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Q9BXU7

- UBP26_HUMAN

UniProt

Q9BXU7 - UBP26_HUMAN

Protein

Ubiquitin carboxyl-terminal hydrolase 26

Gene

USP26

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    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.By similarity1 Publication

    Catalytic activityi

    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).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei304 – 3041NucleophilePROSITE-ProRule annotation
    Active sitei841 – 8411Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. cysteine-type peptidase activity Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. ubiquitinyl hydrolase activity Source: InterPro

    GO - Biological processi

    1. protein deubiquitination Source: UniProtKB
    2. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Ubl conjugation pathway

    Protein family/group databases

    MEROPSiC19.046.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:USP26
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:13485. USP26.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi304 – 3041C → S: Results in increased AR signaling. 1 Publication

    Organism-specific databases

    PharmGKBiPA37782.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 913913Ubiquitin carboxyl-terminal hydrolase 26PRO_0000080655Add
    BLAST

    Proteomic databases

    PaxDbiQ9BXU7.
    PRIDEiQ9BXU7.

    PTM databases

    PhosphoSiteiQ9BXU7.

    Expressioni

    Gene expression databases

    BgeeiQ9BXU7.
    CleanExiHS_USP26.
    GenevestigatoriQ9BXU7.

    Interactioni

    Subunit structurei

    Interacts with AR.1 Publication

    Protein-protein interaction databases

    BioGridi123764. 4 interactions.
    IntActiQ9BXU7. 2 interactions.
    STRINGi9606.ENSP00000359869.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BXU7.
    SMRiQ9BXU7. Positions 16-106, 296-557.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini295 – 886592USPAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase C19 family.Curated
    Contains 1 USP domain.Curated

    Phylogenomic databases

    eggNOGiCOG5533.
    HOGENOMiHOG000060197.
    HOVERGENiHBG055893.
    InParanoidiQ9BXU7.
    KOiK11850.
    OMAiDAYDFER.
    OrthoDBiEOG7HMS09.
    PhylomeDBiQ9BXU7.
    TreeFamiTF323032.

    Family and domain databases

    InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    [Graphical view]
    PfamiPF00443. UCH. 1 hit.
    [Graphical view]
    PROSITEiPS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9BXU7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAALFLRGFV QIGNCKTGIS KSKEAFIEAV ERKKKDRLVL YFKSGKYSTF    50
    RLSDNIQNVV LKSYRGNQNH LHLTLQNNNG LFIEGLSSTD AEQLKIFLDR 100
    VHQNEVQPPV RPGKGGSVFS STTQKEINKT SFHKVDEKSS SKSFEIAKGS 150
    GTGVLQRMPL LTSKLTLTCG ELSENQHKKR KRMLSSSSEM NEEFLKENNS 200
    VEYKKSKADC SRCVSYNREK QLKLKELEEN KKLECESSCI MNATGNPYLD 250
    DIGLLQALTE KMVLVFLLQQ GYSDGYTKWD KLKLFFELFP EKICHGLPNL 300
    GNTCYMNAVL QSLLSIPSFA DDLLNQSFPW GKIPLNALTM CLARLLFFKD 350
    TYNIEIKEML LLNLKKAISA AAEIFHGNAQ NDAHEFLAHC LDQLKDNMEK 400
    LNTIWKPKSE FGEDNFPKQV FADDPDTSGF SCPVITNFEL ELLHSIACKA 450
    CGQVILKTEL NNYLSINLPQ RIKAHPSSIQ STFDLFFGAE ELEYKCAKCE 500
    HKTSVGVHSF SRLPRILIVH LKRYSLNEFC ALKKNDQEVI ISKYLKVSSH 550
    CNEGTRPPLP LSEDGEITDF QLLKVIRKMT SGNISVSWPA TKESKDILAP 600
    HIGSDKESEQ KKGQTVFKGA SRRQQQKYLG KNSKPNELES VYSGDRAFIE 650
    KEPLAHLMTY LEDTSLCQFH KAGGKPASSP GTPLSKVDFQ TVPENPKRKK 700
    YVKTSKFVAF DRIINPTKDL YEDKNIRIPE RFQKVSEQTQ QCDGMRICEQ 750
    APQQALPQSF PKPGTQGHTK NLLRPTKLNL QKSNRNSLLA LGSNKNPRNK 800
    DILDKIKSKA KETKRNDDKG DHTYRLISVV SHLGKTLKSG HYICDAYDFE 850
    KQIWFTYDDM RVLGIQEAQM QEDRRCTGYI FFYMHNEIFE EMLKREENAQ 900
    LNSKEVEETL QKE 913
    Length:913
    Mass (Da):104,047
    Last modified:June 1, 2001 - v1
    Checksum:iBB70B09CDCBA3C48
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti123 – 1231T → TT.1 Publication
    VAR_063413
    Natural varianti165 – 1651L → S.1 Publication
    Corresponds to variant rs61741870 [ dbSNP | Ensembl ].
    VAR_063414
    Natural varianti364 – 3641L → F.3 Publications
    Corresponds to variant rs35397110 [ dbSNP | Ensembl ].
    VAR_063415
    Natural varianti475 – 4751H → Y.2 Publications
    Corresponds to variant rs41299088 [ dbSNP | Ensembl ].
    VAR_063416
    Natural varianti517 – 5171L → F.1 Publication
    VAR_063417
    Natural varianti579 – 5791M → I.1 Publication
    Corresponds to variant rs138385391 [ dbSNP | Ensembl ].
    VAR_063418

