathway databases

ReactomeiR-RNO-3065679. SUMO is proteolytically processed.

Protein family/group databases

MEROPSiC48.007.

Names & Taxonomyi

Protein namesi
Recommended name:
Sentrin-specific protease 2 (EC:3.4.22.68)
Alternative name(s):
Axin-associating molecule
Short name:
Axam
Sentrin/SUMO-specific protease SENP2
Gene namesi
Name:Senp2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 11

Organism-specific databases

RGDi708378. Senp2.

Subcellular locationi

  • Nucleusnuclear pore complex By similarity
  • Nucleus membrane By similarity; Peripheral membrane protein By similarity; Nucleoplasmic side By similarity
  • Cytoplasm By similarity

  • Note: Shuttles between cytoplasm and nucleus.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nuclear pore complex, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi547 – 5471C → S: Abolishes protease activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 588588Sentrin-specific protease 2PRO_0000101720Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei343 – 3431PhosphoserineBy similarity

Post-translational modificationi

Polyubiquitinated; which leads to proteasomal degradation.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9EQE1.
PRIDEiQ9EQE1.

PTM databases

iPTMnetiQ9EQE1.
PhosphoSiteiQ9EQE1.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in brain, lung and testis.

Gene expression databases

ExpressionAtlasiQ9EQE1. baseline.
GenevisibleiQ9EQE1. RN.

Interactioni

Subunit structurei

Binds to SUMO2 and SUMO3. Interacts with the C-terminal domain of NUP153 via its N-terminus. Interacts with MTA1 (By similarity). Binds to axin.By similarity

GO - Molecular functioni

  • protein domain specific binding Source: RGD

Protein-protein interaction databases

BioGridi249380. 2 interactions.
STRINGi10116.ENSRNOP00000002425.

Structurei

3D structure databases

ProteinModelPortaliQ9EQE1.
SMRiQ9EQE1. Positions 363-588.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni72 – 381310Axin-bindingAdd
BLAST
Regioni394 – 558165ProteaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi28 – 314Nuclear localization signalSequence analysis
Motifi47 – 526Nuclear localization signalSequence analysis
Motifi316 – 33116Nuclear export signalBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C48 family.Curated

Phylogenomic databases

eggNOGiKOG0778. Eukaryota.
COG5160. LUCA.
GeneTreeiENSGT00530000062941.
HOGENOMiHOG000070234.
HOVERGENiHBG054228.
InParanoidiQ9EQE1.
KOiK03345.
OMAiRRGYQLE.
OrthoDBiEOG7D59MP.
PhylomeDBiQ9EQE1.
TreeFamiTF316289.

Family and domain databases

InterProiIPR003653. Peptidase_C48_C.
[Graphical view]
PfamiPF02902. Peptidase_C48. 1 hit.
[Graphical view]
PROSITEiPS50600. ULP_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9EQE1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYRWLTKVLG TILRLCERPA PGARALLKRR RSSSSLFSTA VDTDEIPAKR
60 70 80 90 100
PRLDCFIHQV KNSLYNAASL FGFPFQLTTK PMVSSACNGT RNVAPSGEVF
110 120 130 140 150
SNSPSCELTT SGSCSSMLKL GNKSPNGISD YPKIRVTVAR DQPRRVLPSF
160 170 180 190 200
GFTLKSEGYN RRPSGRRHSK SNPESSLPWK PQEQGVTEMI SEEGGKGARR
210 220 230 240 250
PHCTVEEGVQ KDEREKYLKL LERLKEGAHG STFPPAVSHH SSQRTQMDTL
260 270 280 290 300
KTKGWMEEQN HGVRTTHLVP KQYRVVETRG PLCSVRSEKR YSKGKADTEK
310 320 330 340 350
VVGLRFEKDG TRGHQLEPDL SEEVSARLRL GSGSNGLLRR KISVLEAKEK
360 370 380 390 400
NFPSKEKDRR TEDLFELTED MEKEISNALG HGPPDEILSS AFKLRITRGD
410 420 430 440 450
IQTLKNYHWL NDEVINFYMN LLVERSKKQG YPALHALSTF FYPKLKSGGY
460 470 480 490 500
QAVKRWTKGV NLFDQELVLV PIHRKVHWSL VVMDLRKKCL KYLDSMGQKG
510 520 530 540 550
HRICEILLQY LQDESKTKRN TDLNLLEWTH YSMKPHEIPQ QLNGSDCGMF
560 570 580
TCKYADYISR DKPITFTQHQ MPLFRKKMVW EILHQQLL
Length:588
Mass (Da):67,252
Last modified:March 1, 2001 - v1
Checksum:iBEC186367D8284C4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF260129 mRNA. Translation: AAG34653.1.
RefSeqiNP_076479.1. NM_023989.1.
UniGeneiRn.9367.

Genome annotation databases

EnsembliENSRNOT00000002425; ENSRNOP00000002425; ENSRNOG00000001773.
GeneIDi78973.
KEGGirno:78973.
UCSCiRGD:708378. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF260129 mRNA. Translation: AAG34653.1.
RefSeqiNP_076479.1. NM_023989.1.
UniGeneiRn.9367.

3D structure databases

ProteinModelPortaliQ9EQE1.
SMRiQ9EQE1. Positions 363-588.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249380. 2 interactions.
STRINGi10116.ENSRNOP00000002425.

Protein family/group databases

MEROPSiC48.007.

PTM databases

iPTMnetiQ9EQE1.
PhosphoSiteiQ9EQE1.

Proteomic databases

PaxDbiQ9EQE1.
PRIDEiQ9EQE1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000002425; ENSRNOP00000002425; ENSRNOG00000001773.
GeneIDi78973.
KEGGirno:78973.
UCSCiRGD:708378. rat.

Organism-specific databases

CTDi59343.
RGDi708378. Senp2.

Phylogenomic databases

eggNOGiKOG0778. Eukaryota.
COG5160. LUCA.
GeneTreeiENSGT00530000062941.
HOGENOMiHOG000070234.
HOVERGENiHBG054228.
InParanoidiQ9EQE1.
KOiK03345.
OMAiRRGYQLE.
OrthoDBiEOG7D59MP.
PhylomeDBiQ9EQE1.
TreeFamiTF316289.

Enzyme and pathway databases

ReactomeiR-RNO-3065679. SUMO is proteolytically processed.

Miscellaneous databases

PROiQ9EQE1.

Gene expression databases

ExpressionAtlasiQ9EQE1. baseline.
GenevisibleiQ9EQE1. RN.

Family and domain databases

InterProiIPR003653. Peptidase_C48_C.
[Graphical view]
PfamiPF02902. Peptidase_C48. 1 hit.
[Graphical view]
PROSITEiPS50600. ULP_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-547.

Entry informationi

Entry nameiSENP2_RAT
AccessioniPrimary (citable) accession number: Q9EQE1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: March 1, 2001
Last modified: June 8, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.