Q6QN14 (U17L6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase 17-like protein 6
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme 17-like protein 6
Ubiquitin thiolesterase 17-like protein 6
Ubiquitin-specific-processing protease 17-like protein 6

Gene names

Name:	USP17L6
Synonyms:	USP17C, USP17D, USP17N

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	398 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Seems to be non-functional in the regulation of apoptosis. Cleaves ubiquitin fusion protein substrates. Ref.1
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). Ref.1
Subcellular location	Nucleus. Cytoplasm 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 process	Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Molecular function	Hydrolase Protease Thiol protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin thiolesterase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 398	398	Ubiquitin carboxyl-terminal hydrolase 17-like protein 6		PRO_0000331648
Sites
	Active site	89	1	Nucleophile
	Active site	334	1	Proton acceptor By similarity
Experimental info
	Mutagenesis	89	1	C → S: Abolishes enzymatic activity. Ref.1
	Sequence conflict	9	1	R → G in AAS59847. Ref.1
	Sequence conflict	23	1	S → P in AAS59847. Ref.1
	Sequence conflict	364	1	S → T in AAS59847. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q6QN14 [UniParc]. Last modified April 29, 2008. Version 2. Checksum: 350E31797F7EFD44	FASTA	398	44,690
	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 LDMQPYMSQQ NTGPLVYVLY AVLVHAGWSC HNGHYFSYVK AQEGQWYKMD DAEVTASSIT 370 380 390 SVLSQQAYVL FYIQKSEWER HSESVSRGRE PRALGSED

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-89, SUBCELLULAR LOCATION.
[2]	"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. , 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].
[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: IDENTIFICATION, NOMENCLATURE.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY533200 mRNA. Translation: AAS59847.1. AC116655 Genomic DNA. No translation available.
IPI	IPI00740629.
UniGene	Hs.722658.
3D structure databases
HSSP	HSSP built from PDB template 2AYO based on UniProtKB P54578.
ProteinModelPortal	Q6QN14.
SMR	Q6QN14. Positions 76-376.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6QN14.
Polymorphism databases
DMDM	187663985.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000382470; ENSP00000371910; ENSG00000205946.
Organism-specific databases
H-InvDB	HIX0031631.
neXtProt	NX_Q6QN14.
Phylogenomic databases
eggNOG	prNOG14403.
GeneTree	ENSGT00600000084018.
HOGENOM	HBG506630.
HOVERGEN	HBG007129.
InParanoid	Q6QN14.
OMA	EPERDSS.
OrthoDB	EOG42V8G0.
PhylomeDB	Q6QN14.
Gene expression databases
Genevestigator	Q6QN14.
Family and domain databases
InterPro	IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. [Graphical view]
Pfam	PF00443. UCH. 1 hit. [Graphical view]
PROSITE	PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

U17L6_HUMAN

Accession

Primary (citable) accession number: Q6QN14

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	April 29, 2008
Last modified:	January 25, 2012
This is version 51 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.