UBP53_HUMAN
ID UBP53_HUMAN Reviewed; 1073 AA.
AC Q70EK8; Q68DA5; Q8WVQ5; Q9P2J7;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Inactive ubiquitin carboxyl-terminal hydrolase 53;
DE AltName: Full=Inactive ubiquitin-specific peptidase 53;
GN Name=USP53 {ECO:0000312|HGNC:HGNC:29255};
GN Synonyms=KIAA1350 {ECO:0000312|EMBL:BAA92588.1};
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] {ECO:0000305, ECO:0000312|EMBL:CAE47751.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=14715245; DOI=10.1016/j.bbrc.2003.12.050;
RA Quesada V., Diaz-Perales A., Gutierrez-Fernandez A., Garabaya C., Cal S.,
RA Lopez-Otin C.;
RT "Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
RT proteases.";
RL Biochem. Biophys. Res. Commun. 314:54-62(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAA92588.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 163-1073, AND VARIANT ARG-962.
RC TISSUE=Brain {ECO:0000312|EMBL:BAA92588.1};
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAH17382.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 869-1073.
RC TISSUE=Brain {ECO:0000312|EMBL:AAH17382.1};
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).
CC -!- FUNCTION: Tight junction-associated protein that is involved in the
CC survival of auditory hair cells and hearing. Maybe by modulating the
CC barrier properties and mechanical stability of tight junctions (By
CC similarity). Has no peptidase activity (PubMed:14715245).
CC {ECO:0000250|UniProtKB:P15975, ECO:0000269|PubMed:14715245}.
CC -!- SUBUNIT: Interacts (via the C-terminal region) with the heterodimer
CC TJP1:TJP2. {ECO:0000250|UniProtKB:P15975}.
CC -!- INTERACTION:
CC Q70EK8; P46108: CRK; NbExp=12; IntAct=EBI-742050, EBI-886;
CC Q70EK8; P46109: CRKL; NbExp=5; IntAct=EBI-742050, EBI-910;
CC Q70EK8; Q5PRF9: SAMD4B; NbExp=3; IntAct=EBI-742050, EBI-1047489;
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000250|UniProtKB:P15975}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in skeletal muscle and
CC heart. {ECO:0000269|PubMed:14715245}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000255}.
CC -!- CAUTION: Although the active site residues are conserved, lacks the
CC conserved His residue which is normally found 9 residues before the
CC catalytic His. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17382.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ583824; CAE47751.1; -; mRNA.
DR EMBL; CR749490; CAH18315.1; -; mRNA.
DR EMBL; AB037771; BAA92588.1; -; mRNA.
DR EMBL; BC017382; AAH17382.1; ALT_INIT; mRNA.
DR CCDS; CCDS43265.1; -.
DR RefSeq; NP_061923.2; NM_019050.2.
DR RefSeq; XP_005263130.1; XM_005263073.3.
DR RefSeq; XP_011530339.1; XM_011532037.2.
DR RefSeq; XP_016863801.1; XM_017008312.1.
DR RefSeq; XP_016863802.1; XM_017008313.1.
DR RefSeq; XP_016863803.1; XM_017008314.1.
DR RefSeq; XP_016863804.1; XM_017008315.1.
DR AlphaFoldDB; Q70EK8; -.
DR SMR; Q70EK8; -.
DR BioGRID; 120020; 41.
DR IntAct; Q70EK8; 28.
DR STRING; 9606.ENSP00000409906; -.
DR MEROPS; C19.081; -.
DR iPTMnet; Q70EK8; -.
DR PhosphoSitePlus; Q70EK8; -.
DR BioMuta; USP53; -.
DR DMDM; 88943889; -.
DR EPD; Q70EK8; -.
DR jPOST; Q70EK8; -.
DR MassIVE; Q70EK8; -.
DR MaxQB; Q70EK8; -.
DR PaxDb; Q70EK8; -.
DR PeptideAtlas; Q70EK8; -.
DR PRIDE; Q70EK8; -.
DR ProteomicsDB; 68536; -.
DR Antibodypedia; 26664; 113 antibodies from 23 providers.
DR DNASU; 54532; -.
DR Ensembl; ENST00000450251.6; ENSP00000409906.1; ENSG00000145390.12.
DR Ensembl; ENST00000692078.1; ENSP00000509606.1; ENSG00000145390.12.
DR GeneID; 54532; -.
DR KEGG; hsa:54532; -.
DR MANE-Select; ENST00000692078.1; ENSP00000509606.1; NM_001371395.1; NP_001358324.1.
DR UCSC; uc003icr.5; human.
DR CTD; 54532; -.
DR DisGeNET; 54532; -.
DR GeneCards; USP53; -.
DR HGNC; HGNC:29255; USP53.
DR HPA; ENSG00000145390; Low tissue specificity.
DR MalaCards; USP53; -.
DR MIM; 617431; gene.
DR neXtProt; NX_Q70EK8; -.
DR OpenTargets; ENSG00000145390; -.
DR PharmGKB; PA134940368; -.
