SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9HC62

- SENP2_HUMAN

UniProt

Q9HC62 - SENP2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Sentrin-specific protease 2
Gene
SENP2, KIAA1331
Organism
Homo sapiens (Human)
Status
Reviewed - 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 By similarity.2 Publications

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 sitei478 – 4781
Active sitei495 – 4951
Active sitei548 – 5481Nucleophile

GO - Molecular functioni

  1. SUMO-specific protease activity Source: UniProtKB
  2. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. Wnt signaling pathway Source: UniProtKB-KW
  2. cellular protein metabolic process Source: Reactome
  3. dorsal/ventral axis specification Source: Ensembl
  4. heart development Source: Ensembl
  5. labyrinthine layer development Source: Ensembl
  6. mRNA transport Source: UniProtKB-KW
  7. negative regulation of chromatin binding Source: Ensembl
  8. negative regulation of protein binding Source: Ensembl
  9. positive regulation of protein phosphorylation Source: Ensembl
  10. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  11. post-translational protein modification Source: Reactome
  12. protein desumoylation Source: UniProtKB
  13. protein sumoylation Source: Reactome
  14. protein transport Source: UniProtKB-KW
  15. regulation of DNA endoreduplication Source: Ensembl
  16. regulation of G1/S transition of mitotic cell cycle Source: Ensembl
  17. regulation of Wnt signaling pathway Source: UniProtKB
  18. spongiotrophoblast layer development Source: Ensembl
  19. trophoblast giant cell differentiation Source: Ensembl
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

BRENDAi3.4.22.68. 2681.
ReactomeiREACT_163725. 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):
Axam2
SMT3-specific isopeptidase 2
Short name:
Smt3ip2
Sentrin/SUMO-specific protease SENP2
Gene namesi
Name:SENP2
Synonyms:KIAA1331
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:23116. SENP2.

Subcellular locationi

Nucleusnuclear pore complex. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Cytoplasm
Note: Shuttles between cytoplasm and nucleus.3 Publications

GO - Cellular componenti

  1. PML body Source: Ensembl
  2. cytoplasm Source: UniProtKB-SubCell
  3. nuclear membrane Source: UniProtKB-SubCell
  4. nuclear pore Source: UniProtKB
  5. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nuclear pore complex, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134955185.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 589589Sentrin-specific protease 2
PRO_0000101718Add
BLAST

Post-translational modificationi

Polyubiquitinated; which leads to proteasomal degradation.

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiQ9HC62.
PaxDbiQ9HC62.
PRIDEiQ9HC62.

PTM databases

PhosphoSiteiQ9HC62.

Expressioni

Gene expression databases

ArrayExpressiQ9HC62.
BgeeiQ9HC62.
CleanExiHS_SENP2.
GenevestigatoriQ9HC62.

Organism-specific databases

HPAiHPA029247.
HPA029248.

Interactioni

Subunit structurei

Binds to SUMO2 and SUMO3 By similarity. Interacts with the C-terminal domain of NUP153 via its N-terminus.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
IKBKGQ9Y6K93EBI-714881,EBI-81279

Protein-protein interaction databases

BioGridi121885. 16 interactions.
DIPiDIP-29254N.
IntActiQ9HC62. 7 interactions.
MINTiMINT-1389034.
STRINGi9606.ENSP00000296257.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi370 – 38011
Beta strandi381 – 3833
Beta strandi388 – 3925
Beta strandi395 – 3984
Helixi399 – 4024
Helixi403 – 4053
Helixi413 – 43018
Beta strandi435 – 4373
Helixi442 – 45413
Helixi455 – 4584
Helixi463 – 4653
Beta strandi466 – 4749
Beta strandi479 – 4857
Turni486 – 4894
Beta strandi490 – 4945
Beta strandi496 – 4983
Helixi502 – 52019
Helixi526 – 5283
Beta strandi530 – 5334
Turni536 – 5383
Turni543 – 5464
Helixi548 – 56013
Helixi569 – 5713
Helixi572 – 58514

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ9HC62.
SMRiQ9HC62. Positions 364-589.

Miscellaneous databases

EvolutionaryTraceiQ9HC62.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni396 – 560165Protease
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi28 – 314Nuclear localization signal1 Publication
Motifi46 – 516Nuclear localization signal1 Publication
Motifi317 – 33216Nuclear export signal
Add
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the peptidase C48 family.

