UBP43_HUMAN
ID UBP43_HUMAN Reviewed; 1123 AA.
AC Q70EL4; A6NDT9; B7ZLT9; B7ZVX5; Q8N2C5; Q96DQ6;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 43;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 43;
DE AltName: Full=Ubiquitin thioesterase 43;
DE AltName: Full=Ubiquitin-specific-processing protease 43;
GN Name=USP43;
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] (ISOFORM 1), 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] (ISOFORMS 2 AND 3).
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Testis;
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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1041, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q70EL4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q70EL4-2; Sequence=VSP_020466, VSP_020468;
CC Name=3;
CC IsoId=Q70EL4-3; Sequence=VSP_020467;
CC Name=4;
CC IsoId=Q70EL4-4; Sequence=VSP_046779;
CC -!- TISSUE SPECIFICITY: Expressed in brain, aorta and lung at low levels.
CC {ECO:0000269|PubMed:14715245}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB70869.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ583817; CAE47744.2; -; mRNA.
DR EMBL; AK055188; BAB70869.1; ALT_FRAME; mRNA.
DR EMBL; AK090821; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC027045; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC118755; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471108; EAW90022.1; -; Genomic_DNA.
DR EMBL; BC136368; AAI36369.1; -; mRNA.
DR EMBL; BC144041; AAI44042.1; -; mRNA.
DR EMBL; BC171759; AAI71759.1; -; mRNA.
DR CCDS; CCDS45610.1; -. [Q70EL4-1]
DR CCDS; CCDS58516.1; -. [Q70EL4-4]
DR RefSeq; NP_001254505.1; NM_001267576.1. [Q70EL4-4]
DR RefSeq; NP_694942.3; NM_153210.4. [Q70EL4-1]
DR RefSeq; XP_011521944.1; XM_011523642.2. [Q70EL4-3]
DR RefSeq; XP_016879649.1; XM_017024160.1. [Q70EL4-3]
DR RefSeq; XP_016879650.1; XM_017024161.1. [Q70EL4-3]
DR AlphaFoldDB; Q70EL4; -.
DR BioGRID; 125884; 52.
DR IntAct; Q70EL4; 34.
DR MINT; Q70EL4; -.
DR STRING; 9606.ENSP00000285199; -.
DR MEROPS; C19.976; -.
DR iPTMnet; Q70EL4; -.
DR PhosphoSitePlus; Q70EL4; -.
DR BioMuta; USP43; -.
DR DMDM; 296452852; -.
DR EPD; Q70EL4; -.
DR jPOST; Q70EL4; -.
DR MassIVE; Q70EL4; -.
DR MaxQB; Q70EL4; -.
DR PaxDb; Q70EL4; -.
DR PeptideAtlas; Q70EL4; -.
DR PRIDE; Q70EL4; -.
DR ProteomicsDB; 68549; -. [Q70EL4-1]
DR ProteomicsDB; 68550; -. [Q70EL4-2]
DR ProteomicsDB; 68551; -. [Q70EL4-3]
DR ProteomicsDB; 7268; -.
DR Antibodypedia; 6274; 151 antibodies from 25 providers.
DR DNASU; 124739; -.
DR Ensembl; ENST00000285199.12; ENSP00000285199.6; ENSG00000154914.17. [Q70EL4-1]
DR Ensembl; ENST00000570475.5; ENSP00000458963.1; ENSG00000154914.17. [Q70EL4-4]
DR GeneID; 124739; -.
DR KEGG; hsa:124739; -.
DR MANE-Select; ENST00000285199.12; ENSP00000285199.6; NM_153210.5; NP_694942.3.
DR UCSC; uc010cod.5; human. [Q70EL4-1]
DR CTD; 124739; -.
DR DisGeNET; 124739; -.
DR GeneCards; USP43; -.
DR HGNC; HGNC:20072; USP43.
DR HPA; ENSG00000154914; Low tissue specificity.
DR neXtProt; NX_Q70EL4; -.
DR OpenTargets; ENSG00000154914; -.
DR PharmGKB; PA134865304; -.
DR VEuPathDB; HostDB:ENSG00000154914; -.
DR eggNOG; KOG1868; Eukaryota.
DR eggNOG; KOG1870; Eukaryota.
DR GeneTree; ENSGT00940000158772; -.
DR HOGENOM; CLU_001060_6_0_1; -.
DR InParanoid; Q70EL4; -.
DR OMA; QTRPMCV; -.
DR OrthoDB; 1283205at2759; -.
DR PhylomeDB; Q70EL4; -.
DR TreeFam; TF106278; -.
DR PathwayCommons; Q70EL4; -.
DR Reactome; R-HSA-5656169; Termination of translesion DNA synthesis.
DR SignaLink; Q70EL4; -.
DR BioGRID-ORCS; 124739; 18 hits in 1117 CRISPR screens.
DR ChiTaRS; USP43; human.
DR GenomeRNAi; 124739; -.
DR Pharos; Q70EL4; Tdark.
DR PRO; PR:Q70EL4; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q70EL4; protein.
DR Bgee; ENSG00000154914; Expressed in oviduct epithelium and 156 other tissues.
DR ExpressionAtlas; Q70EL4; baseline and differential.
DR Genevisible; Q70EL4; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0019785; F:ISG15-specific peptidase activity; TAS:Reactome.
DR GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR GO; GO:0019985; P:translesion synthesis; TAS:Reactome.
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 Alternative splicing; Hydrolase; Methylation; Phosphoprotein; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..1123
FT /note="Ubiquitin carboxyl-terminal hydrolase 43"
FT /id="PRO_0000249521"
FT DOMAIN 101..710
FT /note="USP"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 959..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..87
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 110
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 668
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 746
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8BUM9"
FT MOD_RES 969
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BUM9"
FT MOD_RES 1041
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..488
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020466"
FT VAR_SEQ 1..311
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020467"
FT VAR_SEQ 489..553
FT /note="HLRRPGGPPHVKLAVEWDSSVKERLFGSLQEERAQDADSVWQQQQAHQQHSC
FT TLDECFQFYTKEE -> MPTVCGSSSRRISSTAVPWMNVFSSTPRRSRSRPGGPCPGRE
FT GGWLPLVGWPRAAGASQSGWFAF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020468"
FT VAR_SEQ 666..670
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046779"
FT CONFLICT 168
FT /note="K -> FQ (in Ref. 1; CAE47744)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="K -> Q (in Ref. 1; CAE47744)"
FT /evidence="ECO:0000305"
FT CONFLICT 976
FT /note="G -> E (in Ref. 2; BAB70869)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1123 AA; 122809 MW; 3B4FE86EC619173C CRC64;
MDLGPGDAAG GGPLAPRPRR RRSLRRLFSR FLLALGSRSR PGDSPPRPQP GHCDGDGEGG
FACAPGPVPA APGSPGEERP PGPQPQLQLP AGDGARPPGA QGLKNHGNTC FMNAVVQCLS
NTDLLAEFLA LGRYRAAPGR AEVTEQLAAL VRALWTREYT PQLSAEFKNA VSKYGSQFQG
NSQHDALEFL LWLLDRVHED LEGSSRGPVS EKLPPEATKT SENCLSPSAQ LPLGQSFVQS
HFQAQYRSSL TCPHCLKQSN TFDPFLCVSL PIPLRQTRFL SVTLVFPSKS QRFLRVGLAV
PILSTVAALR KMVAEEGGVP ADEVILVELY PSGFQRSFFD EEDLNTIAEG DNVYAFQVPP
SPSQGTLSAH PLGLSASPRL AAREGQRFSL SLHSESKVLI LFCNLVGSGQ QASRFGPPFL
IREDRAVSWA QLQQSILSKV RHLMKSEAPV QNLGSLFSIR VVGLSVACSY LSPKDSRPLC
HWAVDRVLHL RRPGGPPHVK LAVEWDSSVK ERLFGSLQEE RAQDADSVWQ QQQAHQQHSC
TLDECFQFYT KEEQLAQDDA WKCPHCQVLQ QGMVKLSLWT LPDILIIHLK RFCQVGERRN
KLSTLVKFPL SGLNMAPHVA QRSTSPEAGL GPWPSWKQPD CLPTSYPLDF LYDLYAVCNH
HGNLQGGHYT AYCRNSLDGQ WYSYDDSTVE PLREDEVNTR GAYILFYQKR NSIPPWSASS
SMRGSTSSSL SDHWLLRLGS HAGSTRGSLL SWSSAPCPSL PQVPDSPIFT NSLCNQEKGG
LEPRRLVRGV KGRSISMKAP TTSRAKQGPF KTMPLRWSFG SKEKPPGASV ELVEYLESRR
RPRSTSQSIV SLLTGTAGED EKSASPRSNV ALPANSEDGG RAIERGPAGV PCPSAQPNHC
LAPGNSDGPN TARKLKENAG QDIKLPRKFD LPLTVMPSVE HEKPARPEGQ KAMNWKESFQ
MGSKSSPPSP YMGFSGNSKD SRRGTSELDR PLQGTLTLLR SVFRKKENRR NERAEVSPQV
PPVSLVSGGL SPAMDGQAPG SPPALRIPEG LARGLGSRLE RDVWSAPSSL RLPRKASRAP
RGSALGMSQR TVPGEQASYG TFQRVKYHTL SLGRKKTLPE SSF