DR VEuPathDB; HostDB:ENSG00000145390; -.
DR eggNOG; KOG1887; Eukaryota.
DR GeneTree; ENSGT00940000156337; -.
DR HOGENOM; CLU_287278_0_0_1; -.
DR InParanoid; Q70EK8; -.
DR OMA; MEQCYSE; -.
DR OrthoDB; 101145at2759; -.
DR PhylomeDB; Q70EK8; -.
DR TreeFam; TF323194; -.
DR PathwayCommons; Q70EK8; -.
DR SignaLink; Q70EK8; -.
DR BioGRID-ORCS; 54532; 16 hits in 1073 CRISPR screens.
DR ChiTaRS; USP53; human.
DR GeneWiki; USP53; -.
DR GenomeRNAi; 54532; -.
DR Pharos; Q70EK8; Tbio.
DR PRO; PR:Q70EK8; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q70EK8; protein.
DR Bgee; ENSG00000145390; Expressed in calcaneal tendon and 182 other tissues.
DR ExpressionAtlas; Q70EK8; baseline and differential.
DR Genevisible; Q70EK8; HS.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR GO; GO:0010996; P:response to auditory stimulus; IBA:GO_Central.
DR GO; GO:0007605; P:sensory perception of sound; IBA:GO_Central.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR040143; USP53.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR22975:SF6; PTHR22975:SF6; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW Cell junction; Reference proteome; Tight junction.
FT CHAIN 1..1073
FT /note="Inactive ubiquitin carboxyl-terminal hydrolase 53"
FT /id="PRO_0000080681"
FT DOMAIN 30..351
FT /note="USP"
FT REGION 391..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 962
FT /note="S -> R (in dbSNP:rs3749591)"
FT /evidence="ECO:0000269|PubMed:10718198"
FT /id="VAR_051541"
FT CONFLICT 190
FT /note="Missing (in Ref. 1; CAE47751)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="A -> V (in Ref. 2; CAH18315)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="F -> FF (in Ref. 2; CAH18315)"
FT /evidence="ECO:0000305"
FT CONFLICT 611
FT /note="P -> A (in Ref. 2; CAH18315)"
FT /evidence="ECO:0000305"
FT CONFLICT 869
FT /note="T -> G (in Ref. 4; AAH17382)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1073 AA; 120806 MW; 2A5E8B0AB4158878 CRC64;
MAWVKFLRKP GGNLGKVYQP GSMLSLAPTK GLLNEPGQNS CFLNSAVQVL WQLDIFRRSL
RVLTGHVCQG DACIFCALKT IFAQFQHSRE KALPSDNIRH ALAESFKDEQ RFQLGLMDDA
AECFENMLER IHFHIVPSRD ADMCTSKSCI THQKFAMTLY EQCVCRSCGA SSDPLPFTEF
VRYISTTALC NEVERMLERH ERFKPEMFAE LLQAANTTDD YRKCPSNCGQ KIKIRRVLMN
CPEIVTIGLV WDSEHSDLTE AVVRNLATHL YLPGLFYRVT DENAKNSELN LVGMICYTSQ
HYCAFAFHTK SSKWVFFDDA NVKEIGTRWK DVVSKCIRCH FQPLLLFYAN PDGTAVSTED
ALRQVISWSH YKSVAENMGC EKPVIHKSDN LKENGFGDQA KQRENQKFPT DNISSSNRSH
SHTGVGKGPA KLSHIDQREK IKDISRECAL KAIEQKNLLS SQRKDLEKGQ RKDLGRHRDL
VDEDLSHFQS GSPPAPNGFK QHGNPHLYHS QGKGSYKHDR VVPQSRASAQ IISSSKSQIL
APGEKITGKV KSDNGTGYDT DSSQDSRDRG NSCDSSSKSR NRGWKPMRET LNVDSIFSES
EKRQHSPRHK PNISNKPKSS KDPSFSNWPK ENPKQKGLMT IYEDEMKQEI GSRSSLESNG
KGAEKNKGLV EGKVHGDNWQ MQRTESGYES SDHISNGSTN LDSPVIDGNG TVMDISGVKE
TVCFSDQITT SNLNKERGDC TSLQSQHHLE GFRKELRNLE AGYKSHEFHP ESHLQIKNHL
IKRSHVHEDN GKLFPSSSLQ IPKDHNAREH IHQSDEQKLE KPNECKFSEW LNIENSERTG
LPFHVDNSAS GKRVNSNEPS SLWSSHLRTV GLKPETAPLI QQQNIMDQCY FENSLSTECI
IRSASRSDGC QMPKLFCQNL PPPLPPKKYA ITSVPQSEKS ESTPDVKLTE VFKATSHLPK
HSLSTASEPS LEVSTHMNDE RHKETFQVRE CFGNTPNCPS SSSTNDFQAN SGAIDAFCQP
ELDSISTCPN ETVSLTTYFS VDSCMTDTYR LKYHQRPKLS FPESSGFCNN SLS
