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Q9HC62

- SENP2_HUMAN

UniProt

Q9HC62 - SENP2_HUMAN

Protein

Sentrin-specific protease 2

Gene

SENP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 3 (03 Apr 2007)
      Previous versions | rss
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    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 MTA1.3 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. protein binding Source: UniProtKB
    2. SUMO-specific protease activity Source: UniProtKB

    GO - Biological processi

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

    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

    GO - Cellular componenti

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

    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 2PRO_0000101718Add
    BLAST

    Post-translational modificationi

    Polyubiquitinated; which leads to proteasomal degradation.1 Publication

    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. Interacts with MTA1.By similarity4 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

    1
    589
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9HC62.

    Family & Domainsi

    Region

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

    Motif

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

    Domaini

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

    Sequence similaritiesi

    Belongs to the peptidase C48 family.Curated

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9HC62-1) [UniParc]FASTAAdd to Basket

    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.

    « 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
    Isoform 2 (identifier: Q9HC62-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-33: MYRWLVRILGTIFRFCDRSVPPARALLKRRRSD → MDSHPCLYCGPQDSEGTNWQTSP

    Note: No experimental confirmation available.

    Show »
    Length:579
    Mass (Da):66,358
    Checksum:i06C0D0649B5BCFC7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti39 – 391T → TA in AAG15309. 1 PublicationCurated
    Sequence conflicti403 – 4031Q → H in BAB55222. (PubMed:14702039)Curated

    Natural variant

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

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3333MYRWL…RRRSD → MDSHPCLYCGPQDSEGTNWQ TSP in isoform 2. 1 PublicationVSP_056697Add
    BLAST

    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.
    AK298628 mRNA. Translation: BAG60804.1.
    AC016961 Genomic DNA. No translation available.
    AC133473 Genomic DNA. No translation available.
    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.
    ENST00000545472; ENSP00000439653; ENSG00000163904.
    GeneIDi59343.
    KEGGihsa:59343.
    UCSCiuc003fpn.3. human.

    Polymorphism databases

    DMDMi143811458.

    Keywords - Coding sequence diversityi

    Alternative splicing, 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 .
    AK298628 mRNA. Translation: BAG60804.1 .
    AC016961 Genomic DNA. No translation available.
    AC133473 Genomic DNA. No translation available.
    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...
    MobiDBi 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 .
    ENST00000545472 ; ENSP00000439653 ; 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

    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] (ISOFORM 1), 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] (ISOFORM 1), 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] (ISOFORMS 1 AND 2), VARIANT LYS-301.
      Tissue: Teratocarcinoma.
    5. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM 1).
      Tissue: Brain.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-589 (ISOFORM 1), VARIANT LYS-301.
      Tissue: Melanoma.
    8. "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.
    9. "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.
    10. "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.
    11. "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].
    12. "SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1 (MTA1) synergistically regulate its transcriptional repressor function."
      Cong L., Pakala S.B., Ohshiro K., Li D.Q., Kumar R.
      J. Biol. Chem. 286:43793-43808(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MTA1.
    13. "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): B4DQ42
    , Q8IW97, Q96SR2, Q9P2L5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2002
    Last sequence update: April 3, 2007
    Last modified: October 1, 2014
    This is version 126 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