USP7
(16p13.2) , HAUSP, TEF1, Herpesvirukseen assosioitunut USP
- Also known as
- TEF1; HAUSP
- Summary
- The protein encoded by this gene belongs to the peptidase C19 family, which includes ubiquitinyl hydrolases. This protein deubiquitinates target proteins such as p53 (a tumor suppressor protein) and WASH (essential for endosomal protein recycling), and regulates their activities by counteracting the opposing ubiquitin ligase activity of proteins such as HDM2 and TRIM27, involved in the respective process. Mutations in this gene have been implicated in a neurodevelopmental disorder. [provided by RefSeq, Mar 2016]
- Expression
- Ubiquitous expression in testis (RPKM 31.0), lymph node (RPKM 24.1) and 25 other tissues
- Preferred Names
- ubiquitin carboxyl-terminal hydrolase 7
- Names
- Herpes virus-associated ubiquitin-specific protease
- deubiquitinating enzyme 7
- ubiquitin specific peptidase 7 (herpes virus-associated)
- ubiquitin specific protease 7 (herpes virus-associated)
- ubiquitin thioesterase 7
- ubiquitin-specific-processing protease 7
Conserved Domains (5) summary
COG5077
Location:39 → 1084
Location:39 → 1084
COG5077; Ubiquitin
carboxyl-terminal hydrolase [Posttranslational modification, protein
turnover, chaperones]
cd02659
Location:196 → 507
Location:196 → 507
peptidase_C19C; A
subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl
hydrolases. They are intracellular peptidases that remove ubiquitin
molecules from polyubiquinated peptides by cleavage of isopeptide
bonds. They hydrolyze bonds involving the carboxyl ...
cd03772
Location:51 → 186
Location:51 → 186
MATH_HAUSP;
Herpesvirus-associated ubiquitin-specific protease (HAUSP, also known
as USP7) family, N-terminal MATH (TRAF-like) domain; composed of
proteins similar to human HAUSP, an enzyme that specifically
catalyzes the deubiquitylation of p53 and MDM2, hence ...
pfam12436
Location:604 → 849
Location:604 → 849
USP7_ICP0_bdg;
ICP0-binding domain of Ubiquitin-specific protease 7
pfam14533
Location:859 → 1070
Location:859 → 1070
USP7_C2;
Ubiquitin-specific protease C-terminal
- Peptide structure, isoform 2
- https://www.ncbi.nlm.nih.gov/protein/NP_001273386.1
ubiquitin carboxyl-terminal hydrolase 7 isoform 2 [Homo sapiens]
NCBI Reference Sequence: NP_001273386.1Identical Proteins FASTA Graphics
LOCUS NP_001273386 1086 aa linear PRI 17-JUN-2018 DEFINITION ubiquitin carboxyl-terminal hydrolase 7 isoform 2 [Homo sapiens]. ACCESSION NP_001273386 XP_005255622 VERSION NP_001273386.1 DBSOURCE REFSEQ: accession NM_001286457.1 KEYWORDS RefSeq. SOURCE Homo sapiens (human) ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 1086) AUTHORS Xiang Q, Ju H, Li Q, Mei SC, Chen D, Choi YB and Nicholas J. TITLE Human Herpesvirus 8 Interferon Regulatory Factors 1 and 3 Mediate Replication and Latency Activities via Interactions with USP7 Deubiquitinase JOURNAL J. Virol. 92 (7), e02003-17 (2018) PUBMED 29343584 REMARK GeneRIF: ubiquitin-specific protease 7 (USP7) deubiquitinase targeting by vIRF-3 (in addition to previously reported USP7 binding by vIRF-1 and vIRF-4); the importance of vIRF-1 and vIRF-3 interactions with USP7 for latent PEL cell growth and viability; and the positive and negative contributions, respectively, of USP7 targeting by vIRF-1 and vIRF-3 to HHV-8 productive replication. Publication Status: Online-Only REFERENCE 2 (residues 1 to 1086) AUTHORS Wang F, Wang L, Wu J, Sokirniy I, Nguyen P, Bregnard T, Weinstock J, Mattern M, Bezsonova I, Hancock WW and Kumar S. TITLE Active site-targeted covalent irreversible inhibitors of USP7 impair the functions of Foxp3+ T-regulatory cells by promoting ubiquitination of Tip60 JOURNAL PLoS ONE 12 (12), e0189744 (2017) PUBMED 29236775 REMARK GeneRIF: demonstrate that both USP7 and various USP7 substrates are subjected to Lys48-mediated ubiquitin modification, consistent with increased proteasomal degradation of these proteins because of USP7 inhibition Publication Status: Online-Only REFERENCE 3 (residues 1 to 1086) AUTHORS Novellasdemunt L, Foglizzo V, Cuadrado L, Antas P, Kucharska A, Encheva V, Snijders AP and Li VSW. TITLE USP7 Is a Tumor-Specific WNT Activator for APC-Mutated Colorectal Cancer by Mediating beta-Catenin Deubiquitination JOURNAL Cell Rep 21 (3), 612-627 (2017) PUBMED 29045831 REMARK GeneRIF: USP7 depletion in APC-mutated colorectal cancer inhibits Wnt activation by restoring beta-catenin ubiquitination, drives differentiation, and suppresses xenograft tumor growth. REFERENCE 4 (residues 1 to 1086) AUTHORS Tang Y, Lv L, Li W, Zhang X, Jiang Y, Ge W and Zhou Y. TITLE Protein deubiquitinase USP7 is required for osteogenic differentiation of human adipose-derived stem cells JOURNAL Stem Cell Res Ther 8 (1), 186 (2017) PUBMED 28807012 REMARK GeneRIF: protein deubiquitinase USP7 is an essential player in osteogenic differentiation of Human adipose-derived stem cells. Publication Status: Online-Only REFERENCE 5 (residues 1 to 1086) AUTHORS Jiang L, Xiong J, Zhan J, Yuan F, Tang M, Zhang C, Cao Z, Chen Y, Lu X, Li Y, Wang H, Wang L, Wang J, Zhu WG and Wang H. TITLE Ubiquitin-specific peptidase 7 (USP7)-mediated deubiquitination of the histone deacetylase SIRT7 regulates gluconeogenesis JOURNAL J. Biol. Chem. 292 (32), 13296-13311 (2017) PUBMED 28655758 REMARK GeneRIF: Data suggest that SIRT7 undergoes Lys-63 polyubiquitination, later removed by USP7 to repress enzymatic activity of SIRT7; USP7 and SIRT7 regulate gluconeogenesis via expression of glucose-6-phosphatase catalytic subunit (G6PC); SIRT7 targets G6PC promoter through ELK4. (SIRT7 = sirtuin 7; USP7 = ubiquitin specific peptidase 7; G6PC = glucose-6-phosphatase catalytic subunit; ELK4 = transcription factor ELK4) REFERENCE 6 (residues 1 to 1086) AUTHORS Hao YH, Fountain MD Jr, Fon Tacer K, Xia F, Bi W, Kang SH, Patel A, Rosenfeld JA, Le Caignec C, Isidor B, Krantz ID, Noon SE, Pfotenhauer JP, Morgan TM, Moran R, Pedersen RC, Saenz MS, Schaaf CP and Potts PR. TITLE USP7 Acts as a Molecular Rheostat to Promote WASH-Dependent Endosomal Protein Recycling and Is Mutated in a Human Neurodevelopmental Disorder JOURNAL Mol. Cell 59 (6), 956-969 (2015) PUBMED 26365382 REMARK GeneRIF: The USP7 deubiquitinating enzyme is an integral component of the MAGE-L2-TRIM27 ligase and is essential for WASH-mediated endosomal actin assembly and protein recycling. REFERENCE 7 (residues 1 to 1086) AUTHORS Robinson PA, Lomonte P, Leek, Markham AF and Everett RD. TITLE Assignment1 of herpesvirus-associated ubiquitin-specific protease gene HAUSP to human chromosome band 16p13.3 by in situ hybridization JOURNAL Cytogenet. Cell Genet. 83 (1-2), 100 (1998) PUBMED 9925944 REFERENCE 8 (residues 1 to 1086) AUTHORS D'Andrea A and Pellman D. TITLE Deubiquitinating enzymes: a new class of biological regulators JOURNAL Crit. Rev. Biochem. Mol. Biol. 33 (5), 337-352 (1998) PUBMED 9827704 REMARK Review article REFERENCE 9 (residues 1 to 1086) AUTHORS Everett RD, Meredith M, Orr A, Cross A, Kathoria M and Parkinson J. TITLE A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein JOURNAL EMBO J. 16 (7), 1519-1530 (1997) PUBMED 9130697 REFERENCE 10 (residues 1 to 1086) AUTHORS Everett RD, Meredith M, Orr A, Cross A, Kathoria M and Parkinson J. TITLE A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein JOURNAL EMBO J. 16 (3), 566-577 (1997) PUBMED 9034339 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from AK316441.1 and AC022167.7. On Nov 6, 2013 this sequence version replaced XP_005255622.1. Summary: The protein encoded by this gene belongs to the peptidase C19 family, which includes ubiquitinyl hydrolases. This protein deubiquitinates target proteins such as p53 (a tumor suppressor protein) and WASH (essential for endosomal protein recycling), and regulates their activities by counteracting the opposing ubiquitin ligase activity of proteins such as HDM2 and TRIM27, involved in the respective process. Mutations in this gene have been implicated in a neurodevelopmental disorder. [provided by RefSeq, Mar 2016]. Transcript Variant: This variant (2) differs in the 5' UTR and coding sequence compared to variant 1. The resulting isoform (2) has a shorter and distinct N-terminus compared to isoform 1. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK316441.1, AY376241.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## FEATURES Location/Qualifiers source 1..1086 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="16" /map="16p13.2" Protein 1..1086 /product="ubiquitin carboxyl-terminal hydrolase 7 isoform 2" /EC_number="3.4.19.12" /note="Herpes virus-associated ubiquitin-specific protease; ubiquitin specific protease 7 (herpes virus-associated); ubiquitin carboxyl-terminal hydrolase 7; ubiquitin thioesterase 7; deubiquitinating enzyme 7; ubiquitin-specific-processing protease 7; ubiquitin specific peptidase 7 (herpes virus-associated)" /calculated_mol_wt=126066 Region 39..1084 /region_name="COG5077" /note="Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]" /db_xref="CDD:227409" Region 51..186 /region_name="MATH_HAUSP" /note="Herpesvirus-associated ubiquitin-specific protease (HAUSP, also known as USP7) family, N-terminal MATH (TRAF-like) domain; composed of proteins similar to human HAUSP, an enzyme that specifically catalyzes the deubiquitylation of p53 and MDM2, hence...; cd03772" /db_xref="CDD:239741" Site order(88,102,136,148..153) /site_type="other" /note="substrate binding site [chemical binding]" /db_xref="CDD:239741" Region 196..507 /region_name="peptidase_C19C" /note="A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl...; cd02659" /db_xref="CDD:239124" Site order(202,207,448,466) /site_type="active" /db_xref="CDD:239124" Region 604..849 /region_name="USP7_ICP0_bdg" /note="ICP0-binding domain of Ubiquitin-specific protease 7; pfam12436" /db_xref="CDD:289221" Region 859..1070 /region_name="USP7_C2" /note="Ubiquitin-specific protease C-terminal; pfam14533" /db_xref="CDD:291217" CDS 1..1086 /gene="USP7" /gene_synonym="HAUSP; TEF1" /coded_by="NM_001286457.1:117..3377" /note="isoform 2 is encoded by transcript variant 2" /db_xref="CCDS:CCDS66941.1" /db_xref="GeneID:7874" /db_xref="HGNC:HGNC:12630" /db_xref="MIM:602519" ORIGIN 1 magnhrlgle agdtddppri tqnpvingnv alsdghntae edmeddtswr seatfqftve 61 rfsrlsesvl sppcfvrnlp wkimvmprfy pdrphqksvg fflqcnaesd stswschaqa 121 vlkiinyrdd eksfsrrish lffhkendwg fsnfmawsev tdpekgfidd dkvtfevfvq 181 adaphgvawd skkhtgyvgl knqgatcymn sllqtlfftn qlrkavymmp tegddssksv 241 plalqrvfye lqhsdkpvgt kkltksfgwe tldsfmqhdv qelcrvlldn venkmkgtcv 301 egtipklfrg kmvsyiqcke vdyrsdrred yydiqlsikg kknifesfvd yvavgqldgd 361 nkydagehgl qeaekgvkfl tlppvlhlql mrfmydpqtd qnikindrfe fpeqlpldef 421 lqktdpkdpa nyilhavlvh sgdnhgghyv vylnpkgdgk wckfdddvvs rctkeeaieh 481 nygghdddls vrhctnayml vyiresklse vlqavtdhdi pqqlverlqe ekrieaqkrk 541 erqeahlymq vqivaedqfc