SubmitCancel

Skip Header

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

P52479

- UBP10_MOUSE

UniProt

P52479 - UBP10_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ubiquitin carboxyl-terminal hydrolase 10

Gene
Usp10, Kiaa0190, Ode-1, Uchrp
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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 regulationi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei418 – 4181Nucleophile By similarity
Active sitei743 – 7431Proton acceptor By similarity

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: UniProtKB
  2. ion channel binding Source: UniProtKB
  3. p53 binding Source: UniProtKB
  4. ubiquitin-specific protease activity Source: UniProtKB
  5. ubiquitin thiolesterase activity Source: UniProtKB

GO - Biological processi

  1. autophagy Source: UniProtKB-KW
  2. DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
  3. DNA repair Source: UniProtKB-KW
  4. protein deubiquitination Source: UniProtKB
  5. regulation of autophagy Source: UniProtKB
  6. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Autophagy, DNA damage, DNA repair, Ubl conjugation pathway

Protein family/group databases

MEROPSiC19.018.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Usp10
Synonyms:Kiaa0190, Ode-1, Uchrp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:894652. Usp10.

Subcellular locationi

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.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. early endosome Source: UniProtKB
  3. intermediate filament cytoskeleton Source: Ensembl
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 792791Ubiquitin carboxyl-terminal hydrolase 10PRO_0000080630Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei24 – 241Phosphothreonine By similarity
Modified residuei223 – 2231Phosphoserine By similarity
Modified residuei330 – 3301Phosphoserine; by ATM By similarity
Modified residuei359 – 3591Phosphoserine1 Publication
Modified residuei364 – 3641Phosphoserine By similarity
Modified residuei570 – 5701Phosphoserine3 Publications

Post-translational modificationi

Phosphorylated by ATM following DNA damage, leading to stablization and translocation it to the nucleus By similarity.
Ubiquitinated. Deubiquitinated by USP13 By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP52479.
PRIDEiP52479.

PTM databases

PhosphoSiteiP52479.

Expressioni

Gene expression databases

ArrayExpressiP52479.
BgeeiP52479.
CleanExiMM_USP10.
GenevestigatoriP52479.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi204424. 3 interactions.
IntActiP52479. 4 interactions.
MINTiMINT-1870263.

Structurei

3D structure databases

ProteinModelPortaliP52479.
SMRiP52479. Positions 410-790.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini409 – 789381USPAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 9998Interaction with p53/TP53 By similarityAdd
BLAST

Sequence similaritiesi

Contains 1 USP domain.

Phylogenomic databases

GeneTreeiENSGT00550000074994.
HOVERGENiHBG059823.
InParanoidiQ6ZQG9.
KOiK11841.
OMAiGQEYQRI.
OrthoDBiEOG7Z69BX.
PhylomeDBiP52479.
TreeFamiTF323203.

Family and domain databases

InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR028767. USP10.
[Graphical view]
PANTHERiPTHR24006:SF69. PTHR24006:SF69. 1 hit.
PfamiPF00443. UCH. 1 hit.
[Graphical view]
PROSITEiPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P52479-1) [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

MALHNPQYIF GDFSPDEFNQ FFVTPRSSVE LPPYSGTLCS IQAEDELPDG    50
QEHQRIEFGV DEVIEPSEGL PPTPSYSISS TLNPQAPEFI LGCTTSKKIP 100
EAVEKDETYS SIDQYPASAL ALESNSNAEA ETLENDSGAG GLGQRERKKK 150
KKRPPGYYSY LKDGGEDSAS PATLVNGHAT SVGTSGEAVE DAEFMDVLPP 200
VMPRTCDSPQ NPVDFISGPV PDSPFPRTLG GDARTAGLCE GCHEADFEQP 250
CLPADSLLRT AGTQPYVGTD TTENFAVANG KILESPGEDT AANGAELHTD 300
EGADLDPAKP ESQSPPAESA LSASGAIPIS QPAKSWASLF HDSKPSASSP 350
MAYVETKCSP PVPSPLASEK QMEVKEGLVP VSEDPVAIKI AELLETVTLI 400
HKPVSLQPRG LINKGNWCYI NATLQALVAC PPMYHLMKFI PLYSKVQRPC 450
TSTPMIDSFV RLMNEFTNMP VPPKPRQALG DKIVRDIRPG AAFEPTYIYR 500
LLTVIKSSLS EKGRQEDAEE YLGFILNGLH EEMLSLKKLL SPTHEKHSVS 550
NGPRSDLIED EELEDTGKGS EDEWEQVGPK NKTSITRQAD FVQTPITGIF 600
GGHIRSVVYQ QSSKESATLQ LFFTLQLDIQ SDKIRTVQDA LESLVARESV 650
QGYTTKTKQE VEVSRRVTLE KLPPVLVLHL KRFVYEKTGG CQKLVKNIDY 700
PVDLEISREL LSPGIKNKNF KCQRTYRLFA VVYHHGNSAT GGHYTTDVFQ 750
IGLNGWLRID DQTVKVINQY QVVKPPADRT AYLLYYRRVD LL 792
Length:792
Mass (Da):87,022
Last modified:March 23, 2010 - v3
Checksum:i02D07A8194215D09
GO
Isoform 2 (identifier: P52479-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:793
Mass (Da):87,093
Checksum:iAC67428E5DBC3D9F
GO

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei49 – 491D → DA in isoform 2. VSP_038870

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 721P → R in AAH07134. 1 Publication
Sequence conflicti101 – 1011E → D in AAH07134. 1 Publication
Sequence conflicti293 – 2931N → S in AAH07134. 1 Publication
Sequence conflicti347 – 3471A → S in AAH07134. 1 Publication
Sequence conflicti448 – 4481R → G in BAE34291. 1 Publication
Sequence conflicti472 – 4721P → T in BAE32139. 1 Publication
Sequence conflicti528 – 5281G → R in BAE38053. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS40495.1. [P52479-2]
RefSeqiNP_033488.1. NM_009462.1. [P52479-2]
XP_006530910.1. XM_006530847.1. [P52479-1]
UniGeneiMm.256910.
Mm.421337.

Genome annotation databases

EnsembliENSMUST00000108988; ENSMUSP00000104616; ENSMUSG00000031826. [P52479-1]
ENSMUST00000144458; ENSMUSP00000123590; ENSMUSG00000031826. [P52479-2]
GeneIDi22224.
KEGGimmu:22224.
UCSCiuc009nqn.1. mouse. [P52479-2]
uc009nqo.1. mouse. [P52479-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS40495.1. [P52479-2 ]
RefSeqi NP_033488.1. NM_009462.1. [P52479-2 ]
XP_006530910.1. XM_006530847.1. [P52479-1 ]
UniGenei Mm.256910.
Mm.421337.

3D structure databases

ProteinModelPortali P52479.
SMRi P52479. Positions 410-790.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204424. 3 interactions.
IntActi P52479. 4 interactions.
MINTi MINT-1870263.

Protein family/group databases

MEROPSi C19.018.

PTM databases

PhosphoSitei P52479.

Proteomic databases

MaxQBi P52479.
PRIDEi P52479.

Protocols and materials databases

DNASUi 22224.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000108988 ; ENSMUSP00000104616 ; ENSMUSG00000031826 . [P52479-1 ]
ENSMUST00000144458 ; ENSMUSP00000123590 ; ENSMUSG00000031826 . [P52479-2 ]
GeneIDi 22224.
KEGGi mmu:22224.
UCSCi uc009nqn.1. mouse. [P52479-2 ]
uc009nqo.1. mouse. [P52479-1 ]

Organism-specific databases

CTDi 9100.
MGIi MGI:894652. Usp10.
Rougei Search...

Phylogenomic databases

GeneTreei ENSGT00550000074994.
HOVERGENi HBG059823.
InParanoidi Q6ZQG9.
KOi K11841.
OMAi GQEYQRI.
OrthoDBi EOG7Z69BX.
PhylomeDBi P52479.
TreeFami TF323203.

Miscellaneous databases

ChiTaRSi USP10. mouse.
NextBioi 302247.
PROi P52479.
SOURCEi Search...

Gene expression databases

ArrayExpressi P52479.
Bgeei P52479.
CleanExi MM_USP10.
Genevestigatori P52479.

Family and domain databases

InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR028767. USP10.
[Graphical view ]
PANTHERi PTHR24006:SF69. PTHR24006:SF69. 1 hit.
Pfami PF00443. UCH. 1 hit.
[Graphical view ]
PROSITEi PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  7. 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].

Entry informationi

Entry nameiUBP10_MOUSE
AccessioniPrimary (citable) accession number: P52479
Secondary accession number(s): Q3T9L4
, Q3TNN5, Q3TZB8, Q3U5E0, Q6ZQG9, Q91VY7
Entry historyi
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 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

External Data

Dasty 3

Similar proteinsi