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Reviewed, UniProtKB/Swiss-Prot Q0WX57 (UBP17_HUMAN)

Last modified July 7, 2009. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ubiquitin carboxyl-terminal hydrolase 17
    EC=3.1.2.15
Alternative name(s):
    Ubiquitin thioesterase 17
    Ubiquitin-specific-processing protease 17
    Deubiquitinating enzyme 17
Gene names
Name: USP17A
Synonyms: USP17
AND
Name: USP17H
Synonyms: USP17
AND
Name: USP17I
Synonyms: USP17
AND
Name: USP17J
Synonyms: USP17
AND
Name: USP17K
Synonyms: USP17
AND
Name: USP17L
Synonyms: USP17
AND
Name: USP17M
Synonyms: USP17
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length530 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Functions in cell apoptosis. Cleaves ubiquitin fusion protein substrates. May also bind hyaluronan and RNA. Ref.1

Catalytic activity

Ubiquitin C-terminal thioester + H2O = ubiquitin + a thiol. Ref.1 Ref.2

Subcellular location

Nucleusnucleolus. Ref.2

Tissue specificity

Expressed in heart, brain, liver and skeletal muscle. Ref.1

Sequence similarities

Belongs to the peptidase C19 family. USP17 subfamily.

Caution

The RS447 megasatellite DNA is a highly polymorphic conserved tandem repetitive sequence which contains a copy of USP17. It is present with an interindividual variation in copy number and between 20 to 103 copies can be found both on chromosome 4 and chromosome 8.

Ontologies

Keywords
   Biological processApoptosis
Ubl conjugation pathway
   Cellular componentNucleus
   Molecular functionHydrolase
Protease
Thiol protease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processapoptosis

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentnucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncysteine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin thiolesterase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 530530Ubiquitin carboxyl-terminal hydrolase 17
PRO_0000331643

Sites

Active site891
Active site3251 By similarity
Active site3341 By similarity

Experimental info

Mutagenesis891C → S: Abolishes enzymatic activity. Loss of the pro-apoptotic function. Ref.1 Ref.2
Sequence conflict91R → G in AAO38845. Ref.2
Sequence conflict91R → G in AAQ11741. Ref.2
Sequence conflict91R → G in AAQ11742. Ref.2
Sequence conflict231S → P in AAQ11742. Ref.2
Sequence conflict2621P → S in AAQ11741. Ref.2
Sequence conflict3101P → Q in AAQ11741. Ref.2
Sequence conflict3101P → Q in AAQ11742. Ref.2
Sequence conflict3601T → I in AAO38845. Ref.2
Sequence conflict3611S → P in AAQ11742. Ref.2
Sequence conflict3641S → T in AAQ11742. Ref.2
Sequence conflict3921R → S in AAO38845. Ref.2
Sequence conflict3981D → A in AAQ11742. Ref.2
Sequence conflict4301Q → H in AAQ11742. Ref.2
Sequence conflict4921S → T in AAO38845. Ref.2
Sequence conflict4921S → T in AAQ11741. Ref.2
Sequence conflict4921S → T in AAQ11742. Ref.2
Sequence conflict5111R → G in AAQ11742. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q0WX57-1 [UniParc].

Last modified April 29, 2008. Version 2.
Checksum: 5B0DC65280B2A098

FASTA53059,711
        10         20         30         40         50         60 
MEDDSLYLRG EWQFNHFSKL TSSRPDAAFA EIQRTSLPEK SPLSCETRVD LCDDLAPVAR 

        70         80         90        100        110        120 
QLAPREKLPL SSRRPAAVGA GLQNMGNTCY VNASLQCLTY TPPLANYMLS REHSQTCHRH 

       130        140        150        160        170        180 
KGCMLCTMQA HITRALHNPG HVIQPSQALA AGFHRGKQED AHEFLMFTVD AMKKACLPGH 

       190        200        210        220        230        240 
KQVDHHSKDT TLIHQIFGGY WRSQIKCLHC HGISDTFDPY LDIALDIQAA QSVQQALEQL 

       250        260        270        280        290        300 
VKPEELNGEN AYHCGVCLQR APASKTLTLH TSAKVLILVL KRFSDVTGNK IAKNVQYPEC 

       310        320        330        340        350        360 
LDMQPYMSQP NTGPLVYVLY AVLVHAGWSC HNGHYFSYVK AQEGQWYKMD DAEVTASSIT 

       370        380        390        400        410        420 
SVLSQQAYVL FYIQKSEWER HSESVSRGRE PRALGAEDTD RRATQGELKR DHPCLQAPEL 

       430        440        450        460        470        480 
DEHLVERATQ ESTLDHWKFL QEQNKTKPEF NVRKVEGTLP PDVLVIHQSK YKCGMKNHHP 

       490        500        510        520        530 
EQQSSLLNLS SSTPTHQESM NTGTLASLRG RARRSKGKNK HSKRALLVCQ 

« Hide

References

« Hide 'large scale' references
[1]"The RS447 human megasatellite tandem repetitive sequence encodes a novel deubiquitinating enzyme with a functional promoter."
Saitoh Y., Miyamoto N., Okada T., Gondo Y., Showguchi-Miyata J., Hadano S., Ikeda J.-E.
Genomics 67:291-300(2000) [PubMed: 10936051] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-89.
[2]"Hyaluronan- and RNA-binding deubiquitinating enzymes of USP17 family members associated with cell viability."
Shin J.-M., Yoo K.-J., Kim M.-S., Kim D., Baek K.-H.
BMC Genomics 7:292-292(2006) [PubMed: 17109758] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], NOMENCLATURE, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-89.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed: 15815621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Unstable transmission of the RS447 human megasatellite tandem repetitive sequence that contains the USP17 deubiquitinating enzyme gene."
Okada T., Gondo Y., Goto J., Kanazawa I., Hadano S., Ikeda J.E.
Hum. Genet. 110:302-313(2002) [PubMed: 11941478] [Abstract]
Cited for: IDENTIFICATION.
[5]"The DUB/USP17 deubiquitinating enzymes, a multigene family within a tandemly repeated sequence."
Burrows J.F., McGrattan M.J., Johnston J.A.
Genomics 85:524-529(2005) [PubMed: 15780755] [Abstract]
Cited for: IDENTIFICATION, NOMENCLATURE.

Cross-references

Sequence databases

AF544011 mRNA. Translation: AAQ11741.1.
AF544012 mRNA. Translation: AAQ11742.1.
AY188990 mRNA. Translation: AAO38845.1.
AC116655 Genomic DNA. No translation available.
IPIIPI00736155.
RefSeqXP_001130410.1.
XP_001130417.1.
XP_001130428.1.
XP_001130444.1.
XP_001130452.1.
XP_001130464.1.
XP_001130476.1.
UniGeneHs.553810
Hs.631527

3D structure databases

ModBaseSearch...

Genome annotation databases

EnsemblENSG00000182945. Homo sapiens. [Contig view]
GeneID728369.
728373.
728379.
728393.
728400.
728405.
728419.
KEGGhsa:728369.
hsa:728373.
hsa:728379.
hsa:728393.
hsa:728400.
hsa:728405.
hsa:728419.
UCSCuc003glq.2. human.

Organism-specific databases

GeneCardsGC04P008935.
GC04P008940.
GC04P008945.
GC04P008954.
GC04P008959.
GC04P008964.
GC04P008971.
GC04P008974.
GC08M012032.
HGNCHGNC:12615. USP17.
MIM607011. gene.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ0WX57.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19.
[Graphical view]
PfamPF00443. UCH. 1 hit.
[Graphical view]
PROSITEPS00972. UCH_2_1. 1 hit.
PS00973. UCH_2_2. 1 hit.
PS50235. UCH_2_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio126977.
SOURCESearch...

Entry information

Entry nameUBP17_HUMAN
AccessionPrimary (citable) accession number: Q0WX57
Secondary accession number(s): A8MRA9, Q0WX56, Q3BEM1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: April 29, 2008
Last modified: July 7, 2009
This is version 26 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents