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   27-MAR-2024, entry version 162.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 25.
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; 9606-ENSP00000254181; -.
DR   PeptideAtlas; Q9HBJ7; -.
DR   ProteomicsDB; 81564; -.
DR   Antibodypedia; 19631; 145 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   AGR; HGNC:18563; -.
DR   CTD; 57663; -.
DR   GeneCards; USP29; -.
DR   HGNC; HGNC:18563; USP29.
DR   HPA; ENSG00000131864; Tissue enhanced (bone marrow, 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; YIPKYLS; -.
DR   OrthoDB; 227085at2759; -.
DR   PhylomeDB; Q9HBJ7; -.
DR   TreeFam; TF323032; -.
DR   PathwayCommons; Q9HBJ7; -.
DR   SignaLink; Q9HBJ7; -.
DR   BioGRID-ORCS; 57663; 8 hits in 1186 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 male germ line stem cell (sensu Vertebrata) in testis and 72 other cell types or tissues.
DR   ExpressionAtlas; Q9HBJ7; baseline and differential.
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:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02257; Peptidase_C19; 2.
DR   CDD; cd13312; PH_USP37_like; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR   Gene3D; 2.30.29.180; Ubiquitin carboxyl-terminal hydrolase 26/29/37, pleckstrin homology-like domain; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
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; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF16674; UCH_N; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   Genevisible; Q9HBJ7; HS.
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
//