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Reviewed, UniProtKB/Swiss-Prot Q91ZX6 (SENP2_MOUSE)

Last modified February 9, 2010. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Sentrin-specific protease 2
    EC=3.4.22.-
Alternative name(s):
    Sentrin/SUMO-specific protease SENP2
    SUMO-1/Smt3-specific isopeptidase 2
      Short name=Smt3ip2
    Axam2
    SUMO-1 protease 1
      Short name=SuPr-1
Gene names
Name: Senp2
Synonyms: Smt3ip2, Supr1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

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 By similarity. Isoform 3 activates transcription. Ref.1 Ref.2

Subunit structure

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

Subcellular location

Nucleus Ref.2.

Isoform 1: Nucleusnuclear pore complex. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side By similarity Ref.2.

Isoform 2: Cytoplasm. Cytoplasmic vesicle. Note: Found in the cytoplasm and in cytoplasmic vesicles, together with axin. Ref.2

Isoform 3: Nucleus. Note: Found in the PML nuclear bodies. Ref.2

Tissue specificity

Highly expressed in testis. Detected in brain, heart and thymus. Ref.2

Domain

The N-terminus is necessary and sufficient for nuclear envelope targeting By similarity.

Post-translational modification

Polyubiquitinated; which leads to proteasomal degradation By similarity.

Sequence similarities

Belongs to the peptidase C48 family.

Ontologies

Keywords
   Biological processProtein transport
Transcription
Transcription regulation
Translocation
Transport
Ubl conjugation pathway
Wnt signaling pathway
mRNA transport
   Cellular componentCytoplasm
Cytoplasmic vesicle
Membrane
Nuclear pore complex
Nucleus
   Coding sequence diversityAlternative splicing
   Molecular functionActivator
Hydrolase
Protease
Thiol protease
   PTMPhosphoprotein
Ubl conjugation
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processWnt receptor signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA transport

Inferred from electronic annotation. Source: UniProtKB-KW

modification-dependent protein catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

protein desumoylation

Inferred from direct assay. Source: MGI

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription

Inferred from electronic annotation. Source: UniProtKB-KW

transcription

Inferred from electronic annotation. Source: UniProtKB-KW

transmembrane transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

extrinsic to 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 binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q91ZX6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q91ZX6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: MYRWLAKVLGTILRLCERPAPGARALLKRRRSSSTLFSTAVDTDEIPAKRPRL → MEQNSK
Note: Found in the cytoplasm and in cytoplasmic vesicles, together with axin. Ref.2 No experimental confirmation available.
Isoform 3 (identifier: Q91ZX6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: Missing.
Note: Found in the PML nuclear bodies. Ref.2

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 588588Sentrin-specific protease 2
PRO_0000101719

Regions

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

Amino acid modifications

Modified residue2171Phosphotyrosine By similarity
Modified residue3321Phosphoserine By similarity

Natural variations

Alternative sequence1 – 8181Missing in isoform 3.
VSP_021942
Alternative sequence1 – 5353MYRWL…KRPRL → MEQNSK in isoform 2.
VSP_005273

Experimental info

Mutagenesis5471C → A: Abolishes protease activity. Ref.1 Ref.2
Sequence conflict2201L → F in AAL14437. Ref.1
Sequence conflict2551W → C in AAL14437. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 28, 2002. Version 2.
Checksum: 09B56796CA194847

FASTA58867,579
        10         20         30         40         50         60 
MYRWLAKVLG TILRLCERPA PGARALLKRR RSSSTLFSTA VDTDEIPAKR PRLDCFIHQV 

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

       130        140        150        160        170        180 
GNKSPNGISD YPKIRVTVTR DQPRRVLPSF GFTLKSEGYN RRPSGRRHSK SNPESSLTWK 

       190        200        210        220        230        240 
PQEQGVTEMI SEEGGKGVRR PHCTVEEGVQ KDEREKYRKL LERLKEGAHG STFPPTVSHH 

