Full text data of USP8
USP8
(KIAA0055, UBPY)
[Confidence: low (only semi-automatic identification from reviews)]
Ubiquitin carboxyl-terminal hydrolase 8; 3.4.19.12 (Deubiquitinating enzyme 8; Ubiquitin isopeptidase Y; hUBPy; Ubiquitin thioesterase 8; Ubiquitin-specific-processing protease 8)
Ubiquitin carboxyl-terminal hydrolase 8; 3.4.19.12 (Deubiquitinating enzyme 8; Ubiquitin isopeptidase Y; hUBPy; Ubiquitin thioesterase 8; Ubiquitin-specific-processing protease 8)
UniProt
P40818
ID UBP8_HUMAN Reviewed; 1118 AA.
AC P40818; Q2TB31; Q7Z3U2; Q86VA0; Q8IWI7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1995, sequence version 1.
DT 22-JAN-2014, entry version 149.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 8;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 8;
DE AltName: Full=Ubiquitin isopeptidase Y;
DE Short=hUBPy;
DE AltName: Full=Ubiquitin thioesterase 8;
DE AltName: Full=Ubiquitin-specific-processing protease 8;
GN Name=USP8; Synonyms=KIAA0055, UBPY;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S.,
RA Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II.
RT The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Lymph;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=9628861; DOI=10.1093/emboj/17.12.3241;
RA Naviglio S., Mattecucci C., Matoskova B., Nagase T., Nomura N.,
RA Di Fiore P.P., Draetta G.F.;
RT "UBPY: a growth-regulated human ubiquitin isopeptidase.";
RL EMBO J. 17:3241-3250(1998).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-786.
RX PubMed=16520378; DOI=10.1074/jbc.M512615200;
RA Row P.E., Prior I.A., McCullough J., Clague M.J., Urbe S.;
RT "The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin
RT dynamics and is essential for receptor down-regulation.";
RL J. Biol. Chem. 281:12618-12624(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP DOMAIN, INTERACTION WITH CHMP1A; CHMP1B AND CHMP7, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17711858; DOI=10.1074/jbc.M704009200;
RA Row P.E., Liu H., Hayes S., Welchman R., Charalabous P., Hofmann K.,
RA Clague M.J., Sanderson C.M., Urbe S.;
RT "The MIT domain of UBPY constitutes a CHMP binding and endosomal
RT localization signal required for efficient epidermal growth factor
RT receptor degradation.";
RL J. Biol. Chem. 282:30929-30937(2007).
RN [8]
RP FUNCTION, AND INTERACTION WITH BIRC6/BRUCE AND KIF23/MKLP1.
RX PubMed=18329369; DOI=10.1016/j.cell.2008.01.012;
RA Pohl C., Jentsch S.;
RT "Final stages of cytokinesis and midbody ring formation are controlled
RT by BRUCE.";
RL Cell 132:832-845(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452; SER-718 AND
RP SER-719, AND MASS SPECTROMETRY.
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP INTERACTION WITH NBR1, AND SUBCELLULAR LOCATION.
RX PubMed=19427866; DOI=10.1016/j.febslet.2009.04.049;
RA Waters S., Marchbank K., Solomon E., Whitehouse C., Gautel M.;
RT "Interactions with LC3 and polyubiquitin chains link nbr1 to
RT autophagic protein turnover.";
RL FEBS Lett. 583:1846-1852(2009).
RN [12]
RP INTERACTION WITH IST1.
RX PubMed=19129480; DOI=10.1091/mbc.E08-05-0474;
RA Agromayor M., Carlton J.G., Phelan J.P., Matthews D.R., Carlin L.M.,
RA Ameer-Beg S., Bowers K., Martin-Serrano J.;
RT "Essential role of hIST1 in cytokinesis.";
RL Mol. Biol. Cell 20:1374-1387(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160 AND SER-718, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-577 AND SER-718, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP STRUCTURE BY NMR OF 174-317.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the rhodanese-like domain in human ubiquitin
RT specific protease 8 (UBP8).";
RL Submitted (NOV-2004) to the PDB data bank.
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 181-318 IN COMPLEX WITH
RP RNF41.
RX PubMed=17035239; DOI=10.1074/jbc.M606704200;
RA Avvakumov G.V., Walker J.R., Xue S., Finerty P.J. Jr., Mackenzie F.,
RA Newman E.M., Dhe-Paganon S.;
RT "Amino-terminal dimerization, NRDP1-rhodanese interaction, and
RT inhibited catalytic domain conformation of the ubiquitin-specific
RT protease 8 (USP8).";
RL J. Biol. Chem. 281:38061-38070(2006).
CC -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from
CC proteins and therefore plays an important regulatory role at the
CC level of protein turnover by preventing degradation. Converts both
CC 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity
CC is enhanced in the M phase. Involved in cell proliferation.
CC Required to enter into S phase in response to serum stimulation.
