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Protein

Sentrin-specific protease 1

Gene

Senp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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. Desumoylates CCAR2 which decreases its interaction with SIRT1 (By similarity).By similarity1 Publication

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 sitei529 – 5291By similarity
Active sitei546 – 5461By similarity
Active sitei599 – 5991NucleophileBy similarity

GO - Molecular functioni

  • SUMO-specific protease activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BRENDAi3.4.22.B70. 3474.
ReactomeiR-MMU-3065679. 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):
SUMO-1 protease 2
Short name:
SuPr-2
Sentrin/SUMO-specific protease SENP1
Gene namesi
Name:Senp1
Synonyms:Supr2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:2445054. Senp1.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity

  • Note: Shuttles between cytoplasm and nucleus.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Death between E13.5 and E14.5 due to abnormalities in fetal vessels.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 640640Sentrin-specific protease 1PRO_0000101717Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei157 – 1571PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP59110.
MaxQBiP59110.
PaxDbiP59110.
PRIDEiP59110.

PTM databases

iPTMnetiP59110.
PhosphoSiteiP59110.

Expressioni

Developmental stagei

Expression starts at E9.5.1 Publication

Gene expression databases

BgeeiP59110.
CleanExiMM_SENP1.
ExpressionAtlasiP59110. baseline and differential.
GenevisibleiP59110. MM.

Interactioni

Subunit structurei

Interacts with MTA1. Interacts with CCAR2 (via N-terminus).By similarity

Protein-protein interaction databases

BioGridi230207. 4 interactions.
IntActiP59110. 1 interaction.
MINTiMINT-4112452.
STRINGi10090.ENSMUSP00000046598.

Structurei

3D structure databases

ProteinModelPortaliP59110.
SMRiP59110. Positions 414-640.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 200200Interaction with CCAR2By similarityAdd
BLAST
Regioni446 – 610165ProteaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi171 – 1777Nuclear localization signalBy similarity
Motifi570 – 5734Nuclear localization signalSequence analysis
Motifi624 – 6307Nuclear localization signalSequence analysis
Motifi631 – 64010Nuclear export signalBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi42 – 170129Ser-richAdd
BLAST
Compositional biasi289 – 2968His-rich

Sequence similaritiesi

Belongs to the peptidase C48 family.Curated

Phylogenomic databases

eggNOGiKOG0778. Eukaryota.
COG5160. LUCA.
GeneTreeiENSGT00530000062941.
HOGENOMiHOG000154286.
HOVERGENiHBG057384.
InParanoidiP59110.
KOiK08592.
OrthoDBiEOG7D59MP.
PhylomeDBiP59110.
TreeFamiTF316289.

Family and domain databases

InterProiIPR003653. Peptidase_C48_C.
IPR033387. SENP1.
[Graphical view]
PANTHERiPTHR12606:SF30. PTHR12606:SF30. 1 hit.
PfamiPF02902. Peptidase_C48. 1 hit.
[Graphical view]
PROSITEiPS50600. ULP_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P59110-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDDTADGVKM DAGEVTLVNH GSTFRTHRPP QSGFPEEQLL LSDQQSLPFR
60 70 80 90 100
QGTLDGSFTC STRSPAYRPD YHSDNPSSDS FLGSGDVRTF GQSANGQWRN
110 120 130 140 150
STPASGSAPQ KPRNSRSLCL ETRKTSSGLS NTFVGKSNHH CHMSAYEKSF
160 170 180 190 200
PIKPAPSPSW SGSCRRSLLS PKKTQRRHFS TAEETVQEEE KEIYRQLLQM
210 220 230 240 250
VTGKQFCVAK PTTHFPLRLS RCLSSNKNSL KDSLLRNGNS CASHVIGSDT
260 270 280 290 300
SSSGSASILT AQEQLSHSAH SLSSGTPDVA FGSKDSDPHH HLAAPHQPNS
310 320 330 340 350
LPASNTQSEG SDSVILLKVK ESQTPASSPT FFQAELWIKE LTSVYDSRAR
360 370 380 390 400
ERLRRIEEQK ALALQLQNQR LQEQEHAVLD SVELHLRVPL EKEIPVTAAQ
410 420 430 440 450
ETRKKSHQLT DSEDEFPEIT EEMEKEIKNV FRNGNQDEVL SEAFRLTITR
460 470 480 490 500
KDIQTLNHLN WLNDEIINFY MNMLMERSKE KGFPSVHAFN TFFFTKLKTA
510 520 530 540 550
GYQAVKRWTK KVDVFSVDIL LVPIHLGVHW CLAVVDFRRK SITYYDSMGG
560 570 580 590 600
INNEACRILL QYLKQESVDK KRKEFDTNGW QLFSKKSQEI PQQMNGSDCG
610 620 630 640
MFACKYADCI TKDRPINFTQ QHMPYFRKRM VWEILHRKLL
Length:640
Mass (Da):72,511
Last modified:November 28, 2002 - v1
Checksum:i59B6BB70268A0477
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti432 – 4321R → H in BAC40442 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK028565 mRNA. Translation: BAC26011.1.
AK035581 mRNA. Translation: BAC29112.1.
AK088597 mRNA. Translation: BAC40442.1.
BC023129 mRNA. Translation: AAH23129.1.
CCDSiCCDS49717.1.
RefSeqiNP_659100.1. NM_144851.5.
UniGeneiMm.384023.
Mm.487443.

