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Q9P0U3

- SENP1_HUMAN

UniProt

Q9P0U3 - SENP1_HUMAN

Protein

Sentrin-specific protease 1

Gene

SENP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (25 Nov 2008)
      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. Deconjugates SUMO1 from HIPK2. Deconjugates SUMO1 from HDAC1 and BHLHE40/DEC1, which decreases its transcriptional repression activity. Deconjugates SUMO1 from CLOCK, which decreases its transcriptional activation activity. Deconjugates SUMO2 from MTA1.7 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 sitei533 – 5331
    Active sitei550 – 5501
    Active sitei603 – 6031Nucleophile

    GO - Molecular functioni

    1. endopeptidase activity Source: ProtInc
    2. protein binding Source: IntAct
    3. SUMO-specific protease activity Source: UniProtKB

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    2. apoptotic signaling pathway Source: UniProtKB
    3. cellular protein metabolic process Source: Reactome
    4. negative regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
    5. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    6. post-translational protein modification Source: Reactome
    7. protein desumoylation Source: UniProtKB
    8. protein sumoylation Source: Reactome
    9. proteolysis Source: ProtInc
    10. regulation of definitive erythrocyte differentiation Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    BRENDAi3.4.22.68. 2681.
    ReactomeiREACT_163725. SUMO is proteolytically processed.

    Protein family/group databases

    MEROPSiC48.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sentrin-specific protease 1 (EC:3.4.22.68)
    Alternative name(s):
    Sentrin/SUMO-specific protease SENP1
    Gene namesi
    Name:SENP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:17927. SENP1.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Shuttles between cytoplasm and nucleus.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. focal adhesion Source: HPA
    3. nuclear membrane Source: HPA
    4. nucleoplasm Source: Reactome
    5. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi441 – 4411D → A: No effect on SUMO2 processing and SUMO2 deconjugating activities. 1 Publication
    Mutagenesisi465 – 4651W → A: Impairs SUMO2 processing and SUMO2 deconjugating activities. 1 Publication
    Mutagenesisi468 – 4681D → A: Slightly impairs SUMO2 processing activity. No effect on SUMO2 deconjugating activity. 1 Publication
    Mutagenesisi496 – 4961F → A: Impairs SUMO2 processing activity. No effect on SUMO2 deconjugating activity. 1 Publication
    Mutagenesisi511 – 5111R → A: Impairs SUMO2 processing activity. No effect on SUMO2 deconjugating activity. 1 Publication
    Mutagenesisi512 – 5121W → A: Impairs SUMO2 processing and SUMO2 deconjugating activities. 1 Publication
    Mutagenesisi529 – 5291H → A: Impairs SUMO2 processing activity. No effect on SUMO2 deconjugating activity. 1 Publication
    Mutagenesisi532 – 5321V → A: No effect on SUMO2 processing and SUMO2 deconjugating activities. 1 Publication
    Mutagenesisi533 – 5331H → A: Abolishes SUMO2 processing and SUMO2 deconjugating activities. 1 Publication
    Mutagenesisi534 – 5341W → A: Abolishes SUMO2 processing and SUMO2 deconjugating activities. 1 Publication
    Mutagenesisi550 – 5501D → A: Abolishes SUMO2 processing and SUMO2 deconjugating activities. 1 Publication
    Mutagenesisi597 – 5971Q → A: Abolishes SUMO2 processing and SUMO2 deconjugating activities. 1 Publication
    Mutagenesisi603 – 6031C → A or S: Abolishes SUMO2 processing and SUMO2 deconjugating activities. 3 Publications
    Mutagenesisi603 – 6031C → S: Exclusively nuclear. 3 Publications

    Organism-specific databases

    PharmGKBiPA134947038.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 644644Sentrin-specific protease 1PRO_0000101716Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei157 – 1571Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9P0U3.
    PaxDbiQ9P0U3.
    PRIDEiQ9P0U3.

    PTM databases

    PhosphoSiteiQ9P0U3.

    Expressioni

    Tissue specificityi

    Highly expressed in testis. Expressed at lower levels in thymus, pancreas, spleen, liver, ovary and small intestine.1 Publication

    Gene expression databases

    ArrayExpressiQ9P0U3.
    BgeeiQ9P0U3.
    CleanExiHS_SENP1.
    GenevestigatoriQ9P0U3.

