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Protein Page:
USP10 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
USP10 a carboxyl-terminal ubiquitin-processing protease. Ras-GAP SH3 domain-binding protein (G3BP) appears to inhibit its ability to disassemble ubiquitin chains. Note: This description may include information from UniProtKB.
Protein type: Ubiquitin-specific protease; Ubiquitin conjugating system; Protease; EC 3.4.19.12; EC 3.1.2.15
Cellular Component: cytoplasm; early endosome; nucleus
Molecular Function: ubiquitin thiolesterase activity; protein binding; p53 binding; cysteine-type endopeptidase activity; ubiquitin-specific protease activity
Biological Process: ubiquitin-dependent protein catabolic process; protein deubiquitination; DNA damage response, signal transduction by p53 class mediator; autophagy; regulation of autophagy; DNA repair
Reference #:  Q14694 (UniProtKB)
Alt. Names/Synonyms: Deubiquitinating enzyme 10; KIAA0190; MGC2621; Ubiquitin carboxyl-terminal hydrolase 10; ubiquitin specific peptidase 10; ubiquitin specific protease 10; Ubiquitin thioesterase 10; Ubiquitin-specific-processing protease 10; UBP10; UBPO; USP10
Gene Symbols: USP10
Molecular weight: 87,134 Da
Basal Isoelectric point: 5.19  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

USP10

Protein Structure Not Found.


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Sites Implicated In
carcinogenesis, inhibited: T42‑p, S337‑p
cell growth, altered: T42‑p, S337‑p
intracellular localization: T42‑p, S337‑p
protein stabilization: T42‑p, S337‑p
ubiquitination: T42‑p, S337‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 S5-p ___MALHsPQYIFGD
0 1 S14-p QYIFGDFsPDEFNQF
0 1 T24-p EFNQFFVtPRSSVEL
1 0 T42-p SGTVLCGtQAVDKLP
0 12 Y54-p KLPDGQEyQRIEFGV
0 1 S68-p VDEVIEPsDtLPRtP
0 1 T70-p EVIEPsDtLPRtPsy
0 8 T74-p PsDtLPRtPsySISS
0 8 S76-p DtLPRtPsySISStL
0 3 Y77-p tLPRtPsySISStLN
0 3 T82-p PsySISStLNPQAPE
0 1 T95-p PEFILGCtASKItPD
0 2 T100-p GCtASKItPDGITKE
0 2 Y110-p GITKEASyGSIDCQY
0 19 Y159-p KKKRPPGyysyLKDG
0 12 Y160-p KKRPPGyysyLKDGG
0 5 S161-p KRPPGyysyLKDGGD
0 15 Y162-p RPPGyysyLKDGGDD
0 6 T205-p GDMPPSVtPRtCNsP
0 7 T208-p PPSVtPRtCNsPQNs
0 27 S211-p VtPRtCNsPQNstDs
0 2 S215-p tCNsPQNstDsVSDI
0 3 T216-p CNsPQNstDsVSDIV
0 2 S218-p sPQNstDsVSDIVPD
0 19 S226-p VSDIVPDsPFPGALG
0 7 T263-p PAEAGRDtLSRTAGA
1 0 S337-p ASGTLPVsQPKSWAS
0 1 S355-p DSKPSSSsPVAyVET
0 18 Y359-p SSSsPVAyVETKysP
0 4 Y364-p VAyVETKysPPAIsP
0 16 S365-p AyVETKysPPAIsPL
0 7 S370-p KysPPAIsPLVSEKQ
0 2 K395-u SEDPVAIkIAELLEN
0 2 K408-u ENVTLIHkPVSLQPR
0 1 K451 KFIPLYSKVQRPCTS
0 7 S547-p LNLKKLLsPsNEKLT
0 2 S549-p LKKLLsPsNEKLTIS
0 2 S563-p SNGPKNHsVNEEEQE
0 2 Q572 NEEEQEEQGEGsEDE
0 70 S576-p QEEQGEGsEDEWEQV
0 2 Y659-p ARESVQGyTTKTKQE
0 1 K677 SRRVTLEKLPPVLVL
0 1 K702 GGCQKLIKNIEYPVD
0 2 S718-p EISKELLsPGVKNKN
0 1 K780-u INQYQVVkPTAERTA
  mouse

