SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O94782

- UBP1_HUMAN

UniProt

O94782 - UBP1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ubiquitin carboxyl-terminal hydrolase 1

Gene
USP1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

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).1 Publication

Kineticsi

  1. KM=0.7 µM for ubiquitin vinyl sulfone (in presence of WDR48)1 Publication
  2. KM=1.4 µM for ubiquitin vinyl sulfone (in absence of WDR48)

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei90 – 901Nucleophile
Active sitei593 – 5931Proton acceptor By similarity
Sitei671 – 6722Cleavage; by autolysis

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: ProtInc
  2. protein binding Source: UniProtKB
  3. ubiquitin-specific protease activity Source: UniProtKB
  4. ubiquitin thiolesterase activity Source: UniProtKB

GO - Biological processi

  1. DNA repair Source: Reactome
  2. monoubiquitinated protein deubiquitination Source: UniProtKB
  3. protein deubiquitination Source: UniProtKB
  4. regulation of DNA repair Source: UniProtKB
  5. response to UV Source: UniProtKB
  6. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_18265. Regulation of the Fanconi anemia pathway.

Protein family/group databases

MEROPSiC19.019.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 1 (EC:3.4.19.12)
Alternative name(s):
Deubiquitinating enzyme 1
Short name:
hUBP
Ubiquitin thioesterase 1
Ubiquitin-specific-processing protease 1
Gene namesi
Name:USP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:12607. USP1.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi90 – 901C → S: Loss of catalytic activity including autolysis. 2 Publications
Mutagenesisi670 – 6712GG → AA: Loss of autolysis-mediated degradation upon UV irradiation. No effect on catalytic activity.

Organism-specific databases

PharmGKBiPA37233.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 785785Ubiquitin carboxyl-terminal hydrolase 1PRO_0000080615Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421Phosphoserine2 Publications
Modified residuei67 – 671Phosphoserine1 Publication
Modified residuei475 – 4751Phosphoserine1 Publication

Post-translational modificationi

Autocatalytic cleavage of USP1 following UV irradiation inactivates it leading to an increase in ubiquitinated PCNA, recruitment of POLH and translesion synthesis.
Ubiquitinated; leading to its subsequent proteasomal degradation By similarity.1 Publication

Keywords - PTMi

Autocatalytic cleavage, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO94782.
PaxDbiO94782.
PRIDEiO94782.

2D gel databases

OGPiO94782.

PTM databases

PhosphoSiteiO94782.

Expressioni

Developmental stagei

Cell cycle-regulated. Highest level during S phase.1 Publication

Inductioni

Down-regulated following DNA damage.1 Publication

Gene expression databases

ArrayExpressiO94782.
BgeeiO94782.
CleanExiHS_USP1.
GenevestigatoriO94782.

Organism-specific databases

HPAiHPA028440.

Interactioni

Subunit structurei

Interacts with FANCD2 and PCNA. Interacts with WDR48.2 Publications

Protein-protein interaction databases

BioGridi113241. 38 interactions.
IntActiO94782. 22 interactions.
MINTiMINT-4719170.
STRINGi9606.ENSP00000343526.

Structurei

3D structure databases

ProteinModelPortaliO94782.
SMRiO94782. Positions 395-599.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini81 – 785705USPAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C19 family.
Contains 1 USP domain.

Phylogenomic databases

eggNOGiCOG5077.
HOVERGENiHBG017288.
InParanoidiO94782.
KOiK11832.
OMAiFAVVMHS.
OrthoDBiEOG7JT6VZ.
PhylomeDBiO94782.
TreeFamiTF331057.

Family and domain databases

InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view]
PfamiPF00443. UCH. 2 hits.
[Graphical view]
PROSITEiPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O94782-1 [UniParc]FASTAAdd to Basket

« Hide

MPGVIPSESN GLSRGSPSKK NRLSLKFFQK KETKRALDFT DSQENEEKAS    50
EYRASEIDQV VPAAQSSPIN CEKRENLLPF VGLNNLGNTC YLNSILQVLY 100
FCPGFKSGVK HLFNIISRKK EALKDEANQK DKGNCKEDSL ASYELICSLQ 150
SLIISVEQLQ ASFLLNPEKY TDELATQPRR LLNTLRELNP MYEGYLQHDA 200
QEVLQCILGN IQETCQLLKK EEVKNVAELP TKVEEIPHPK EEMNGINSIE 250
MDSMRHSEDF KEKLPKGNGK RKSDTEFGNM KKKVKLSKEH QSLEENQRQT 300
RSKRKATSDT LESPPKIIPK YISENESPRP SQKKSRVKIN WLKSATKQPS 350
ILSKFCSLGK ITTNQGVKGQ SKENECDPEE DLGKCESDNT TNGCGLESPG 400
NTVTPVNVNE VKPINKGEEQ IGFELVEKLF QGQLVLRTRC LECESLTERR 450
EDFQDISVPV QEDELSKVEE SSEISPEPKT EMKTLRWAIS QFASVERIVG 500
EDKYFCENCH HYTEAERSLL FDKMPEVITI HLKCFAASGL EFDCYGGGLS 550
KINTPLLTPL KLSLEEWSTK PTNDSYGLFA VVMHSGITIS SGHYTASVKV 600
TDLNSLELDK GNFVVDQMCE IGKPEPLNEE EARGVVENYN DEEVSIRVGG 650
NTQPSKVLNK KNVEAIGLLG GQKSKADYEL YNKASNPDKV ASTAFAENRN 700
SETSDTTGTH ESDRNKESSD QTGINISGFE NKISYVVQSL KEYEGKWLLF 750
DDSEVKVTEE KDFLNSLSPS TSPTSTPYLL FYKKL 785
Length:785
Mass (Da):88,207
Last modified:May 1, 1999 - v1
Checksum:i50AA2817A60810AF
GO

Sequence cautioni

The sequence AAH18745.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence AAH32364.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence BAD92130.1 differs from that shown. Reason: Frameshift at position 230.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti621 – 6211I → M in AAD11441. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB014458 mRNA. Translation: BAA34703.1.
AF117386 mRNA. Translation: AAD11441.1.
AL117575 mRNA. Translation: CAB55999.1.
AL117503 mRNA. Translation: CAB55967.1.
AB208893 mRNA. Translation: BAD92130.1. Frameshift.
CH471059 Genomic DNA. Translation: EAX06585.1.
CH471059 Genomic DNA. Translation: EAX06586.1.
BC050525 mRNA. Translation: AAH50525.1.
BC018745 mRNA. Translation: AAH18745.1. Sequence problems.
BC032364 mRNA. Translation: AAH32364.1. Sequence problems.
CCDSiCCDS621.1.
PIRiT17309.
RefSeqiNP_001017415.1. NM_001017415.1.
NP_001017416.1. NM_001017416.1.
NP_003359.3. NM_003368.4.
UniGeneiHs.35086.

Genome annotation databases

EnsembliENST00000339950; ENSP00000343526; ENSG00000162607.
ENST00000371146; ENSP00000360188; ENSG00000162607.
GeneIDi7398.
KEGGihsa:7398.
UCSCiuc001daj.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB014458 mRNA. Translation: BAA34703.1 .
AF117386 mRNA. Translation: AAD11441.1 .
AL117575 mRNA. Translation: CAB55999.1 .
AL117503 mRNA. Translation: CAB55967.1 .
AB208893 mRNA. Translation: BAD92130.1 . Frameshift.
CH471059 Genomic DNA. Translation: EAX06585.1 .
CH471059 Genomic DNA. Translation: EAX06586.1 .
BC050525 mRNA. Translation: AAH50525.1 .
BC018745 mRNA. Translation: AAH18745.1 . Sequence problems.
BC032364 mRNA. Translation: AAH32364.1 . Sequence problems.
CCDSi CCDS621.1.
PIRi T17309.
RefSeqi NP_001017415.1. NM_001017415.1.
NP_001017416.1. NM_001017416.1.
NP_003359.3. NM_003368.4.
UniGenei Hs.35086.