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS14635.1.
    RefSeqiNP_114113.1. NM_031907.1.
    UniGeneiHs.333137.

    Genome annotation databases

    EnsembliENST00000370832; ENSP00000359869; ENSG00000134588.
    ENST00000511190; ENSP00000423390; ENSG00000134588.
    GeneIDi83844.
    KEGGihsa:83844.
    UCSCiuc010nrm.1. human.

    Polymorphism databases

    DMDMi18202739.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS14635.1.
    RefSeqi NP_114113.1. NM_031907.1.
    UniGenei Hs.333137.

    3D structure databases

    ProteinModelPortali Q9BXU7.
    SMRi Q9BXU7. Positions 16-106, 296-557.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123764. 4 interactions.
    IntActi Q9BXU7. 2 interactions.
    STRINGi 9606.ENSP00000359869.

    Protein family/group databases

    MEROPSi C19.046.

    PTM databases

    PhosphoSitei Q9BXU7.

    Polymorphism databases

    DMDMi 18202739.

    Proteomic databases

    PaxDbi Q9BXU7.
    PRIDEi Q9BXU7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000370832 ; ENSP00000359869 ; ENSG00000134588 .
    ENST00000511190 ; ENSP00000423390 ; ENSG00000134588 .
    GeneIDi 83844.
    KEGGi hsa:83844.
    UCSCi uc010nrm.1. human.

    Organism-specific databases

    CTDi 83844.
    GeneCardsi GC0XM132158.
    HGNCi HGNC:13485. USP26.
    MIMi 300309. gene.
    neXtProti NX_Q9BXU7.
    PharmGKBi PA37782.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5533.
    HOGENOMi HOG000060197.
    HOVERGENi HBG055893.
    InParanoidi Q9BXU7.
    KOi K11850.
    OMAi DAYDFER.
    OrthoDBi EOG7HMS09.
    PhylomeDBi Q9BXU7.
    TreeFami TF323032.

    Miscellaneous databases

    GenomeRNAii 83844.
    NextBioi 72811.
    PROi Q9BXU7.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9BXU7.
    CleanExi HS_USP26.
    Genevestigatori Q9BXU7.

    Family and domain databases

    InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    [Graphical view ]
    Pfami PF00443. UCH. 1 hit.
    [Graphical view ]
    PROSITEi PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. Cited for: VARIANTS THR-123 INS; SER-165; PHE-364; TYR-475 AND ILE-579.

    Entry informationi

    Entry nameiUBP26_HUMAN
    AccessioniPrimary (citable) accession number: Q9BXU7
    Secondary accession number(s): B9WRT6, Q5H9H4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 108 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3