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P52479 (UBP10_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase 10

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 10
Ubiquitin thioesterase 10
Ubiquitin-specific-processing protease 10
Gene names
Name:Usp10
Synonyms:Kiaa0190, Ode-1, Uchrp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length792 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolase that can remove conjugated ubiquitin from target proteins such as p53/TP53, BECN1, SNX3 and CFTR. Acts as an essential regulator of p53/TP53 stability: in unstressed cells, specifically deubiquitinates p53/TP53 in the cytoplasm, leading to counteract MDM2 action and stabilize p53/TP53. Following DNA damage, translocates to the nucleus and deubiquitinates p53/TP53, leading to regulate the p53/TP53-dependent DNA damage response. Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. In turn, PIK3C3/VPS34-containing complexes regulate USP10 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Does not deubiquitinate MDM2. Deubiquitinates CFTR in early endosomes, enhancing its endocytic recycling By similarity.

Catalytic activity

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

Enzyme regulation

Specifically inhibited by spautin-1 (specific and potent autophagy inhibitor-1), a derivative of MBCQ that binds to USP10 and inhibits deubiquitinase activity. Regulated by PIK3C3/VPS34-containing complexes By similarity.

Subunit structure

Interacts with G3BP, which may regulate its function. Interacts with p53/TP53, SNX3 and CFTR By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Early endosome By similarity. Note: Cytoplasmic in normal conditions. After DNA damage, translocates to the nucleus following phosphorylation by ATM By similarity.

Post-translational modification

Phosphorylated by ATM following DNA damage, leading to stablization and translocation it to the nucleus By similarity.

Ubiquitinated. Deubiquitinated by USP13 By similarity.

Sequence similarities

Belongs to the peptidase C19 family. USP10 subfamily.

Contains 1 USP domain.

Sequence caution

The sequence BAC97893.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processAutophagy
DNA damage
DNA repair
Ubl conjugation pathway
   Cellular componentCytoplasm
Endosome
Nucleus
   Coding sequence diversityAlternative splicing
   Molecular functionHydrolase
Protease
Thiol protease
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator

Inferred from sequence or structural similarity. Source: UniProtKB

DNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

autophagy

Inferred from electronic annotation. Source: UniProtKB-KW

protein deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of autophagy

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

early endosome

Inferred from sequence or structural similarity. Source: UniProtKB

intermediate filament cytoskeleton

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncysteine-type endopeptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

ion channel binding

Inferred from sequence or structural similarity. Source: UniProtKB

p53 binding

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin thiolesterase activity

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin-specific protease activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P52479-1)

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.
Isoform 2 (identifier: P52479-2)

The sequence of this isoform differs from the canonical sequence as follows:
     49-49: D → DA

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 792791Ubiquitin carboxyl-terminal hydrolase 10
PRO_0000080630

Regions

Domain409 – 789381USP
Region2 – 9998Interaction with p53/TP53 By similarity

Sites

Active site4181Nucleophile By similarity
Active site7431Proton acceptor By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue241Phosphothreonine By similarity
Modified residue2231Phosphoserine By similarity
Modified residue3301Phosphoserine; by ATM By similarity
Modified residue3591Phosphoserine Ref.6
Modified residue3641Phosphoserine By similarity
Modified residue5701Phosphoserine Ref.7 Ref.8 Ref.9

Natural variations

Alternative sequence491D → DA in isoform 2.
VSP_038870

Experimental info

Sequence conflict721P → R in AAH07134. Ref.5
Sequence conflict1011E → D in AAH07134. Ref.5
Sequence conflict2931N → S in AAH07134. Ref.5
Sequence conflict3471A → S in AAH07134. Ref.5
Sequence conflict4481R → G in BAE34291. Ref.3
Sequence conflict4721P → T in BAE32139. Ref.3
Sequence conflict5281G → R in BAE38053. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 23, 2010. Version 3.
Checksum: 02D07A8194215D09

FASTA79287,022
        10         20         30         40         50         60 
MALHNPQYIF GDFSPDEFNQ FFVTPRSSVE LPPYSGTLCS IQAEDELPDG QEHQRIEFGV 

        70         80         90        100        110        120 
DEVIEPSEGL PPTPSYSISS TLNPQAPEFI LGCTTSKKIP EAVEKDETYS SIDQYPASAL 

       130        140        150        160        170        180 
ALESNSNAEA ETLENDSGAG GLGQRERKKK KKRPPGYYSY LKDGGEDSAS PATLVNGHAT 

       190        200        210        220        230        240 
SVGTSGEAVE DAEFMDVLPP VMPRTCDSPQ NPVDFISGPV PDSPFPRTLG GDARTAGLCE 

       250        260        270        280        290        300 
GCHEADFEQP CLPADSLLRT AGTQPYVGTD TTENFAVANG KILESPGEDT AANGAELHTD 

