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O94782

- UBP1_HUMAN

UniProt

O94782 - UBP1_HUMAN

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
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    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. 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

    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

    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.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

    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.
    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.
    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

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    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.

    Experimental Info

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

    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

    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: October 1, 2014
    This is version 129 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