Genome annotation databases

EnsembliENSMUST00000044189; ENSMUSP00000046598; ENSMUSG00000033075.
GeneIDi223870.
KEGGimmu:223870.
UCSCiuc007xls.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK028565 mRNA. Translation: BAC26011.1.
AK035581 mRNA. Translation: BAC29112.1.
AK088597 mRNA. Translation: BAC40442.1.
BC023129 mRNA. Translation: AAH23129.1.
CCDSiCCDS49717.1.
RefSeqiNP_659100.1. NM_144851.5.
UniGeneiMm.384023.
Mm.487443.

3D structure databases

ProteinModelPortaliP59110.
SMRiP59110. Positions 414-640.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230207. 4 interactions.
IntActiP59110. 1 interaction.
MINTiMINT-4112452.
STRINGi10090.ENSMUSP00000046598.

Protein family/group databases

MEROPSiC48.002.

PTM databases

iPTMnetiP59110.
PhosphoSiteiP59110.

Proteomic databases

EPDiP59110.
MaxQBiP59110.
PaxDbiP59110.
PRIDEiP59110.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000044189; ENSMUSP00000046598; ENSMUSG00000033075.
GeneIDi223870.
KEGGimmu:223870.
UCSCiuc007xls.3. mouse.

Organism-specific databases

CTDi29843.
MGIiMGI:2445054. Senp1.

Phylogenomic databases

eggNOGiKOG0778. Eukaryota.
COG5160. LUCA.
GeneTreeiENSGT00530000062941.
HOGENOMiHOG000154286.
HOVERGENiHBG057384.
InParanoidiP59110.
KOiK08592.
OrthoDBiEOG7D59MP.
PhylomeDBiP59110.
TreeFamiTF316289.

Enzyme and pathway databases

BRENDAi3.4.22.B70. 3474.
ReactomeiR-MMU-3065679. SUMO is proteolytically processed.

Miscellaneous databases

ChiTaRSiSenp1. mouse.
PROiP59110.
SOURCEiSearch...

Gene expression databases

BgeeiP59110.
CleanExiMM_SENP1.
ExpressionAtlasiP59110. baseline and differential.
GenevisibleiP59110. MM.

Family and domain databases

InterProiIPR003653. Peptidase_C48_C.
IPR033387. SENP1.
[Graphical view]
PANTHERiPTHR12606:SF30. PTHR12606:SF30. 1 hit.
PfamiPF02902. Peptidase_C48. 1 hit.
[Graphical view]
PROSITEiPS50600. ULP_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Skin.
  2. "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].
    Strain: FVB/N.
    Tissue: Mammary cancer.
  3. "Mutation of SENP1/SuPr-2 reveals an essential role for desumoylation in mouse development."
    Yamaguchi T., Sharma P., Athanasiou M., Kumar A., Yamada S., Kuehn M.R.
    Mol. Cell. Biol. 25:5171-5182(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiSENP1_MOUSE
AccessioniPrimary (citable) accession number: P59110
Secondary accession number(s): Q8BTV5, Q8BZF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: November 28, 2002
Last modified: June 8, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.