UBP43_MOUSE
ID UBP43_MOUSE Reviewed; 1132 AA.
AC Q8BUM9; Q8VDP5;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 137.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 21-1132 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 207-1132 (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-970, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-746, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
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=2;
CC Name=1;
CC IsoId=Q8BUM9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BUM9-2; Sequence=VSP_020469, VSP_020470;
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH21474.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC38837.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL732570; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK083271; BAC38837.1; ALT_INIT; mRNA.
DR EMBL; BC021474; AAH21474.1; ALT_INIT; mRNA.
DR CCDS; CCDS24861.2; -. [Q8BUM9-1]
DR RefSeq; NP_001277978.1; NM_001291049.1.
DR RefSeq; NP_776115.2; NM_173754.4. [Q8BUM9-1]
DR AlphaFoldDB; Q8BUM9; -.
DR STRING; 10090.ENSMUSP00000021288; -.
DR MEROPS; C19.979; -.
DR iPTMnet; Q8BUM9; -.
DR PhosphoSitePlus; Q8BUM9; -.
DR MaxQB; Q8BUM9; -.
DR PaxDb; Q8BUM9; -.
DR PRIDE; Q8BUM9; -.
DR ProteomicsDB; 297705; -. [Q8BUM9-1]
DR ProteomicsDB; 297706; -. [Q8BUM9-2]
DR Antibodypedia; 6274; 151 antibodies from 25 providers.
DR DNASU; 216835; -.
DR Ensembl; ENSMUST00000021288; ENSMUSP00000021288; ENSMUSG00000020905. [Q8BUM9-1]
DR GeneID; 216835; -.
DR KEGG; mmu:216835; -.
DR UCSC; uc007jne.1; mouse. [Q8BUM9-1]
DR CTD; 124739; -.
DR MGI; MGI:2444541; Usp43.
DR VEuPathDB; HostDB:ENSMUSG00000020905; -.
DR eggNOG; KOG1868; Eukaryota.
DR eggNOG; KOG1870; Eukaryota.
DR GeneTree; ENSGT00940000158772; -.
DR HOGENOM; CLU_001060_6_0_1; -.
DR InParanoid; Q8BUM9; -.
DR OMA; QTRPMCV; -.
DR OrthoDB; 1283205at2759; -.
DR PhylomeDB; Q8BUM9; -.
DR TreeFam; TF106278; -.
DR Reactome; R-MMU-5656169; Termination of translesion DNA synthesis.
DR BioGRID-ORCS; 216835; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Usp43; mouse.
DR PRO; PR:Q8BUM9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BUM9; protein.
DR Bgee; ENSMUSG00000020905; Expressed in animal zygote and 117 other tissues.
DR ExpressionAtlas; Q8BUM9; baseline and differential.
DR Genevisible; Q8BUM9; MM.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
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..1132
FT /note="Ubiquitin carboxyl-terminal hydrolase 43"
FT /id="PRO_0000249522"
FT DOMAIN 101..710
FT /note="USP"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1057..1106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1077
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1106
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:0007744|PubMed:24129315"
FT MOD_RES 970
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1047
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020469"
FT VAR_SEQ 1052
FT /note="Q -> QARGSSP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020470"
FT CONFLICT 760
FT /note="M -> V (in Ref. 3; AAH21474)"
FT /evidence="ECO:0000305"
FT CONFLICT 982
FT /note="S -> N (in Ref. 3; AAH21474)"
FT /evidence="ECO:0000305"
FT CONFLICT 1002
FT /note="D -> G (in Ref. 3; AAH21474)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1132 AA; 123874 MW; 3E9E9E46B75E67FA CRC64;
MDPGVGNALG EGPPAPRPRR RRSLRRLLNR FLLALGSRSR SGDSPPRPPA QPSPYDGDGE
GGFACAPGPA PASAGSPGPD RPPGSQPQIS SGDGARPPGA QGLKNHGNTC FMNAVVQCLS
NTDLLAEFLA LGRYRAAPGR AEVTEQLAAL VRALWTREYT PQLSAEFKNA VSKYGSQFQG
NSQHDALEFL LWLLDRVHED LEGSAHGLVS EQLPPEVSKI SEDLRPSAAP TSLGPSFVQS
HFQAQYRSSL TCPHCLKQSN TFDPFLCVSL PIPLRQTRFL SVTLVFPSKS QRFLRVGLAV
PILSTVAALR KMVAEEGGVP AEEVILVELY PNGFQRSFFD EEDLNTIAEG DNVYAFQVPP
SPGLGTLSAH PSGLSVSPRL PVRDSQRFSG PLHSENRVVF LFCNLVGSGQ QASRFGPPFL
IREDRTISWA QLQQCILSKV RCLMRSEVSA QDLGTLFSIR VVGLSLACSY LSPKDNRPLC
HWAVDRALHL RRPGGPPHVK LAVEWDSSVT ERLFGSLQEE RVQDADSVWR QQQAHQQPSC
TLDECFQSYT KEEQLAQDDA WKCPHCQVLQ QGVVKLSLWT LPDILIIHLK RFCQVGERRN
KLSTLVKFPL SGLNMAPHVA RRSTNSKAGP GPWSSWKQPI CLPTTYPLDF LYDLYAVCNH
HGSLQGGHYT AYCRNSLDGQ WYSYDDSTVE ALREDEVNTR GAYILFYQKR NSIPPWSASS
SMRGSTSSSL SDHWLMRLGS LNNSTRGSLL SWSSAPCPSM ARVPDSPVFT NGVCHQDKGG
VETRPLVRGV GGRSISMKAS PASRSRHGPF KTMPLRWSFG HREKRPGASV ELVEYLESRR
RPRSTSQSIV PLLTRAAGGE ETSASPRSDG TLPAKSEDSG RAIGQGTTGV PLSSCHLNHH
PALGSLDDSL HTARTRTGNV SQDIRLPKKF DLPLTVMPSV GDEKPARPEG QKMTPWKGSS
QVGSQSSPPS PSTGLLRNFK DSGPGTLPKM KSKAAMEERA PDKDRGQGTF TLLKSVFWKK
EHKRTVRTES SPPAPPISLG SDRLSPAAMN EQALRIRESP AKGLGNHMER DIRSAPSSLH
LPRKASRPPR ASTAGTSQRT IPGEQISYGT LQRVKYHTLS LGRKKSLPES SF