3D structure databases

ProteinModelPortali O94782.
SMRi O94782. Positions 395-599.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113241. 38 interactions.
IntActi O94782. 22 interactions.
MINTi MINT-4719170.
STRINGi 9606.ENSP00000343526.

Chemistry

ChEMBLi CHEMBL1795087.

Protein family/group databases

MEROPSi C19.019.

PTM databases

PhosphoSitei O94782.

2D gel databases

OGPi O94782.

Proteomic databases

MaxQBi O94782.
PaxDbi O94782.
PRIDEi O94782.

Protocols and materials databases

DNASUi 7398.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000339950 ; ENSP00000343526 ; ENSG00000162607 .
ENST00000371146 ; ENSP00000360188 ; ENSG00000162607 .
GeneIDi 7398.
KEGGi hsa:7398.
UCSCi uc001daj.2. human.

Organism-specific databases

CTDi 7398.
GeneCardsi GC01P062837.
H-InvDB HIX0159950.
HGNCi HGNC:12607. USP1.
HPAi HPA028440.
MIMi 603478. gene.
neXtProti NX_O94782.
PharmGKBi PA37233.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5077.
HOVERGENi HBG017288.
InParanoidi O94782.
KOi K11832.
OMAi FAVVMHS.
OrthoDBi EOG7JT6VZ.
PhylomeDBi O94782.
TreeFami TF331057.

Enzyme and pathway databases

Reactomei REACT_18265. Regulation of the Fanconi anemia pathway.

Miscellaneous databases

GeneWikii USP1.
GenomeRNAii 7398.
NextBioi 28954.
PROi O94782.
SOURCEi Search...

Gene expression databases

ArrayExpressi O94782.
Bgeei O94782.
CleanExi HS_USP1.
Genevestigatori O94782.

Family and domain databases

InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view ]
Pfami PF00443. UCH. 2 hits.
[Graphical view ]
PROSITEi PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and chromosomal assignment of USP1, a novel gene encoding a human ubiquitin-specific protease."
    Fjiwara T., Saito A., Suzuki M., Shinomiya H., Suzuki T., Takahashi E., Tanigami A., Ichiyama A., Chung C.H., Nakamura Y., Tanaka K.
    Genomics 54:155-158(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetal brain.
  2. "Molecular cloning of a novel human ubiquitin-specific protease."
    Seibold S., Marx M.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Eye, Testis and Uterus.
  7. "The deubiquitinating enzyme USP1 regulates the Fanconi Anemia pathway."
    Nijman S.M.B., Huang T.T., Dirac A.M.G., Brummelkamp T.R., Kerkhoven R.M., D'Andrea A.D., Bernards R.
    Mol. Cell 17:331-339(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, UBIQUITINATION, INTERACTION WITH FANCD2, MUTAGENESIS OF CYS-90.
  8. Cited for: FUNCTION, CLEAVAGE SITE, MUTAGENESIS OF CYS-90 AND 670-GLY-GLY-671.
  9. "A UAF1-containing multisubunit protein complex regulates the Fanconi anemia pathway."
    Cohn M.A., Kowal P., Yang K., Haas W., Huang T.T., Gygi S.P., D'Andrea A.D.
    Mol. Cell 28:786-797(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, INTERACTION WITH WDR48, INDUCTION.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiUBP1_HUMAN
AccessioniPrimary (citable) accession number: O94782
Secondary accession number(s): A0PJ95
, D3DQ57, Q05BX7, Q59H66, Q9UFR0, Q9UNJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: September 3, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

HEK293T cells expressing reduced levels of USP1 show a higher level of ubiquitinated PCNA and an increase in point mutations upon UV irradiation.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi