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Reviewed, UniProtKB/Swiss-Prot Q6R6M4 (U17L2_HUMAN)

Last modified November 3, 2009. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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-like protein 2
    EC=3.1.2.15
Alternative name(s):
    Ubiquitin thioesterase 17-like protein 2
    Ubiquitin-specific-processing protease 17-like protein 2
    Deubiquitinating enzyme 17-like protein 2
    Deubiquitinating protein 3
      Short name=DUB-3
Gene names
Name: USP17L2
Synonyms: DUB3
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. Ref.1

Catalytic activity

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

Subcellular location

Nucleus By similarity.

Tissue specificity

Broadly expressed. Ref.1

Induction

Up-regulated by interleukin-4 and interleukin-6 (at protein level). 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 in the genome both on chromosome 4 and chromosome 8.

Ontologies

Keywords
   Biological processApoptosis
Ubl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   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 componentnucleus

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-like protein 2
PRO_0000331644

Sites

Active site891 By similarity
Active site3251 By similarity
Active site3341 By similarity

Natural variations

Natural variant4381K → R: dbSNP rs12543578.
VAR_059750

Experimental info

Mutagenesis891C → S: Abolishes both enzymatic activity and effects on cell proliferation. Ref.1
Sequence conflict661K → E in AAR91701. Ref.1
Sequence conflict2141S → P in AAR91701. Ref.1
Sequence conflict3321D → N in AAR91701. Ref.1
Sequence conflict3531K → E in AAR91701. Ref.1
Sequence conflict3571C → S in AAR91701. Ref.1
Sequence conflict4231R → H in AAR91701. Ref.1
Sequence conflict4401P → L in AAR91701. Ref.1
Sequence conflict4621N → D in AAR91701. Ref.1
Sequence conflict4941R → P in AAR91701. Ref.1
Sequence conflict4961D → H in AAR91701. Ref.1
Sequence conflict5001V → M in AAR91701. Ref.1
Sequence conflict5091Q → R in AAR91701. Ref.1
Sequence conflict5121T → A in AAR91701. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q6R6M4-1 [UniParc].

Last modified April 29, 2008. Version 2.
Checksum: B117BB171376B0E4

FASTA53059,619
        10         20         30         40         50         60 
MEDDSLYLGG EWQFNHFSKL TSSRPDAAFA EIQRTSLPEK SPLSSEARVD LCDDLAPVAR 

        70         80         90        100        110        120 
QLAPRKKLPL SSRRPAAVGA GLQNMGNTCY ENASLQCLTY TPPLANYMLS REHSQTCQRP 

       130        140        150        160        170        180 
KCCMLCTMQA HITWALHSPG HVIQPSQALA AGFHRGKQED AHEFLMFTVD AMKKACLPGH 

       190        200        210        220        230        240 
KQVDHHSKDT TLIHQIFGGC WRSQIKCLHC HGISDTFDPY LDIALDIQAA QSVKQALEQL 

       250        260        270        280        290        300 
VKPEELNGEN AYHCGLCLQR APASKTLTLH TSAKVLILVL KRFSDVTGNK LAKNVQYPEC 

       310        320        330        340        350        360 
LDMQPYMSQQ NTGPLVYVLY AVLVHAGWSC HDGHYFSYVK AQEGQWYKMD DAKVTACSIT 

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

       430        440        450        460        470        480 
DERLVERATQ ESTLDHWKFP QEQNKTKPEF NVRKVEGTLP PNVLVIHQSK YKCGMKNHHP 

       490        500        510        520        530 
EQQSSLLNLS STTRTDQESV NTGTLASLQG RTRRSKGKNK HSKRALLVCQ 

« Hide

References

« Hide 'large scale' references
[1]"DUB-3, a cytokine-inducible deubiquitinating enzyme that blocks proliferation."
Burrows J.F., McGrattan M.J., Rascle A., Humbert M., Baek K.-H., Johnston J.A.
J. Biol. Chem. 279:13993-14000(2004) [PubMed: 14699124] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, INDUCTION BY CYTOKINES, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-89.
[2]"DNA sequence and analysis of human chromosome 8."
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. expand/collapse author list , 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.
Nature 439:331-335(2006) [PubMed: 16421571] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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: NOMENCLATURE.
[4]"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: NOMENCLATURE.
+Additional computationally mapped references.

Cross-references

Sequence databases

AY509884 mRNA. Translation: AAR91701.1.
AC130366 Genomic DNA. No translation available.
IPIIPI00883911.
RefSeqNP_958804.2.
UniGeneHs.531448

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ6R6M4.

Proteomic databases

PRIDEQ6R6M4.

Genome annotation databases

EnsemblENST00000333796; ENSP00000333329; ENSG00000223443; Homo sapiens. [Genome view]
GeneID377630.
KEGGhsa:377630.
UCSCuc003wvc.1. human.

Organism-specific databases

CTD377630.
GeneCardsGC04P008935.
GC04P008940.
GC04P008945.
GC04P008954.
GC04P008959.
GC04P008964.
GC04P008971.
GC04P008974.
GC08M012032.
HGNCHGNC:34434. USP17L2.
MIM610186. gene.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ6R6M4.
HOVERGENQ6R6M4.
OMAVTACSIT.

Gene expression databases

GenevestigatorQ6R6M4.

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. False negative.
PS00973. UCH_2_2. 1 hit.
PS50235. UCH_2_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio100679.
SOURCESearch...

Entry information

Entry nameU17L2_HUMAN
AccessionPrimary (citable) accession number: Q6R6M4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: April 29, 2008
Last modified: November 3, 2009
This is version 38 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

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