    Organism-specific databases

    HPAiHPA011765.
    HPA046491.

    Interactioni

    Subunit structurei

    Interacts with MTA1.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SUMO1P631652EBI-2822935,EBI-80140

    Protein-protein interaction databases

    BioGridi118930. 22 interactions.
    DIPiDIP-29252N.
    IntActiQ9P0U3. 4 interactions.
    MINTiMINT-1714015.
    STRINGi9606.ENSP00000394791.

    Structurei

    Secondary structure

    1
    644
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi425 – 43410
    Beta strandi435 – 4384
    Beta strandi445 – 4473
    Beta strandi450 – 4523
    Helixi454 – 4585
    Helixi468 – 48114
    Beta strandi482 – 4843
    Beta strandi490 – 4923
    Turni495 – 4984
    Helixi499 – 5024
    Helixi506 – 5094
    Turni510 – 5156
    Helixi518 – 5203
    Beta strandi521 – 53010
    Beta strandi533 – 5408
    Turni541 – 5444
    Beta strandi545 – 5495
    Helixi557 – 57519
    Beta strandi585 – 5884
    Beta strandi591 – 5944
    Helixi600 – 6023
    Helixi603 – 61513
    Helixi624 – 6263
    Helixi627 – 64014

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CKGX-ray2.45A/B419-644[»]
    2CKHX-ray3.20A419-644[»]
    2G4DX-ray2.80A/C440-644[»]
    2IY0X-ray2.77A419-643[»]
    2IY1X-ray2.46A/C419-643[»]
    2IYCX-ray2.45A/B419-643[»]
    2IYDX-ray3.20A419-643[»]
    2XPHX-ray2.40A/B415-644[»]
    2XREX-ray2.45A/B415-644[»]
    ProteinModelPortaliQ9P0U3.
    SMRiQ9P0U3. Positions 418-644.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9P0U3.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni450 – 613164ProteaseAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi171 – 1777Nuclear localization signal1 Publication
    Motifi574 – 5774Nuclear localization signalSequence Analysis
    Motifi628 – 6347Nuclear localization signalSequence Analysis
    Motifi635 – 64410Nuclear export signalCurated

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi45 – 170126Ser-richAdd
    BLAST
    Compositional biasi290 – 30011His-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase C48 family.Curated

    Phylogenomic databases

    eggNOGiCOG5160.
    HOGENOMiHOG000154286.
    HOVERGENiHBG057384.
    InParanoidiQ9P0U3.
    KOiK08592.
    OMAiVNHNSIF.
    OrthoDBiEOG7D59MP.
    PhylomeDBiQ9P0U3.
    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: Q9P0U3-1) [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

    MDDIADRMRM DAGEVTLVNH NSVFKTHLLP QTGFPEDQLS LSDQQILSSR    50
    QGHLDRSFTC STRSAAYNPS YYSDNPSSDS FLGSGDLRTF GQSANGQWRN 100
    STPSSSSSLQ KSRNSRSLYL ETRKTSSGLS NSFAGKSNHH CHVSAYEKSF 150
    PIKPVPSPSW SGSCRRSLLS PKKTQRRHVS TAEETVQEEE REIYRQLLQM 200
    VTGKQFTIAK PTTHFPLHLS RCLSSSKNTL KDSLFKNGNS CASQIIGSDT 250
    SSSGSASILT NQEQLSHSVY SLSSYTPDVA FGSKDSGTLH HPHHHHSVPH 300
    QPDNLAASNT QSEGSDSVIL LKVKDSQTPT PSSTFFQAEL WIKELTSVYD 350
    SRARERLRQI EEQKALALQL QNQRLQEREH SVHDSVELHL RVPLEKEIPV 400
    TVVQETQKKG HKLTDSEDEF PEITEEMEKE IKNVFRNGNQ DEVLSEAFRL 450
    TITRKDIQTL NHLNWLNDEI INFYMNMLME RSKEKGLPSV HAFNTFFFTK 500
    LKTAGYQAVK RWTKKVDVFS VDILLVPIHL GVHWCLAVVD FRKKNITYYD 550
    SMGGINNEAC RILLQYLKQE SIDKKRKEFD TNGWQLFSKK SQEIPQQMNG 600
    SDCGMFACKY ADCITKDRPI NFTQQHMPYF RKRMVWEILH RKLL 644
    Length:644
    Mass (Da):73,481
    Last modified:November 25, 2008 - v2
    Checksum:i941951A8B341EC64
    GO
    Isoform 2 (identifier: Q9P0U3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         593-593: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:643
    Mass (Da):73,351
    Checksum:i1556864F1BDEE337
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti193 – 1931I → V.1 Publication
    Corresponds to variant rs17854369 [ dbSNP | Ensembl ].
    VAR_029648
    Natural varianti280 – 2801A → T.
    Corresponds to variant rs35130318 [ dbSNP | Ensembl ].
    VAR_047547
    Natural varianti350 – 3501D → G.1 Publication
    Corresponds to variant rs17854368 [ dbSNP | Ensembl ].
    VAR_029649

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei593 – 5931Missing in isoform 2. 1 PublicationVSP_035777

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF149770 mRNA. Translation: AAF31171.1.
    AK292060 mRNA. Translation: BAF84749.1.
    AC074029 Genomic DNA. No translation available.
    BC045639 mRNA. Translation: AAH45639.2.
    CCDSiCCDS44868.2. [Q9P0U3-1]
    RefSeqiNP_001254523.1. NM_001267594.1. [Q9P0U3-1]
    NP_001254524.1. NM_001267595.1. [Q9P0U3-1]
    UniGeneiHs.371957.

    Genome annotation databases

    EnsembliENST00000448372; ENSP00000394791; ENSG00000079387. [Q9P0U3-2]
    ENST00000549518; ENSP00000447328; ENSG00000079387. [Q9P0U3-1]
    ENST00000549595; ENSP00000450076; ENSG00000079387. [Q9P0U3-2]
    GeneIDi29843.
    KEGGihsa:29843.
    UCSCiuc001rqx.4. human. [Q9P0U3-1]
    uc031qhb.1. human. [Q9P0U3-2]

    Polymorphism databases

    DMDMi215273882.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF149770 mRNA. Translation: AAF31171.1 .
    AK292060 mRNA. Translation: BAF84749.1 .
    AC074029 Genomic DNA. No translation available.
    BC045639 mRNA. Translation: AAH45639.2 .
    CCDSi CCDS44868.2. [Q9P0U3-1 ]
    RefSeqi NP_001254523.1. NM_001267594.1. [Q9P0U3-1 ]
    NP_001254524.1. NM_001267595.1. [Q9P0U3-1 ]
    UniGenei Hs.371957.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CKG X-ray 2.45 A/B 419-644 [» ]
    2CKH X-ray 3.20 A 419-644 [» ]
    2G4D X-ray 2.80 A/C 440-644 [» ]
    2IY0 X-ray 2.77 A 419-643 [» ]
    2IY1 X-ray 2.46 A/C 419-643 [» ]
    2IYC X-ray 2.45 A/B 419-643 [» ]
    2IYD X-ray 3.20 A 419-643 [» ]
    2XPH X-ray 2.40 A/B 415-644 [» ]
    2XRE X-ray 2.45 A/B 415-644 [» ]
    ProteinModelPortali Q9P0U3.
    SMRi Q9P0U3. Positions 418-644.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118930. 22 interactions.
    DIPi DIP-29252N.
    IntActi Q9P0U3. 4 interactions.
    MINTi MINT-1714015.
    STRINGi 9606.ENSP00000394791.

    Chemistry

    BindingDBi Q9P0U3.
    ChEMBLi CHEMBL1909484.

    Protein family/group databases

    MEROPSi C48.002.

    PTM databases

    PhosphoSitei Q9P0U3.

    Polymorphism databases

    DMDMi 215273882.

    Proteomic databases

    MaxQBi Q9P0U3.
    PaxDbi Q9P0U3.
    PRIDEi Q9P0U3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000448372 ; ENSP00000394791 ; ENSG00000079387 . [Q9P0U3-2 ]
    ENST00000549518 ; ENSP00000447328 ; ENSG00000079387 . [Q9P0U3-1 ]
    ENST00000549595 ; ENSP00000450076 ; ENSG00000079387 . [Q9P0U3-2 ]
    GeneIDi 29843.
    KEGGi hsa:29843.
    UCSCi uc001rqx.4. human. [Q9P0U3-1 ]
    uc031qhb.1. human. [Q9P0U3-2 ]

    Organism-specific databases

    CTDi 29843.
    GeneCardsi GC12M048436.
    HGNCi HGNC:17927. SENP1.
    HPAi HPA011765.
    HPA046491.
    MIMi 612157. gene.
    neXtProti NX_Q9P0U3.
    PharmGKBi PA134947038.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5160.
    HOGENOMi HOG000154286.
    HOVERGENi HBG057384.
    InParanoidi Q9P0U3.
    KOi K08592.
    OMAi VNHNSIF.
    OrthoDBi EOG7D59MP.
    PhylomeDBi Q9P0U3.
    TreeFami TF316289.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi SENP1. human.
    EvolutionaryTracei Q9P0U3.
    GeneWikii SENP1.
    GenomeRNAii 29843.
    NextBioi 52379.
    PROi Q9P0U3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9P0U3.
    Bgeei Q9P0U3.
    CleanExi HS_SENP1.
    Genevestigatori Q9P0U3.

    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. "Differential regulation of sentrinized proteins by a novel sentrin-specific protease."
      Gong L., Millas S., Maul G.G., Yeh E.T.H.
      J. Biol. Chem. 275:3355-3359(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION.
      Tissue: Placenta.
    2. "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] (ISOFORM 1).
      Tissue: Stomach.
    3. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., 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., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS VAL-193 AND GLY-350.
      Tissue: Testis.
    5. "Characterization of the localization and proteolytic activity of the SUMO-specific protease, SENP1."
      Bailey D., O'Hare P.
      J. Biol. Chem. 279:692-703(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-603.
    6. "SENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1."
      Cheng J., Wang D., Wang Z., Yeh E.T.H.
      Mol. Cell. Biol. 24:6021-6028(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1."
      Xu Z., Au S.W.N.
      Biochem. J. 386:325-330(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    8. "Desumoylation of homeodomain-interacting protein kinase 2 (HIPK2) through the cytoplasmic-nuclear shuttling of the SUMO-specific protease SENP1."
      Kim Y.H., Sung K.S., Lee S.-J., Kim Y.-O., Choi C.Y., Kim Y.
      FEBS Lett. 579:6272-6278(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEAR EXPORT SIGNAL, SUBCELLULAR LOCATION, FUNCTION.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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.
    11. "SUMOylation of DEC1 protein regulates its transcriptional activity and enhances its stability."
      Hong Y., Xing X., Li S., Bi H., Yang C., Zhao F., Liu Y., Ao X., Chang A.K., Wu H.
      PLoS ONE 6:E23046-E23046(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "CLOCK is a substrate of SUMO and sumoylation of CLOCK upregulates the transcriptional activity of estrogen receptor-alpha."
      Li S., Wang M., Ao X., Chang A.K., Yang C., Zhao F., Bi H., Liu Y., Xiao L., Wu H.
      Oncogene 32:4883-4891(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing."
      Shen L.N., Dong C., Liu H., Naismith J.H., Hay R.T.
      Biochem. J. 397:279-288(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 419-644, X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 419-644 IN COMPLEX WITH SUMO3, MUTAGENESIS OF ASP-441; TRP-465; ASP-468; PHE-496; ARG-511; TRP-512; HIS-529; VAL-532; HIS-533; TRP-534; ASP-550; GLN-597 AND CYS-603, FUNCTION.
    14. "Crystal structure of the SENP1 mutant C603S-SUMO complex reveals the hydrolytic mechanism of SUMO-specific protease."
      Xu Z., Chau S.F., Lam K.H., Chan H.Y., Ng T.B., Au S.W.N.
      Biochem. J. 398:345-352(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 439-644 IN COMPLEX WITH SUMO1, MUTAGENESIS OF CYS-603.
    15. "SUMO protease SENP1 induces isomerization of the scissile peptide bond."
      Shen L., Tatham M.H., Dong C., Zagorska A., Naismith J.H., Hay R.T.
      Nat. Struct. Mol. Biol. 13:1069-1077(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF 439-644 IN COMPLEX WITH RANGAP1 AND SUMO1.

    Entry informationi

    Entry nameiSENP1_HUMAN
    AccessioniPrimary (citable) accession number: Q9P0U3
    Secondary accession number(s): A8K7P5, Q86XC8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2002
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 118 of the entry and version 2 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 12
      Human chromosome 12: 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

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