CC May regulate T-cell anergy mediated by RNF128 via the formation of
CC a complex containing RNF128 and OTUB1. Probably regulates the
CC stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin
CC dynamics, cargo sorting, membrane traffic at early endosomes, and
CC maintenance of ESCRT-0 stability. The level of protein
CC ubiquitination on endosomes is essential for maintaining the
CC morphology of the organelle. Deubiquitinates EPS15 and controles
CC tyrosine kinase stability. Removes conjugated ubiquitin from EGFR
CC thus regulating EGFR degradation and downstream MAPK signaling.
CC Involved in acrosome biogenesis through interaction with the
CC spermatid ESCRT-0 complex and microtubules. Deubiquitinates
CC BIRC6/bruce and KIF23/MKLP1.
CC -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC thioester, amide, peptide and isopeptide bonds formed by the C-
CC terminal Gly of ubiquitin (a 76-residue protein attached to
CC proteins as an intracellular targeting signal).
CC -!- SUBUNIT: Forms a ternary complex with RNF128 and OTUB1. Interacts
CC (via C-terminal UCH catalytic domain) with OTUB1 isoform 1.
CC Interacts with STAM2 (via SH3 domain). Interacts with DNAJB3,
CC EGFR, EPS15, RASGRF1, RNF41, YWHAE, YWHAG and YWHAZ (By
CC similarity). Interacts with NBR1, RASGRF1, RNF41 and IST1.
CC Associates with the ESCRT-0 complex and with microtubules (By
CC similarity). Interacts with BIRC6/bruce and KIF23/MKLP1.
CC -!- INTERACTION:
CC Q9HD42:CHMP1A; NbExp=3; IntAct=EBI-1050865, EBI-1057156;
CC Q7LBR1:CHMP1B; NbExp=5; IntAct=EBI-1050865, EBI-2118090;
CC Q96CF2:CHMP4C; NbExp=2; IntAct=EBI-1050865, EBI-1221015;
CC Q14596:NBR1; NbExp=3; IntAct=EBI-1050865, EBI-742698;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus (By similarity). Endosome
CC membrane; Peripheral membrane protein. Cell membrane; Peripheral
CC membrane protein.
CC -!- INDUCTION: Upon growth stimulation in starved human fibroblasts.
CC Decreases in response to growth arrest induced by cell-cell
CC contact.
CC -!- DOMAIN: The MIT domain is required for endosomal localization,
CC CHMP1B-binding, maintenance of ESCRT-0 stability and EGFR
CC degradation.
CC -!- DOMAIN: The rhodanese domain is sufficent for RNF41-binding (By
CC similarity).
CC -!- PTM: Phosphorylation of Ser-718 is essential for interaction with
CC YWHAE and for cytosol localization (By similarity). Undergoes
CC dephosphorylation at Ser-718 in the M phase (By similarity).
CC Tyrosine-phosphorylated in its N-terminal half in an EGFR-
CC dependent manner (By similarity).
CC -!- PTM: Ubiquitinated. Inactive form is mostly monoubiquitinated, but
CC polyubiquitination happens too. Ubiquitination is increased in
CC EGF-stimulated cells. Ubiquitination of active form is
CC undetectable, suggesting a possibility that USP8 deubiquitinates
CC itself, thereby regulating its own function (By similarity).
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC -!- SIMILARITY: Contains 1 MIT domain.
CC -!- SIMILARITY: Contains 1 rhodanese domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH38801.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC Sequence=AAH51345.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
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DR EMBL; D29956; BAA06225.2; -; mRNA.
DR EMBL; BX537420; CAD97662.1; -; mRNA.
DR EMBL; BC038801; AAH38801.1; ALT_SEQ; mRNA.
DR EMBL; BC051345; AAH51345.1; ALT_SEQ; mRNA.
DR EMBL; BC110590; AAI10591.1; -; mRNA.
DR RefSeq; NP_001122082.1; NM_001128610.2.
DR RefSeq; NP_001269978.1; NM_001283049.1.
DR RefSeq; NP_005145.3; NM_005154.4.
DR UniGene; Hs.443731; -.
DR PDB; 1WHB; NMR; -; A=176-317.
DR PDB; 2A9U; X-ray; 2.10 A; A/B=1-142.
DR PDB; 2GFO; X-ray; 2.00 A; A=734-1110.
DR PDB; 2GWF; X-ray; 2.30 A; A/C/E=181-318.
DR PDB; 3N3K; X-ray; 2.60 A; A=734-1110.
DR PDBsum; 1WHB; -.
DR PDBsum; 2A9U; -.
DR PDBsum; 2GFO; -.
DR PDBsum; 2GWF; -.
DR PDBsum; 3N3K; -.
DR ProteinModelPortal; P40818; -.
DR SMR; P40818; 6-139, 181-316, 756-1110.
DR DIP; DIP-40365N; -.
DR IntAct; P40818; 19.
DR MINT; MINT-244406; -.
DR STRING; 9606.ENSP00000302239; -.
DR ChEMBL; CHEMBL2157854; -.
DR MEROPS; C19.011; -.
DR PhosphoSite; P40818; -.
DR DMDM; 731046; -.
DR PaxDb; P40818; -.
DR PeptideAtlas; P40818; -.
DR PRIDE; P40818; -.
DR Ensembl; ENST00000307179; ENSP00000302239; ENSG00000138592.
DR Ensembl; ENST00000396444; ENSP00000379721; ENSG00000138592.
DR Ensembl; ENST00000433963; ENSP00000405537; ENSG00000138592.
DR GeneID; 9101; -.
DR KEGG; hsa:9101; -.
DR UCSC; uc001zyl.4; human.
DR CTD; 9101; -.
DR GeneCards; GC15P050716; -.
DR H-InvDB; HIX0172812; -.
DR HGNC; HGNC:12631; USP8.
DR HPA; HPA004869; -.
DR MIM; 603158; gene.
DR neXtProt; NX_P40818; -.
DR PharmGKB; PA37256; -.
DR eggNOG; COG5533; -.
DR HOGENOM; HOG000231497; -.
DR HOVERGEN; HBG012631; -.
DR InParanoid; P40818; -.
DR KO; K11839; -.
DR OMA; QIDRTKK; -.
DR OrthoDB; EOG7FR7GN; -.
DR PhylomeDB; P40818; -.
DR BRENDA; 3.1.2.15; 2681.
DR Reactome; REACT_111102; Signal Transduction.
DR SignaLink; P40818; -.
DR ChiTaRS; USP8; human.
DR EvolutionaryTrace; P40818; -.
DR GeneWiki; USP8; -.
DR GenomeRNAi; 9101; -.
DR NextBio; 34117; -.
DR PRO; PR:P40818; -.
DR ArrayExpress; P40818; -.
DR Bgee; P40818; -.
DR CleanEx; HS_USP8; -.
DR Genevestigator; P40818; -.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019897; C:extrinsic to plasma membrane; IDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; TAS:ProtInc.
DR GO; GO:0004843; F:deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:InterPro.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0007032; P:endosome organization; IMP:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:MGI.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR InterPro; IPR001394; Peptidase_C19/C67.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR015063; USP8_dimer.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF08969; USP8_dimer; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS00972; UCH_2_1; 1.
DR PROSITE; PS00973; UCH_2_2; 1.
DR PROSITE; PS50235; UCH_2_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell membrane; Complete proteome; Cytoplasm;
KW Endosome; Hydrolase; Membrane; Nucleus; Phosphoprotein; Polymorphism;
KW Protease; Reference proteome; SH3-binding; Thiol protease;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1 1118 Ubiquitin carboxyl-terminal hydrolase 8.
FT /FTId=PRO_0000080627.
FT DOMAIN 33 116 MIT.
FT DOMAIN 195 313 Rhodanese.
FT MOTIF 405 413 SH3-binding (By similarity).
FT ACT_SITE 786 786 Nucleophile (By similarity).
FT ACT_SITE 1067 1067 Proton acceptor (By similarity).
FT MOD_RES 160 160 Phosphoserine.
FT MOD_RES 452 452 Phosphoserine.
FT MOD_RES 577 577 Phosphothreonine.
FT MOD_RES 718 718 Phosphoserine.
FT MOD_RES 719 719 Phosphoserine.
FT MOD_RES 945 945 Phosphothreonine (By similarity).
FT VARIANT 443 443 D -> G (in dbSNP:rs3743044).
FT /FTId=VAR_017796.
FT VARIANT 739 739 T -> A (in dbSNP:rs11638390).
FT /FTId=VAR_051525.
FT VARIANT 827 827 A -> G (in dbSNP:rs1056577).
FT /FTId=VAR_017797.
FT MUTAGEN 786 786 C->S: Impairs deubiquitination activity
FT and leads to endosome membrane
FT accumulation.
FT CONFLICT 526 526 E -> G (in Ref. 2; CAD97662).
FT CONFLICT 717 717 Y -> H (in Ref. 2; CAD97662).
FT CONFLICT 945 945 T -> A (in Ref. 2; CAD97662).
FT HELIX 17 21
FT HELIX 22 24
FT HELIX 28 30
FT HELIX 33 52
FT HELIX 56 73
FT HELIX 77 81
FT HELIX 83 90
FT HELIX 92 138
FT STRAND 181 183
FT HELIX 185 193
FT STRAND 195 197
FT STRAND 199 203
FT HELIX 207 212
FT STRAND 219 221
FT HELIX 223 225
FT HELIX 232 237
FT HELIX 241 248
FT TURN 249 252
FT STRAND 253 259
FT HELIX 265 267
FT HELIX 273 282
FT STRAND 295 297
FT HELIX 300 307
FT HELIX 309 311
FT HELIX 763 765
FT STRAND 782 784
FT HELIX 786 796
FT HELIX 799 806
FT TURN 807 809
FT HELIX 810 813
FT HELIX 825 839
FT STRAND 842 845
FT HELIX 848 857
FT HELIX 859 861
FT STRAND 862 865
FT HELIX 869 884
FT HELIX 903 917
FT HELIX 921 926
FT STRAND 928 936
FT TURN 937 939
FT STRAND 942 954
FT STRAND 959 963
FT HELIX 964 971
FT STRAND 975 977
FT HELIX 979 981
FT STRAND 983 985
FT TURN 986 989
FT STRAND 990 992
FT STRAND 994 1002
FT STRAND 1005 1011
FT STRAND 1014 1016
FT STRAND 1018 1023
FT STRAND 1027 1029
FT HELIX 1038 1040
FT STRAND 1051 1061
FT TURN 1063 1065
FT STRAND 1067 1074
FT TURN 1075 1078
FT STRAND 1079 1084
FT STRAND 1087 1090
FT HELIX 1093 1095
FT STRAND 1101 1107
SQ SEQUENCE 1118 AA; 127523 MW; 8B884B7A842F9A9A CRC64;
MPAVASVPKE LYLSSSLKDL NKKTEVKPEK ISTKSYVHSA LKIFKTAEEC RLDRDEERAY
VLYMKYVTVY NLIKKRPDFK QQQDYFHSIL GPGNIKKAVE EAERLSESLK LRYEEAEVRK
KLEEKDRQEE AQRLQQKRQE TGREDGGTLA KGSLENVLDS KDKTQKSNGE KNEKCETKEK
GAITAKELYT MMTDKNISLI IMDARRMQDY QDSCILHSLS VPEEAISPGV TASWIEAHLP
DDSKDTWKKR GNVEYVVLLD WFSSAKDLQI GTTLRSLKDA LFKWESKTVL RNEPLVLEGG
YENWLLCYPQ YTTNAKVTPP PRRQNEEVSI SLDFTYPSLE ESIPSKPAAQ TPPASIEVDE
NIELISGQNE RMGPLNISTP VEPVAASKSD VSPIIQPVPS IKNVPQIDRT KKPAVKLPEE
HRIKSESTNH EQQSPQSGKV IPDRSTKPVV FSPTLMLTDE EKARIHAETA LLMEKNKQEK
ELRERQQEEQ KEKLRKEEQE QKAKKKQEAE ENEITEKQQK AKEEMEKKES EQAKKEDKET
SAKRGKEITG VKRQSKSEHE TSDAKKSVED RGKRCPTPEI QKKSTGDVPH TSVTGDSGSG
KPFKIKGQPE SGILRTGTFR EDTDDTERNK AQREPLTRAR SEEMGRIVPG LPSGWAKFLD
PITGTFRYYH SPTNTVHMYP PEMAPSSAPP STPPTHKAKP QIPAERDREP SKLKRSYSSP
DITQAIQEEE KRKPTVTPTV NRENKPTCYP KAEISRLSAS QIRNLNPVFG GSGPALTGLR
NLGNTCYMNS ILQCLCNAPH LADYFNRNCY QDDINRSNLL GHKGEVAEEF GIIMKALWTG
QYRYISPKDF KITIGKINDQ FAGYSQQDSQ ELLLFLMDGL HEDLNKADNR KRYKEENNDH
LDDFKAAEHA WQKHKQLNES IIVALFQGQF KSTVQCLTCH KKSRTFEAFM YLSLPLASTS
KCTLQDCLRL FSKEEKLTDN NRFYCSHCRA RRDSLKKIEI WKLPPVLLVH LKRFSYDGRW
KQKLQTSVDF PLENLDLSQY VIGPKNNLKK YNLFSVSNHY GGLDGGHYTA YCKNAARQRW
FKFDDHEVSD ISVSSVKSSA AYILFYTSLG PRVTDVAT
//
ID UBP8_HUMAN Reviewed; 1118 AA.
AC P40818; Q2TB31; Q7Z3U2; Q86VA0; Q8IWI7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1995, sequence version 1.
DT 22-JAN-2014, entry version 149.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 8;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 8;
DE AltName: Full=Ubiquitin isopeptidase Y;
DE Short=hUBPy;
DE AltName: Full=Ubiquitin thioesterase 8;
DE AltName: Full=Ubiquitin-specific-processing protease 8;
GN Name=USP8; Synonyms=KIAA0055, UBPY;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S.,
RA Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II.
RT The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Lymph;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=9628861; DOI=10.1093/emboj/17.12.3241;
RA Naviglio S., Mattecucci C., Matoskova B., Nagase T., Nomura N.,
RA Di Fiore P.P., Draetta G.F.;
RT "UBPY: a growth-regulated human ubiquitin isopeptidase.";
RL EMBO J. 17:3241-3250(1998).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-786.
RX PubMed=16520378; DOI=10.1074/jbc.M512615200;
RA Row P.E., Prior I.A., McCullough J., Clague M.J., Urbe S.;
RT "The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin
RT dynamics and is essential for receptor down-regulation.";
RL J. Biol. Chem. 281:12618-12624(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP DOMAIN, INTERACTION WITH CHMP1A; CHMP1B AND CHMP7, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17711858; DOI=10.1074/jbc.M704009200;
RA Row P.E., Liu H., Hayes S., Welchman R., Charalabous P., Hofmann K.,
RA Clague M.J., Sanderson C.M., Urbe S.;
RT "The MIT domain of UBPY constitutes a CHMP binding and endosomal
RT localization signal required for efficient epidermal growth factor
RT receptor degradation.";
RL J. Biol. Chem. 282:30929-30937(2007).
RN [8]
RP FUNCTION, AND INTERACTION WITH BIRC6/BRUCE AND KIF23/MKLP1.
RX PubMed=18329369; DOI=10.1016/j.cell.2008.01.012;
RA Pohl C., Jentsch S.;
RT "Final stages of cytokinesis and midbody ring formation are controlled
RT by BRUCE.";
RL Cell 132:832-845(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452; SER-718 AND
RP SER-719, AND MASS SPECTROMETRY.
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP INTERACTION WITH NBR1, AND SUBCELLULAR LOCATION.
RX PubMed=19427866; DOI=10.1016/j.febslet.2009.04.049;
RA Waters S., Marchbank K., Solomon E., Whitehouse C., Gautel M.;
RT "Interactions with LC3 and polyubiquitin chains link nbr1 to
RT autophagic protein turnover.";
RL FEBS Lett. 583:1846-1852(2009).
RN [12]
RP INTERACTION WITH IST1.
RX PubMed=19129480; DOI=10.1091/mbc.E08-05-0474;
RA Agromayor M., Carlton J.G., Phelan J.P., Matthews D.R., Carlin L.M.,
RA Ameer-Beg S., Bowers K., Martin-Serrano J.;
RT "Essential role of hIST1 in cytokinesis.";
RL Mol. Biol. Cell 20:1374-1387(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160 AND SER-718, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-577 AND SER-718, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP STRUCTURE BY NMR OF 174-317.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the rhodanese-like domain in human ubiquitin
RT specific protease 8 (UBP8).";
RL Submitted (NOV-2004) to the PDB data bank.
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 181-318 IN COMPLEX WITH
RP RNF41.
RX PubMed=17035239; DOI=10.1074/jbc.M606704200;
RA Avvakumov G.V., Walker J.R., Xue S., Finerty P.J. Jr., Mackenzie F.,
RA Newman E.M., Dhe-Paganon S.;
RT "Amino-terminal dimerization, NRDP1-rhodanese interaction, and
RT inhibited catalytic domain conformation of the ubiquitin-specific
RT protease 8 (USP8).";
RL J. Biol. Chem. 281:38061-38070(2006).
CC -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from
CC proteins and therefore plays an important regulatory role at the
CC level of protein turnover by preventing degradation. Converts both
CC 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity
CC is enhanced in the M phase. Involved in cell proliferation.
CC Required to enter into S phase in response to serum stimulation.
CC May regulate T-cell anergy mediated by RNF128 via the formation of
CC a complex containing RNF128 and OTUB1. Probably regulates the
CC stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin
CC dynamics, cargo sorting, membrane traffic at early endosomes, and
CC maintenance of ESCRT-0 stability. The level of protein
CC ubiquitination on endosomes is essential for maintaining the
CC morphology of the organelle. Deubiquitinates EPS15 and controles
CC tyrosine kinase stability. Removes conjugated ubiquitin from EGFR
CC thus regulating EGFR degradation and downstream MAPK signaling.
CC Involved in acrosome biogenesis through interaction with the
CC spermatid ESCRT-0 complex and microtubules. Deubiquitinates
CC BIRC6/bruce and KIF23/MKLP1.
CC -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC thioester, amide, peptide and isopeptide bonds formed by the C-
CC terminal Gly of ubiquitin (a 76-residue protein attached to
CC proteins as an intracellular targeting signal).
CC -!- SUBUNIT: Forms a ternary complex with RNF128 and OTUB1. Interacts
CC (via C-terminal UCH catalytic domain) with OTUB1 isoform 1.
CC Interacts with STAM2 (via SH3 domain). Interacts with DNAJB3,
CC EGFR, EPS15, RASGRF1, RNF41, YWHAE, YWHAG and YWHAZ (By
CC similarity). Interacts with NBR1, RASGRF1, RNF41 and IST1.
CC Associates with the ESCRT-0 complex and with microtubules (By
CC similarity). Interacts with BIRC6/bruce and KIF23/MKLP1.
CC -!- INTERACTION:
CC Q9HD42:CHMP1A; NbExp=3; IntAct=EBI-1050865, EBI-1057156;
CC Q7LBR1:CHMP1B; NbExp=5; IntAct=EBI-1050865, EBI-2118090;
CC Q96CF2:CHMP4C; NbExp=2; IntAct=EBI-1050865, EBI-1221015;
CC Q14596:NBR1; NbExp=3; IntAct=EBI-1050865, EBI-742698;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus (By similarity). Endosome
CC membrane; Peripheral membrane protein. Cell membrane; Peripheral
CC membrane protein.
CC -!- INDUCTION: Upon growth stimulation in starved human fibroblasts.
CC Decreases in response to growth arrest induced by cell-cell
CC contact.
CC -!- DOMAIN: The MIT domain is required for endosomal localization,
CC CHMP1B-binding, maintenance of ESCRT-0 stability and EGFR
CC degradation.
CC -!- DOMAIN: The rhodanese domain is sufficent for RNF41-binding (By
CC similarity).
CC -!- PTM: Phosphorylation of Ser-718 is essential for interaction with
CC YWHAE and for cytosol localization (By similarity). Undergoes
CC dephosphorylation at Ser-718 in the M phase (By similarity).
CC Tyrosine-phosphorylated in its N-terminal half in an EGFR-
CC dependent manner (By similarity).
CC -!- PTM: Ubiquitinated. Inactive form is mostly monoubiquitinated, but
CC polyubiquitination happens too. Ubiquitination is increased in
CC EGF-stimulated cells. Ubiquitination of active form is
CC undetectable, suggesting a possibility that USP8 deubiquitinates
CC itself, thereby regulating its own function (By similarity).
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC -!- SIMILARITY: Contains 1 MIT domain.
CC -!- SIMILARITY: Contains 1 rhodanese domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH38801.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC Sequence=AAH51345.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
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DR EMBL; D29956; BAA06225.2; -; mRNA.
DR EMBL; BX537420; CAD97662.1; -; mRNA.
DR EMBL; BC038801; AAH38801.1; ALT_SEQ; mRNA.
DR EMBL; BC051345; AAH51345.1; ALT_SEQ; mRNA.
DR EMBL; BC110590; AAI10591.1; -; mRNA.
DR RefSeq; NP_001122082.1; NM_001128610.2.
DR RefSeq; NP_001269978.1; NM_001283049.1.
DR RefSeq; NP_005145.3; NM_005154.4.
DR UniGene; Hs.443731; -.
DR PDB; 1WHB; NMR; -; A=176-317.
DR PDB; 2A9U; X-ray; 2.10 A; A/B=1-142.
DR PDB; 2GFO; X-ray; 2.00 A; A=734-1110.
DR PDB; 2GWF; X-ray; 2.30 A; A/C/E=181-318.
DR PDB; 3N3K; X-ray; 2.60 A; A=734-1110.
DR PDBsum; 1WHB; -.
DR PDBsum; 2A9U; -.
DR PDBsum; 2GFO; -.
DR PDBsum; 2GWF; -.
DR PDBsum; 3N3K; -.
DR ProteinModelPortal; P40818; -.
DR SMR; P40818; 6-139, 181-316, 756-1110.
DR DIP; DIP-40365N; -.
DR IntAct; P40818; 19.
DR MINT; MINT-244406; -.
DR STRING; 9606.ENSP00000302239; -.
DR ChEMBL; CHEMBL2157854; -.
DR MEROPS; C19.011; -.
DR PhosphoSite; P40818; -.
DR DMDM; 731046; -.
DR PaxDb; P40818; -.
DR PeptideAtlas; P40818; -.
DR PRIDE; P40818; -.
DR Ensembl; ENST00000307179; ENSP00000302239; ENSG00000138592.
DR Ensembl; ENST00000396444; ENSP00000379721; ENSG00000138592.
DR Ensembl; ENST00000433963; ENSP00000405537; ENSG00000138592.
DR GeneID; 9101; -.
DR KEGG; hsa:9101; -.
DR UCSC; uc001zyl.4; human.
DR CTD; 9101; -.
DR GeneCards; GC15P050716; -.
DR H-InvDB; HIX0172812; -.
DR HGNC; HGNC:12631; USP8.
DR HPA; HPA004869; -.
DR MIM; 603158; gene.
DR neXtProt; NX_P40818; -.
DR PharmGKB; PA37256; -.
DR eggNOG; COG5533; -.
DR HOGENOM; HOG000231497; -.
DR HOVERGEN; HBG012631; -.
DR InParanoid; P40818; -.
DR KO; K11839; -.
DR OMA; QIDRTKK; -.
DR OrthoDB; EOG7FR7GN; -.
DR PhylomeDB; P40818; -.
DR BRENDA; 3.1.2.15; 2681.
DR Reactome; REACT_111102; Signal Transduction.
DR SignaLink; P40818; -.
DR ChiTaRS; USP8; human.
DR EvolutionaryTrace; P40818; -.
DR GeneWiki; USP8; -.
DR GenomeRNAi; 9101; -.
DR NextBio; 34117; -.
DR PRO; PR:P40818; -.
DR ArrayExpress; P40818; -.
DR Bgee; P40818; -.
DR CleanEx; HS_USP8; -.
DR Genevestigator; P40818; -.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019897; C:extrinsic to plasma membrane; IDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; TAS:ProtInc.
DR GO; GO:0004843; F:deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:InterPro.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0007032; P:endosome organization; IMP:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:MGI.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR InterPro; IPR001394; Peptidase_C19/C67.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR015063; USP8_dimer.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF08969; USP8_dimer; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS00972; UCH_2_1; 1.
DR PROSITE; PS00973; UCH_2_2; 1.
DR PROSITE; PS50235; UCH_2_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell membrane; Complete proteome; Cytoplasm;
KW Endosome; Hydrolase; Membrane; Nucleus; Phosphoprotein; Polymorphism;
KW Protease; Reference proteome; SH3-binding; Thiol protease;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1 1118 Ubiquitin carboxyl-terminal hydrolase 8.
FT /FTId=PRO_0000080627.
FT DOMAIN 33 116 MIT.
FT DOMAIN 195 313 Rhodanese.
FT MOTIF 405 413 SH3-binding (By similarity).
FT ACT_SITE 786 786 Nucleophile (By similarity).
FT ACT_SITE 1067 1067 Proton acceptor (By similarity).
FT MOD_RES 160 160 Phosphoserine.
FT MOD_RES 452 452 Phosphoserine.
FT MOD_RES 577 577 Phosphothreonine.
FT MOD_RES 718 718 Phosphoserine.
FT MOD_RES 719 719 Phosphoserine.
FT MOD_RES 945 945 Phosphothreonine (By similarity).
FT VARIANT 443 443 D -> G (in dbSNP:rs3743044).
FT /FTId=VAR_017796.
FT VARIANT 739 739 T -> A (in dbSNP:rs11638390).
FT /FTId=VAR_051525.
FT VARIANT 827 827 A -> G (in dbSNP:rs1056577).
FT /FTId=VAR_017797.
FT MUTAGEN 786 786 C->S: Impairs deubiquitination activity
FT and leads to endosome membrane
FT accumulation.
FT CONFLICT 526 526 E -> G (in Ref. 2; CAD97662).
FT CONFLICT 717 717 Y -> H (in Ref. 2; CAD97662).
FT CONFLICT 945 945 T -> A (in Ref. 2; CAD97662).
FT HELIX 17 21
FT HELIX 22 24
FT HELIX 28 30
FT HELIX 33 52
FT HELIX 56 73
FT HELIX 77 81
FT HELIX 83 90
FT HELIX 92 138
FT STRAND 181 183
FT HELIX 185 193
FT STRAND 195 197
FT STRAND 199 203
FT HELIX 207 212
FT STRAND 219 221
FT HELIX 223 225
FT HELIX 232 237
FT HELIX 241 248
FT TURN 249 252
FT STRAND 253 259
FT HELIX 265 267
FT HELIX 273 282
FT STRAND 295 297
FT HELIX 300 307
FT HELIX 309 311
FT HELIX 763 765
FT STRAND 782 784
FT HELIX 786 796
FT HELIX 799 806
FT TURN 807 809
FT HELIX 810 813
FT HELIX 825 839
FT STRAND 842 845
FT HELIX 848 857
FT HELIX 859 861
FT STRAND 862 865
FT HELIX 869 884
FT HELIX 903 917
FT HELIX 921 926
FT STRAND 928 936
FT TURN 937 939
FT STRAND 942 954
FT STRAND 959 963
FT HELIX 964 971
FT STRAND 975 977
FT HELIX 979 981
FT STRAND 983 985
FT TURN 986 989
FT STRAND 990 992
FT STRAND 994 1002
FT STRAND 1005 1011
FT STRAND 1014 1016
FT STRAND 1018 1023
FT STRAND 1027 1029
FT HELIX 1038 1040
FT STRAND 1051 1061
FT TURN 1063 1065
FT STRAND 1067 1074
FT TURN 1075 1078
FT STRAND 1079 1084
FT STRAND 1087 1090
FT HELIX 1093 1095
FT STRAND 1101 1107
SQ SEQUENCE 1118 AA; 127523 MW; 8B884B7A842F9A9A CRC64;
MPAVASVPKE LYLSSSLKDL NKKTEVKPEK ISTKSYVHSA LKIFKTAEEC RLDRDEERAY
VLYMKYVTVY NLIKKRPDFK QQQDYFHSIL GPGNIKKAVE EAERLSESLK LRYEEAEVRK
KLEEKDRQEE AQRLQQKRQE TGREDGGTLA KGSLENVLDS KDKTQKSNGE KNEKCETKEK
GAITAKELYT MMTDKNISLI IMDARRMQDY QDSCILHSLS VPEEAISPGV TASWIEAHLP
DDSKDTWKKR GNVEYVVLLD WFSSAKDLQI GTTLRSLKDA LFKWESKTVL RNEPLVLEGG
YENWLLCYPQ YTTNAKVTPP PRRQNEEVSI SLDFTYPSLE ESIPSKPAAQ TPPASIEVDE
NIELISGQNE RMGPLNISTP VEPVAASKSD VSPIIQPVPS IKNVPQIDRT KKPAVKLPEE
HRIKSESTNH EQQSPQSGKV IPDRSTKPVV FSPTLMLTDE EKARIHAETA LLMEKNKQEK
ELRERQQEEQ KEKLRKEEQE QKAKKKQEAE ENEITEKQQK AKEEMEKKES EQAKKEDKET
SAKRGKEITG VKRQSKSEHE TSDAKKSVED RGKRCPTPEI QKKSTGDVPH TSVTGDSGSG
KPFKIKGQPE SGILRTGTFR EDTDDTERNK AQREPLTRAR SEEMGRIVPG LPSGWAKFLD
PITGTFRYYH SPTNTVHMYP PEMAPSSAPP STPPTHKAKP QIPAERDREP SKLKRSYSSP
DITQAIQEEE KRKPTVTPTV NRENKPTCYP KAEISRLSAS QIRNLNPVFG GSGPALTGLR
NLGNTCYMNS ILQCLCNAPH LADYFNRNCY QDDINRSNLL GHKGEVAEEF GIIMKALWTG
QYRYISPKDF KITIGKINDQ FAGYSQQDSQ ELLLFLMDGL HEDLNKADNR KRYKEENNDH
LDDFKAAEHA WQKHKQLNES IIVALFQGQF KSTVQCLTCH KKSRTFEAFM YLSLPLASTS
KCTLQDCLRL FSKEEKLTDN NRFYCSHCRA RRDSLKKIEI WKLPPVLLVH LKRFSYDGRW
KQKLQTSVDF PLENLDLSQY VIGPKNNLKK YNLFSVSNHY GGLDGGHYTA YCKNAARQRW
FKFDDHEVSD ISVSSVKSSA AYILFYTSLG PRVTDVAT
//
MIM
603158
*RECORD*
*FIELD* NO
603158
*FIELD* TI
*603158 UBIQUITIN-SPECIFIC PROTEASE 8; USP8
;;DEUBIQUITINATING ENZYME HUMORF8; HUMORF8
read moreUSP8/PIK3R2 FUSION GENE, INCLUDED
*FIELD* TX
CLONING
During analysis of randomly sampled human coding sequences from the
myeloid cell line KG-1, Nomura et al. (1994) identified a novel cDNA,
which they referred to as KIAA0055, that was related to the tre2
oncogene. Janssen et al. (1998) found that HUMORF8 encodes a putative
deubiquitinating enzyme.
GENE FUNCTION
- Fusion Gene
Janssen et al. (1998) analyzed DNA from a patient with chronic
myeloproliferative disorder. They identified an oncogenic fusion of the
5-prime end of p85-beta (603157) with the 3-prime end of HUMORF8.
*FIELD* RF
1. Janssen, J. W. G.; Schleithoff, L.; Bartram, C. R.; Schulz, A.
S.: An oncogenic fusion product of the phosphatidylinositol 3-kinase
p85-beta subunit and HUMORF8, a putative deubiquitinating enzyme. Oncogene 16:
1767-1772, 1998.
2. Nomura, N.; Nagase, T.; Miyajima, N.; Sazuka, T.; Tanaka, A.; Sato,
S.; Seki, N.; Kawarabayasi, Y.; Ishikawa, K.; Tabata, S.: Prediction
of the coding sequences of unidentified human genes. II. The coding
sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis
of cDNA clones from human cell line KG-1. DNA Res. 1: 223-229, 1994.
*FIELD* CD
Jennifer P. Macke: 10/19/1998
*FIELD* ED
carol: 04/23/2003
alopez: 2/5/1999
alopez: 10/19/1998
*RECORD*
*FIELD* NO
603158
*FIELD* TI
*603158 UBIQUITIN-SPECIFIC PROTEASE 8; USP8
;;DEUBIQUITINATING ENZYME HUMORF8; HUMORF8
read moreUSP8/PIK3R2 FUSION GENE, INCLUDED
*FIELD* TX
CLONING
During analysis of randomly sampled human coding sequences from the
myeloid cell line KG-1, Nomura et al. (1994) identified a novel cDNA,
which they referred to as KIAA0055, that was related to the tre2
oncogene. Janssen et al. (1998) found that HUMORF8 encodes a putative
deubiquitinating enzyme.
GENE FUNCTION
- Fusion Gene
Janssen et al. (1998) analyzed DNA from a patient with chronic
myeloproliferative disorder. They identified an oncogenic fusion of the
5-prime end of p85-beta (603157) with the 3-prime end of HUMORF8.
*FIELD* RF
1. Janssen, J. W. G.; Schleithoff, L.; Bartram, C. R.; Schulz, A.
S.: An oncogenic fusion product of the phosphatidylinositol 3-kinase
p85-beta subunit and HUMORF8, a putative deubiquitinating enzyme. Oncogene 16:
1767-1772, 1998.
2. Nomura, N.; Nagase, T.; Miyajima, N.; Sazuka, T.; Tanaka, A.; Sato,
S.; Seki, N.; Kawarabayasi, Y.; Ishikawa, K.; Tabata, S.: Prediction
of the coding sequences of unidentified human genes. II. The coding
sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis
of cDNA clones from human cell line KG-1. DNA Res. 1: 223-229, 1994.
*FIELD* CD
Jennifer P. Macke: 10/19/1998
*FIELD* ED
carol: 04/23/2003
alopez: 2/5/1999
alopez: 10/19/1998