Phylogenomic databases

eggNOGiCOG5160.
HOGENOMiHOG000070234.
HOVERGENiHBG054228.
InParanoidiQ9HC62.
KOiK03345.
OMAiRRGYQLE.
OrthoDBiEOG7D59MP.
PhylomeDBiQ9HC62.
TreeFamiTF316289.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q9HC62-1 [UniParc]FASTAAdd to Basket

« Hide

MYRWLVRILG TIFRFCDRSV PPARALLKRR RSDSTLFSTV DTDEIPAKRP    50
RLDCFIHQVK NSLYNAASLF GFPFQLTTKP MVTSACNGTR NVAPSGEVFS 100
NSSSCELTGS GSWNNMLKLG NKSPNGISDY PKIRVTVTRD QPRRVLPSFG 150
FTLNSEGCNR RPGGRRHSKG NPESSLMWKP QEQAVTEMIS EESGKGLRRP 200
HCTVEEGVQK EEREKYRKLL ERLKESGHGN SVCPVTSNYH SSQRSQMDTL 250
KTKGWGEEQN HGVKTTQFVP KQYRLVETRG PLCSLRSEKR CSKGKITDTE 300
TMVGIRFENE SRRGYQLEPD LSEEVSARLR LGSGSNGLLR RKVSIIETKE 350
KNCSGKERDR RTDDLLELTE DMEKEISNAL GHGPQDEILS SAFKLRITRG 400
DIQTLKNYHW LNDEVINFYM NLLVERNKKQ GYPALHVFST FFYPKLKSGG 450
YQAVKRWTKG VNLFEQEIIL VPIHRKVHWS LVVIDLRKKC LKYLDSMGQK 500
GHRICEILLQ YLQDESKTKR NSDLNLLEWT HHSMKPHEIP QQLNGSDCGM 550
FTCKYADYIS RDKPITFTQH QMPLFRKKMV WEILHQQLL 589
Length:589
Mass (Da):67,855
Last modified:April 3, 2007 - v3
Checksum:i712707DCC2C5431C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti301 – 3011T → K.4 Publications
Corresponds to variant rs6762208 [ dbSNP | Ensembl ].
VAR_029650

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti39 – 391T → TA in AAG15309. 1 Publication
Sequence conflicti403 – 4031Q → H in BAB55222. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS33902.1.
RefSeqiNP_067640.2. NM_021627.2.
UniGeneiHs.401388.

Genome annotation databases

EnsembliENST00000296257; ENSP00000296257; ENSG00000163904.
GeneIDi59343.
KEGGihsa:59343.
UCSCiuc003fpn.3. human.

Polymorphism databases

DMDMi143811458.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS33902.1.
RefSeqi NP_067640.2. NM_021627.2.
UniGenei Hs.401388.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1TGZ X-ray 2.80 A 364-589 [» ]
1TH0 X-ray 2.20 A/B 364-589 [» ]
2IO0 X-ray 2.30 A 364-589 [» ]
2IO1 X-ray 2.60 A/C/E 364-589 [» ]
2IO2 X-ray 2.90 A 364-589 [» ]
2IO3 X-ray 3.20 A 364-589 [» ]
3ZO5 X-ray 2.15 A 363-589 [» ]
ProteinModelPortali Q9HC62.
SMRi Q9HC62. Positions 364-589.
ModBasei Search...

Protein-protein interaction databases

BioGridi 121885. 16 interactions.
DIPi DIP-29254N.
IntActi Q9HC62. 7 interactions.
MINTi MINT-1389034.
STRINGi 9606.ENSP00000296257.

Chemistry

BindingDBi Q9HC62.
ChEMBLi CHEMBL2176776.

Protein family/group databases

MEROPSi C48.007.

PTM databases

PhosphoSitei Q9HC62.

Polymorphism databases

DMDMi 143811458.

Proteomic databases

MaxQBi Q9HC62.
PaxDbi Q9HC62.
PRIDEi Q9HC62.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000296257 ; ENSP00000296257 ; ENSG00000163904 .
GeneIDi 59343.
KEGGi hsa:59343.
UCSCi uc003fpn.3. human.

Organism-specific databases

CTDi 59343.
GeneCardsi GC03P185301.
HGNCi HGNC:23116. SENP2.
HPAi HPA029247.
HPA029248.
MIMi 608261. gene.
neXtProti NX_Q9HC62.
PharmGKBi PA134955185.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5160.
HOGENOMi HOG000070234.
HOVERGENi HBG054228.
InParanoidi Q9HC62.
KOi K03345.
OMAi RRGYQLE.
OrthoDBi EOG7D59MP.
PhylomeDBi Q9HC62.
TreeFami TF316289.

Enzyme and pathway databases

BRENDAi 3.4.22.68. 2681.
Reactomei REACT_163725. SUMO is proteolytically processed.

Miscellaneous databases

ChiTaRSi SENP2. human.
EvolutionaryTracei Q9HC62.
GeneWikii SENP2.
GenomeRNAii 59343.
NextBioi 65238.
PROi Q9HC62.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9HC62.
Bgeei Q9HC62.
CleanExi HS_SENP2.
Genevestigatori Q9HC62.

Family and domain databases

InterProi IPR003653. Peptidase_C48.
[Graphical view ]
Pfami PF02902. Peptidase_C48. 1 hit.
[Graphical view ]
PROSITEi PS50600. ULP_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiSENP2_HUMAN
AccessioniPrimary (citable) accession number: Q9HC62
Secondary accession number(s): Q8IW97, Q96SR2, Q9P2L5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: April 3, 2007
Last modified: September 3, 2014
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi