Q9BXU7 (UBP26_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase 26
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme 26
Ubiquitin thioesterase 26
Ubiquitin-specific-processing protease 26

Gene names

Name:

USP26

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	913 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the ubiquitin-dependent proteolytic pathway in conjunction with the 26S proteasome By similarity. Deubiquitinates the androgen receptor and regulates the androgen receptor signaling pathway. Ref.4
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).
Subunit structure	Interacts with AR. Ref.4
Subcellular location	Nucleus Ref.4.
Sequence similarities	Belongs to the peptidase C19 family.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Molecular function	Hydrolase Protease Thiol protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein deubiquitination Inferred from direct assay Ref.4. Source: UniProtKB ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	nucleus Inferred from direct assay Ref.4. Source: UniProtKB
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 – 913	913	Ubiquitin carboxyl-terminal hydrolase 26		PRO_0000080655
Sites
	Active site	304	1	Nucleophile By similarity
	Active site	841	1	Proton acceptor By similarity
Natural variations
	Natural variant	123	1	T → TT. Ref.7		VAR_063413
	Natural variant	165	1	L → S. Ref.7		VAR_063414
	Natural variant	364	1	L → F. Ref.5 Ref.6 Ref.7		VAR_063415
	Natural variant	475	1	H → Y. Ref.5 Ref.7		VAR_063416
	Natural variant	517	1	L → F. Ref.6		VAR_063417
	Natural variant	579	1	M → I. Ref.7		VAR_063418
Experimental info
	Mutagenesis	304	1	C → S: Results in increased AR signaling. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9BXU7 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: BB70B09CDCBA3C48	FASTA	913	104,047
	10 20 30 40 50 60 MAALFLRGFV QIGNCKTGIS KSKEAFIEAV ERKKKDRLVL YFKSGKYSTF RLSDNIQNVV 70 80 90 100 110 120 LKSYRGNQNH LHLTLQNNNG LFIEGLSSTD AEQLKIFLDR VHQNEVQPPV RPGKGGSVFS 130 140 150 160 170 180 STTQKEINKT SFHKVDEKSS SKSFEIAKGS GTGVLQRMPL LTSKLTLTCG ELSENQHKKR 190 200 210 220 230 240 KRMLSSSSEM NEEFLKENNS VEYKKSKADC SRCVSYNREK QLKLKELEEN KKLECESSCI 250 260 270 280 290 300 MNATGNPYLD DIGLLQALTE KMVLVFLLQQ GYSDGYTKWD KLKLFFELFP EKICHGLPNL 310 320 330 340 350 360 GNTCYMNAVL QSLLSIPSFA DDLLNQSFPW GKIPLNALTM CLARLLFFKD TYNIEIKEML 370 380 390 400 410 420 LLNLKKAISA AAEIFHGNAQ NDAHEFLAHC LDQLKDNMEK LNTIWKPKSE FGEDNFPKQV 430 440 450 460 470 480 FADDPDTSGF SCPVITNFEL ELLHSIACKA CGQVILKTEL NNYLSINLPQ RIKAHPSSIQ 490 500 510 520 530 540 STFDLFFGAE ELEYKCAKCE HKTSVGVHSF SRLPRILIVH LKRYSLNEFC ALKKNDQEVI 550 560 570 580 590 600 ISKYLKVSSH CNEGTRPPLP LSEDGEITDF QLLKVIRKMT SGNISVSWPA TKESKDILAP 610 620 630 640 650 660 HIGSDKESEQ KKGQTVFKGA SRRQQQKYLG KNSKPNELES VYSGDRAFIE KEPLAHLMTY 670 680 690 700 710 720 LEDTSLCQFH KAGGKPASSP GTPLSKVDFQ TVPENPKRKK YVKTSKFVAF DRIINPTKDL 730 740 750 760 770 780 YEDKNIRIPE RFQKVSEQTQ QCDGMRICEQ APQQALPQSF PKPGTQGHTK NLLRPTKLNL 790 800 810 820 830 840 QKSNRNSLLA LGSNKNPRNK DILDKIKSKA KETKRNDDKG DHTYRLISVV SHLGKTLKSG 850 860 870 880 890 900 HYICDAYDFE KQIWFTYDDM RVLGIQEAQM QEDRRCTGYI FFYMHNEIFE EMLKREENAQ 910 LNSKEVEETL QKE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"An abundance of X-linked genes expressed in spermatogonia." Wang P.J., McCarrey J.R., Yang F., Page D.C. Nat. Genet. 27:422-426(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis.
[2]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The deubiquitinating enzyme USP26 is a regulator of androgen receptor signaling." Dirac A.M., Bernards R. Mol. Cancer Res. 8:844-854(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-304, INTERACTION WITH AR.
[5]	"Novel mutations in testis-specific ubiquitin protease 26 gene may cause male infertility and hypogonadism." Paduch D.A., Mielnik A., Schlegel P.N. Reprod. BioMed. Online 10:747-754(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PHE-364 AND TYR-475.
[6]	"Sequence analysis of the X-linked USP26 gene in severe male factor infertility patients and fertile controls." Christensen G.L., Griffin J., Carrell D.T. Fertil. Steril. 90:851-852(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PHE-364 AND PHE-517.
[7]	"USP26 gene variations in fertile and infertile men." Ribarski I., Lehavi O., Yogev L., Hauser R., Bar-Shira Maymon B., Botchan A., Paz G., Yavetz H., Kleiman S.E. Hum. Reprod. 24:477-484(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS THR-123 INS; SER-165; PHE-364; TYR-475 AND ILE-579.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF285593 mRNA. Translation: AAK31972.1. Z81365 Genomic DNA. Translation: CAX30813.1. BC069073 mRNA. Translation: AAH69073.1. BC101190 mRNA. Translation: AAI01191.1. BC101191 mRNA. Translation: AAI01192.1.
IPI	IPI00011092.
RefSeq	NP_114113.1. NM_031907.1.
UniGene	Hs.333137. Hs.731249.
3D structure databases
ProteinModelPortal	Q9BXU7.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9BXU7. 2 interactions.
STRING	9606.ENSP00000359869.
Protein family/group databases
MEROPS	C19.046.
PTM databases
PhosphoSite	Q9BXU7.
Polymorphism databases
DMDM	18202739.
Proteomic databases
PaxDb	Q9BXU7.
PRIDE	Q9BXU7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000370832; ENSP00000359869; ENSG00000134588. ENST00000406273; ENSP00000384360; ENSG00000134588. ENST00000511190; ENSP00000423390; ENSG00000134588.
GeneID	83844.
KEGG	hsa:83844.
UCSC	uc010nrm.1. human.
Organism-specific databases
CTD	83844.
GeneCards	GC0XM132158.
HGNC	HGNC:13485. USP26.
MIM	300309. gene.
neXtProt	NX_Q9BXU7.
PharmGKB	PA37782.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5533.
HOGENOM	HOG000060197.
HOVERGEN	HBG055893.
InParanoid	Q9BXU7.
KO	K11850.
OMA	VVSHLGK.
OrthoDB	EOG49P9XV.
PhylomeDB	Q9BXU7.
Gene expression databases
Bgee	Q9BXU7.
CleanEx	HS_USP26.
Genevestigator	Q9BXU7.
GermOnline	ENSG00000134588. Homo sapiens.
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...
Other
GenomeRNAi	83844.
NextBio	72811.
SOURCE	Search...

Entry information

Entry name

UBP26_HUMAN

Accession

Primary (citable) accession number: Q9BXU7
Secondary accession number(s): B9WRT6, Q5H9H4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 95 of the entry and version 1 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.