Ubiquitin carboxyl-terminal hydrolase 10

Names and origin

Protein names

Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 10
    EC=3.1.2.15
Alternative name(s):
    Ubiquitin thioesterase 10
    Ubiquitin-specific-processing protease 10
    Deubiquitinating enzyme 10

Gene names

Name:	USP10
Synonyms:	KIAA0190

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	798 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Ubiquitin specific protease are required to remove ubiquitin from specific proteins or peptides to which ubiquitin is attached. Ref.1
Catalytic activity	Ubiquitin C-terminal thioester + H₂O = ubiquitin + a thiol.
Subunit structure	Interacts with G3BP, which may regulate its function. Ref.1
Tissue specificity	Widely expressed. Ref.1
Sequence similarities	Belongs to the peptidase C19 family.

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Ontologies

Keywords
Biological process	Ubl conjugation pathway
Coding sequence diversity	Polymorphism
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin thiolesterase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 798

798

Ubiquitin carboxyl-terminal hydrolase 10

PRO_0000080629

Sites

Active site

424

1

By similarity

Active site

741

1

By similarity

Active site

749

1

By similarity

Amino acid modifications

Modified residue

100

1

Phosphothreonine Ref.12

Modified residue

208

1

Phosphothreonine By similarity

Modified residue

211

1

Phosphoserine Ref.6

Modified residue

220

1

Phosphoserine Ref.12

Modified residue

226

1

Phosphoserine Ref.12

Modified residue

364

1

Phosphotyrosine Ref.8

Modified residue

365

1

Phosphoserine Ref.8

Modified residue

370

1

Phosphoserine Ref.12 Ref.8

Modified residue

563

1

Phosphoserine Ref.12

Modified residue

576

1

Phosphoserine Ref.12 Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.13

Natural variations

Natural variant

200

1

M → V: dbSNP rs1862792. Ref.3

VAR_015859

Natural variant

203

1

S → P: dbSNP rs2326391. Ref.5

VAR_015860

Natural variant

204

1

V → L: dbSNP rs1812061. Ref.5

VAR_015861

Experimental info

Mutagenesis

424

1

C → A: Abolishes de-ubiquitinating activity. Ref.1

Sequence conflict

1

M → MCSKDTVLSVCALYWRKGIQ SHTPLIGAWRRGKQREQPED RGVPMKRAA Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

Q14694-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: E6BA77E2B5CE2B3F
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FASTA

798

87,134

        10         20         30         40         50         60 
MALHSPQYIF GDFSPDEFNQ FFVTPRSSVE LPPYSGTVLC GTQAVDKLPD GQEYQRIEFG 

        70         80         90        100        110        120 
VDEVIEPSDT LPRTPSYSIS STLNPQAPEF ILGCTASKIT PDGITKEASY GSIDCQYPGS 

       130        140        150        160        170        180 
ALALDGSSNV EAEVLENDGV SGGLGQRERK KKKKRPPGYY SYLKDGGDDS ISTEALVNGH 

       190        200        210        220        230        240 
ANSAVPNSVS AEDAEFMGDM PPSVTPRTCN SPQNSTDSVS DIVPDSPFPG ALGSDTRTAG 

       250        260        270        280        290        300 
QPEGGPGADF GQSCFPAEAG RDTLSRTAGA QPCVGTDTTE NLGVANGQIL ESSGEGTATN 

       310        320        330        340        350        360 
GVELHTTESI DLDPTKPESA SPPADGTGSA SGTLPVSQPK SWASLFHDSK PSSSSPVAYV 

       370        380        390        400        410        420 
ETKYSPPAIS PLVSEKQVEV KEGLVPVSED PVAIKIAELL ENVTLIHKPV SLQPRGLINK 

       430        440        450        460        470        480 
GNWCYINATL QALVACPPMY HLMKFIPLYS KVQRPCTSTP MIDSFVRLMN EFTNMPVPPK 

