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Protein

Ubiquitin carboxyl-terminal hydrolase 1

Gene

Usp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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 (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. cysteine-type endopeptidase activity Source: GO_Central
  2. ubiquitin-specific protease activity Source: UniProtKB

GO - Biological processi

  1. DNA repair Source: UniProtKB-KW
  2. monoubiquitinated protein deubiquitination Source: UniProtKB
  3. proteasome-mediated ubiquitin-dependent protein catabolic process Source: GO_Central
  4. protein deubiquitination Source: UniProtKB
  5. regulation of DNA repair Source: UniProtKB
  6. regulation of proteasomal protein catabolic process Source: GO_Central
  7. response to UV Source: UniProtKB
  8. skeletal system development Source: MGI
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_260435. 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
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
Complete GO annotation...

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

MaxQBiQ8BJQ2.
PaxDbiQ8BJQ2.
PRIDEiQ8BJQ2.

PTM databases

PhosphoSiteiQ8BJQ2.

Expressioni

Gene expression databases

BgeeiQ8BJQ2.
CleanExiMM_USP1.
ExpressionAtlasiQ8BJQ2. baseline and differential.
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.
OMAiEYRASEI.
OrthoDBiEOG7JT6VZ.
PhylomeDBiQ8BJQ2.
TreeFamiTF331057.

Family and domain databases

InterProiIPR001394. Peptidase_C19_UCH.
IPR018200. USP_CS.
IPR028889. USP_dom.
[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

        10         20         30         40         50
MPGVIPSESN GLSRGSPSKK NRLSLKFFQK KETKRALDFT DSQENEEKTS
60 70 80 90 100
EYRGSEIDQV VPAAQSSPVS CEKRENLLPF VGLNNLGNTC YLNSILQVLY
110 120 130 140 150
FCPGFKTGVK HLFNIISRKK EALKDDSNQK DKGSCKEESL ASYELICSLQ
160 170 180 190 200
SLIISVEQLQ ASFLLNPEKY TDELATQPRR LLNTLRELNP MYEGFLQHDA
210 220 230 240 250
QEVLQCILGN IQETCQLLKK EEIKNLAELS GKVEEQSLQK EETGGITSTE
260 270 280 290 300
IDSMRNTEDV KEQLPKGNWK RKSDSESSNV KKKVKLSRES QPLEENQRQT
310 320 330 340 350
RSKRKAIGDT LEAAPKIIPK CVSESESAKP SQKKSKVKIN WLKPSTKQPS
360 370 380 390 400
ILSKFCSLGK ITTNQRSKGQ PKEKEGDVEE DLEKYGSDHT ANGGPESPGS
410 420 430 440 450
SVTPVDSSEA KSGNKGAEQI GFELVEKLFQ GQLVLRTRCL ECESLTERRE
460 470 480 490 500
DFQDISVPVQ EDELSKVEES SEISPEPKTE MKTLRWAISQ FASVERIVGE
510 520 530 540 550
DKYFCENCHH YTEAERSLLF DKMPEVITIH LKCFAASGLE FDCYGGGLSK
560 570 580 590 600
INTPLLTPLK LSLEEWSTKP TNDSYGLFAV VMHSGITISS GHYTASVKVT
610 620 630 640 650
DLNSLELDEG NFVVDQMCEL GKPEPLTEEQ ARGTAGNYDD EVSIRVGGNA
660 670 680 690 700
QPSKVLNKKN VEGIGLLGGQ KSKADYELYN KASNPDKVVG TPFTDNRNSE
710 720 730 740 750
TNDTTNGTHE SDRNKESSDQ TGVNMNGLEN KISYVVQSLK EYEGKWLLFD
760 770 780
DSEVKVTEEK DFLNSLSPST SPTSTPYLLF YKKL
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:
EMBLi
GenBanki
DDBJi
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_001288343.1. NM_001301414.1.
NP_666256.2. NM_146144.4.
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:
EMBLi
GenBanki
DDBJi
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_001288343.1. NM_001301414.1.
NP_666256.2. NM_146144.4.
UniGeneiMm.371692.

3D structure databases

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

Protein-protein interaction databases

BioGridi230966. 1 interaction.

Protein family/group databases

MEROPSiC19.019.

PTM databases

PhosphoSiteiQ8BJQ2.

Proteomic databases

MaxQBiQ8BJQ2.
PaxDbiQ8BJQ2.
PRIDEiQ8BJQ2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7398.
MGIiMGI:2385198. Usp1.

Phylogenomic databases

eggNOGiCOG5077.
GeneTreeiENSGT00650000093027.
HOGENOMiHOG000154756.
HOVERGENiHBG017288.
InParanoidiQ8BJQ2.
KOiK11832.
OMAiEYRASEI.
OrthoDBiEOG7JT6VZ.
PhylomeDBiQ8BJQ2.
TreeFamiTF331057.

Enzyme and pathway databases

ReactomeiREACT_260435. Regulation of the Fanconi anemia pathway.

Miscellaneous databases

NextBioi379913.
PROiQ8BJQ2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BJQ2.
CleanExiMM_USP1.
ExpressionAtlasiQ8BJQ2. baseline and differential.
GenevestigatoriQ8BJQ2.

Family and domain databases

InterProiIPR001394. Peptidase_C19_UCH.
IPR018200. USP_CS.
IPR028889. USP_dom.
[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]
ProtoNetiSearch...

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: March 4, 2015
This is version 91 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.