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Ubiquitin carboxyl-terminal hydrolase 17 (USP17) (EC 3.4.19.12) (Deubiquitinating enzyme 17-like protein 2) (Deubiquitinating protein 3) (DUB-3) (Ubiquitin carboxyl-terminal hydrolase 17-like protein 2) (Ubiquitin thioesterase 17-like protein 2) (Ubiquitin-specific-processing protease 17-like protein 2)

 U17L2_HUMAN             Reviewed;         530 AA.
Q6R6M4;
29-APR-2008, integrated into UniProtKB/Swiss-Prot.
29-APR-2008, sequence version 2.
27-SEP-2017, entry version 108.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase 17;
Short=USP17;
EC=3.4.19.12 {ECO:0000269|PubMed:14699124, ECO:0000269|PubMed:20228808, ECO:0000269|PubMed:20368735};
AltName: Full=Deubiquitinating enzyme 17-like protein 2;
AltName: Full=Deubiquitinating protein 3;
Short=DUB-3;
AltName: Full=Ubiquitin carboxyl-terminal hydrolase 17-like protein 2;
AltName: Full=Ubiquitin thioesterase 17-like protein 2;
AltName: Full=Ubiquitin-specific-processing protease 17-like protein 2;
Name=USP17L2;
Synonyms=DUB3, USP17, USP17H, USP17I, USP17J, USP17K, USP17L, USP17M;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, INDUCTION BY
CYTOKINES, TISSUE SPECIFICITY, AND MUTAGENESIS OF CYS-89.
PubMed=14699124; DOI=10.1074/jbc.M311291200;
Burrows J.F., McGrattan M.J., Rascle A., Humbert M., Baek K.-H.,
Johnston J.A.;
"DUB-3, a cytokine-inducible deubiquitinating enzyme that blocks
proliferation.";
J. Biol. Chem. 279:13993-14000(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[3]
NOMENCLATURE.
PubMed=15780755; DOI=10.1016/j.ygeno.2004.11.013;
Burrows J.F., McGrattan M.J., Johnston J.A.;
"The DUB/USP17 deubiquitinating enzymes, a multigene family within a
tandemly repeated sequence.";
Genomics 85:524-529(2005).
[4]
NOMENCLATURE, AND FUNCTION IN APOPTOSIS.
PubMed=17109758; DOI=10.1186/1471-2164-7-292;
Shin J.-M., Yoo K.-J., Kim M.-S., Kim D., Baek K.-H.;
"Hyaluronan- and RNA-binding deubiquitinating enzymes of USP17 family
members associated with cell viability.";
BMC Genomics 7:292-292(2006).
[5]
FUNCTION IN CELL PROLIFERATION, AND SUBCELLULAR LOCATION.
PubMed=19188362; DOI=10.1074/jbc.M807216200;
Burrows J.F., Kelvin A.A., McFarlane C., Burden R.E., McGrattan M.J.,
De la Vega M., Govender U., Quinn D.J., Dib K., Gadina M., Scott C.J.,
Johnston J.A.;
"USP17 regulates Ras activation and cell proliferation by blocking
RCE1 activity.";
J. Biol. Chem. 284:9587-9595(2009).
[6]
IDENTIFICATION.
PubMed=20403174; DOI=10.1186/1471-2164-11-250;
Burrows J.F., Scott C.J., Johnston J.A.;
"The DUB/USP17 deubiquitinating enzymes: a gene family within a
tandemly repeated sequence, is also embedded within the copy number
variable beta-defensin cluster.";
BMC Genomics 11:250-250(2010).
[7]
FUNCTION, AND INDUCTION.
PubMed=20388806; DOI=10.1158/0008-5472.CAN-09-4152;
McFarlane C., Kelvin A.A., de la Vega M., Govender U., Scott C.J.,
Burrows J.F., Johnston J.A.;
"The deubiquitinating enzyme USP17 is highly expressed in tumor
biopsies, is cell cycle regulated, and is required for G1-S
progression.";
Cancer Res. 70:3329-3339(2010).
[8]
CATALYTIC ACTIVITY, AND FUNCTION IN CELLULAR ANTIVIRAL RESPONSE.
PubMed=20368735; DOI=10.1038/cr.2010.41;
Chen R., Zhang L., Zhong B., Tan B., Liu Y., Shu H.B.;
"The ubiquitin-specific protease 17 is involved in virus-triggered
type I IFN signaling.";
Cell Res. 20:802-811(2010).
[9]
FUNCTION.
PubMed=20147298; DOI=10.1074/jbc.M109.081448;
de la Vega M., Burrows J.F., McFarlane C., Govender U., Scott C.J.,
Johnston J.A.;
"The deubiquitinating enzyme USP17 blocks N-Ras membrane trafficking
and activation but leaves K-Ras unaffected.";
J. Biol. Chem. 285:12028-12036(2010).
[10]
CATALYTIC ACTIVITY, AND FUNCTION IN CELL PROLIFERATION.
PubMed=20228808; DOI=10.1038/ncb2041;
Pereg Y., Liu B.Y., O'Rourke K.M., Sagolla M., Dey A., Komuves L.,
French D.M., Dixit V.M.;
"Ubiquitin hydrolase Dub3 promotes oncogenic transformation by
stabilizing Cdc25A.";
Nat. Cell Biol. 12:400-406(2010).
[11]
FUNCTION, INTERACTION WITH SUDS3, AND SUBCELLULAR LOCATION.
PubMed=21239494; DOI=10.1074/jbc.M110.162321;
Ramakrishna S., Suresh B., Lee E.J., Lee H.J., Ahn W.S., Baek K.H.;
"Lys-63-specific deubiquitination of SDS3 by USP17 regulates HDAC
activity.";
J. Biol. Chem. 286:10505-10514(2011).
[12]
FUNCTION IN CELL MIGRATION, AND INDUCTION BY CHEMOKINE.
PubMed=21448158; DOI=10.1038/ncomms1243;
de la Vega M., Kelvin A.A., Dunican D.J., McFarlane C., Burrows J.F.,
Jaworski J., Stevenson N.J., Dib K., Rappoport J.Z., Scott C.J.,
Long A., Johnston J.A.;
"The deubiquitinating enzyme USP17 is essential for GTPase subcellular
localization and cell motility.";
Nat. Commun. 2:259-259(2011).
-!- FUNCTION: Deubiquitinating enzyme that removes conjugated
ubiquitin from specific proteins to regulate different cellular
processes. Regulates cell proliferation by deubiquitinating and
inhibiting RCE1 thereby controlling the small GTPases NRAS and
HRAS localization and activation. In parallel, mediates
deubiquitination of CDC25A, preventing CDC25A degradation by the
proteasome during the G1/S and G2/M phases promoting cell-cycle
progression. Also regulates cell proliferation and apoptosis
through deubiquitination of SUDS3 a regulator of histone
deacetylation. Through activation of the Rho family GTPases RAC1A,
CDC42 and RHOA, regulates cell migration. Through the cleavage of
'Lys-48'- and 'Lys-63'-linked polyubiquitin chains of the
cytoplasmic innate immune receptors DDX58 and IFIH1 stimulates the
cellular response to viral infection.
{ECO:0000269|PubMed:14699124, ECO:0000269|PubMed:17109758,
ECO:0000269|PubMed:19188362, ECO:0000269|PubMed:20147298,
ECO:0000269|PubMed:20228808, ECO:0000269|PubMed:20368735,
ECO:0000269|PubMed:20388806, ECO:0000269|PubMed:21239494,
ECO:0000269|PubMed:21448158}.
-!- 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:14699124, ECO:0000269|PubMed:20228808,
ECO:0000269|PubMed:20368735}.
-!- SUBUNIT: Interacts with SUDS3; the interaction is direct.
{ECO:0000269|PubMed:21239494}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21239494}.
Endoplasmic reticulum {ECO:0000269|PubMed:19188362}.
-!- TISSUE SPECIFICITY: Broadly expressed.
{ECO:0000269|PubMed:14699124}.
-!- INDUCTION: Up-regulated by IL4/interleukin-4, IL6/interleukin-6
and chemokines including CXCL8 and CXCL12 (at protein level). Up-
regulated during the G1/S transition of the cell cycle.
{ECO:0000269|PubMed:14699124, ECO:0000269|PubMed:20388806,
ECO:0000269|PubMed:21448158}.
-!- MISCELLANEOUS: Overexpressed in a subset of human breast cancers,
overexpression leading to an abnormally high level of CDC25A,
which arrests cells through replication stress or premature
mitosis, the latter occurring when CDK1 is activated
inappropriately. {ECO:0000305|PubMed:20228808}.
-!- SIMILARITY: Belongs to the peptidase C19 family. USP17 subfamily.
{ECO:0000305}.
-!- CAUTION: The RS447 megasatellite DNA is a highly polymorphic
conserved tandem repetitive sequence which contains a copy of the
USP17 gene. It is present with an interindividual variation in
copy number, ranging from 20 to 103, and can be found in the
genome both on chromosome 4 and chromosome 8. USP17 is also
frequently named DUB3 in the literature. The high similarity
between the UPS17-like genes makes impossible to clearly assign
data to one of the genes of the family. Oligonucleotides designed
in RNAi experiments are for instance not specific of a given
UPS17-like gene. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY509884; AAR91701.1; -; mRNA.
EMBL; AC130366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS43713.1; -.
RefSeq; NP_958804.2; NM_201402.2.
UniGene; Hs.531448; -.
ProteinModelPortal; Q6R6M4; -.
SMR; Q6R6M4; -.
BioGrid; 132019; 13.
IntAct; Q6R6M4; 4.
STRING; 9606.ENSP00000333329; -.
ChEMBL; CHEMBL3739248; -.
MEROPS; C19.023; -.
iPTMnet; Q6R6M4; -.
PhosphoSitePlus; Q6R6M4; -.
BioMuta; USP17L2; -.
DMDM; 187663988; -.
PaxDb; Q6R6M4; -.
PeptideAtlas; Q6R6M4; -.
PRIDE; Q6R6M4; -.
DNASU; 377630; -.
Ensembl; ENST00000333796; ENSP00000333329; ENSG00000223443.
GeneID; 377630; -.
KEGG; hsa:377630; -.
UCSC; uc003wvc.2; human.
CTD; 377630; -.
DisGeNET; 377630; -.
EuPathDB; HostDB:ENSG00000223443.2; -.
GeneCards; USP17L2; -.
H-InvDB; HIX0034323; -.
HGNC; HGNC:34434; USP17L2.
HPA; HPA045642; -.
MIM; 610186; gene.
neXtProt; NX_Q6R6M4; -.
OpenTargets; ENSG00000223443; -.
PharmGKB; PA165586023; -.
eggNOG; KOG1865; Eukaryota.
eggNOG; ENOG410XQ92; LUCA.
GeneTree; ENSGT00890000139343; -.
HOGENOM; HOG000144638; -.
HOVERGEN; HBG007129; -.
InParanoid; Q6R6M4; -.
KO; K11845; -.
OMA; NATACDI; -.
OrthoDB; EOG091G06D5; -.
PhylomeDB; Q6R6M4; -.
TreeFam; TF315281; -.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
GenomeRNAi; 377630; -.
PRO; PR:Q6R6M4; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000223443; -.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:UniProtKB.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IMP:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0071586; P:CAAX-box protein processing; IMP:UniProtKB.
GO; GO:0007093; P:mitotic cell cycle checkpoint; IMP:UniProtKB.
GO; GO:0034260; P:negative regulation of GTPase activity; IDA:UniProtKB.
GO; GO:0031064; P:negative regulation of histone deacetylation; IMP:UniProtKB.
GO; GO:0010955; P:negative regulation of protein processing; IMP:UniProtKB.
GO; GO:0090315; P:negative regulation of protein targeting to membrane; IMP:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB.
GO; GO:1900245; P:positive regulation of MDA-5 signaling pathway; IMP:UniProtKB.
GO; GO:1900246; P:positive regulation of RIG-I signaling pathway; IMP:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
GO; GO:0071108; P:protein K48-linked deubiquitination; IMP:UniProtKB.
GO; GO:0070536; P:protein K63-linked deubiquitination; IDA:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0030334; P:regulation of cell migration; IMP:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0050691; P:regulation of defense response to virus by host; IMP:UniProtKB.
GO; GO:1900027; P:regulation of ruffle assembly; IMP:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
InterPro; IPR001394; Peptidase_C19_UCH.
InterPro; IPR018200; USP_CS.
InterPro; IPR028889; USP_dom.
Pfam; PF00443; UCH; 1.
PROSITE; PS00973; USP_2; 1.
PROSITE; PS50235; USP_3; 1.
1: Evidence at protein level;
Apoptosis; Cell cycle; Complete proteome; Endoplasmic reticulum;
Hydrolase; Nucleus; Polymorphism; Protease; Reference proteome;
Thiol protease; Ubl conjugation pathway.
CHAIN 1 530 Ubiquitin carboxyl-terminal hydrolase 17.
/FTId=PRO_0000331644.
DOMAIN 80 375 USP.
REGION 399 530 Mediates interaction with SUDS3.
{ECO:0000269|PubMed:21239494}.
ACT_SITE 89 89 Nucleophile.
ACT_SITE 334 334 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10093}.
VARIANT 438 438 K -> R (in dbSNP:rs12543578).
/FTId=VAR_059750.
MUTAGEN 89 89 C->S: Abolishes both enzymatic activity
and effects on cell proliferation.
{ECO:0000269|PubMed:14699124}.
CONFLICT 66 66 K -> E (in Ref. 1; AAR91701).
{ECO:0000305}.
CONFLICT 214 214 S -> P (in Ref. 1; AAR91701).
{ECO:0000305}.
CONFLICT 332 332 D -> N (in Ref. 1; AAR91701).
{ECO:0000305}.
CONFLICT 353 353 K -> E (in Ref. 1; AAR91701).
{ECO:0000305}.
CONFLICT 357 357 C -> S (in Ref. 1; AAR91701).
{ECO:0000305}.
CONFLICT 423 423 R -> H (in Ref. 1; AAR91701).
{ECO:0000305}.
CONFLICT 440 440 P -> L (in Ref. 1; AAR91701).
{ECO:0000305}.
CONFLICT 462 462 N -> D (in Ref. 1; AAR91701).
{ECO:0000305}.
CONFLICT 494 494 R -> P (in Ref. 1; AAR91701).
{ECO:0000305}.
CONFLICT 496 496 D -> H (in Ref. 1; AAR91701).
{ECO:0000305}.
CONFLICT 500 500 V -> M (in Ref. 1; AAR91701).
{ECO:0000305}.
CONFLICT 509 509 Q -> R (in Ref. 1; AAR91701).
{ECO:0000305}.
CONFLICT 512 512 T -> A (in Ref. 1; AAR91701).
{ECO:0000305}.
SEQUENCE 530 AA; 59619 MW; B117BB171376B0E4 CRC64;
MEDDSLYLGG EWQFNHFSKL TSSRPDAAFA EIQRTSLPEK SPLSSEARVD LCDDLAPVAR
QLAPRKKLPL SSRRPAAVGA GLQNMGNTCY ENASLQCLTY TPPLANYMLS REHSQTCQRP
KCCMLCTMQA HITWALHSPG HVIQPSQALA AGFHRGKQED AHEFLMFTVD AMKKACLPGH
KQVDHHSKDT TLIHQIFGGC WRSQIKCLHC HGISDTFDPY LDIALDIQAA QSVKQALEQL
VKPEELNGEN AYHCGLCLQR APASKTLTLH TSAKVLILVL KRFSDVTGNK LAKNVQYPEC
LDMQPYMSQQ NTGPLVYVLY AVLVHAGWSC HDGHYFSYVK AQEGQWYKMD DAKVTACSIT
SVLSQQAYVL FYIQKSEWER HSESVSRGRE PRALGAEDTD RRATQGELKR DHPCLQAPEL
DERLVERATQ ESTLDHWKFP QEQNKTKPEF NVRKVEGTLP PNVLVIHQSK YKCGMKNHHP
EQQSSLLNLS STTRTDQESV NTGTLASLQG RTRRSKGKNK HSKRALLVCQ


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