       250        260        270        280        290        300 
SSQRIQMDTL KTKGWVEEQN HGVRTTHFVP KQYRVVETRG PLCSMRSEKR YSKGKADTEK 

       310        320        330        340        350        360 
VVGLRFEKEG TRGHQMEPDL SEEVSARLRL GSGSNGLLRR KISVLEIKEK NFPSKEKDRR 

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

       430        440        450        460        470        480 
LLVERSKKQG YPALHAFSTF FYPKLKSGGY QAVKRWTKGV NLFEQELVLV PIHRKVHWSL 

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

       550        560        570        580 
QLNGSDCGMF TCKYADYISR DKPITFTQHQ MPLFRKKMVW EILHQQLL 

« Hide

Isoform 2.

Checksum: F25085A3FE0E0AE9
Show »

FASTA54162,276
Isoform 3.

Checksum: CB6F154A1BABF39A
Show »

FASTA50758,389

References

« Hide 'large scale' references
[1]"Characterization of a novel mammalian SUMO-1/Smt3-specific isopeptidase, a homologue of rat Axam, which is an Axin-binding protein promoting beta-Catenin degradation."
Nishida T., Kaneko F., Kitagawa M., Yasuda H.
J. Biol. Chem. 276:39060-39066(2001) [PubMed: 11489887] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, MUTAGENESIS OF CYS-547.
Tissue: Osteoblast.
[2]"SUMO-1 protease-1 regulates gene transcription through PML."
Best J.L., Ganiatsas S., Agarwal S., Changou A., Salomoni P., Shirihai O., Meluh P.B., Pandolfi P.P., Zon L.I.
Mol. Cell 10:843-855(2002) [PubMed: 12419228] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), MUTAGENESIS OF CYS-547, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Testis and Thymus.
[4]"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] (ISOFORM 1).
Tissue: Mammary tumor.
[5]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 342-348 AND 489-499, MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF368904 mRNA. Translation: AAL14437.1.
AY188288 mRNA. Translation: AAO27902.1.
AK015987 mRNA. Translation: BAB30067.1.
AK031030 mRNA. Translation: BAC27222.1.
BC031652 mRNA. Translation: AAH31652.1.
IPIIPI00138091.
IPI00230049.
IPI00817049.
RefSeqNP_083733.1.
UniGeneMm.297431

3D structure databases

SMRQ91ZX6. Positions 363-588.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ91ZX6.

Protein family/group databases

MEROPSC48.007.

PTM databases

PhosphoSiteQ91ZX6.

Proteomic databases

PRIDEQ91ZX6.

Genome annotation databases

EnsemblENSMUST00000023561; ENSMUSP00000023561; ENSMUSG00000022855; Mus musculus. [Genome view]
ENSMUST00000115380; ENSMUSP00000111038; ENSMUSG00000022855; Mus musculus. [Genome view]
GeneID75826.
KEGGmmu:75826.
UCSCuc007yrw.1. mouse.
uc007yrx.1. mouse.

Organism-specific databases

CTD75826.
MGIMGI:1923076. Senp2.

Phylogenomic databases

eggNOGroNOG06700.
HOGENOMHBG506560.
HOVERGENQ91ZX6.
InParanoidQ91ZX6.
OMAIDLRKKC.
OrthoDBEOG9SR0GC.
PhylomeDBQ91ZX6.

Gene expression databases

ArrayExpressQ91ZX6.
BgeeQ91ZX6.
CleanExMM_SENP2.
GenevestigatorQ91ZX6.
GermOnlineENSMUSG00000022855. Mus musculus.

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

NextBio344054.
SOURCESearch...

Entry information

Entry nameSENP2_MOUSE
AccessionPrimary (citable) accession number: Q91ZX6
Secondary accession number(s): Q544T8, Q811R3, Q9D4Z0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: November 28, 2002
Last modified: February 9, 2010
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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 · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents