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A6NNY8

- UBP27_HUMAN

UniProt

A6NNY8 - UBP27_HUMAN

Protein

Ubiquitin carboxyl-terminal hydrolase 27

Gene

USP27X

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 3 (24 Mar 2009)
      Previous versions | rss
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    Functioni

    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 sitei87 – 871NucleophilePROSITE-ProRule annotation
    Active sitei380 – 3801Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Ubl conjugation pathway

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 27 (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme 27
    Ubiquitin carboxyl-terminal hydrolase 22-like
    Ubiquitin thioesterase 27
    Ubiquitin-specific-processing protease 27
    X-linked ubiquitin carboxyl-terminal hydrolase 27
    Gene namesi
    Name:USP27X
    Synonyms:USP22L, USP27
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:13486. USP27X.

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134993614.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 438438Ubiquitin carboxyl-terminal hydrolase 27PRO_0000306334Add
    BLAST

    Proteomic databases

    MaxQBiA6NNY8.
    PRIDEiA6NNY8.

    PTM databases

    PhosphoSiteiA6NNY8.

    Expressioni

    Gene expression databases

    CleanExiHS_USP27X.
    GenevestigatoriA6NNY8.

    Interactioni

    Protein-protein interaction databases

    BioGridi133302. 2 interactions.
    IntActiA6NNY8. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliA6NNY8.
    SMRiA6NNY8. Positions 76-418.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini78 – 421344USPAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    HOVERGENiHBG058014.
    InParanoidiA6NNY8.
    KOiK11366.
    OMAiTEKHIHE.
    PhylomeDBiA6NNY8.

    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.

    A6NNY8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MCKDYVYDKD IEQIAKEEQG EALKLQASTS TEVSHQQCSV PGLGEKFPTW    50
    ETTKPELELL GHNPRRRRIT SSFTIGLRGL INLGNTCFMN CIVQALTHTP 100
    ILRDFFLSDR HRCEMPSPEL CLVCEMSSLF RELYSGNPSP HVPYKLLHLV 150
    WIHARHLAGY RQQDAHEFLI AALDVLHRHC KGDDVGKAAN NPNHCNCIID 200
    QIFTGGLQSD VTCQACHGVS TTIDPCWDIS LDLPGSCTSF WPMSPGRESS 250
    VNGESHIPGI TTLTDCLRRF TRPEHLGSSA KIKCGSCQSY QESTKQLTMN 300
    KLPVVACFHF KRFEHSAKQR RKITTYISFP LELDMTPFMA SSKESRMNGQ 350
    LQLPTNSGNN ENKYSLFAVV NHQGTLESGH YTSFIRHHKD QWFKCDDAVI 400
    TKASIKDVLD SEGYLLFYHK QVLEHESEKV KEMNTQAY 438
    Length:438
    Mass (Da):49,630
    Last modified:March 24, 2009 - v3
    Checksum:iB6BFD18C62B3774C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti32 – 321E → D in DR004246. 1 PublicationCurated
    Sequence conflicti45 – 451E → D in DR004246. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF238380 Genomic DNA. No translation available.
    DR004246 mRNA. No translation available.
    CCDSiCCDS65260.1.
    RefSeqiNP_001138545.1. NM_001145073.2.
    UniGeneiHs.143587.

    Genome annotation databases

    GeneIDi389856.
    KEGGihsa:389856.
    UCSCiuc004dop.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF238380 Genomic DNA. No translation available.
    DR004246 mRNA. No translation available.
    CCDSi CCDS65260.1.
    RefSeqi NP_001138545.1. NM_001145073.2.
    UniGenei Hs.143587.

    3D structure databases

    ProteinModelPortali A6NNY8.
    SMRi A6NNY8. Positions 76-418.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 133302. 2 interactions.
    IntActi A6NNY8. 1 interaction.

    PTM databases

    PhosphoSitei A6NNY8.

    Proteomic databases

    MaxQBi A6NNY8.
    PRIDEi A6NNY8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 389856.
    KEGGi hsa:389856.
    UCSCi uc004dop.3. human.

    Organism-specific databases

    CTDi 389856.
    GeneCardsi GC0XP049646.
    H-InvDB HIX0077135.
    HGNCi HGNC:13486. USP27X.
    neXtProti NX_A6NNY8.
    PharmGKBi PA134993614.
    GenAtlasi Search...

    Phylogenomic databases

    HOVERGENi HBG058014.
    InParanoidi A6NNY8.
    KOi K11366.
    OMAi TEKHIHE.
    PhylomeDBi A6NNY8.

    Miscellaneous databases

    GenomeRNAii 389856.
    NextBioi 103162.
    PROi A6NNY8.

    Gene expression databases

    CleanExi HS_USP27X.
    Genevestigatori A6NNY8.

    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. "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].
    2. "High-throughput cloning of full-length human cDNAs directly from cDNA libraries optimized for large and rare transcripts."
      Birkett C., Cho J., Gau Y., Hamer R., Kelly S., Kovacs K., Liu L., Liu X., Porter J., Sachs A., Shu Y., Sun Z., Wong J., Wu M., Zhang X., Jay G., He W.
      Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-45.
      Tissue: Placenta.
    3. "Human and mouse proteases: a comparative genomic approach."
      Puente X.S., Sanchez L.M., Overall C.M., Lopez-Otin C.
      Nat. Rev. Genet. 4:544-558(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.

    Entry informationi

    Entry nameiUBP27_HUMAN
    AccessioniPrimary (citable) accession number: A6NNY8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 2, 2007
    Last sequence update: March 24, 2009
    Last modified: October 1, 2014
    This is version 59 of the entry and version 3 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

    Caution

    Although strongly related to USP22, which deubiquitinates histones, lacks the N-terminal UBP-type zinc finger, suggesting it does not have the ability to deubiquitinate histones.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3