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Q8BJQ2 (UBP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Usp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length784 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

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).

Subunit structure

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

Subcellular location

Nucleus By similarity UniProtKB O94782.

Post-translational modification

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.

Sequence similarities

Belongs to the peptidase C19 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 784784Ubiquitin carboxyl-terminal hydrolase 1
PRO_0000306287

Sites

Active site901Nucleophile By similarity UniProtKB Q93009
Active site5921Proton acceptor By similarity UniProtKB Q93009
Site669 – 6702Cleavage; by autolysis By similarity UniProtKB O94782

Amino acid modifications

Modified residue421Phosphoserine By similarity UniProtKB O94782
Modified residue671Phosphoserine By similarity
Modified residue4741Phosphoserine By similarity

Experimental info

Sequence conflict841N → K in AAH20007. Ref.3
Sequence conflict3441P → S in AAH18179. Ref.3
Sequence conflict3441P → S in AAH20007. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q8BJQ2 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 56F849DC1ADE3D81

FASTA78487,456
        10         20         30         40         50         60 
MPGVIPSESN GLSRGSPSKK NRLSLKFFQK KETKRALDFT DSQENEEKTS EYRGSEIDQV 

        70         80         90        100        110        120 
VPAAQSSPVS CEKRENLLPF VGLNNLGNTC YLNSILQVLY FCPGFKTGVK HLFNIISRKK 

       130        140        150        160        170        180 
EALKDDSNQK DKGSCKEESL ASYELICSLQ SLIISVEQLQ ASFLLNPEKY TDELATQPRR 

       190        200        210        220        230        240 
LLNTLRELNP MYEGFLQHDA QEVLQCILGN IQETCQLLKK EEIKNLAELS GKVEEQSLQK 

       250        260        270        280        290        300 
EETGGITSTE IDSMRNTEDV KEQLPKGNWK RKSDSESSNV KKKVKLSRES QPLEENQRQT 

       310        320        330        340        350        360 
RSKRKAIGDT LEAAPKIIPK CVSESESAKP SQKKSKVKIN WLKPSTKQPS ILSKFCSLGK 

       370        380        390        400        410        420 
ITTNQRSKGQ PKEKEGDVEE DLEKYGSDHT ANGGPESPGS SVTPVDSSEA KSGNKGAEQI 

       430        440        450        460        470        480 
GFELVEKLFQ GQLVLRTRCL ECESLTERRE DFQDISVPVQ EDELSKVEES SEISPEPKTE 

       490        500        510        520        530        540 
MKTLRWAISQ FASVERIVGE DKYFCENCHH YTEAERSLLF DKMPEVITIH LKCFAASGLE 

       550        560        570        580        590        600 
FDCYGGGLSK INTPLLTPLK LSLEEWSTKP TNDSYGLFAV VMHSGITISS GHYTASVKVT 

       610        620        630        640        650        660 
DLNSLELDEG NFVVDQMCEL GKPEPLTEEQ ARGTAGNYDD EVSIRVGGNA QPSKVLNKKN 

       670        680        690        700        710        720 
VEGIGLLGGQ KSKADYELYN KASNPDKVVG TPFTDNRNSE TNDTTNGTHE SDRNKESSDQ 

       730        740        750        760        770        780 
TGVNMNGLEN KISYVVQSLK EYEGKWLLFD DSEVKVTEEK DFLNSLSPST SPTSTPYLLF 


YKKL

« Hide

References

[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. expand/collapse author list , 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/6J.
Tissue: Adipose tissue.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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/N.
Tissue: Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK080882 mRNA. Translation: BAC38059.1.
AL627349 Genomic DNA. Translation: CAM21066.1.
BC018179 mRNA. Translation: AAH18179.1.
BC020007 mRNA. Translation: AAH20007.1.
IPIIPI00330276.
RefSeqNP_666256.2. NM_146144.3.
UniGeneMm.371692.

3D structure databases

ProteinModelPortalQ8BJQ2.
SMRQ8BJQ2. Positions 378-650.
ModBaseSearch...

Protein family/group databases

MEROPSC19.019.

PTM databases

PhosphoSiteQ8BJQ2.

Proteomic databases

PaxDbQ8BJQ2.
PRIDEQ8BJQ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030289; ENSMUSP00000030289; ENSMUSG00000028560.
ENSMUST00000091358; ENSMUSP00000088917; ENSMUSG00000028560.
GeneID230484.
KEGGmmu:230484.
UCSCuc008tum.1. mouse.

Organism-specific databases

CTD7398.
MGIMGI:2385198. Usp1.

Phylogenomic databases

eggNOGCOG5077.
GeneTreeENSGT00650000093027.
HOGENOMHOG000154756.
HOVERGENHBG017288.
InParanoidQ8BJQ2.
KOK11832.
OMAISSGHYT.
OrthoDBEOG4XSKP7.

Gene expression databases

ArrayExpressQ8BJQ2.
BgeeQ8BJQ2.
CleanExMM_USP1.
GenevestigatorQ8BJQ2.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19.
[Graphical view]
PfamPF00443. UCH. 1 hit.
[Graphical view]
PROSITEPS00972. UCH_2_1. 1 hit.
PS00973. UCH_2_2. 1 hit.
PS50235. UCH_2_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio379913.
SOURCESearch...

Entry information

Entry nameUBP1_MOUSE
AccessionPrimary (citable) accession number: Q8BJQ2
Secondary accession number(s): Q8VE17, Q8VEM4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: March 1, 2003
Last modified: May 29, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents