UBP41_HUMAN
ID UBP41_HUMAN Reviewed; 358 AA.
AC Q3LFD5; A8MXD0; Q70BM7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Putative ubiquitin carboxyl-terminal hydrolase 41;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 41;
DE AltName: Full=Ubiquitin thioesterase 41;
DE AltName: Full=Ubiquitin-specific-processing protease 41;
GN Name=USP41;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-358.
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).
CC -!- FUNCTION: May recognize and hydrolyze the peptide bond at the C-
CC terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin
CC precursors as well as that of ubiquitinated proteins (By similarity).
CC {ECO:0000250}.
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;
CC -!- INTERACTION:
CC Q3LFD5; Q9UMW8: USP18; NbExp=2; IntAct=EBI-2511843, EBI-356206;
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; AC007731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJ583822; CAE47749.1; -; mRNA.
DR EMBL; AJ586979; CAE52971.1; -; mRNA.
DR AlphaFoldDB; Q3LFD5; -.
DR SMR; Q3LFD5; -.
DR IntAct; Q3LFD5; 2.
DR STRING; 9606.ENSP00000414922; -.
DR MEROPS; C19.070; -.
DR iPTMnet; Q3LFD5; -.
DR PhosphoSitePlus; Q3LFD5; -.
DR BioMuta; USP41; -.
DR DMDM; 182702223; -.
DR jPOST; Q3LFD5; -.
DR MassIVE; Q3LFD5; -.
DR MaxQB; Q3LFD5; -.
DR PaxDb; Q3LFD5; -.
DR PeptideAtlas; Q3LFD5; -.
DR PRIDE; Q3LFD5; -.
DR ProteomicsDB; 61753; -.
DR UCSC; uc062bsg.1; human.
DR GeneCards; USP41; -.
DR HGNC; HGNC:20070; USP41.
DR neXtProt; NX_Q3LFD5; -.
DR VEuPathDB; HostDB:ENSG00000161133; -.
DR eggNOG; KOG1863; Eukaryota.
DR InParanoid; Q3LFD5; -.
DR PhylomeDB; Q3LFD5; -.
DR PathwayCommons; Q3LFD5; -.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR SignaLink; Q3LFD5; -.
DR ChiTaRS; USP41; human.
DR Pharos; Q3LFD5; Tdark.
DR PRO; PR:Q3LFD5; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q3LFD5; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 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 1: Evidence at protein level;
KW Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..358
FT /note="Putative ubiquitin carboxyl-terminal hydrolase 41"
FT /id="PRO_0000328882"
FT DOMAIN 55..358
FT /note="USP"
FT ACT_SITE 64
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 318
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT VARIANT 130
FT /note="Y -> C (in dbSNP:rs2542134)"
FT /id="VAR_042574"
FT VARIANT 325
FT /note="N -> S (in dbSNP:rs2277833)"
FT /id="VAR_042575"
FT CONFLICT 134
FT /note="L -> V (in Ref. 2; CAE47749)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 41394 MW; 6CBF79560927FB11 CRC64;
MDGVLFRAHQ CQYVHPCVHV YVTVGLMDPL CERKEKASKQ ERENPLAHLA AWGLVGLHNI
GQTCCLNSLI QVFVMNVDFA RILKRITVPR GADEQRRSVP FQMLLLLEKM QDSRQKAVWP
LELAYCLQKY NVPLFVQHDA AQLYLKLWNL IKDQIADVHL VERLQALYMI RMKDSLICLD
CAMESSRNSS MLTLRLSFFD VDSKPLKTLE DALHCFFQPR ELSSKSKCFC ENCGKKTRGK
QVLKLTHLPQ TLTIHLMRFS IRNSQTRKIC HSLYFPQSLD FSQILPMKRE SCDAEEQSGG
QYELFAVIAH VGMADSGHYC VYIRNAVDGK WFCFNDSNIC LVSWEDIQCT YGNPNYHW
