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Protein Page:
USP1 (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
USP1 Negative regulator of DNA damage repair which specifically deubiquitinates monoubiquitinated FANCD2. Also involved in PCNA-mediated translesion synthesis (TLS) by deubiquitinating monoubiquitinated PCNA. Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high activity. Interacts with FANCD2 and PCNA. Interacts with WDR48. Down-regulated following DNA damage. Belongs to the peptidase C19 family. Note: This description may include information from UniProtKB.
Protein type: Protease; Ubiquitin conjugating system; EC 3.4.19.12; EC 3.1.2.15; Ubiquitin-specific protease
Cellular Component: nucleoplasm; nucleus
Molecular Function: ubiquitin thiolesterase activity; protein binding; cysteine-type endopeptidase activity; ubiquitin-specific protease activity
Biological Process: regulation of DNA repair; ubiquitin-dependent protein catabolic process; protein deubiquitination; DNA repair; response to UV
Reference #:  O94782 (UniProtKB)
Alt. Names/Synonyms: Deubiquitinating enzyme 1; hUBP; ubiquitin carboxyl terminal hydrolase 1; Ubiquitin carboxyl-terminal hydrolase 1; ubiquitin specific peptidase 1; ubiquitin specific processing protease 1; ubiquitin specific protease 1; Ubiquitin thioesterase 1; ubiquitin thiolesterase 1; Ubiquitin-specific-processing protease 1; UBP; UBP1; USP1
Gene Symbols: USP1
Molecular weight: 88,207 Da
Basal Isoelectric point: 5.37  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

USP1

Protein Structure Not Found.


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Sites Implicated In
enzymatic activity, induced: S313‑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 S7-p _MPGVIPsESNGLsR
0 1 S9 PGVIPsESNGLsRGs
0 1 S13-p PsESNGLsRGsPSKK
0 4 S16-p SNGLsRGsPSKKNRL
0 1 S18 GLsRGsPSKKNRLSL
0 1 T33-p KFFQKKEtKRALDFT
1 5 S42-p RALDFTDsQENEEKA
0 2 S66-p QVVPAAQssPINCEK
1 6 S67-p VVPAAQssPINCEKR
0 1 N70 AAQssPINCEKRENL
0 1 A127 KEALKDEANQkDKGN
0 1 K130-ac LKDEANQkDKGNCKE
0 1 S253 INSIEMDSMRHSEDF
0 1 S273-p KGNGKRKsDTEFGNM
0 7 T307-p TRSKRKAtsDtLEsP
0 3 S308-p RSKRKAtsDtLEsPP
0 1 T310-p KRKAtsDtLEsPPKI
1 12 S313-p AtsDtLEsPPKIIPK
0 2 S323-p KIIPKYIsENEsPRP
0 3 S327-p KYIsENEsPRPSQKK
0 2 S398-p TNGCGLEsPGNTVTP
0 9 S475-p VEESSEIsPEPKTEM
0 1 T529-p DKMPEVItIHLKCFA
0 7 Y678-p GQKSKADyELyNKAS
0 1 Y681-p SKADyELyNKASNPD
0 4 K689-ub NKASNPDkVASTAFA
0 1 K716-ac THESDRNkESSDQTG
0 1 S727-p DQTGINIsGFENkIS
0 9 K732-ub NIsGFENkISYVVQS
0 1 K741-ub SYVVQSLkEYEGkWL
0 2 K746-ub SLkEYEGkWLLFDDS
0 1 K761-ub EVKVTEEkDFLNSLs
0 3 S768-p kDFLNSLsPSTsPTS
0 2 S772-p NSLsPSTsPTSTPYL
  mouse

 
S7 _MPGVIPSEsNGLSR
S9-p PGVIPSEsNGLSRGs
S13 PSEsNGLSRGsPsKK
S16-p sNGLSRGsPsKKNRL
S18-p GLSRGsPsKKNRLSL
T33 KFFQKKETKRALDFT
S42 RALDFTDSQENEEKT
S66-p QVVPAAQssPVsCEK
S67-p VVPAAQssPVsCEKR
S70-p AAQssPVsCEKRENL
S127-p KEALKDDsNQKDKGS
K130 LKDDsNQKDKGSCKE
S253-p ITSTEIDsMRNTEDV
S273 KGNWKRKSDSESSNV
I307 TRSKRKAIGDTLEAA
G308 RSKRKAIGDTLEAAP
T310 KRKAIGDTLEAAPKI
A313 AIGDTLEAAPKIIPK
S323 KIIPKCVSESESAKP
S327 KCVSESESAKPSQKK
S397-p TANGGPEsPGSSVTP
S474-p VEESSEIsPEPKTEM
T528 DKMPEVITIHLKCFA
Y676 GQKSKADYELYNKAS
Y679 SKADYELYNKASNPD
K687-ub NKASNPDkVVGTPFT
K715 THESDRNKESSDQTG
N726 DQTGVNMNGLENKIS
K731 NMNGLENKISYVVQS
K740 SYVVQSLKEYEGKWL
K745 SLKEYEGKWLLFDDS
K760 EVKVTEEKDFLNSLs
S767-p KDFLNSLsPSTsPTS
S771-p NSLsPSTsPTSTPYL
  rat

 
S7 _MPGVIPSESNGLSR
S9 PGVIPSESNGLSRGS
S13 PSESNGLSRGSPSKK
S16 SNGLSRGSPSKKNRL
S18 GLSRGSPSKKNRLSL
T33 KFFQKKETKRALDFT
S42 RALDFTDSQEDEEKA
S66 QVVPAAQSSPVSCEK
S67 VVPAAQSSPVSCEKR
S70 AAQSSPVSCEKRENL
S127 KEALKDDSIQKDKGS
K130 LKDDSIQKDKGSCKE
S253 ISSTETDSTRNLDDL
S273 KGNWKRKSDGESGNM
T307 TRSKRKATGDTLEAS
G308 RSKRKATGDTLEASP
T310 KRKATGDTLEASPKI
A313 ATGDTLEASPKIIPK
S323 KIIPKCVSENESAKP
S327 KCVSENESAKPSQKK
S398 VNGSGPASPGSSVTP
S475-p VEESSEIsPEPKTEM
T529 DKMPEVITIHLKCFA
Y677 GQKSKADYELCSKAS
C680 SKADYELCSKASNPE
K688 SKASNPEKVVGTPFT
K715 TQESDRSKESSDQTG
S726 DQTGINVSGLENKIS
K731 NVSGLENKISYVVQS
K740 SYVVQSLKEYEGKWL
K745 SLKEYEGKWLLFDDS
K760 EVKVTEEKDFLNSLS
S767 KDFLNSLSPSTSPTS
S771 NSLSPSTSPTSTPYL
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