ghqgndmyde ekvkytvfkv lknsslaefv qslsqtmgfp 601 qdqirlwpmq arsngtkrpa mldneadgnk tmielsdnen pwtifletvd pelaasgatl 661 pkfdkdhdvm lflkmydpkt rslnycghiy tpisckirdl lpvmcdragf iqdtslilye 721 evkpnlteri qdydvsldka ldelmdgdii vfqkddpend nselptakey frdlyhrvdv 781 ifcdktipnd pgfvvtlsnr mnyfqvaktv aqrlntdpml lqffksqgyr dgpgnplrhn 841 yegtlrdllq ffkprqpkkl yyqqlkmkit dfenrrsfkc iwlnsqfree eitlypdkhg 901 cvrdlleeck kavelgekas gklrlleivs ykiigvhqed elleclspat srtfrieeip 961 ldqvdidken emlvtvahfh kevfgtfgip fllrihqgeh frevmkriqs lldiqekefe 1021 kfkfaivmmg rhqyinedey evnlkdfepq pgnmshprpw lgldhfnkap krsrytylek 1081 aikihn //
Musitiin ilman suomennosta 5.6. 2018
Lisäartikkeleita on vielä PubMed lähteessä. Teen myöhemmin yhteenvetoa.
Related articles in PubMed
- Protein deubiquitinase USP7 is required for osteogenic differentiation of human adipose-derived stem cells. Tang Y, et al. Stem Cell Res Ther, 2017 Aug 14. PMID 28807012, Free PMC Article
- Structure of USP7 catalytic domain and three Ubl-domains reveals a connector α-helix with regulatory role. Kim RQ, et al. J Struct Biol, 2016 Jul. PMID 27183903
- Small-molecule inhibitors of USP7 induce apoptosis through oxidative and endoplasmic reticulum stress in cancer cells. Lee G, et al. Biochem Biophys Res Commun, 2016 Jan 29. PMID 26768359
- USP7 overexpression predicts a poor prognosis in lung squamous cell carcinoma and large cell carcinoma. Zhao GY, et al. Tumour Biol, 2015 Mar. PMID 25519684, Free PMC Article
- HAUSP compartmentalization in chronic myeloid leukemia. Morotti A, et al. Eur J Haematol, 2015 Apr. PMID 25082234
GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?
- USP7 depletion in APC-mutated colorectal cancer inhibits Wnt activation by restoring beta-catenin ubiquitination, drives differentiation, and suppresses xenograft tumor growth.
- USP7 is RNF169 interacting protein.Expression of USP7 and RNF169 positively correlated in breast cancer.
- protein deubiquitinase USP7 is an essential player in osteogenic differentiation of Human adipose-derived stem cells.
- ubiquitin-specific protease 7 (USP7) deubiquitinase targeting by vIRF-3 (in addition to previously reported USP7 binding by vIRF-1 and vIRF-4); the importance of vIRF-1 and vIRF-3 interactions with USP7 for latent PEL cell growth and viability; and the positive and negative contributions, respectively, of USP7 targeting by vIRF-1 and vIRF-3 to HHV-8 productive replication.
- demonstrate that both USP7 and various USP7 substrates are subjected to Lys48-mediated ubiquitin modification, consistent with increased proteasomal degradation of these proteins because of USP7 inhibition
- Here we study the transition between USP7 states. We provide a crystal structure of USP7(CD123) and show that catalytic domain CD and the first 3 Ubl domains Ubl123 are connected via an extended charged alpha helix. Mutational analysis is used to determine whether the charge and rigidity of this 'connector helix' are important for full USP7 activity
- the overexpression of USP7 might promote cell proliferation by deubiquitinating Ki-67 protein
- these data identify DUB3 and USP7 as factors that regulate DNA replication by controlling Geminin protein stability, and suggest that USP7 may be involved in Geminin dysregulation during breast cancer progression.
- Molecular mechanisms of USP7 substrate recognition and C-terminal activation have been described.
- USP7 promotes breast carcinogenesis by stabilizing PHF8 and upregulating cyclin A2. and the interaction between USP7 and PHF8 is augmented during DNA damage.
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