UBP31_HUMAN
ID UBP31_HUMAN Reviewed; 1352 AA.
AC Q70CQ4; Q6AW97; Q6ZTC0; Q6ZTN2; Q9ULL7;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 31;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 31;
DE AltName: Full=Ubiquitin thioesterase 31;
DE AltName: Full=Ubiquitin-specific-processing protease 31;
GN Name=USP31; Synonyms=KIAA1203;
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] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 110-1352 (ISOFORM 1), AND VARIANT THR-538.
RC TISSUE=Cerebellum, and Uterus;
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 MRNA] OF 626-1352 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 539-709 (ISOFORM 1).
RC TISSUE=Uterine endothelium;
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).
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=Q70CQ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q70CQ4-2; Sequence=VSP_020459, VSP_020460, VSP_020461,
CC VSP_020462;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:14715245}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK126752; Type=Frameshift; Evidence={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; AJ586135; CAE51935.2; -; mRNA.
DR EMBL; AK126447; BAC86554.1; -; mRNA.
DR EMBL; AK126752; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB033029; BAA86517.1; -; mRNA.
DR EMBL; BX648357; CAH10383.1; -; mRNA.
DR CCDS; CCDS10607.1; -. [Q70CQ4-1]
DR RefSeq; NP_065769.3; NM_020718.3. [Q70CQ4-1]
DR AlphaFoldDB; Q70CQ4; -.
DR BioGRID; 121548; 15.
DR IntAct; Q70CQ4; 2.
DR MINT; Q70CQ4; -.
DR STRING; 9606.ENSP00000219689; -.
DR MEROPS; C19.071; -.
DR GlyGen; Q70CQ4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q70CQ4; -.
DR PhosphoSitePlus; Q70CQ4; -.
DR BioMuta; USP31; -.
DR DMDM; 134047944; -.
DR EPD; Q70CQ4; -.
DR jPOST; Q70CQ4; -.
DR MassIVE; Q70CQ4; -.
DR MaxQB; Q70CQ4; -.
DR PaxDb; Q70CQ4; -.
DR PeptideAtlas; Q70CQ4; -.
DR PRIDE; Q70CQ4; -.
DR ProteomicsDB; 68525; -. [Q70CQ4-1]
DR ProteomicsDB; 68526; -. [Q70CQ4-2]
DR TopDownProteomics; Q70CQ4-2; -. [Q70CQ4-2]
DR Antibodypedia; 1717; 59 antibodies from 22 providers.
DR DNASU; 57478; -.
DR Ensembl; ENST00000219689.12; ENSP00000219689.7; ENSG00000103404.15. [Q70CQ4-1]
DR GeneID; 57478; -.
DR KEGG; hsa:57478; -.
DR MANE-Select; ENST00000219689.12; ENSP00000219689.7; NM_020718.4; NP_065769.3.
DR UCSC; uc002dll.4; human. [Q70CQ4-1]
DR CTD; 57478; -.
DR GeneCards; USP31; -.
DR HGNC; HGNC:20060; USP31.
DR HPA; ENSG00000103404; Tissue enhanced (brain).
DR MIM; 619536; gene.
DR neXtProt; NX_Q70CQ4; -.
DR OpenTargets; ENSG00000103404; -.
DR PharmGKB; PA164742780; -.
DR VEuPathDB; HostDB:ENSG00000103404; -.
DR eggNOG; KOG1870; Eukaryota.
DR GeneTree; ENSGT00940000156355; -.
DR HOGENOM; CLU_001060_4_0_1; -.
DR InParanoid; Q70CQ4; -.
DR OrthoDB; 1283205at2759; -.
DR PhylomeDB; Q70CQ4; -.
DR TreeFam; TF106278; -.
DR PathwayCommons; Q70CQ4; -.
DR SignaLink; Q70CQ4; -.
DR BioGRID-ORCS; 57478; 18 hits in 1120 CRISPR screens.
DR ChiTaRS; USP31; human.
DR GenomeRNAi; 57478; -.
DR Pharos; Q70CQ4; Tbio.
DR PRO; PR:Q70CQ4; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q70CQ4; protein.
DR Bgee; ENSG00000103404; Expressed in inferior vagus X ganglion and 181 other tissues.
DR ExpressionAtlas; Q70CQ4; baseline and differential.
DR Genevisible; Q70CQ4; HS.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:FlyBase.
DR GO; GO:0016579; P:protein deubiquitination; IDA:FlyBase.
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 2: Evidence at transcript level;
KW Alternative splicing; Hydrolase; Protease; Reference proteome;
KW Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..1352
FT /note="Ubiquitin carboxyl-terminal hydrolase 31"
FT /id="PRO_0000249518"
FT DOMAIN 128..765
FT /note="USP"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 919..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..1352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..119
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..973
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..1001
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1066
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1306..1352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 137
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 723
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT VAR_SEQ 1..697
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020459"
FT VAR_SEQ 698..725
FT /note="LGRDPEDYIYDLYAVCNHHGTMQGGHYT -> MSQRDGVCGSHEVAGAASPG
FT ADGGLSLA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020460"
FT VAR_SEQ 1095..1140
FT /note="PKKESSPKSQDSVSSPSPQKQKSASALTYTASSTSAKKASGPATRS -> TQ
FT FPSGEPGPSRGGQGGREARAELLHGQPALPQHKHQVWFEEGQQV (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020461"
FT VAR_SEQ 1141..1352
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020462"
FT VARIANT 445
FT /note="D -> Y (in dbSNP:rs1978066)"
FT /id="VAR_027422"
FT VARIANT 532
FT /note="Q -> H (in dbSNP:rs4597335)"
FT /id="VAR_027423"
FT VARIANT 538
FT /note="I -> T (in dbSNP:rs13339649)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_027424"
FT VARIANT 552
FT /note="A -> T (in dbSNP:rs9932912)"
FT /id="VAR_027425"
FT VARIANT 931
FT /note="R -> L (in dbSNP:rs10083789)"
FT /id="VAR_027426"
FT VARIANT 1269
FT /note="D -> N (in dbSNP:rs35541113)"
FT /id="VAR_051534"
FT VARIANT 1309
FT /note="R -> C (in dbSNP:rs35254998)"
FT /id="VAR_051535"
FT CONFLICT 568
FT /note="L -> P (in Ref. 1; CAE51935)"
FT /evidence="ECO:0000305"
FT CONFLICT 624
FT /note="Q -> H (in Ref. 2; AK126752)"
FT /evidence="ECO:0000305"
FT CONFLICT 1082
FT /note="R -> S (in Ref. 2; AK126752)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1352 AA; 146651 MW; F68A90EC45D23EDF CRC64;
MSKVTAPGSG PPAAASGKEK RSFSKRLFRS GRAGGGGAGG PGASGPAAPS SPSSPSSARS
VGSFMSRVLK TLSTLSHLSS EGAAPDRGGL RSCFPPGPAA APTPPPCPPP PASPAPPACA
AEPVPGVAGL RNHGNTCFMN ATLQCLSNTE LFAEYLALGQ YRAGRPEPSP DPEQPAGRGA
QGQGEVTEQL AHLVRALWTL EYTPQHSRDF KTIVSKNALQ YRGNSQHDAQ EFLLWLLDRV
HEDLNHSVKQ SGQPPLKPPS ETDMMPEGPS FPVCSTFVQE LFQAQYRSSL TCPHCQKQSN
TFDPFLCISL PIPLPHTRPL YVTVVYQGKC SHCMRIGVAV PLSGTVARLR EAVSMETKIP
TDQIVLTEMY YDGFHRSFCD TDDLETVHES DCIFAFETPE IFRPEGILSQ RGIHLNNNLN
HLKFGLDYHR LSSPTQTAAK QGKMDSPTSR AGSDKIVLLV CNRACTGQQG KRFGLPFVLH
LEKTIAWDLL QKEILEKMKY FLRPTVCIQV CPFSLRVVSV VGITYLLPQE EQPLCHPIVE
RALKSCGPGG TAHVKLVVEW DKETRDFLFV NTEDEYIPDA ESVRLQRERH HQPQTCTLSQ
CFQLYTKEER LAPDDAWRCP HCKQLQQGSI TLSLWTLPDV LIIHLKRFRQ EGDRRMKLQN
MVKFPLTGLD MTPHVVKRSQ SSWSLPSHWS PWRRPYGLGR DPEDYIYDLY AVCNHHGTMQ
GGHYTAYCKN SVDGLWYCFD DSDVQQLSED EVCTQTAYIL FYQRRTAIPS WSANSSVAGS
TSSSLCEHWV SRLPGSKPAS VTSAASSRRT SLASLSESVE MTGERSEDDG GFSTRPFVRS
VQRQSLSSRS SVTSPLAVNE NCMRPSWSLS AKLQMRSNSP SRFSGDSPIH SSASTLEKIG
EAADDKVSIS CFGSLRNLSS SYQEPSDSHS RREHKAVGRA PLAVMEGVFK DESDTRRLNS
SVVDTQSKHS AQGDRLPPLS GPFDNNNQIA YVDQSDSVDS SPVKEVKAPS HPGSLAKKPE
STTKRSPSSK GTSEPEKSLR KGRPALASQE SSLSSTSPSS PLPVKVSLKP SRSRSKADSS
SRGSGRHSSP APAQPKKESS PKSQDSVSSP SPQKQKSASA LTYTASSTSA KKASGPATRS
PFPPGKSRTS DHSLSREGSR QSLGSDRASA TSTSKPNSPR VSQARAGEGR GAGKHVRSSS
MASLRSPSTS IKSGLKRDSK SEDKGLSFFK SALRQKETRR STDLGKTALL SKKAGGSSVK
SVCKNTGDDE AERGHQPPAS QQPNANTTGK EQLVTKDPAS AKHSLLSARK SKSSQLDSGV
PSSPGGRQSA EKSSKKLSSS MQTSARPSQK PQ