       310        320        330        340        350        360 
EGADLDPAKP ESQSPPAESA LSASGAIPIS QPAKSWASLF HDSKPSASSP MAYVETKCSP 

       370        380        390        400        410        420 
PVPSPLASEK QMEVKEGLVP VSEDPVAIKI AELLETVTLI HKPVSLQPRG LINKGNWCYI 

       430        440        450        460        470        480 
NATLQALVAC PPMYHLMKFI PLYSKVQRPC TSTPMIDSFV RLMNEFTNMP VPPKPRQALG 

       490        500        510        520        530        540 
DKIVRDIRPG AAFEPTYIYR LLTVIKSSLS EKGRQEDAEE YLGFILNGLH EEMLSLKKLL 

       550        560        570        580        590        600 
SPTHEKHSVS NGPRSDLIED EELEDTGKGS EDEWEQVGPK NKTSITRQAD FVQTPITGIF 

       610        620        630        640        650        660 
GGHIRSVVYQ QSSKESATLQ LFFTLQLDIQ SDKIRTVQDA LESLVARESV QGYTTKTKQE 

       670        680        690        700        710        720 
VEVSRRVTLE KLPPVLVLHL KRFVYEKTGG CQKLVKNIDY PVDLEISREL LSPGIKNKNF 

       730        740        750        760        770        780 
KCQRTYRLFA VVYHHGNSAT GGHYTTDVFQ IGLNGWLRID DQTVKVINQY QVVKPPADRT 

       790 
AYLLYYRRVD LL 

« Hide

Isoform 2 [UniParc].

Checksum: AC67428E5DBC3D9F
Show »

FASTA79387,093

References

« Hide 'large scale' references
[1]"Cloning from a mouse osteoblastic cell line of a gene, encoding a ubiquitin carboxyl-terminal hydrolase related polypeptide, down regulated during ascorbic acid dependent differentiation."
Ito M., Hitomi K., Tsukagoshi N.
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Embryonic tail.
[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. expand/collapse author list , 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] (ISOFORMS 1 AND 2).
Strain: C57BL/6J and NOD.
Tissue: Inner ear, Spleen and Thymus.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORM 1).
Tissue: Mammary tumor.
[6]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[7]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[8]"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[9]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D84096 mRNA. Translation: BAA12220.1.
AK129083 mRNA. Translation: BAC97893.1. Different initiation.
AK153675 mRNA. Translation: BAE32139.1.
AK157970 mRNA. Translation: BAE34291.1.
AK165156 mRNA. Translation: BAE38053.1.
AK172443 mRNA. Translation: BAE43006.1.
CH466525 Genomic DNA. Translation: EDL11620.1.
BC007134 mRNA. Translation: AAH07134.1.
CCDSCCDS40495.1. [P52479-2]
RefSeqNP_033488.1. NM_009462.1. [P52479-2]
XP_006530910.1. XM_006530847.1. [P52479-1]
UniGeneMm.256910.
Mm.421337.

3D structure databases

ProteinModelPortalP52479.
SMRP52479. Positions 410-790.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204424. 3 interactions.
IntActP52479. 4 interactions.
MINTMINT-1870263.

Protein family/group databases

MEROPSC19.018.

PTM databases

PhosphoSiteP52479.

Proteomic databases

MaxQBP52479.
PRIDEP52479.

Protocols and materials databases

DNASU22224.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000108988; ENSMUSP00000104616; ENSMUSG00000031826. [P52479-1]
ENSMUST00000144458; ENSMUSP00000123590; ENSMUSG00000031826. [P52479-2]
GeneID22224.
KEGGmmu:22224.
UCSCuc009nqn.1. mouse. [P52479-2]
uc009nqo.1. mouse. [P52479-1]

Organism-specific databases

CTD9100.
MGIMGI:894652. Usp10.
RougeSearch...

Phylogenomic databases

GeneTreeENSGT00550000074994.
HOVERGENHBG059823.
InParanoidQ6ZQG9.
KOK11841.
OMAGQEYQRI.
OrthoDBEOG7Z69BX.
PhylomeDBP52479.
TreeFamTF323203.

Gene expression databases

ArrayExpressP52479.
BgeeP52479.
CleanExMM_USP10.
GenevestigatorP52479.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR028767. USP10.
[Graphical view]
PANTHERPTHR24006:SF69. PTHR24006:SF69. 1 hit.
PfamPF00443. UCH. 1 hit.
[Graphical view]
PROSITEPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUSP10. mouse.
NextBio302247.
PROP52479.
SOURCESearch...

Entry information

Entry nameUBP10_MOUSE
AccessionPrimary (citable) accession number: P52479
Secondary accession number(s): Q3T9L4 expand/collapse secondary AC list , Q3TNN5, Q3TZB8, Q3U5E0, Q6ZQG9, Q91VY7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: March 23, 2010
Last modified: July 9, 2014
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot