UBP35_HUMAN
ID UBP35_HUMAN Reviewed; 1018 AA.
AC Q9P2H5;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 35;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 35;
DE AltName: Full=Ubiquitin thioesterase 35;
DE AltName: Full=Ubiquitin-specific-processing protease 35;
GN Name=USP35; Synonyms=KIAA1372, USP34;
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), CATALYTIC ACTIVITY, AND TISSUE
RP 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).
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613, 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 -!- 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; Evidence={ECO:0000269|PubMed:14715245};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P2H5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P2H5-2; Sequence=VSP_040291;
CC -!- TISSUE SPECIFICITY: Expressed in testis, pancreas and skeletal muscle.
CC {ECO:0000269|PubMed:14715245}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92610.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ586137; CAE51937.1; -; mRNA.
DR EMBL; AB037793; BAA92610.1; ALT_INIT; mRNA.
DR EMBL; AP002985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS41693.1; -. [Q9P2H5-1]
DR RefSeq; NP_065849.1; NM_020798.2. [Q9P2H5-1]
DR RefSeq; XP_011543489.1; XM_011545187.2. [Q9P2H5-2]
DR RefSeq; XP_011543490.1; XM_011545188.2. [Q9P2H5-2]
DR RefSeq; XP_016873541.1; XM_017018052.1.
DR PDB; 5TXK; X-ray; 1.84 A; A=423-944.
DR PDBsum; 5TXK; -.
DR AlphaFoldDB; Q9P2H5; -.
DR SMR; Q9P2H5; -.
DR BioGRID; 121613; 10.
DR IntAct; Q9P2H5; 4.
DR STRING; 9606.ENSP00000431876; -.
DR BindingDB; Q9P2H5; -.
DR ChEMBL; CHEMBL4630862; -.
DR MEROPS; C19.059; -.
DR iPTMnet; Q9P2H5; -.
DR PhosphoSitePlus; Q9P2H5; -.
DR BioMuta; USP35; -.
DR EPD; Q9P2H5; -.
DR jPOST; Q9P2H5; -.
DR MassIVE; Q9P2H5; -.
DR MaxQB; Q9P2H5; -.
DR PaxDb; Q9P2H5; -.
DR PeptideAtlas; Q9P2H5; -.
DR PRIDE; Q9P2H5; -.
DR ProteomicsDB; 83817; -. [Q9P2H5-1]
DR ProteomicsDB; 83818; -. [Q9P2H5-2]
DR Antibodypedia; 31304; 84 antibodies from 23 providers.
DR DNASU; 57558; -.
DR Ensembl; ENST00000526425.1; ENSP00000434942.1; ENSG00000118369.13. [Q9P2H5-2]
DR Ensembl; ENST00000529308.6; ENSP00000431876.1; ENSG00000118369.13. [Q9P2H5-1]
DR GeneID; 57558; -.
DR KEGG; hsa:57558; -.
DR MANE-Select; ENST00000529308.6; ENSP00000431876.1; NM_020798.4; NP_065849.1.
DR UCSC; uc001ozf.4; human. [Q9P2H5-1]
DR CTD; 57558; -.
DR DisGeNET; 57558; -.
DR GeneCards; USP35; -.
DR HGNC; HGNC:20061; USP35.
DR HPA; ENSG00000118369; Low tissue specificity.
DR neXtProt; NX_Q9P2H5; -.
DR OpenTargets; ENSG00000118369; -.
DR PharmGKB; PA134883706; -.
DR VEuPathDB; HostDB:ENSG00000118369; -.
DR eggNOG; KOG1864; Eukaryota.
DR GeneTree; ENSGT00940000160942; -.
DR HOGENOM; CLU_010910_0_0_1; -.
DR InParanoid; Q9P2H5; -.
DR OMA; HKVFHDE; -.
DR OrthoDB; 802596at2759; -.
DR PhylomeDB; Q9P2H5; -.
DR TreeFam; TF324529; -.
DR PathwayCommons; Q9P2H5; -.
DR SignaLink; Q9P2H5; -.
DR BioGRID-ORCS; 57558; 22 hits in 1078 CRISPR screens.
DR ChiTaRS; USP35; human.
DR GenomeRNAi; 57558; -.
DR Pharos; Q9P2H5; Tbio.
DR PRO; PR:Q9P2H5; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9P2H5; protein.
DR Bgee; ENSG00000118369; Expressed in secondary oocyte and 114 other tissues.
DR ExpressionAtlas; Q9P2H5; baseline and differential.
DR Genevisible; Q9P2H5; HS.
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; IDA:FlyBase.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; IDA:FlyBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR016024; ARM-type_fold.
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; SSF48371; SSF48371; 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 3D-structure; Alternative splicing; Hydrolase; Phosphoprotein; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..1018
FT /note="Ubiquitin carboxyl-terminal hydrolase 35"
FT /id="PRO_0000080665"
FT DOMAIN 441..926
FT /note="USP"
FT REGION 544..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 450
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 862
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..269
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10718198"
FT /id="VSP_040291"
FT VARIANT 236
FT /note="V -> M (in dbSNP:rs2510044)"
FT /id="VAR_057042"
FT CONFLICT 224
FT /note="Missing (in Ref. 1; CAE51937)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="D -> E (in Ref. 1; CAE51937)"
FT /evidence="ECO:0000305"
FT HELIX 450..461
FT /evidence="ECO:0007829|PDB:5TXK"
FT HELIX 463..470
FT /evidence="ECO:0007829|PDB:5TXK"
FT HELIX 479..493
FT /evidence="ECO:0007829|PDB:5TXK"
FT STRAND 496..499
FT /evidence="ECO:0007829|PDB:5TXK"
FT HELIX 502..507
FT /evidence="ECO:0007829|PDB:5TXK"
FT HELIX 521..549
FT /evidence="ECO:0007829|PDB:5TXK"
FT HELIX 565..570
FT /evidence="ECO:0007829|PDB:5TXK"
FT STRAND 572..580
FT /evidence="ECO:0007829|PDB:5TXK"
FT TURN 581..583
FT /evidence="ECO:0007829|PDB:5TXK"
FT STRAND 586..598
FT /evidence="ECO:0007829|PDB:5TXK"
FT HELIX 761..768
FT /evidence="ECO:0007829|PDB:5TXK"
FT STRAND 772..774
FT /evidence="ECO:0007829|PDB:5TXK"
FT HELIX 776..778
FT /evidence="ECO:0007829|PDB:5TXK"
FT STRAND 780..782
FT /evidence="ECO:0007829|PDB:5TXK"
FT TURN 783..786
FT /evidence="ECO:0007829|PDB:5TXK"
FT STRAND 787..789
FT /evidence="ECO:0007829|PDB:5TXK"
FT STRAND 791..799
FT /evidence="ECO:0007829|PDB:5TXK"
FT STRAND 802..808
FT /evidence="ECO:0007829|PDB:5TXK"
FT STRAND 811..814
FT /evidence="ECO:0007829|PDB:5TXK"
FT TURN 815..818
FT /evidence="ECO:0007829|PDB:5TXK"
FT STRAND 819..822
FT /evidence="ECO:0007829|PDB:5TXK"
FT STRAND 831..836
FT /evidence="ECO:0007829|PDB:5TXK"
FT HELIX 838..840
FT /evidence="ECO:0007829|PDB:5TXK"
FT STRAND 842..854
FT /evidence="ECO:0007829|PDB:5TXK"
FT STRAND 856..860
FT /evidence="ECO:0007829|PDB:5TXK"
FT STRAND 862..867
FT /evidence="ECO:0007829|PDB:5TXK"
FT STRAND 891..894
FT /evidence="ECO:0007829|PDB:5TXK"
FT STRAND 897..900
FT /evidence="ECO:0007829|PDB:5TXK"
FT HELIX 903..912
FT /evidence="ECO:0007829|PDB:5TXK"
FT STRAND 916..925
FT /evidence="ECO:0007829|PDB:5TXK"
SQ SEQUENCE 1018 AA; 113405 MW; 79DECFF920B3666A CRC64;
MDKILEAVVT SSYPVSVKQG LVRRVLEAAR QPLEREQCLA LLALGARLYV GGAEELPRRV
GCQLLHVAGR HHPDVFAEFF SARRVLRLLQ GGAGPPGPRA LACVQLGLQL LPEGPAADEV
FALLRREVLR TVCERPGPAA CAQVARLLAR HPRCVPDGPH RLLFCQQLVR CLGRFRCPAE
GEEGAVEFLE QAQQVSGLLA QLWRAQPAAI LPCLKELFAV ISCAEEEPPS SALASVVQHL
PLELMDGVVR NLSNDDSVTD SQMLTAISRM IDWVSWPLGK NIDKWIIALL KGLAAVKKFS
ILIEVSLTKI EKVFSKLLYP IVRGAALSVL KYMLLTFQHS HEAFHLLLPH IPPMVASLVK
EDSNSGTSCL EQLAELVHCM VFRFPGFPDL YEPVMEAIKD LHVPNEDRIK QLLGQDAWTS
QKSELAGFYP RLMAKSDTGK IGLINLGNTC YVNSILQALF MASDFRHCVL RLTENNSQPL
MTKLQWLFGF LEHSQRPAIS PENFLSASWT PWFSPGTQQD CSEYLKYLLD RLHEEEKTGT
RICQKLKQSS SPSPPEEPPA PSSTSVEKMF GGKIVTRICC LCCLNVSSRE EAFTDLSLAF
PPPERCRRRR LGSVMRPTED ITARELPPPT SAQGPGRVGP RRQRKHCITE DTPPTSLYIE
GLDSKEAGGQ SSQEERIERE EEGKEERTEK EEVGEEEEST RGEGEREKEE EVEEEEEKVE
KETEKEAEQE KEEDSLGAGT HPDAAIPSGE RTCGSEGSRS VLDLVNYFLS PEKLTAENRY
YCESCASLQD AEKVVELSQG PCYLILTLLR FSFDLRTMRR RKILDDVSIP LLLRLPLAGG
RGQAYDLCSV VVHSGVSSES GHYYCYAREG AARPAASLGT ADRPEPENQW YLFNDTRVSF
SSFESVSNVT SFFPKDTAYV LFYRQRPREG PEAELGSSRV RTEPTLHKDL MEAISKDNIL
YLQEQEKEAR SRAAYISALP TSPHWGRGFD EDKDEDEGSP GGCNPAGGNG GDFHRLVF