 
N5 ___MALHNPQYIFGD
S14 QYIFGDFSPDEFNQF
T24 EFNQFFVTPRSSVEL
I41 YSGTLCSIQAEDELP
H53 ELPDGQEHQRIEFGV
S67 VDEVIEPSEGLPPTP
G69 EVIEPSEGLPPTPSY
T73 PSEGLPPTPSYSISS
S75 EGLPPTPSYSISSTL
Y76 GLPPTPSYSISSTLN
T81 PSYSISSTLNPQAPE
T94 PEFILGCTTSKKIPE
I99 GCTTSKKIPEAVEKD
Y109 AVEKDETYSSIDQYP
Y157 KKKRPPGYYSYLKDG
Y158 KKRPPGYYSYLKDGG
S159 KRPPGYYSYLKDGGE
Y160 RPPGYYSYLKDGGED
M202 MDVLPPVMPRtCDsP
T205-p LPPVMPRtCDsPQNP
S208-p VMPRtCDsPQNPVDF
P212 tCDsPQNPVDFISGP
V213 CDsPQNPVDFISGPV
F215 sPQNPVDFISGPVPD
S223-p ISGPVPDsPFPRTLG
- gap
S330 ASGAIPISQPAKSWA
S349 DSKPSASSPMAYVET
Y353 SASSPMAYVETKCsP
- gap
S359-p AYVETKCsPPVPsPL
S364-p KCsPPVPsPLASEKQ
K389 SEDPVAIKIAELLET
K402-u ETVTLIHkPVSLQPR
K445-u KFIPLYSkVQRPCTS
S541-p LSLKKLLsPtHEKHS
T543-p LKKLLsPtHEKHSVS
L557 SNGPRSDLIEDEELE
T566-p EDEELEDtGKGsEDE
S570-p LEDtGKGsEDEWEQV
Y653 ARESVQGYTTKTKQE
K671-u SRRVTLEkLPPVLVL
K696-u GGCQKLVkNIDYPVD
S712 EISRELLSPGIKNKN
K774 INQYQVVKPPADRTA
  rat

 
N5 ___MALHNPQYIFGD
S14 QYIFGDFSPDEFNQF
T24 EFNQFFVTPRSSVEL
I41 YSGTQCGIQAEEELL
H53 ELLDGQEHQRIEFGV
S67 VDEVIEPSDGLQRAP
G69 EVIEPSDGLQRAPSY
A73 PSDGLQRAPSYSISS
S75 DGLQRAPSYSISSTL
Y76 GLQRAPSYSISSTLN
T81 PSYSISSTLNPQAPE
P94 PEFILGCPTSKKTPD
T99 GCPTSKKTPDDIEKD
Y109 DIEKDETYSSIDQYP
Y157 KKKRPPGYYSYLKDG
Y158 KKRPPGYYSYLKDGS
S159 KRPPGYYSYLKDGSE
Y160 RPPGYYSYLKDGSEE
M203 VDMLPSVMPRtCDsP
T206-p LPSVMPRtCDsPQNP
S209-p VMPRtCDsPQNPMDL
P213 tCDsPQNPMDLISDP
M214 CDsPQNPMDLISDPV
L216 sPQNPMDLISDPVPD
S224 ISDPVPDSPFPRTLG
- gap
S332 VSGAISISQPAKSWA
S351 DSKPSSSSPVAYVET
Y355 SSSSPVAYVETKCsP
- gap
S361-p AYVETKCsPPVPSPL
S366 KCsPPVPSPLASEKQ
K391 SEDPVAIKIAELLET
K404 ETVTLVHKPVSLQPR
K447 KFIPLYSKVQRPCTS
S543 LSLKKLLSPTHEKHS
T545 LKKLLSPTHEKHSVS
L559 SNGPGSHLIEDEELE
T568 EDEELEDTGEGsEDE
S572-p LEDTGEGsEDEWEQV
Y655 ARESVQGYTTKTKQE
K673 SRRVTLEKLPPVLVL
K698 GGCQKLVKNIEYPVD
S714 EISRELLSPGVKNKN
R776 INQYQVVRPSADRTA
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