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Ubiquitin carboxyl-terminal hydrolase 8 (EC 3.4.19.12) (Deubiquitinating enzyme 8) (Ubiquitin isopeptidase Y) (hUBPy) (Ubiquitin thioesterase 8) (Ubiquitin-specific-processing protease 8)

 UBP8_HUMAN              Reviewed;        1118 AA.
P40818; B4DKA8; Q2TB31; Q7Z3U2; Q86VA0; Q8IWI7;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
27-SEP-2017, entry version 190.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase 8;
EC=3.4.19.12 {ECO:0000269|PubMed:9628861};
AltName: Full=Deubiquitinating enzyme 8;
AltName: Full=Ubiquitin isopeptidase Y;
Short=hUBPy;
AltName: Full=Ubiquitin thioesterase 8;
AltName: Full=Ubiquitin-specific-processing protease 8;
Name=USP8; Synonyms=KIAA0055, UBPY;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow;
PubMed=7584044; DOI=10.1093/dnares/1.5.223;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, and Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
PubMed=9628861; DOI=10.1093/emboj/17.12.3241;
Naviglio S., Mattecucci C., Matoskova B., Nagase T., Nomura N.,
Di Fiore P.P., Draetta G.F.;
"UBPY: a growth-regulated human ubiquitin isopeptidase.";
EMBO J. 17:3241-3250(1998).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-786.
PubMed=16520378; DOI=10.1074/jbc.M512615200;
Row P.E., Prior I.A., McCullough J., Clague M.J., Urbe S.;
"The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin
dynamics and is essential for receptor down-regulation.";
J. Biol. Chem. 281:12618-12624(2006).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[9]
DOMAIN, INTERACTION WITH CHMP1A; CHMP1B AND CHMP7, FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=17711858; DOI=10.1074/jbc.M704009200;
Row P.E., Liu H., Hayes S., Welchman R., Charalabous P., Hofmann K.,
Clague M.J., Sanderson C.M., Urbe S.;
"The MIT domain of UBPY constitutes a CHMP binding and endosomal
localization signal required for efficient epidermal growth factor
receptor degradation.";
J. Biol. Chem. 282:30929-30937(2007).
[10]
FUNCTION, AND INTERACTION WITH BIRC6/BRUCE AND KIF23/MKLP1.
PubMed=18329369; DOI=10.1016/j.cell.2008.01.012;
Pohl C., Jentsch S.;
"Final stages of cytokinesis and midbody ring formation are controlled
by BRUCE.";
Cell 132:832-845(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452; SER-718 AND
SER-719, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
INTERACTION WITH NBR1, AND SUBCELLULAR LOCATION.
PubMed=19427866; DOI=10.1016/j.febslet.2009.04.049;
Waters S., Marchbank K., Solomon E., Whitehouse C., Gautel M.;
"Interactions with LC3 and polyubiquitin chains link nbr1 to
autophagic protein turnover.";
FEBS Lett. 583:1846-1852(2009).
[14]
INTERACTION WITH IST1.
PubMed=19129480; DOI=10.1091/mbc.E08-05-0474;
Agromayor M., Carlton J.G., Phelan J.P., Matthews D.R., Carlin L.M.,
Ameer-Beg S., Bowers K., Martin-Serrano J.;
"Essential role of hIST1 in cytokinesis.";
Mol. Biol. Cell 20:1374-1387(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160 AND SER-718, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-577 AND SER-718, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; SER-392; SER-400;
SER-452; THR-577 AND SER-718, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
STRUCTURE BY NMR OF 174-317.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the rhodanese-like domain in human ubiquitin
specific protease 8 (UBP8).";
Submitted (NOV-2004) to the PDB data bank.
[22]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 181-318 IN COMPLEX WITH
RNF41.
PubMed=17035239; DOI=10.1074/jbc.M606704200;
Avvakumov G.V., Walker J.R., Xue S., Finerty P.J. Jr., Mackenzie F.,
Newman E.M., Dhe-Paganon S.;
"Amino-terminal dimerization, NRDP1-rhodanese interaction, and
inhibited catalytic domain conformation of the ubiquitin-specific
protease 8 (USP8).";
J. Biol. Chem. 281:38061-38070(2006).
[23]
VARIANT LYS-310.
PubMed=24482476; DOI=10.1126/science.1247363;
Novarino G., Fenstermaker A.G., Zaki M.S., Hofree M., Silhavy J.L.,
Heiberg A.D., Abdellateef M., Rosti B., Scott E., Mansour L.,
Masri A., Kayserili H., Al-Aama J.Y., Abdel-Salam G.M., Karminejad A.,
Kara M., Kara B., Bozorgmehri B., Ben-Omran T., Mojahedi F.,
Mahmoud I.G., Bouslam N., Bouhouche A., Benomar A., Hanein S.,
Raymond L., Forlani S., Mascaro M., Selim L., Shehata N.,
Al-Allawi N., Bindu P.S., Azam M., Gunel M., Caglayan A., Bilguvar K.,
Tolun A., Issa M.Y., Schroth J., Spencer E.G., Rosti R.O., Akizu N.,
Vaux K.K., Johansen A., Koh A.A., Megahed H., Durr A., Brice A.,
Stevanin G., Gabriel S.B., Ideker T., Gleeson J.G.;
"Exome sequencing links corticospinal motor neuron disease to common
neurodegenerative disorders.";
Science 343:506-511(2014).
-!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from
proteins and therefore plays an important regulatory role at the
level of protein turnover by preventing degradation. Converts both
'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity
is enhanced in the M phase. Involved in cell proliferation.
Required to enter into S phase in response to serum stimulation.
May regulate T-cell anergy mediated by RNF128 via the formation of
a complex containing RNF128 and OTUB1. Probably regulates the
stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin
dynamics, cargo sorting, membrane traffic at early endosomes, and
maintenance of ESCRT-0 stability. The level of protein
ubiquitination on endosomes is essential for maintaining the
morphology of the organelle. Deubiquitinates EPS15 and controles
tyrosine kinase stability. Removes conjugated ubiquitin from EGFR
thus regulating EGFR degradation and downstream MAPK signaling.
Involved in acrosome biogenesis through interaction with the
spermatid ESCRT-0 complex and microtubules. Deubiquitinates
BIRC6/bruce and KIF23/MKLP1. {ECO:0000269|PubMed:16520378,
ECO:0000269|PubMed:17711858, ECO:0000269|PubMed:18329369,
ECO:0000269|PubMed:9628861}.
-!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
thioester, amide, peptide and isopeptide bonds formed by the C-
terminal Gly of ubiquitin (a 76-residue protein attached to
proteins as an intracellular targeting signal).
{ECO:0000269|PubMed:9628861}.
-!- SUBUNIT: Forms a ternary complex with RNF128 and OTUB1. Interacts
(via C-terminal UCH catalytic domain) with OTUB1 isoform 1.
Interacts with STAM2 (via SH3 domain). Interacts with DNAJB3,
EGFR, EPS15, RASGRF1, RNF41, YWHAE, YWHAG and YWHAZ (By
similarity). Interacts with NBR1, RASGRF1, RNF41 and IST1.
Associates with the ESCRT-0 complex and with microtubules (By
similarity). Interacts with BIRC6/bruce and KIF23/MKLP1.
{ECO:0000250, ECO:0000269|PubMed:17035239,
ECO:0000269|PubMed:17711858, ECO:0000269|PubMed:18329369,
ECO:0000269|PubMed:19129480, ECO:0000269|PubMed:19427866}.
-!- INTERACTION:
Q9HD42:CHMP1A; NbExp=3; IntAct=EBI-1050865, EBI-1057156;
Q7LBR1:CHMP1B; NbExp=5; IntAct=EBI-1050865, EBI-2118090;
Q96CF2:CHMP4C; NbExp=2; IntAct=EBI-1050865, EBI-1221015;
Q99814:EPAS1; NbExp=2; IntAct=EBI-1050865, EBI-447470;
O89100:Grap2 (xeno); NbExp=3; IntAct=EBI-1050865, EBI-642151;
Q16665:HIF1A; NbExp=2; IntAct=EBI-1050865, EBI-447269;
Q14596:NBR1; NbExp=3; IntAct=EBI-1050865, EBI-742698;
P31946:YWHAB; NbExp=4; IntAct=EBI-1050865, EBI-359815;
P61981:YWHAG; NbExp=2; IntAct=EBI-1050865, EBI-359832;
P27348:YWHAQ; NbExp=2; IntAct=EBI-1050865, EBI-359854;
P63104:YWHAZ; NbExp=3; IntAct=EBI-1050865, EBI-347088;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16520378,
ECO:0000269|PubMed:17711858, ECO:0000269|PubMed:19427866}. Nucleus
{ECO:0000250|UniProtKB:Q80U87}. Endosome membrane
{ECO:0000269|PubMed:16520378, ECO:0000269|PubMed:17711858};
Peripheral membrane protein {ECO:0000305}. Cell membrane
{ECO:0000269|PubMed:16520378}; Peripheral membrane protein
{ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P40818-1; Sequence=Displayed;
Name=2;
IsoId=P40818-2; Sequence=VSP_054594, VSP_054595;
Note=No experimental confirmation available.;
-!- INDUCTION: Upon growth stimulation in starved human fibroblasts.
