UBP1_MOUSE
ID UBP1_MOUSE Reviewed; 784 AA.
AC Q8BJQ2; Q8VE17; Q8VEM4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 1;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:O94782};
DE AltName: Full=Deubiquitinating enzyme 1;
DE AltName: Full=Ubiquitin thioesterase 1;
DE AltName: Full=Ubiquitin-specific-processing protease 1;
DE Contains:
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 1, N-terminal fragment {ECO:0000250|UniProtKB:O94782};
GN Name=Usp1 {ECO:0000312|MGI:MGI:2385198};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000312|EMBL:BAC38059.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC38059.1};
RC TISSUE=Adipose tissue {ECO:0000312|EMBL:BAC38059.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000312|EMBL:AAH20007.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH20007.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH20007.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-767, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Negative regulator of DNA damage repair which specifically
CC deubiquitinates monoubiquitinated FANCD2. Also involved in PCNA-
CC mediated translesion synthesis (TLS) by deubiquitinating
CC monoubiquitinated PCNA. Has almost no deubiquitinating activity by
CC itself and requires the interaction with WDR48 to have a high activity.
CC {ECO:0000250|UniProtKB:O94782}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:O94782};
CC -!- SUBUNIT: Interacts with FANCD2 and PCNA. Interacts with WDR48.
CC Interacts with ATAD5; the interaction regulates USP1-mediated PCNA
CC deubiquitination. {ECO:0000250|UniProtKB:O94782}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O94782}.
CC -!- PTM: Autocatalytic cleavage of USP1 following UV irradiation
CC inactivates it leading to an increase in ubiquitinated PCNA,
CC recruitment of POLH and translesion synthesis.
CC {ECO:0000250|UniProtKB:O94782}.
CC -!- PTM: [Ubiquitin carboxyl-terminal hydrolase 1, N-terminal fragment]:
CC Ubiquitinated by the CRL2(KLHDC2) complex following autocatalytic
CC cleavage, leading to its degradation: the CRL2(KLHDC2) complex
CC recognizes the diglycine (Gly-Gly) at the C-terminus.
CC {ECO:0000250|UniProtKB:O94782}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000255}.
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DR EMBL; AK080882; BAC38059.1; -; mRNA.
DR EMBL; AL627349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018179; AAH18179.1; -; mRNA.
DR EMBL; BC020007; AAH20007.1; -; mRNA.
DR CCDS; CCDS18381.1; -.
DR RefSeq; NP_001288343.1; NM_001301414.1.
DR RefSeq; NP_666256.2; NM_146144.4.
DR AlphaFoldDB; Q8BJQ2; -.
DR SMR; Q8BJQ2; -.
DR BioGRID; 230966; 33.
DR STRING; 10090.ENSMUSP00000030289; -.
DR MEROPS; C19.019; -.
DR iPTMnet; Q8BJQ2; -.
DR PhosphoSitePlus; Q8BJQ2; -.
DR EPD; Q8BJQ2; -.
DR jPOST; Q8BJQ2; -.
DR MaxQB; Q8BJQ2; -.
DR PaxDb; Q8BJQ2; -.
DR PeptideAtlas; Q8BJQ2; -.
DR PRIDE; Q8BJQ2; -.
DR ProteomicsDB; 297791; -.
DR Antibodypedia; 33332; 357 antibodies from 34 providers.
DR DNASU; 230484; -.
DR Ensembl; ENSMUST00000030289; ENSMUSP00000030289; ENSMUSG00000028560.
DR Ensembl; ENSMUST00000091358; ENSMUSP00000088917; ENSMUSG00000028560.
DR GeneID; 230484; -.
DR KEGG; mmu:230484; -.
DR UCSC; uc008tum.2; mouse.
DR CTD; 7398; -.
DR MGI; MGI:2385198; Usp1.
DR VEuPathDB; HostDB:ENSMUSG00000028560; -.
DR eggNOG; KOG1864; Eukaryota.
DR GeneTree; ENSGT00910000144243; -.
DR HOGENOM; CLU_019874_0_0_1; -.
DR InParanoid; Q8BJQ2; -.
DR OMA; HAIQDVN; -.
DR OrthoDB; 439300at2759; -.
DR PhylomeDB; Q8BJQ2; -.
DR TreeFam; TF331057; -.
DR Reactome; R-MMU-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-MMU-6783310; Fanconi Anemia Pathway.
DR BioGRID-ORCS; 230484; 5 hits in 108 CRISPR screens.
DR ChiTaRS; Usp1; mouse.
DR PRO; PR:Q8BJQ2; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BJQ2; protein.
DR Bgee; ENSMUSG00000028560; Expressed in cleaving embryo and 259 other tissues.
DR ExpressionAtlas; Q8BJQ2; baseline and differential.
DR Genevisible; Q8BJQ2; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; ISO:MGI.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0035520; P:monoubiquitinated protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0006282; P:regulation of DNA repair; ISS:UniProtKB.
DR GO; GO:0009411; P:response to UV; ISS:UniProtKB.
DR GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd02671; Peptidase_C19O; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR033815; USP1.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW Autocatalytic cleavage; DNA damage; DNA repair; Hydrolase; Nucleus;
KW Phosphoprotein; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..784
FT /note="Ubiquitin carboxyl-terminal hydrolase 1"
FT /id="PRO_0000306287"
FT CHAIN 1..669
FT /note="Ubiquitin carboxyl-terminal hydrolase 1, N-terminal
FT fragment"
FT /evidence="ECO:0000250|UniProtKB:O94782"
FT /id="PRO_0000453163"
FT DOMAIN 81..784
FT /note="USP"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 34..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 90
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 592
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT SITE 669..670
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:O94782"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94782"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94782"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94782"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94782"
FT MOD_RES 767
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 84
FT /note="N -> K (in Ref. 3; AAH20007)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="P -> S (in Ref. 3; AAH18179/AAH20007)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 784 AA; 87456 MW; 56F849DC1ADE3D81 CRC64;
MPGVIPSESN GLSRGSPSKK NRLSLKFFQK KETKRALDFT DSQENEEKTS EYRGSEIDQV
VPAAQSSPVS CEKRENLLPF VGLNNLGNTC YLNSILQVLY FCPGFKTGVK HLFNIISRKK
EALKDDSNQK DKGSCKEESL ASYELICSLQ SLIISVEQLQ ASFLLNPEKY TDELATQPRR
LLNTLRELNP MYEGFLQHDA QEVLQCILGN IQETCQLLKK EEIKNLAELS GKVEEQSLQK
EETGGITSTE IDSMRNTEDV KEQLPKGNWK RKSDSESSNV KKKVKLSRES QPLEENQRQT
RSKRKAIGDT LEAAPKIIPK CVSESESAKP SQKKSKVKIN WLKPSTKQPS ILSKFCSLGK
ITTNQRSKGQ PKEKEGDVEE DLEKYGSDHT ANGGPESPGS SVTPVDSSEA KSGNKGAEQI
GFELVEKLFQ GQLVLRTRCL ECESLTERRE DFQDISVPVQ EDELSKVEES SEISPEPKTE
MKTLRWAISQ FASVERIVGE DKYFCENCHH YTEAERSLLF DKMPEVITIH LKCFAASGLE
FDCYGGGLSK INTPLLTPLK LSLEEWSTKP TNDSYGLFAV VMHSGITISS GHYTASVKVT
DLNSLELDEG NFVVDQMCEL GKPEPLTEEQ ARGTAGNYDD EVSIRVGGNA QPSKVLNKKN
VEGIGLLGGQ KSKADYELYN KASNPDKVVG TPFTDNRNSE TNDTTNGTHE SDRNKESSDQ
TGVNMNGLEN KISYVVQSLK EYEGKWLLFD DSEVKVTEEK DFLNSLSPST SPTSTPYLLF
YKKL
