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Protein

Ubiquitin carboxyl-terminal hydrolase 27

Gene

USP27X

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 – 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
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 Componenti: 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. 4 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

GeneTreeiENSGT00780000121889.
HOVERGENiHBG058014.
InParanoidiA6NNY8.
KOiK11366.
OMAiTEKHIHE.
PhylomeDBiA6NNY8.

Family and domain databases

InterProiIPR001394. Peptidase_C19_UCH.
IPR018200. USP_CS.
IPR028889. USP_dom.
[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

        10         20         30         40         50
MCKDYVYDKD IEQIAKEEQG EALKLQASTS TEVSHQQCSV PGLGEKFPTW
60 70 80 90 100
ETTKPELELL GHNPRRRRIT SSFTIGLRGL INLGNTCFMN CIVQALTHTP
110 120 130 140 150
ILRDFFLSDR HRCEMPSPEL CLVCEMSSLF RELYSGNPSP HVPYKLLHLV
160 170 180 190 200
WIHARHLAGY RQQDAHEFLI AALDVLHRHC KGDDVGKAAN NPNHCNCIID
210 220 230 240 250
QIFTGGLQSD VTCQACHGVS TTIDPCWDIS LDLPGSCTSF WPMSPGRESS
260 270 280 290 300
VNGESHIPGI TTLTDCLRRF TRPEHLGSSA KIKCGSCQSY QESTKQLTMN
310 320 330 340 350
KLPVVACFHF KRFEHSAKQR RKITTYISFP LELDMTPFMA SSKESRMNGQ
360 370 380 390 400
LQLPTNSGNN ENKYSLFAVV NHQGTLESGH YTSFIRHHKD QWFKCDDAVI
410 420 430
TKASIKDVLD SEGYLLFYHK QVLEHESEKV KEMNTQAY
Length:438
Mass (Da):49,630
Last modified:March 23, 2009 - v3
Checksum:iB6BFD18C62B3774C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321E → D in DR004246 (Ref. 2) Curated
Sequence conflicti45 – 451E → D in DR004246 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

EnsembliENST00000621775; ENSP00000483631; ENSG00000273820.
GeneIDi389856.
KEGGihsa:389856.
UCSCiuc004dop.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF238380 Genomic DNA. No translation available.
DR004246 mRNA. No translation available.
CCDSiCCDS65260.1.
RefSeqiNP_001138545.1. NM_001145073.2.
UniGeneiHs.143587.

3D structure databases

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

Protein-protein interaction databases

BioGridi133302. 4 interactions.
IntActiA6NNY8. 1 interaction.

PTM databases

PhosphoSiteiA6NNY8.

Proteomic databases

MaxQBiA6NNY8.
PRIDEiA6NNY8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000621775; ENSP00000483631; ENSG00000273820.
GeneIDi389856.
KEGGihsa:389856.
UCSCiuc004dop.3. human.

Organism-specific databases

CTDi389856.
GeneCardsiGC0XP049646.
H-InvDBHIX0077135.
HGNCiHGNC:13486. USP27X.
neXtProtiNX_A6NNY8.
PharmGKBiPA134993614.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00780000121889.
HOVERGENiHBG058014.
InParanoidiA6NNY8.
KOiK11366.
OMAiTEKHIHE.
PhylomeDBiA6NNY8.

Miscellaneous databases

GenomeRNAii389856.
NextBioi103162.
PROiA6NNY8.

Gene expression databases

CleanExiHS_USP27X.
GenevestigatoriA6NNY8.

Family and domain databases

InterProiIPR001394. Peptidase_C19_UCH.
IPR018200. USP_CS.
IPR028889. USP_dom.
[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]
ProtoNetiSearch...

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(2004) [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 (APR-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(2002) [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 1, 2007
Last sequence update: March 23, 2009
Last modified: February 3, 2015
This is version 62 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.