Decreases in response to growth arrest induced by cell-cell
contact. {ECO:0000269|PubMed:9628861}.
-!- DOMAIN: The MIT domain is required for endosomal localization,
CHMP1B-binding, maintenance of ESCRT-0 stability and EGFR
degradation. {ECO:0000269|PubMed:17711858}.
-!- DOMAIN: The rhodanese domain is sufficient for RNF41-binding.
{ECO:0000250}.
-!- PTM: Phosphorylation of Ser-718 is essential for interaction with
YWHAE and for cytosol localization. Undergoes dephosphorylation at
Ser-718 in the M phase. Tyrosine-phosphorylated in its N-terminal
half in an EGFR-dependent manner. {ECO:0000250}.
-!- PTM: Ubiquitinated. Inactive form is mostly monoubiquitinated, but
polyubiquitination happens too. Ubiquitination is increased in
EGF-stimulated cells. Ubiquitination of active form is
undetectable, suggesting a possibility that USP8 deubiquitinates
itself, thereby regulating its own function (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH38801.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH51345.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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EMBL; D29956; BAA06225.2; -; mRNA.
EMBL; AK296480; BAG59120.1; -; mRNA.
EMBL; BX537420; CAD97662.1; -; mRNA.
EMBL; AC012170; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC038801; AAH38801.1; ALT_SEQ; mRNA.
EMBL; BC051345; AAH51345.1; ALT_SEQ; mRNA.
EMBL; BC110590; AAI10591.1; -; mRNA.
CCDS; CCDS10137.1; -. [P40818-1]
CCDS; CCDS61632.1; -. [P40818-2]
RefSeq; NP_001122082.1; NM_001128610.2. [P40818-1]
RefSeq; NP_001269978.1; NM_001283049.1. [P40818-2]
RefSeq; NP_005145.3; NM_005154.4. [P40818-1]
RefSeq; XP_006720824.1; XM_006720761.3. [P40818-1]
RefSeq; XP_011520495.1; XM_011522193.2. [P40818-1]
UniGene; Hs.443731; -.
PDB; 1WHB; NMR; -; A=174-317.
PDB; 2A9U; X-ray; 2.10 A; A/B=1-142.
PDB; 2GFO; X-ray; 2.00 A; A=734-1110.
PDB; 2GWF; X-ray; 2.30 A; A/C/E=181-318.
PDB; 3N3K; X-ray; 2.60 A; A=734-1110.
PDBsum; 1WHB; -.
PDBsum; 2A9U; -.
PDBsum; 2GFO; -.
PDBsum; 2GWF; -.
PDBsum; 3N3K; -.
ProteinModelPortal; P40818; -.
SMR; P40818; -.
BioGrid; 114555; 80.
DIP; DIP-40365N; -.
IntAct; P40818; 29.
MINT; MINT-244406; -.
STRING; 9606.ENSP00000302239; -.
BindingDB; P40818; -.
ChEMBL; CHEMBL2157854; -.
MEROPS; C19.011; -.
iPTMnet; P40818; -.
PhosphoSitePlus; P40818; -.
BioMuta; USP8; -.
DMDM; 731046; -.
EPD; P40818; -.
MaxQB; P40818; -.
PaxDb; P40818; -.
PeptideAtlas; P40818; -.
PRIDE; P40818; -.
Ensembl; ENST00000307179; ENSP00000302239; ENSG00000138592. [P40818-1]
Ensembl; ENST00000396444; ENSP00000379721; ENSG00000138592. [P40818-1]
Ensembl; ENST00000425032; ENSP00000412682; ENSG00000138592. [P40818-2]
GeneID; 9101; -.
KEGG; hsa:9101; -.
UCSC; uc001zyl.6; human. [P40818-1]
CTD; 9101; -.
DisGeNET; 9101; -.
EuPathDB; HostDB:ENSG00000138592.13; -.
GeneCards; USP8; -.
H-InvDB; HIX0172812; -.
HGNC; HGNC:12631; USP8.
HPA; HPA004869; -.
HPA; HPA050215; -.
MalaCards; USP8; -.
MIM; 603158; gene.
neXtProt; NX_P40818; -.
OpenTargets; ENSG00000138592; -.
Orphanet; 401795; Autosomal recessive spastic paraplegia type 59.
PharmGKB; PA37256; -.
eggNOG; KOG1868; Eukaryota.
eggNOG; ENOG410XP8T; LUCA.
GeneTree; ENSGT00860000133682; -.
HOGENOM; HOG000231497; -.
HOVERGEN; HBG012631; -.
InParanoid; P40818; -.
KO; K11839; -.
OMA; LMDWLHS; -.
OrthoDB; EOG091G0120; -.
PhylomeDB; P40818; -.
TreeFam; TF106277; -.
BRENDA; 3.4.19.12; 2681.
Reactome; R-HSA-1358803; Downregulation of ERBB2:ERBB3 signaling.
Reactome; R-HSA-4641263; Regulation of FZD by ubiquitination.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-6807004; Negative regulation of MET activity.
SignaLink; P40818; -.
ChiTaRS; USP8; human.
EvolutionaryTrace; P40818; -.
GeneWiki; USP8; -.
GenomeRNAi; 9101; -.
PRO; PR:P40818; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000138592; -.
CleanEx; HS_USP8; -.
ExpressionAtlas; P40818; baseline and differential.
Genevisible; P40818; HS.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0031313; C:extrinsic component of endosome membrane; IBA:GO_Central.
GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:UniProtKB.
GO; GO:0030496; C:midbody; IDA:MGI.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0014069; C:postsynaptic density of dendrite; IEA:Ensembl.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0004197; F:cysteine-type endopeptidase activity; TAS:ProtInc.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:UniProtKB.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0007032; P:endosome organization; IMP:UniProtKB.
GO; GO:0000281; P:mitotic cytokinesis; IMP:MGI.
GO; GO:0016579; P:protein deubiquitination; IMP:MGI.
GO; GO:0071108; P:protein K48-linked deubiquitination; IDA:UniProtKB.
GO; GO:0070536; P:protein K63-linked deubiquitination; IDA:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
Gene3D; 3.40.250.10; -; 1.
InterPro; IPR001394; Peptidase_C19_UCH.
InterPro; IPR001763; Rhodanese-like_dom.
InterPro; IPR015063; USP8_dimer.
InterPro; IPR018200; USP_CS.
InterPro; IPR028889; USP_dom.
Pfam; PF00581; Rhodanese; 1.
Pfam; PF00443; UCH; 1.
Pfam; PF08969; USP8_dimer; 1.
SUPFAM; SSF52821; SSF52821; 1.
PROSITE; PS50206; RHODANESE_3; 1.
PROSITE; PS00972; USP_1; 1.
PROSITE; PS00973; USP_2; 1.
PROSITE; PS50235; USP_3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell cycle; Cell membrane;
Complete proteome; Cytoplasm; Endosome; Hydrolase; Membrane; Nucleus;
Phosphoprotein; Polymorphism; Protease; Reference proteome;
SH3-binding; Thiol protease; Ubl conjugation; Ubl conjugation pathway.
CHAIN 1 1118 Ubiquitin carboxyl-terminal hydrolase 8.
/FTId=PRO_0000080627.
DOMAIN 33 116 MIT.
DOMAIN 195 313 Rhodanese. {ECO:0000255|PROSITE-
ProRule:PRU00173}.
DOMAIN 777 1109 USP.
MOTIF 405 413 SH3-binding. {ECO:0000250}.
ACT_SITE 786 786 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
ACT_SITE 1067 1067 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
MOD_RES 160 160 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 392 392 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 400 400 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 452 452 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 577 577 Phosphothreonine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 718 718 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 719 719 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 945 945 Phosphothreonine.
{ECO:0000250|UniProtKB:Q80U87}.
VAR_SEQ 35 111 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054594.
VAR_SEQ 601 629 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054595.
VARIANT 310 310 Q -> K (found in a patient with spastic
paraplegia; unknown pathological
significance; dbSNP:rs587777201).
{ECO:0000269|PubMed:24482476}.
/FTId=VAR_077850.
VARIANT 443 443 D -> G (in dbSNP:rs3743044).
/FTId=VAR_017796.
VARIANT 739 739 T -> A (in dbSNP:rs11638390).
/FTId=VAR_051525.
VARIANT 827 827 A -> G (in dbSNP:rs1056577).
/FTId=VAR_017797.
MUTAGEN 786 786 C->S: Impairs deubiquitination activity
and leads to endosome membrane
accumulation.
{ECO:0000269|PubMed:16520378}.
CONFLICT 526 526 E -> G (in Ref. 3; CAD97662).
{ECO:0000305}.
CONFLICT 717 717 Y -> H (in Ref. 3; CAD97662).
{ECO:0000305}.
CONFLICT 945 945 T -> A (in Ref. 3; CAD97662).
{ECO:0000305}.
HELIX 17 21 {ECO:0000244|PDB:2A9U}.
HELIX 22 24 {ECO:0000244|PDB:2A9U}.
HELIX 28 30 {ECO:0000244|PDB:2A9U}.
HELIX 33 52 {ECO:0000244|PDB:2A9U}.
HELIX 56 73 {ECO:0000244|PDB:2A9U}.
HELIX 77 81 {ECO:0000244|PDB:2A9U}.
HELIX 83 90 {ECO:0000244|PDB:2A9U}.
HELIX 92 138 {ECO:0000244|PDB:2A9U}.
STRAND 181 183 {ECO:0000244|PDB:1WHB}.
HELIX 185 193 {ECO:0000244|PDB:2GWF}.
STRAND 195 197 {ECO:0000244|PDB:1WHB}.
STRAND 199 203 {ECO:0000244|PDB:2GWF}.
HELIX 207 212 {ECO:0000244|PDB:2GWF}.
STRAND 219 221 {ECO:0000244|PDB:1WHB}.
HELIX 223 225 {ECO:0000244|PDB:2GWF}.
HELIX 232 237 {ECO:0000244|PDB:2GWF}.
HELIX 241 248 {ECO:0000244|PDB:2GWF}.
TURN 249 252 {ECO:0000244|PDB:2GWF}.
STRAND 253 259 {ECO:0000244|PDB:2GWF}.
HELIX 265 267 {ECO:0000244|PDB:2GWF}.
HELIX 273 282 {ECO:0000244|PDB:2GWF}.
STRAND 295 297 {ECO:0000244|PDB:2GWF}.
HELIX 300 307 {ECO:0000244|PDB:2GWF}.
HELIX 309 311 {ECO:0000244|PDB:2GWF}.
HELIX 763 765 {ECO:0000244|PDB:2GFO}.
STRAND 782 784 {ECO:0000244|PDB:2GFO}.
HELIX 786 796 {ECO:0000244|PDB:2GFO}.
HELIX 799 806 {ECO:0000244|PDB:2GFO}.
TURN 807 809 {ECO:0000244|PDB:2GFO}.
HELIX 810 813 {ECO:0000244|PDB:2GFO}.
HELIX 825 839 {ECO:0000244|PDB:2GFO}.
STRAND 842 845 {ECO:0000244|PDB:2GFO}.
HELIX 848 857 {ECO:0000244|PDB:2GFO}.
HELIX 859 861 {ECO:0000244|PDB:2GFO}.
STRAND 862 865 {ECO:0000244|PDB:2GFO}.
HELIX 869 884 {ECO:0000244|PDB:2GFO}.
HELIX 903 917 {ECO:0000244|PDB:2GFO}.
HELIX 921 926 {ECO:0000244|PDB:2GFO}.
STRAND 928 936 {ECO:0000244|PDB:2GFO}.
TURN 937 939 {ECO:0000244|PDB:2GFO}.
STRAND 942 954 {ECO:0000244|PDB:2GFO}.
STRAND 959 963 {ECO:0000244|PDB:2GFO}.
HELIX 964 971 {ECO:0000244|PDB:2GFO}.
STRAND 975 977 {ECO:0000244|PDB:2GFO}.
HELIX 979 981 {ECO:0000244|PDB:3N3K}.
STRAND 983 985 {ECO:0000244|PDB:2GFO}.
TURN 986 989 {ECO:0000244|PDB:2GFO}.
STRAND 990 992 {ECO:0000244|PDB:2GFO}.
STRAND 994 1002 {ECO:0000244|PDB:2GFO}.
STRAND 1005 1011 {ECO:0000244|PDB:2GFO}.
STRAND 1014 1016 {ECO:0000244|PDB:2GFO}.
STRAND 1018 1023 {ECO:0000244|PDB:2GFO}.
STRAND 1027 1029 {ECO:0000244|PDB:2GFO}.
HELIX 1038 1040 {ECO:0000244|PDB:2GFO}.
STRAND 1051 1061 {ECO:0000244|PDB:2GFO}.
TURN 1063 1065 {ECO:0000244|PDB:2GFO}.
STRAND 1067 1074 {ECO:0000244|PDB:2GFO}.
TURN 1075 1078 {ECO:0000244|PDB:2GFO}.
STRAND 1079 1084 {ECO:0000244|PDB:2GFO}.
STRAND 1087 1090 {ECO:0000244|PDB:2GFO}.
HELIX 1093 1095 {ECO:0000244|PDB:2GFO}.
STRAND 1101 1107 {ECO:0000244|PDB:2GFO}.
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


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