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Identification
HMDB Protein ID HMDBP10123
Secondary Accession Numbers
  • 16079
Name Ubiquitin carboxyl-terminal hydrolase 1
Synonyms
  1. Deubiquitinating enzyme 1
  2. Ubiquitin thiolesterase 1
  3. Ubiquitin-specific-processing protease 1
  4. hUBP
Gene Name USP1
Protein Type Enzyme
Biological Properties
General Function Involved in ubiquitin thiolesterase activity
Specific 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
Pathways Not Available
Reactions Not Available
GO Classification
Function
hydrolase activity, acting on ester bonds
catalytic activity
hydrolase activity
ubiquitin thiolesterase activity
thiolester hydrolase activity
Process
metabolic process
catabolic process
macromolecule catabolic process
cellular macromolecule catabolic process
modification-dependent macromolecule catabolic process
modification-dependent protein catabolic process
ubiquitin-dependent protein catabolic process
Cellular Location
  1. Nucleus
Gene Properties
Chromosome Location Chromosome:1
Locus 1p31.3
SNPs USP1
Gene Sequence
>2358 bp
ATGCCTGGTGTCATACCTAGTGAAAGTAATGGACTTTCAAGAGGTAGCCCTTCAAAGAAA
AACAGACTTTCCTTAAAGTTTTTTCAGAAAAAGGAAACTAAGAGAGCTTTGGATTTCACA
GATTCTCAAGAAAATGAAGAAAAAGCTTCTGAATATAGAGCATCTGAAATTGATCAAGTT
GTTCCTGCAGCACAGTCTTCACCTATAAACTGTGAGAAGAGAGAAAACTTGTTACCATTT
GTGGGACTGAATAATCTCGGCAATACTTGCTATCTTAATAGTATACTTCAGGTATTATAT
TTTTGTCCCGGTTTTAAATCTGGAGTAAAGCACTTATTTAATATTATTTCAAGGAAGAAA
GAAGCTCTAAAGGATGAAGCCAATCAAAAAGACAAGGGAAATTGCAAAGAAGATTCTTTG
GCAAGTTATGAATTGATATGCAGTTTACAGTCCTTAATCATTTCGGTTGAACAGCTCCAG
GCTAGTTTTCTCTTAAATCCAGAGAAATATACTGATGAACTTGCCACTCAGCCAAGGCGA
CTGCTTAACACACTGAGGGAACTCAACCCTATGTATGAAGGATATCTACAGCATGATGCA
CAGGAAGTATTACAATGTATTTTGGGAAACATTCAAGAAACATGCCAACTCCTAAAAAAA
GAAGAAGTAAAAAATGTGGCAGAATTACCTACTAAGGTAGAAGAAATACCTCATCCGAAA
GAGGAAATGAATGGTATTAACAGCATAGAGATGGACAGTATGAGGCATTCTGAAGACTTT
AAAGAGAAACTCCCAAAAGGAAATGGGAAAAGAAAAAGTGACACTGAATTTGGTAACATG
AAGAAAAAAGTTAAATTATCCAAGGAACACCAGTCATTGGAAGAGAACCAGAGACAAACT
AGATCAAAAAGAAAAGCTACAAGTGATACATTAGAGAGTCCTCCTAAAATAATTCCCAAG
TATATTTCTGAAAATGAGAGTCCAAGACCCTCACAAAAGAAATCAAGAGTTAAAATAAAT
TGGTTAAAGTCTGCAACTAAGCAACCCAGCATTCTTTCTAAATTTTGTAGTCTGGGAAAA
ATAACAACAAACCAAGGAGTCAAAGGACAATCTAAAGAAAATGAATGTGATCCTGAAGAG
GACTTGGGGAAGTGTGAAAGTGATAACACAACTAATGGTTGTGGACTTGAATCTCCAGGA
AATACTGTTACACCTGTAAATGTTAATGAAGTTAAACCCATAAACAAAGGTGAAGAACAA
ATTGGTTTTGAGCTAGTGGAGAAATTATTTCAAGGTCAGCTGGTATTAAGGACGCGTTGC
TTGGAATGTGAAAGTTTAACAGAAAGAAGAGAAGATTTTCAAGACATCAGTGTGCCAGTA
CAAGAAGATGAGCTTTCCAAAGTAGAGGAGAGTTCTGAAATTTCTCCAGAGCCAAAAACA
GAAATGAAGACCCTGAGATGGGCAATTTCACAATTTGCTTCAGTAGAAAGGATTGTAGGA
GAAGATAAATATTTCTGTGAAAACTGCCATCATTATACTGAAGCTGAACGAAGTCTTTTG
TTTGACAAAATGCCTGAAGTTATAACTATTCATTTGAAGTGCTTTGCTGCTAGTGGTTTG
GAGTTTGATTGTTATGGTGGTGGACTTTCCAAGATCAACACTCCTTTATTGACACCTCTT
AAATTGTCACTAGAAGAATGGAGCACAAAGCCAACTAACGACAGCTATGGATTATTTGCG
GTTGTGATGCATAGTGGCATTACAATTAGTAGTGGGCATTACACTGCTTCTGTTAAAGTC
ACTGACCTTAACAGTTTAGAACTAGATAAAGGAAATTTTGTGGTTGACCAAATGTGTGAA
ATAGGTAAGCCAGAACCATTGAATGAGGAGGAAGCAAGGGGTGTGGTTGAGAATTATAAT
GATGAAGAAGTGTCAATTAGAGTTGGTGGAAATACACAGCCAAGTAAAGTTTTGAACAAA
AAAAATGTAGAAGCTATTGGACTTCTTGGAGGACAAAAGAGCAAAGCAGATTATGAGCTA
TACAACAAAGCCTCTAATCCTGATAAGGTTGCTAGTACAGCGTTTGCTGAAAATAGAAAT
TCTGAGACTAGTGATACTACTGGGACCCATGAATCTGATAGAAACAAGGAATCCAGTGAC
CAAACAGGCATTAATATTAGTGGATTTGAGAACAAAATTTCATACGTAGTGCAAAGCTTA
AAGGAGTATGAGGGGAAGTGGTTGCTTTTTGATGATTCTGAAGTCAAAGTTACTGAAGAG
AAGGACTTTCTGAATTCTCTTTCCCCTTCTACATCTCCTACTTCTACTCCTTACTTGCTA
TTTTATAAGAAATTATAG
Protein Properties
Number of Residues 785
Molecular Weight 88206.5
Theoretical pI 5.13
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Ubiquitin carboxyl-terminal hydrolase 1
MPGVIPSESNGLSRGSPSKKNRLSLKFFQKKETKRALDFTDSQENEEKASEYRASEIDQV
VPAAQSSPINCEKRENLLPFVGLNNLGNTCYLNSILQVLYFCPGFKSGVKHLFNIISRKK
EALKDEANQKDKGNCKEDSLASYELICSLQSLIISVEQLQASFLLNPEKYTDELATQPRR
LLNTLRELNPMYEGYLQHDAQEVLQCILGNIQETCQLLKKEEVKNVAELPTKVEEIPHPK
EEMNGINSIEMDSMRHSEDFKEKLPKGNGKRKSDTEFGNMKKKVKLSKEHQSLEENQRQT
RSKRKATSDTLESPPKIIPKYISENESPRPSQKKSRVKINWLKSATKQPSILSKFCSLGK
ITTNQGVKGQSKENECDPEEDLGKCESDNTTNGCGLESPGNTVTPVNVNEVKPINKGEEQ
IGFELVEKLFQGQLVLRTRCLECESLTERREDFQDISVPVQEDELSKVEESSEISPEPKT
EMKTLRWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKMPEVITIHLKCFAASGL
EFDCYGGGLSKINTPLLTPLKLSLEEWSTKPTNDSYGLFAVVMHSGITISSGHYTASVKV
TDLNSLELDKGNFVVDQMCEIGKPEPLNEEEARGVVENYNDEEVSIRVGGNTQPSKVLNK
KNVEAIGLLGGQKSKADYELYNKASNPDKVASTAFAENRNSETSDTTGTHESDRNKESSD
QTGINISGFENKISYVVQSLKEYEGKWLLFDDSEVKVTEEKDFLNSLSPSTSPTSTPYLL
FYKKL
GenBank ID Protein 3928762
UniProtKB/Swiss-Prot ID O94782
UniProtKB/Swiss-Prot Entry Name UBP1_HUMAN
PDB IDs Not Available
GenBank Gene ID AB014458
GeneCard ID USP1
GenAtlas ID USP1
HGNC ID HGNC:12607
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  3. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed:17924679 ]
  4. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  5. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed:11230166 ]
  6. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed:17525332 ]
  7. Fujiwara T, Saito A, Suzuki M, Shinomiya H, Suzuki T, Takahashi E, Tanigami A, Ichiyama A, Chung CH, Nakamura Y, Tanaka K: Identification and chromosomal assignment of USP1, a novel gene encoding a human ubiquitin-specific protease. Genomics. 1998 Nov 15;54(1):155-8. [PubMed:9806842 ]
  8. Nijman SM, Huang TT, Dirac AM, Brummelkamp TR, Kerkhoven RM, D'Andrea AD, Bernards R: The deubiquitinating enzyme USP1 regulates the Fanconi anemia pathway. Mol Cell. 2005 Feb 4;17(3):331-9. [PubMed:15694335 ]
  9. Huang TT, Nijman SM, Mirchandani KD, Galardy PJ, Cohn MA, Haas W, Gygi SP, Ploegh HL, Bernards R, D'Andrea AD: Regulation of monoubiquitinated PCNA by DUB autocleavage. Nat Cell Biol. 2006 Apr;8(4):339-47. Epub 2006 Mar 12. [PubMed:16531995 ]
  10. Cohn MA, Kowal P, Yang K, Haas W, Huang TT, Gygi SP, D'Andrea AD: A UAF1-containing multisubunit protein complex regulates the Fanconi anemia pathway. Mol Cell. 2007 Dec 14;28(5):786-97. [PubMed:18082604 ]