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O94782

- UBP1_HUMAN

UniProt

O94782 - UBP1_HUMAN

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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)1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei90 – 901Nucleophile
Active sitei593 – 5931Proton acceptorPROSITE-ProRule annotation
Sitei671 – 6722Cleavage; by autolysis

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: ProtInc
  2. ubiquitin-specific protease activity Source: UniProtKB
  3. 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. skeletal system development Source: Ensembl
  7. 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. 1 Publication

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.2 Publications
Ubiquitinated; leading to its subsequent proteasomal degradation.By similarity

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

BgeeiO94782.
CleanExiHS_USP1.
ExpressionAtlasiO94782. baseline and differential.
GenevestigatoriO94782.

Organism-specific databases

HPAiHPA028440.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi113241. 40 interactions.
IntActiO94782. 22 interactions.
MINTiMINT-4719170.
STRINGi9606.ENSP00000343526.

Structurei

3D structure databases

ProteinModelPortaliO94782.
SMRiO94782. Positions 395-599.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5077.
GeneTreeiENSGT00650000093027.
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

        10         20         30         40         50
MPGVIPSESN GLSRGSPSKK NRLSLKFFQK KETKRALDFT DSQENEEKAS
60 70 80 90 100
EYRASEIDQV VPAAQSSPIN CEKRENLLPF VGLNNLGNTC YLNSILQVLY
110 120 130 140 150
FCPGFKSGVK HLFNIISRKK EALKDEANQK DKGNCKEDSL ASYELICSLQ
160 170 180 190 200
SLIISVEQLQ ASFLLNPEKY TDELATQPRR LLNTLRELNP MYEGYLQHDA
210 220 230 240 250
QEVLQCILGN IQETCQLLKK EEVKNVAELP TKVEEIPHPK EEMNGINSIE
260 270 280 290 300
MDSMRHSEDF KEKLPKGNGK RKSDTEFGNM KKKVKLSKEH QSLEENQRQT
310 320 330 340 350
RSKRKATSDT LESPPKIIPK YISENESPRP SQKKSRVKIN WLKSATKQPS
360 370 380 390 400
ILSKFCSLGK ITTNQGVKGQ SKENECDPEE DLGKCESDNT TNGCGLESPG
410 420 430 440 450
NTVTPVNVNE VKPINKGEEQ IGFELVEKLF QGQLVLRTRC LECESLTERR
460 470 480 490 500
EDFQDISVPV QEDELSKVEE SSEISPEPKT EMKTLRWAIS QFASVERIVG
510 520 530 540 550
EDKYFCENCH HYTEAERSLL FDKMPEVITI HLKCFAASGL EFDCYGGGLS
560 570 580 590 600
KINTPLLTPL KLSLEEWSTK PTNDSYGLFA VVMHSGITIS SGHYTASVKV
610 620 630 640 650
TDLNSLELDK GNFVVDQMCE IGKPEPLNEE EARGVVENYN DEEVSIRVGG
660 670 680 690 700
NTQPSKVLNK KNVEAIGLLG GQKSKADYEL YNKASNPDKV ASTAFAENRN
710 720 730 740 750
SETSDTTGTH ESDRNKESSD QTGINISGFE NKISYVVQSL KEYEGKWLLF
760 770 780
DDSEVKVTEE KDFLNSLSPS TSPTSTPYLL FYKKL
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.Curated
The sequence AAH32364.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAD92130.1 differs from that shown. Reason: Frameshift at position 230. Curated

Experimental Info

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 40 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.
GeneTreei ENSGT00650000093027.
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

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

Gene expression databases

Bgeei O94782.
CleanExi HS_USP1.
ExpressionAtlasi O94782. baseline and differential.
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: November 26, 2014
This is version 131 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