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Protein Page:
USP8 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
USP8 Hydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. Converts both 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the M phase. Involved in cell proliferation. Required to enter into S phase in response to serum stimulation. May regulate T-cell anergy mediated by RNF128 via the formation of a complex containing RNF128 and OTUB1. Probably regulates the stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintenance of ESCRT-0 stability. The level of protein ubiquitination on endosomes is essential for maintaining the morphology of the organelle. Deubiquitinates EPS15 and controles tyrosine kinase stability. Removes conjugated ubiquitin from EGFR thus regulating EGFR degradation and downstream MAPK signaling. Involved in acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Deubiquitinates BIRC6/bruce and KIF23/MKLP1. Forms a ternary complex with RNF128 and OTUB1. Interacts (via C-terminal UCH catalytic domain) with OTUB1 isoform 1. Interacts with STAM2 (via SH3 domain). Interacts with DNAJB3, EGFR, EPS15, RASGRF1, RNF41, YWHAE, YWHAG and YWHAZ. Interacts with NBR1, RASGRF1, RNF41 and IST1. Associates with the ESCRT-0 complex and with microtubules. Interacts with BIRC6/bruce and KIF23/MKLP1. Upon growth stimulation in starved human fibroblasts. Decreases in response to growth arrest induced by cell-cell contact. Belongs to the peptidase C19 family. Note: This description may include information from UniProtKB.
Protein type: EC 3.4.19.12; EC 3.1.2.15; Ubiquitin conjugating system; Ubiquitin-specific protease; Protease
Chromosomal Location of Human Ortholog: 15q21.2
Cellular Component: extrinsic to plasma membrane; cytoplasm; early endosome; acrosome; endosome membrane; midbody; nucleus; cytosol
Molecular Function: protein binding; cysteine-type endopeptidase activity; ubiquitin-specific protease activity; SH3 domain binding
Biological Process: ubiquitin-dependent protein catabolic process; cell proliferation; protein deubiquitination; endosome organization and biogenesis; cytokinesis after mitosis; Ras protein signal transduction
Reference #:  P40818 (UniProtKB)
Alt. Names/Synonyms: Deubiquitinating enzyme 8; FLJ34456; hUBPy; HumORF8; KIAA0055; MGC129718; Ubiquitin carboxyl-terminal hydrolase 8; Ubiquitin isopeptidase Y; ubiquitin specific peptidase 8; ubiquitin specific protease 8; Ubiquitin thioesterase 8; Ubiquitin-specific-processing protease 8; UBP8; UBPY; USP8
Gene Symbols: USP8
Molecular weight: 127,523 Da
Basal Isoelectric point: 8.7  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

USP8

Protein Structure Not Found.


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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 S108-p EAERLSEsLKLRYEE
0 5 S153-p GGTLAKGsLENVLDs
0 5 S160-p sLENVLDsKDKTQKS
0 1 T351-p PSKPAAQtPPASIEV
0 2 S378-p RMGPLNIstPVEPVA
0 14 T379-p MGPLNIstPVEPVAA
0 6 S389-p EPVAASKsDVsPIIQ
0 9 S392-p AASKsDVsPIIQPVP
0 4 S400-p PIIQPVPsIKNVPQI
0 1 T410-p NVPQIDRtKKPAVKL
0 3 S434-p STNHEQQsPQSGKVI
0 1 T446 KVIPDRSTKPVVFsP
0 13 S452-p STKPVVFsPtLMLTD
0 2 T454-p KPVVFsPtLMLTDEE
0 1 K528 AKEEMEKKESEQAKK
0 1 E531 EMEKKESEQAKKEDk
0 1 K534 KKESEQAKKEDkETS
0 1 K538-ac EQAKKEDkETSAKRG
0 1 K566-ub HETSDAKkSVEDRGK
0 21 T577-p DRGKRCPtPEIQKKS
0 1 S597-p HTSVTGDsGsGkPFK
0 1 S599-p SVTGDsGsGkPFKIK
0 1 K601-ac TGDsGsGkPFKIKGQ
0 1 S611-p KIKGQPEsGILRTGt
0 7 T618-p sGILRTGtFREDTDD
0 23 S641-p EPLTRARsEEMGRIV
0 1 S653-p RIVPGLPsGWAKFLD
0 1 Y668-p PITGTFRyYHsPtNt
0 4 S671-p GTFRyYHsPtNtVHM
0 1 T673-p FRyYHsPtNtVHMYP
0 1 T675-p yYHsPtNtVHMYPPE
0 1 S686-p YPPEMAPssAPPstP
0 1 S687-p PPEMAPssAPPstPP
0 11 S691-p APssAPPstPPtHKA
0 16 T692-p PssAPPstPPtHKAK
0 3 T695-p APPstPPtHKAKPQI
0 1 S711-p AERDREPsKLKRsys
0 8 S716-p EPsKLKRsyssPDIt
0 4 Y717-p PsKLKRsyssPDItQ
2 60 S718-p sKLKRsyssPDItQA
0 10 S719-p KLKRsyssPDItQAI
0 3 T723-p syssPDItQAIQEEE
0 2 T737-p EKRKPTVtPtVNREN
0 1 T739-p RKPTVtPtVNRENKP
0 1 S760 EISRLSASQIRNLNP
0 1 Y810-p DYFNRNCyQDDINRS
0 1 Y842-p KALWTGQyRYISPKD
1 0 T945 TCHKKSRTFEAFMyL
0 1 Y951-p RTFEAFMyLSLPLAS
0 1 S1015-p LVHLKRFsyDGRWKQ
0 1 Y1016-p VHLKRFsyDGRWKQK
0 1 Y1068-p GGLDGGHyTAYCKNA
  mouse

 
S108 EAERLSESLKLRYEE
S153-p SGAAAKRsVENLLDs
S160-p sVENLLDsKTKTQRI
M351 PSKLPTQMPPPPIET
S375 QDEKLRLSTQPALAG
T376 DEKLRLSTQPALAGP
A389 GPGAAPRAEAsPIIQ
S392-p AAPRAEAsPIIQPAP
T401 IIQPAPATKSVPQVD
T410 SVPQVDRTKKPSVKL
- gap
T440-p RVLSDRStKPVFPSP
S446 StKPVFPSPTTMLTD
T448 KPVFPSPTTMLTDEE
K522-ac AKDGQEKkDSkQTkT
K525-ac GQEKkDSkQTkTEDR
K528-ac KkDSkQTkTEDRELS
R532 kQTkTEDRELSADGA
V560 HEASDAKVPVEGKRC
T569 VEGKRCPTSEAQKRP
- gap
- gap
- gap
- gap
- gap
S603-p EPLTRARsEEMGRIV
L615 RIVPGLPLGWAKFLD
Y630 PITGTFRYYHSPTNT
S633 GTFRYYHSPTNTVHM
T635 FRYYHSPTNTVHMYP
T637 YYHSPTNTVHMYPPE
S648 YPPEMAPSSAPPSTP
S649 PPEMAPSSAPPSTPP
S653 APSSAPPSTPPTHKV
T654 PSSAPPSTPPTHKVK
T657 APPSTPPTHKVKPQV
S673 AERDREPSKLKRsys
S678-p EPSKLKRsyssPDIt
Y679-p PSKLKRsyssPDItQ
S680-p SKLKRsyssPDItQA
S681-p KLKRsyssPDItQAL
T685-p syssPDItQALQEEE
T699 EKRRPAVTPMVNREN
M701 RRPAVTPMVNRENKP
S722-p EISRLSAsQIRNLNP
Y772 DYFNRNCYQDDINRS
Y804 KALWTGQYRYISPKD
T907-p TCRRRSRtFEAFMYL
Y913 RtFEAFMYLSLPLAS
S977 LVHLKRFSYDGRWKQ
Y978 VHLKRFSYDGRWKQK
Y1030 GGLDGGHYTAYCKNA
  rat

 
S108 EAERLSESLKLRYEE
S153-p SGAAAKRsVENLLDS
S160 sVENLLDSKTKIQRV
M351 PSKLPAQMPPPPLEA
S378 KPRPLVQSALAGPSV
A379 PRPLVQSALAGPSVA
A389 GPSVAPKAEASPIIQ
S392 VAPKAEASPIIQPVP
T401 IIQPVPATKNVPQVD
T410 NVPQVDRTKKPAVKL
- gap
T440 RVLSDRSTKPVFTSP
S446 STKPVFTSPATMLTD
A448 KPVFTSPATMLTDEE
R522 AKDGQEKRDSKQTKA
K525 GQEKRDSKQTKAEDR
K528 KRDSKQTKAEDREPP
R532 KQTKAEDREPPADGA
V560 HDASDAKVSVEGKRC
M569 VEGKRCPMSEVQKRP
- gap
- gap
- gap
- gap
- gap
S604 EPLTRARSEEMGRIV
L616 RIVPGLPLGWAKFLD
Y631 PITGTFRYYHSPTNT
S634 GTFRYYHSPTNTVHM
T636 FRYYHSPTNTVHMYP
T638 YYHSPTNTVHMYPPE
S649 YPPEMAPSSVPPSTP
S650 PPEMAPSSVPPSTPP
S654 APSSVPPSTPPTHKV
T655 PSSVPPSTPPTHKVK
T658 VPPSTPPTHKVKPQI
S674 AERDREPSKLKRsYs
S679-p EPSKLKRsYsSPDIT
Y680 PSKLKRsYsSPDITQ
S681-p SKLKRsYsSPDITQA
S682 KLKRsYsSPDITQAL
T686 sYsSPDITQALQEEE
T700 EKRRPAVTPTVNREN
T702 RRPAVTPTVNRENKP
S723 EISRLSASQIRNLNP
Y773 DYFNRNCYQDDINRS
Y805 KALWTGQYRYISPKD
T908 TCHKKSRTFEAFMYL
Y914 RTFEAFMYLSLPLAS
S978 LVHLKRFSYDGRWKQ
Y979 VHLKRFSYDGRWKQK
Y1031 GGLDGGHYTAYCKNA
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