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Q9HC62 (SENP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sentrin-specific protease 2

EC=3.4.22.68
Alternative name(s):
Axam2
SMT3-specific isopeptidase 2
Short name=Smt3ip2
Sentrin/SUMO-specific protease SENP2
Gene names
Name:SENP2
Synonyms:KIAA1331
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length589 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. Ref.7 Ref.8

Catalytic activity

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.

Subunit structure

Binds to SUMO2 and SUMO3 By similarity. Interacts with the C-terminal domain of NUP153 via its N-terminus. Ref.7 Ref.8

Subcellular location

Nucleusnuclear pore complex. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Cytoplasm. Note: Shuttles between cytoplasm and nucleus. Ref.7 Ref.8 Ref.9

Domain

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

Post-translational modification

Polyubiquitinated; which leads to proteasomal degradation.

Sequence similarities

Belongs to the peptidase C48 family.

Ontologies

Keywords
   Biological processmRNA transport
Protein transport
Translocation
Transport
Ubl conjugation pathway
Wnt signaling pathway
   Cellular componentCytoplasm
Membrane
Nuclear pore complex
Nucleus
   Coding sequence diversityPolymorphism
   Molecular functionHydrolase
Protease
Thiol protease
   PTMUbl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

cellular protein metabolic process

Traceable author statement. Source: Reactome

dorsal/ventral axis specification

Inferred from electronic annotation. Source: Ensembl

heart development

Inferred from electronic annotation. Source: Ensembl

labyrinthine layer development

Inferred from electronic annotation. Source: Ensembl

mRNA transport

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of chromatin binding

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein binding

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

post-translational protein modification

Traceable author statement. Source: Reactome

protein desumoylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein sumoylation

Traceable author statement. Source: Reactome

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of DNA endoreduplication

Inferred from electronic annotation. Source: Ensembl

regulation of G1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

regulation of Wnt signaling pathway

Non-traceable author statement Ref.8. Source: UniProtKB

spongiotrophoblast layer development

Inferred from electronic annotation. Source: Ensembl

trophoblast giant cell differentiation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentPML body

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear pore

Inferred from direct assay Ref.7. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionSUMO-specific protease activity

Inferred from direct assay Ref.8. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

IKBKGQ9Y6K93EBI-714881,EBI-81279

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 589589Sentrin-specific protease 2
PRO_0000101718

Regions

Region396 – 560165Protease
Motif28 – 314Nuclear localization signal Ref.9
Motif46 – 516Nuclear localization signal Ref.9
Motif317 – 33216Nuclear export signal

Sites

Active site4781
Active site4951
Active site5481Nucleophile

Natural variations

Natural variant3011T → K. Ref.1 Ref.2 Ref.4 Ref.6
Corresponds to variant rs6762208 [ dbSNP | Ensembl ].
VAR_029650

Experimental info

Sequence conflict391T → TA in AAG15309. Ref.1
Sequence conflict4031Q → H in BAB55222. Ref.4

Secondary structure

......................................... 589
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9HC62 [UniParc].

Last modified April 3, 2007. Version 3.
Checksum: 712707DCC2C5431C

FASTA58967,855
        10         20         30         40         50         60 
MYRWLVRILG TIFRFCDRSV PPARALLKRR RSDSTLFSTV DTDEIPAKRP RLDCFIHQVK 

        70         80         90        100        110        120 
NSLYNAASLF GFPFQLTTKP MVTSACNGTR NVAPSGEVFS NSSSCELTGS GSWNNMLKLG 

       130        140        150        160        170        180 
NKSPNGISDY PKIRVTVTRD QPRRVLPSFG FTLNSEGCNR RPGGRRHSKG NPESSLMWKP 

       190        200        210        220        230        240 
QEQAVTEMIS EESGKGLRRP HCTVEEGVQK EEREKYRKLL ERLKESGHGN SVCPVTSNYH 

       250        260        270        280        290        300 
SSQRSQMDTL KTKGWGEEQN HGVKTTQFVP KQYRLVETRG PLCSLRSEKR CSKGKITDTE 

       310        320        330        340        350        360 
TMVGIRFENE SRRGYQLEPD LSEEVSARLR LGSGSNGLLR RKVSIIETKE KNCSGKERDR 

       370        380        390        400        410        420 
RTDDLLELTE DMEKEISNAL GHGPQDEILS SAFKLRITRG DIQTLKNYHW LNDEVINFYM 

       430        440        450        460        470        480 
NLLVERNKKQ GYPALHVFST FFYPKLKSGG YQAVKRWTKG VNLFEQEIIL VPIHRKVHWS 

       490        500        510        520        530        540 
LVVIDLRKKC LKYLDSMGQK GHRICEILLQ YLQDESKTKR NSDLNLLEWT HHSMKPHEIP 

       550        560        570        580 
QQLNGSDCGM FTCKYADYIS RDKPITFTQH QMPLFRKKMV WEILHQQLL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of SENP2, a novel member of sentrin-specific protease family."
Gong L., Yeh E.T.H.
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LYS-301.
[2]"Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LYS-301.
Tissue: Brain.
[3]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LYS-301.
Tissue: Teratocarcinoma.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[6]"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., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-589, VARIANT LYS-301.
Tissue: Melanoma.
[7]"Enzymes of the SUMO modification pathway localize to filaments of the nuclear pore complex."
Zhang H., Saitoh H., Matunis M.J.
Mol. Cell. Biol. 22:6498-6508(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NUP153.
Tissue: Fetal brain.
[8]"Association of the human SUMO-1 protease SENP2 with the nuclear pore."
Hang J., Dasso M.
J. Biol. Chem. 277:19961-19966(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NUP153.
[9]"Nucleocytoplasmic shuttling modulates activity and ubiquitination-dependent turnover of SUMO-specific protease 2."
Itahana Y., Yeh E.T.H., Zhang Y.
Mol. Cell. Biol. 26:4675-4689(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEAR LOCALIZATION SIGNAL, NUCLEAR EXPORT SIGNAL, SUBCELLULAR LOCATION, UBIQUITINATION.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex."
Reverter D., Lima C.D.
Structure 12:1519-1531(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 364-589, X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 364-589 IN COMPLEX WITH SUMO1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF151697 mRNA. Translation: AAG15309.2.
AB037752 mRNA. Translation: BAA92569.2.
AK027599 mRNA. Translation: BAB55222.1.
BC040609 mRNA. Translation: AAH40609.1.
AL834380 mRNA. Translation: CAD39043.1.
CCDSCCDS33902.1.
RefSeqNP_067640.2. NM_021627.2.
UniGeneHs.401388.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TGZX-ray2.80A364-589[»]
1TH0X-ray2.20A/B364-589[»]
2IO0X-ray2.30A364-589[»]
2IO1X-ray2.60A/C/E364-589[»]
2IO2X-ray2.90A364-589[»]
2IO3X-ray3.20A364-589[»]
3ZO5X-ray2.15A363-589[»]
ProteinModelPortalQ9HC62.
SMRQ9HC62. Positions 364-589.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121885. 16 interactions.
DIPDIP-29254N.
IntActQ9HC62. 7 interactions.
MINTMINT-1389034.
STRING9606.ENSP00000296257.

Chemistry

BindingDBQ9HC62.
ChEMBLCHEMBL2176776.

Protein family/group databases

MEROPSC48.007.

PTM databases

PhosphoSiteQ9HC62.

Polymorphism databases

DMDM143811458.

Proteomic databases

MaxQBQ9HC62.
PaxDbQ9HC62.
PRIDEQ9HC62.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296257; ENSP00000296257; ENSG00000163904.
GeneID59343.
KEGGhsa:59343.
UCSCuc003fpn.3. human.

Organism-specific databases

CTD59343.
GeneCardsGC03P185301.
HGNCHGNC:23116. SENP2.
HPAHPA029247.
HPA029248.
MIM608261. gene.
neXtProtNX_Q9HC62.
PharmGKBPA134955185.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5160.
HOGENOMHOG000070234.
HOVERGENHBG054228.
InParanoidQ9HC62.
KOK03345.
OMARRGYQLE.
OrthoDBEOG7D59MP.
PhylomeDBQ9HC62.
TreeFamTF316289.

Enzyme and pathway databases

BRENDA3.4.22.68. 2681.
ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ9HC62.
BgeeQ9HC62.
CleanExHS_SENP2.
GenevestigatorQ9HC62.

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

ChiTaRSSENP2. human.
EvolutionaryTraceQ9HC62.
GeneWikiSENP2.
GenomeRNAi59343.
NextBio65238.
PROQ9HC62.
SOURCESearch...

Entry information

Entry nameSENP2_HUMAN
AccessionPrimary (citable) accession number: Q9HC62
Secondary accession number(s): Q8IW97, Q96SR2, Q9P2L5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: April 3, 2007
Last modified: July 9, 2014
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM