UBP29_HUMAN
ID UBP29_HUMAN Reviewed; 922 AA.
AC Q9HBJ7;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 29 {ECO:0000305};
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q9ES63};
DE AltName: Full=Deubiquitinating enzyme 29;
DE AltName: Full=Ubiquitin thioesterase 29;
DE AltName: Full=Ubiquitin-specific-processing protease 29;
GN Name=USP29 {ECO:0000303|PubMed:10958632, ECO:0000312|HGNC:HGNC:18563};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10958632; DOI=10.1101/gr.10.8.1138;
RA Kim J., Noskov V.N., Lu X., Bergmann A., Ren X., Warth T., Richardson P.,
RA Kouprina N., Stubbs L.;
RT "Discovery of a novel, paternally expressed ubiquitin-specific processing
RT protease gene through comparative analysis of an imprinted region of mouse
RT chromosome 7 and human chromosome 19q13.4.";
RL Genome Res. 10:1138-1147(2000).
RN [2]
RP FUNCTION.
RX PubMed=32457395; DOI=10.1038/s41422-020-0341-6;
RA Zhang Q., Tang Z., An R., Ye L., Zhong B.;
RT "USP29 maintains the stability of cGAS and promotes cellular antiviral
RT responses and autoimmunity.";
RL Cell Res. 30:914-927(2020).
CC -!- FUNCTION: Deubiquitinase involved in innate antiviral immunity by
CC mediating 'Lys-48'-linked deubiquitination of CGAS, thereby promoting
CC its stabilization. {ECO:0000269|PubMed:32457395}.
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:Q9ES63};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q9ES63}. Note=Localizes to perinuclear region in
CC response to herpes simplex virus-1 (HSV-1) infection.
CC {ECO:0000250|UniProtKB:Q9ES63}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; AF229438; AAG10401.1; -; mRNA.
DR CCDS; CCDS33124.1; -.
DR RefSeq; NP_065954.1; NM_020903.2.
DR AlphaFoldDB; Q9HBJ7; -.
DR SMR; Q9HBJ7; -.
DR BioGRID; 121696; 19.
DR IntAct; Q9HBJ7; 2.
DR MINT; Q9HBJ7; -.
DR STRING; 9606.ENSP00000254181; -.
DR MEROPS; C19.040; -.
DR iPTMnet; Q9HBJ7; -.
DR PhosphoSitePlus; Q9HBJ7; -.
DR BioMuta; USP29; -.
DR DMDM; 23396891; -.
DR EPD; Q9HBJ7; -.
DR MassIVE; Q9HBJ7; -.
DR PaxDb; Q9HBJ7; -.
DR PeptideAtlas; Q9HBJ7; -.
DR PRIDE; Q9HBJ7; -.
DR ProteomicsDB; 81564; -.
DR Antibodypedia; 19631; 137 antibodies from 25 providers.
DR DNASU; 57663; -.
DR Ensembl; ENST00000254181.9; ENSP00000254181.3; ENSG00000131864.11.
DR Ensembl; ENST00000598197.1; ENSP00000470747.1; ENSG00000131864.11.
DR GeneID; 57663; -.
DR KEGG; hsa:57663; -.
DR MANE-Select; ENST00000254181.9; ENSP00000254181.3; NM_020903.3; NP_065954.1.
DR UCSC; uc002qny.4; human.
DR CTD; 57663; -.
DR GeneCards; USP29; -.
DR HGNC; HGNC:18563; USP29.
DR HPA; ENSG00000131864; Tissue enhanced (brain, testis).
DR MIM; 609546; gene.
DR neXtProt; NX_Q9HBJ7; -.
DR OpenTargets; ENSG00000131864; -.
DR PharmGKB; PA38349; -.
DR VEuPathDB; HostDB:ENSG00000131864; -.
DR eggNOG; KOG1868; Eukaryota.
DR GeneTree; ENSGT00940000161929; -.
DR HOGENOM; CLU_012557_0_0_1; -.
DR InParanoid; Q9HBJ7; -.
DR OMA; YNCEMCK; -.
DR OrthoDB; 129045at2759; -.
DR PhylomeDB; Q9HBJ7; -.
DR TreeFam; TF323032; -.
DR PathwayCommons; Q9HBJ7; -.
DR SignaLink; Q9HBJ7; -.
DR BioGRID-ORCS; 57663; 8 hits in 1109 CRISPR screens.
DR GenomeRNAi; 57663; -.
DR Pharos; Q9HBJ7; Tbio.
DR PRO; PR:Q9HBJ7; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9HBJ7; protein.
DR Bgee; ENSG00000131864; Expressed in right testis and 70 other tissues.
DR ExpressionAtlas; Q9HBJ7; baseline and differential.
DR Genevisible; Q9HBJ7; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd13312; PH_USP37_like; 1.
DR Gene3D; 2.30.29.180; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR033381; USP29.
DR InterPro; IPR032069; USP37-like_PH.
DR InterPro; IPR038093; USP37-like_PH_sf.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006:SF667; PTHR24006:SF667; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF16674; UCH_N; 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 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Immunity; Innate immunity; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..922
FT /note="Ubiquitin carboxyl-terminal hydrolase 29"
FT /id="PRO_0000080660"
FT DOMAIN 285..885
FT /note="USP"
FT REGION 160..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 294
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 840
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT VARIANT 368
FT /note="N -> S (in dbSNP:rs1027392)"
FT /id="VAR_024590"
FT VARIANT 586
FT /note="E -> K (in dbSNP:rs3795003)"
FT /id="VAR_022055"
SQ SEQUENCE 922 AA; 104156 MW; 122B56AE6FFFF364 CRC64;
MISLKVCGFI QIWSQKTGMT KLKEALIETV QRQKEIKLVV TFKSGKFIRI FQLSNNIRSV
VLRHCKKRQS HLRLTLKNNV FLFIDKLSYR DAKQLNMFLD IIHQNKSQQP MKSDDDWSVF
ESRNMLKEID KTSFYSICNK PSYQKMPLFM SKSPTHVKKG ILENQGGKGQ NTLSSDVQTN
EDILKEDNPV PNKKYKTDSL KYIQSNRKNP SSLEDLEKDR DLKLGPSFNT NCNGNPNLDE
TVLATQTLNA KNGLTSPLEP EHSQGDPRCN KAQVPLDSHS QQLQQGFPNL GNTCYMNAVL
QSLFAIPSFA DDLLTQGVPW EYIPFEALIM TLTQLLALKD FCSTKIKREL LGNVKKVISA
VAEIFSGNMQ NDAHEFLGQC LDQLKEDMEK LNATLNTGKE CGDENSSPQM HVGSAATKVF
VCPVVANFEF ELQLSLICKA CGHAVLKVEP NNYLSINLHQ ETKPLPLSIQ NSLDLFFKEE
ELEYNCQMCK QKSCVARHTF SRLSRVLIIH LKRYSFNNAW LLVKNNEQVY IPKSLSLSSY
CNESTKPPLP LSSSAPVGKC EVLEVSQEMI SEINSPLTPS MKLTSESSDS LVLPVEPDKN
ADLQRFQRDC GDASQEQHQR DLENGSALES ELVHFRDRAI GEKELPVADS LMDQGDISLP
VMYEDGGKLI SSPDTRLVEV HLQEVPQHPE LQKYEKTNTF VEFNFDSVTE STNGFYDCKE
NRIPEGSQGM AEQLQQCIEE SIIDEFLQQA PPPGVRKLDA QEHTEETLNQ STELRLQKAD
LNHLGALGSD NPGNKNILDA ENTRGEAKEL TRNVKMGDPL QAYRLISVVS HIGSSPNSGH
YISDVYDFQK QAWFTYNDLC VSEISETKMQ EARLHSGYIF FYMHNGIFEE LLRKAENSRL
PSTQAGVIPQ GEYEGDSLYR PA
