Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q3KR59 (UBP10_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length794 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

Ontologies

Keywords
   Biological processAutophagy
DNA damage
DNA repair
Ubl conjugation pathway
   Cellular componentCytoplasm
Endosome
Nucleus
   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_componentearly 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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 794793Ubiquitin carboxyl-terminal hydrolase 10
PRO_0000393000

Regions

Domain411 – 791381USP
Region2 – 9998Interaction with p53/TP53 By similarity

Sites

Active site4201Nucleophile By similarity
Active site7451Proton acceptor By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue241Phosphothreonine By similarity
Modified residue991Phosphothreonine By similarity
Modified residue2241Phosphoserine By similarity
Modified residue3321Phosphoserine; by ATM By similarity
Modified residue3611Phosphoserine By similarity
Modified residue3661Phosphoserine By similarity
Modified residue5721Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3KR59 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: F8D1A3D6C66D0926

FASTA79487,311
        10         20         30         40         50         60 
MALHNPQYIF GDFSPDEFNQ FFVTPRSSVE LPPYSGTQCG IQAEEELLDG QEHQRIEFGV 

        70         80         90        100        110        120 
DEVIEPSDGL QRAPSYSISS TLNPQAPEFI LGCPTSKKTP DDIEKDETYS SIDQYPASAL 

       130        140        150        160        170        180 
ALESSSNAEA ETLENDSGAG GLGQRERKKK KKRPPGYYSY LKDGSEEGAS PAALVNGHAT 

       190        200        210        220        230        240 
SVGTNSEGVE DPEFMVDMLP SVMPRTCDSP QNPMDLISDP VPDSPFPRTL GGDARTAGLP 

       250        260        270        280        290        300 
EGCRETDFEQ PCLPTDNLLR TAVTQPNAGA DTTENLAVAN GKILESLGEG TAAANGVELH 

       310        320        330        340        350        360 
TDESADLDPA KPESQSPPAE SALSVSGAIS ISQPAKSWAS LFHDSKPSSS SPVAYVETKC 

       370        380        390        400        410        420 
SPPVPSPLAS EKQMEVKEGL VPVSEDPVAI KIAELLETVT LVHKPVSLQP RGLINKGNWC 

       430        440        450        460        470        480 
YINATLQALV ACPPMYHLMK FIPLYSKVQR PCTSTPMIDS FVRLMNEFTN MPVPPKPRQA 

       490        500        510        520        530        540 
LGDKIVRDIR PGAAFEPTYI YRLLTVIKSS LSEKGRQEDA EEYLGFILNG LHEEMLSLKK 

       550        560        570        580        590        600 
LLSPTHEKHS VSNGPGSHLI EDEELEDTGE GSEDEWEQVG PKNKTSVTRQ ADFVQTPITG 

       610        620        630        640        650        660 
IFGGHIRSVV YQQSSKESAT LQPFFTLQLD IQSDKIRTVQ DALESLVARE SVQGYTTKTK 

       670        680        690        700        710        720 
QEVEVSRRVT LEKLPPVLVL HLKRFVYEKT GGCQKLVKNI EYPVDLEISR ELLSPGVKNK 

       730        740        750        760        770        780 
NFKCHRTYRL FAVVYHHGNS ATGGHYTTDV FQIGLNGWLR IDDQTVKVIN QYQVVRPSAD 

       790 
RTAYLLYYRR VDLL 

« Hide

References

[1]"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: Spleen.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC105892 mRNA. Translation: AAI05893.1.
RefSeqNP_001029318.1. NM_001034146.1.
UniGeneRn.24862.

3D structure databases

ProteinModelPortalQ3KR59.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000022432.

Protein family/group databases

MEROPSC19.018.

PTM databases

PhosphoSiteQ3KR59.

Proteomic databases

PaxDbQ3KR59.
PRIDEQ3KR59.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000022432; ENSRNOP00000022432; ENSRNOG00000016509.
GeneID307905.
KEGGrno:307905.
UCSCRGD:1561965. rat.

Organism-specific databases

CTD9100.
RGD1561965. Usp10.

Phylogenomic databases

eggNOGCOG5533.
GeneTreeENSGT00550000074994.
HOGENOMHOG000285959.
HOVERGENHBG059823.
InParanoidQ3KR59.
KOK11841.
OMAGQEYQRI.
OrthoDBEOG7Z69BX.
TreeFamTF323203.

Gene expression databases

GenevestigatorQ3KR59.

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

NextBio658066.
PROQ3KR59.

Entry information

Entry nameUBP10_RAT
AccessionPrimary (citable) accession number: Q3KR59
Entry history
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: November 8, 2005
Last modified: March 19, 2014
This is version 60 of the entry and version 1 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