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Q9P0U3

- SENP1_HUMAN

UniProt

Q9P0U3 - SENP1_HUMAN

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Protein

Sentrin-specific protease 1

Gene
SENP1
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. 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.6 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
Complete GO annotation...

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.3 Publications

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
Complete GO annotation...

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

Binary interactionsi

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

Protein-protein interaction databases

BioGridi118930. 21 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.

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 signal Inferred
Motifi574 – 5774Nuclear localization signal Reviewed prediction
Motifi628 – 6347Nuclear localization signal Reviewed prediction
Motifi635 – 64410Nuclear export signal Inferred

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.

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. VSP_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

EnsembliENST00000004980; ENSP00000004980; ENSG00000079387. [Q9P0U3-1]
ENST00000448372; ENSP00000394791; ENSG00000079387. [Q9P0U3-2]
ENST00000549518; ENSP00000447328; ENSG00000079387. [Q9P0U3-1]
ENST00000549595; ENSP00000450076; ENSG00000079387. [Q9P0U3-2]
ENST00000551330; ENSP00000446681; ENSG00000079387. [Q9P0U3-1]
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. 21 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 ENST00000004980 ; ENSP00000004980 ; ENSG00000079387 . [Q9P0U3-1 ]
ENST00000448372 ; ENSP00000394791 ; ENSG00000079387 . [Q9P0U3-2 ]
ENST00000549518 ; ENSP00000447328 ; ENSG00000079387 . [Q9P0U3-1 ]
ENST00000549595 ; ENSP00000450076 ; ENSG00000079387 . [Q9P0U3-2 ]
ENST00000551330 ; ENSP00000446681 ; ENSG00000079387 . [Q9P0U3-1 ]
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

« Hide 'large scale' publications
  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 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.
  11. "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.
  12. "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.
  13. "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.
  14. "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: September 3, 2014
This is version 117 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

Dasty 3

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