       490        500        510        520        530        540 
PRQALGDKIV RDIRPGAAFE PTYIYRLLTV NKSSLSEKGR QEDAEEYLGF ILNGLHEEML 

       550        560        570        580        590        600 
NLKKLLSPSN EKLTISNGPK NHSVNEEEQE EQGEGSEDEW EQVGPRNKTS VTRQADFVQT 

       610        620        630        640        650        660 
PITGIFGGHI RSVVYQQSSK ESATLQPFFT LQLDIQSDKI RTVQDALESL VARESVQGYT 

       670        680        690        700        710        720 
TKTKQEVEIS RRVTLEKLPP VLVLHLKRFV YEKTGGCQKL IKNIEYPVDL EISKELLSPG 

       730        740        750        760        770        780 
VKNKNFKCHR TYRLFAVVYH HGNSATGGHY TTDVFQIGLN GWLRIDDQTV KVINQYQVVK 

       790 
PTAERTAYLL YYRRVDLL

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Ras-GAP SH3 domain binding protein (G3BP) is a modulator of USP10, a novel human ubiquitin specific protease." Soncini C., Berdo I., Draetta G. Oncogene 20:3869-3879(2001) [PubMed: 11439350] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH G3BP, MUTAGENESIS OF CYS-424.
[2]	"Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1." Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N. DNA Res. 3:17-24(1996) [PubMed: 8724849] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Bone marrow.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[4]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-200. Tissue: Melanoma and Retina.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS PRO-203 AND LEU-204. Tissue: Brain.
[6]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211 AND SER-576, MASS SPECTROMETRY. Tissue: Epithelium.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, MASS SPECTROMETRY. Tissue: Epithelium.
[8]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-364; SER-365 AND SER-370, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line." Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S. Electrophoresis 28:2027-2034(2007) [PubMed: 17487921] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, MASS SPECTROMETRY.
[10]	"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction." Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R. Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed: 17693683] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, MASS SPECTROMETRY.
[11]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, MASS SPECTROMETRY.
[12]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-100; SER-220; SER-226; SER-370; SER-563 AND SER-576, MASS SPECTROMETRY.
[13]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, MASS SPECTROMETRY. Tissue: Liver.
[14]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	D80012 mRNA. Translation: BAA11507.1. Different initiation. AK315570 mRNA. Translation: BAG37945.1. AL162049 mRNA. Translation: CAB82392.2. BX537402 mRNA. Translation: CAD97644.1. Different initiation. BC000263 mRNA. Translation: AAH00263.1.
IPI	IPI00291946.
RefSeq	NP_005144.2.
UniGene	Hs.136778
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	C19.018.
PTM databases
PhosphoSite	Q14694.
Proteomic databases
PRIDE	Q14694.
Genome annotation databases
Ensembl	ENSG00000103194. Homo sapiens. [Contig view]
GeneID	9100.
KEGG	hsa:9100.
Organism-specific databases
GeneCards	GC16P083291.
H-InvDB	HIX0013304.
HGNC	HGNC:12608. USP10.
HPA	HPA006731. HPA006749.
MIM	609818. gene.
PharmGKB	PA27520.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q14694.
HOVERGEN	Q14694.
Enzyme and pathway databases
BRENDA	3.1.2.15. 247.
Gene expression databases
ArrayExpress	Q14694.
Bgee	Q14694.
CleanEx	HS_USP10.
GermOnline	ENSG00000103194. Homo sapiens.
Family and domain databases
InterPro	IPR009818. Ataxin-2_C. IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. [Graphical view]
Pfam	PF07145. PAM2. 1 hit. PF00443. UCH. 1 hit. [Graphical view]
PROSITE	PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	34113.
SOURCE	Search...

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Entry information

Entry name

UBP10_HUMAN

Accession

Primary (citable) accession number: Q14694
Secondary accession number(s): B2RDJ8, Q9BWG7, Q9NSL7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Human chromosome 16: entries, gene names and cross-references to MIM

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents