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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. 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. 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.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  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

BgeeiQ9P0U3.
CleanExiHS_SENP1.
ExpressionAtlasiQ9P0U3. baseline and differential.
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. 23 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 – 43410Combined sources
Beta strandi435 – 4384Combined sources
Beta strandi445 – 4473Combined sources
Beta strandi450 – 4523Combined sources
Helixi454 – 4585Combined sources
Helixi468 – 48114Combined sources
Beta strandi482 – 4843Combined sources
Beta strandi490 – 4923Combined sources
Turni495 – 4984Combined sources
Helixi499 – 5024Combined sources
Helixi506 – 5094Combined sources
Turni510 – 5156Combined sources
Helixi518 – 5203Combined sources
Beta strandi521 – 53010Combined sources
Beta strandi533 – 5408Combined sources
Turni541 – 5444Combined sources
Beta strandi545 – 5495Combined sources
Helixi557 – 57519Combined sources
Beta strandi585 – 5884Combined sources
Beta strandi591 – 5944Combined sources
Helixi600 – 6023Combined sources
Helixi603 – 61513Combined sources
Helixi624 – 6263Combined sources
Helixi627 – 64014Combined sources

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.
GeneTreeiENSGT00530000062941.
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

        10         20         30         40         50
MDDIADRMRM DAGEVTLVNH NSVFKTHLLP QTGFPEDQLS LSDQQILSSR
60 70 80 90 100
QGHLDRSFTC STRSAAYNPS YYSDNPSSDS FLGSGDLRTF GQSANGQWRN
110 120 130 140 150
STPSSSSSLQ KSRNSRSLYL ETRKTSSGLS NSFAGKSNHH CHVSAYEKSF
160 170 180 190 200
PIKPVPSPSW SGSCRRSLLS PKKTQRRHVS TAEETVQEEE REIYRQLLQM
210 220 230 240 250
VTGKQFTIAK PTTHFPLHLS RCLSSSKNTL KDSLFKNGNS CASQIIGSDT
260 270 280 290 300
SSSGSASILT NQEQLSHSVY SLSSYTPDVA FGSKDSGTLH HPHHHHSVPH
310 320 330 340 350
QPDNLAASNT QSEGSDSVIL LKVKDSQTPT PSSTFFQAEL WIKELTSVYD
360 370 380 390 400
SRARERLRQI EEQKALALQL QNQRLQEREH SVHDSVELHL RVPLEKEIPV
410 420 430 440 450
TVVQETQKKG HKLTDSEDEF PEITEEMEKE IKNVFRNGNQ DEVLSEAFRL
460 470 480 490 500
TITRKDIQTL NHLNWLNDEI INFYMNMLME RSKEKGLPSV HAFNTFFFTK
510 520 530 540 550
LKTAGYQAVK RWTKKVDVFS VDILLVPIHL GVHWCLAVVD FRKKNITYYD
560 570 580 590 600
SMGGINNEAC RILLQYLKQE SIDKKRKEFD TNGWQLFSKK SQEIPQQMNG
610 620 630 640
SDCGMFACKY ADCITKDRPI NFTQQHMPYF RKRMVWEILH RKLL
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. [Q9P0U3-1]
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. 23 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 . [Q9P0U3-1 ]
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.
GeneTreei ENSGT00530000062941.
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

Bgeei Q9P0U3.
CleanExi HS_SENP1.
ExpressionAtlasi Q9P0U3. baseline and differential.
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 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 29, 2014
This is version 119 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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