Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Sentrin-specific protease 3

Gene

Senp3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protease that releases SUMO2 and SUMO3 monomers from sumoylated substrates, but has only weak activity against SUMO1 conjugates. Deconjugates SUMO2 from MEF2D, which increases its transcriptional activation capability. Deconjugates SUMO2 and SUMO3 from CDCA8. Redox sensor that, when redistributed into nucleoplasm, can act as an effector to enhance HIF1A transcriptional activity by desumoylating EP300. Required for rRNA processing through deconjugation of SUMO2 and SUMO3 from nucleophosmin. Plays a role in the regulation of sumoylation status of ZNF148. Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes.2 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.

Enzyme regulationi

On oxidative stress, SENP3 degradation is blocked by inhibition of its ubiquitination, which stabilizes it as it accumulates in the nucleoplasm.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei459 – 4591By similarity
Active sitei476 – 4761By similarity
Active sitei526 – 5261By similarity

GO - Molecular functioni

  • thiol-dependent ubiquitin-specific protease activity Source: MGI

GO - Biological processi

  • protein metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BRENDAi3.4.22.B72. 3474.

Protein family/group databases

MEROPSiC48.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Sentrin-specific protease 3 (EC:3.4.22.68)
Alternative name(s):
SUMO-1-specific protease 3
Sentrin/SUMO-specific protease SENP3
Smt3-specific isopeptidase 1
Short name:
Smt3ip1
Gene namesi
Name:Senp3
Synonyms:Smt3ip, Smt3ip1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2158736. Senp3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • MLL1 complex Source: UniProtKB
  • nucleolus Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 568568Sentrin-specific protease 3PRO_0000101722Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei71 – 711PhosphoserineCombined sources
Modified residuei73 – 731PhosphoserineCombined sources
Modified residuei163 – 1631PhosphoserineCombined sources
Modified residuei170 – 1701PhosphothreonineCombined sources
Modified residuei175 – 1751PhosphoserineCombined sources
Modified residuei182 – 1821PhosphoserineCombined sources
Modified residuei206 – 2061PhosphoserineCombined sources
Modified residuei226 – 2261PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9EP97.
MaxQBiQ9EP97.
PaxDbiQ9EP97.
PRIDEiQ9EP97.

PTM databases

iPTMnetiQ9EP97.
PhosphoSiteiQ9EP97.

Expressioni

Gene expression databases

BgeeiQ9EP97.
CleanExiMM_SENP3.
ExpressionAtlasiQ9EP97. baseline and differential.
GenevisibleiQ9EP97. MM.

Interactioni

Subunit structurei

Binds to SUMO1 and SUMO3. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with EP300, NPM1 and CDCA8 (By similarity). Component of the 5FMC complex, at least composed of PELP1, LAS1L, TEX10, WDR18 and SENP3; the complex interacts with methylated CHTOP and ZNF148. Interacts with NOL9. Interacts with CCAR2 (By similarity).By similarity1 Publication

Protein-protein interaction databases

BioGridi219830. 3 interactions.
DIPiDIP-59204N.
STRINGi10090.ENSMUSP00000005336.

Structurei

3D structure databases

ProteinModelPortaliQ9EP97.
SMRiQ9EP97. Positions 354-566.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni380 – 537158ProteaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi119 – 1224Nuclear localization signalSequence analysis
Motifi147 – 1537Nuclear localization signalSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi13 – 6654Pro-richAdd
BLAST
Compositional biasi70 – 8617Glu-richAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C48 family.Curated

Phylogenomic databases

eggNOGiKOG0778. Eukaryota.
COG5160. LUCA.
GeneTreeiENSGT00530000062941.
HOGENOMiHOG000154287.
HOVERGENiHBG059450.
InParanoidiQ9EP97.
KOiK08593.
OMAiFQMLLYS.
OrthoDBiEOG7D59MP.
PhylomeDBiQ9EP97.
TreeFamiTF316289.

Family and domain databases

InterProiIPR003653. Peptidase_C48_C.
[Graphical view]
PfamiPF02902. Peptidase_C48. 1 hit.
[Graphical view]
PROSITEiPS50600. ULP_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9EP97-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKETIQGTGS WGPEPPGPGT TYSNPRRERL RWPLPPKPRL KSGGGFGPDP
60 70 80 90 100
GSGTTVPTRR LPAPRPSFDA SASEEEEEEE EEDEEEVAAW RLPPRWGQLG
110 120 130 140 150
ASQRSRALRP SHRKTCSQRR RRAMRAFQML LYSKSTSLTF HWKLWGRHRG
160 170 180 190 200
RRRNLAHPKN HLSPQEGGAT PQVPSPCCRF DSPRGLPPPR LGLLGALMAE
210 220 230 240 250
DGMRGSPPVP SGPPMEEDGL RWTPKSPLDP DSGLLSCTLP NGFGGLSGPE
260 270 280 290 300
GERSLAPPDA SILISNVCSI GDHVAQELFQ SSDLGIAEEA DRTGEKAGQH
310 320 330 340 350
SPLREEHVTC VQSILDEFLQ TYGSLIPLST DEVVEKLEDI FQQEFSTPSR
360 370 380 390 400
KSLVLQLIQS YQRMPGNAMV RGFRVSYKRH VLTMDDLGTL YGQNWLNDQV
410 420 430 440 450
MNMYGDLVMD TVPEKVHFFN SFFYDKLRTK GYDGVKRWTK NVDIFNKELL
460 470 480 490 500
LIPIHLEVHW SLISVDVRRR TITYFDSQRT LNRRCPKHIA KYLQAEAVKK
510 520 530 540 550
DRLDFHQGWK GYFKMNVARQ NNDSDCGAFV LQYCKHLALS QPFSFTQQDM
560
PKLRRQIYKE LCHCKLTV
Length:568
Mass (Da):64,403
Last modified:March 1, 2001 - v1
Checksum:i655F1FAB1AB62EA8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti229 – 2291D → G in BAC32209 (PubMed:16141072).Curated
Sequence conflicti440 – 4401K → E in BAC40451 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF194031 mRNA. Translation: AAG28418.1.
AY008764 mRNA. Translation: AAG33253.1.
AK045071 mRNA. Translation: BAC32209.1.
AK088608 mRNA. Translation: BAC40451.1.
AL603707 Genomic DNA. Translation: CAI51945.1.
BC037014 mRNA. Translation: AAH37014.1.
CCDSiCCDS24905.1.
RefSeqiNP_001157043.1. NM_001163571.1.
NP_109627.3. NM_030702.4.
UniGeneiMm.284592.
Mm.422171.

Genome annotation databases

EnsembliENSMUST00000005336; ENSMUSP00000005336; ENSMUSG00000005204.
ENSMUST00000066760; ENSMUSP00000066581; ENSMUSG00000005204.
GeneIDi80886.
KEGGimmu:80886.
UCSCiuc007jrb.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF194031 mRNA. Translation: AAG28418.1.
AY008764 mRNA. Translation: AAG33253.1.
AK045071 mRNA. Translation: BAC32209.1.
AK088608 mRNA. Translation: BAC40451.1.
AL603707 Genomic DNA. Translation: CAI51945.1.
BC037014 mRNA. Translation: AAH37014.1.
CCDSiCCDS24905.1.
RefSeqiNP_001157043.1. NM_001163571.1.
NP_109627.3. NM_030702.4.
UniGeneiMm.284592.
Mm.422171.

3D structure databases

ProteinModelPortaliQ9EP97.
SMRiQ9EP97. Positions 354-566.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi219830. 3 interactions.
DIPiDIP-59204N.
STRINGi10090.ENSMUSP00000005336.

Protein family/group databases

MEROPSiC48.003.

PTM databases

iPTMnetiQ9EP97.
PhosphoSiteiQ9EP97.

Proteomic databases

EPDiQ9EP97.
MaxQBiQ9EP97.
PaxDbiQ9EP97.
PRIDEiQ9EP97.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000005336; ENSMUSP00000005336; ENSMUSG00000005204.
ENSMUST00000066760; ENSMUSP00000066581; ENSMUSG00000005204.
GeneIDi80886.
KEGGimmu:80886.
UCSCiuc007jrb.2. mouse.

Organism-specific databases

CTDi26168.
MGIiMGI:2158736. Senp3.

Phylogenomic databases

eggNOGiKOG0778. Eukaryota.
COG5160. LUCA.
GeneTreeiENSGT00530000062941.
HOGENOMiHOG000154287.
HOVERGENiHBG059450.
InParanoidiQ9EP97.
KOiK08593.
OMAiFQMLLYS.
OrthoDBiEOG7D59MP.
PhylomeDBiQ9EP97.
TreeFamiTF316289.

Enzyme and pathway databases

BRENDAi3.4.22.B72. 3474.

Miscellaneous databases

NextBioi350207.
PROiQ9EP97.
SOURCEiSearch...

Gene expression databases

BgeeiQ9EP97.
CleanExiMM_SENP3.
ExpressionAtlasiQ9EP97. baseline and differential.
GenevisibleiQ9EP97. MM.

Family and domain databases

InterProiIPR003653. Peptidase_C48_C.
[Graphical view]
PfamiPF02902. Peptidase_C48. 1 hit.
[Graphical view]
PROSITEiPS50600. ULP_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel mammalian Smt3-specific isopeptidase 1 (SMT3IP1) localized in the nucleolus at interphase."
    Nishida T., Tanaka H., Yasuda H.
    Eur. J. Biochem. 267:6423-6427(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, FUNCTION.
    Tissue: T-cell lymphoma.
  2. "Ubiquitin-like proteins: new wines in new bottles."
    Yeh E.T.H., Gong L., Kamitani T.
    Gene 248:1-14(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
  3. "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: NOD.
    Tissue: Embryo and Thymus.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "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].
    Tissue: Mammary tumor.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-73; SER-163; THR-170; SER-175; SER-182; SER-206 AND SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. "Five friends of methylated chromatin target of protein-arginine-methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation to desumoylation."
    Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J., Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S., van Dijk T.B.
    Mol. Cell. Proteomics 11:1263-1273(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE 5FMC COMPLEX, INTERACTION OF THE 5FMC COMPLEX WITH CHTOP AND ZNF148, INTERACTION WITH NOL9, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiSENP3_MOUSE
AccessioniPrimary (citable) accession number: Q9EP97
Secondary accession number(s): Q5F2A5, Q8BRD5, Q8C2H5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: March 1, 2001
Last modified: May 11, 2016
This is version 117 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.