Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

Q8BJQ2

- UBP1_MOUSE

UniProt

Q8BJQ2 - UBP1_MOUSE

Protein

Ubiquitin carboxyl-terminal hydrolase 1

Gene

Usp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 By similarity.By similarity

    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).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei90 – 901NucleophilePROSITE-ProRule annotation
    Active sitei592 – 5921Proton acceptorPROSITE-ProRule annotation
    Sitei669 – 6702Cleavage; by autolysisBy similarity

    GO - Molecular functioni

    1. ubiquitin-specific protease activity Source: UniProtKB
    2. ubiquitin thiolesterase activity Source: UniProtKB

    GO - Biological processi

    1. DNA repair Source: UniProtKB-KW
    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: MGI
    7. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    DNA damage, DNA repair, Ubl conjugation 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
    Ubiquitin thioesterase 1
    Ubiquitin-specific-processing protease 1
    Gene namesi
    Name:Usp1Imported
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:2385198. Usp1.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 784784Ubiquitin carboxyl-terminal hydrolase 1PRO_0000306287Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei42 – 421PhosphoserineBy similarity
    Modified residuei67 – 671PhosphoserineBy similarity
    Modified residuei474 – 4741PhosphoserineBy similarity

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

    Keywords - PTMi

    Autocatalytic cleavage, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ8BJQ2.
    PRIDEiQ8BJQ2.

    PTM databases

    PhosphoSiteiQ8BJQ2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8BJQ2.
    BgeeiQ8BJQ2.
    CleanExiMM_USP1.
    GenevestigatoriQ8BJQ2.

    Interactioni

    Subunit structurei

    Interacts with FANCD2 and PCNA. Interacts with WDR48 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi230966. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BJQ2.
    SMRiQ8BJQ2. Positions 378-650.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini81 – 784704USPAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5077.
    GeneTreeiENSGT00650000093027.
    HOGENOMiHOG000154756.
    HOVERGENiHBG017288.
    InParanoidiQ8BJQ2.
    KOiK11832.
    OMAiFAVVMHS.
    OrthoDBiEOG7JT6VZ.
    PhylomeDBiQ8BJQ2.
    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.

    Q8BJQ2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPGVIPSESN GLSRGSPSKK NRLSLKFFQK KETKRALDFT DSQENEEKTS    50
    EYRGSEIDQV VPAAQSSPVS CEKRENLLPF VGLNNLGNTC YLNSILQVLY 100
    FCPGFKTGVK HLFNIISRKK EALKDDSNQK DKGSCKEESL ASYELICSLQ 150
    SLIISVEQLQ ASFLLNPEKY TDELATQPRR LLNTLRELNP MYEGFLQHDA 200
    QEVLQCILGN IQETCQLLKK EEIKNLAELS GKVEEQSLQK EETGGITSTE 250
    IDSMRNTEDV KEQLPKGNWK RKSDSESSNV KKKVKLSRES QPLEENQRQT 300
    RSKRKAIGDT LEAAPKIIPK CVSESESAKP SQKKSKVKIN WLKPSTKQPS 350
    ILSKFCSLGK ITTNQRSKGQ PKEKEGDVEE DLEKYGSDHT ANGGPESPGS 400
    SVTPVDSSEA KSGNKGAEQI GFELVEKLFQ GQLVLRTRCL ECESLTERRE 450
    DFQDISVPVQ EDELSKVEES SEISPEPKTE MKTLRWAISQ FASVERIVGE 500
    DKYFCENCHH YTEAERSLLF DKMPEVITIH LKCFAASGLE FDCYGGGLSK 550
    INTPLLTPLK LSLEEWSTKP TNDSYGLFAV VMHSGITISS GHYTASVKVT 600
    DLNSLELDEG NFVVDQMCEL GKPEPLTEEQ ARGTAGNYDD EVSIRVGGNA 650
    QPSKVLNKKN VEGIGLLGGQ KSKADYELYN KASNPDKVVG TPFTDNRNSE 700
    TNDTTNGTHE SDRNKESSDQ TGVNMNGLEN KISYVVQSLK EYEGKWLLFD 750
    DSEVKVTEEK DFLNSLSPST SPTSTPYLLF YKKL 784
    Length:784
    Mass (Da):87,456
    Last modified:March 1, 2003 - v1
    Checksum:i56F849DC1ADE3D81
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti84 – 841N → K in AAH20007. (PubMed:15489334)Curated
    Sequence conflicti344 – 3441P → S in AAH18179. (PubMed:15489334)Curated
    Sequence conflicti344 – 3441P → S in AAH20007. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK080882 mRNA. Translation: BAC38059.1.
    AL627349 Genomic DNA. Translation: CAM21066.1.
    BC018179 mRNA. Translation: AAH18179.1.
    BC020007 mRNA. Translation: AAH20007.1.
    CCDSiCCDS18381.1.
    RefSeqiNP_666256.2. NM_146144.3.
    XP_006503001.1. XM_006502938.1.
    UniGeneiMm.371692.

    Genome annotation databases

    EnsembliENSMUST00000030289; ENSMUSP00000030289; ENSMUSG00000028560.
    ENSMUST00000091358; ENSMUSP00000088917; ENSMUSG00000028560.
    GeneIDi230484.
    KEGGimmu:230484.
    UCSCiuc008tum.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK080882 mRNA. Translation: BAC38059.1 .
    AL627349 Genomic DNA. Translation: CAM21066.1 .
    BC018179 mRNA. Translation: AAH18179.1 .
    BC020007 mRNA. Translation: AAH20007.1 .
    CCDSi CCDS18381.1.
    RefSeqi NP_666256.2. NM_146144.3.
    XP_006503001.1. XM_006502938.1.
    UniGenei Mm.371692.

    3D structure databases

    ProteinModelPortali Q8BJQ2.
    SMRi Q8BJQ2. Positions 378-650.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 230966. 1 interaction.

    Protein family/group databases

    MEROPSi C19.019.

    PTM databases

    PhosphoSitei Q8BJQ2.

    Proteomic databases

    PaxDbi Q8BJQ2.
    PRIDEi Q8BJQ2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030289 ; ENSMUSP00000030289 ; ENSMUSG00000028560 .
    ENSMUST00000091358 ; ENSMUSP00000088917 ; ENSMUSG00000028560 .
    GeneIDi 230484.
    KEGGi mmu:230484.
    UCSCi uc008tum.1. mouse.

    Organism-specific databases

    CTDi 7398.
    MGIi MGI:2385198. Usp1.

    Phylogenomic databases

    eggNOGi COG5077.
    GeneTreei ENSGT00650000093027.
    HOGENOMi HOG000154756.
    HOVERGENi HBG017288.
    InParanoidi Q8BJQ2.
    KOi K11832.
    OMAi FAVVMHS.
    OrthoDBi EOG7JT6VZ.
    PhylomeDBi Q8BJQ2.
    TreeFami TF331057.

    Miscellaneous databases

    NextBioi 379913.
    PROi Q8BJQ2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8BJQ2.
    Bgeei Q8BJQ2.
    CleanExi MM_USP1.
    Genevestigatori Q8BJQ2.

    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6JImported.
      Tissue: Adipose tissueImported.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "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].
      Strain: FVB/NImported.
      Tissue: Mammary glandImported.

    Entry informationi

    Entry nameiUBP1_MOUSE
    AccessioniPrimary (citable) accession number: Q8BJQ2
    Secondary accession number(s): Q8VE17, Q8VEM4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 2, 2007
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 86 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3