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A6NNY8

- UBP27_HUMAN

UniProt

A6NNY8 - UBP27_HUMAN

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Protein

Ubiquitin carboxyl-terminal hydrolase 27

Gene
USP27X, USP22L, USP27
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

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 – 871Nucleophile By similarity
Active sitei380 – 3801Proton acceptor By similarity

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
Complete GO annotation...

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.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

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

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

Sequence conflict

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

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

EnsembliENST00000508866; ENSP00000475071; ENSG00000242013.
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

Ensembli ENST00000508866 ; ENSP00000475071 ; ENSG00000242013 .
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 58 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.

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

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