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Ubiquitin carboxyl-terminal hydrolase 27 (EC 3.4.19.12) (Deubiquitinating enzyme 27) (Ubiquitin carboxyl-terminal hydrolase 22-like) (Ubiquitin thioesterase 27) (Ubiquitin-specific-processing protease 27) (X-linked ubiquitin carboxyl-terminal hydrolase 27)

 UBP27_HUMAN             Reviewed;         438 AA.
A6NNY8;
02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
24-MAR-2009, sequence version 3.
12-SEP-2018, entry version 91.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase 27;
EC=3.4.19.12;
AltName: Full=Deubiquitinating enzyme 27;
AltName: Full=Ubiquitin carboxyl-terminal hydrolase 22-like;
AltName: Full=Ubiquitin thioesterase 27;
AltName: Full=Ubiquitin-specific-processing protease 27;
AltName: Full=X-linked ubiquitin carboxyl-terminal hydrolase 27;
Name=USP27X; Synonyms=USP22L, USP27;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
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.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-45.
TISSUE=Placenta;
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.;
"High-throughput cloning of full-length human cDNAs directly from cDNA
libraries optimized for large and rare transcripts.";
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
[3]
IDENTIFICATION.
PubMed=12838346; DOI=10.1038/nrg1111;
Puente X.S., Sanchez L.M., Overall C.M., Lopez-Otin C.;
"Human and mouse proteases: a comparative genomic approach.";
Nat. Rev. Genet. 4:544-558(2003).
[4]
INVOLVEMENT IN MRX105, AND VARIANT MRX105 HIS-381.
PubMed=25644381; DOI=10.1038/mp.2014.193;
Hu H., Haas S.A., Chelly J., Van Esch H., Raynaud M., de Brouwer A.P.,
Weinert S., Froyen G., Frints S.G., Laumonnier F., Zemojtel T.,
Love M.I., Richard H., Emde A.K., Bienek M., Jensen C., Hambrock M.,
Fischer U., Langnick C., Feldkamp M., Wissink-Lindhout W., Lebrun N.,
Castelnau L., Rucci J., Montjean R., Dorseuil O., Billuart P.,
Stuhlmann T., Shaw M., Corbett M.A., Gardner A., Willis-Owen S.,
Tan C., Friend K.L., Belet S., van Roozendaal K.E.,
Jimenez-Pocquet M., Moizard M.P., Ronce N., Sun R., O'Keeffe S.,
Chenna R., van Boemmel A., Goeke J., Hackett A., Field M.,
Christie L., Boyle J., Haan E., Nelson J., Turner G., Baynam G.,
Gillessen-Kaesbach G., Mueller U., Steinberger D., Budny B.,
Badura-Stronka M., Latos-Bielenska A., Ousager L.B., Wieacker P.,
Rodriguez Criado G., Bondeson M.L., Anneren G., Dufke A., Cohen M.,
Van Maldergem L., Vincent-Delorme C., Echenne B., Simon-Bouy B.,
Kleefstra T., Willemsen M., Fryns J.P., Devriendt K., Ullmann R.,
Vingron M., Wrogemann K., Wienker T.F., Tzschach A., van Bokhoven H.,
Gecz J., Jentsch T.J., Chen W., Ropers H.H., Kalscheuer V.M.;
"X-exome sequencing of 405 unresolved families identifies seven novel
intellectual disability genes.";
Mol. Psychiatry 21:133-148(2016).
-!- FUNCTION: Deubiquitinase that can reduce the levels of BCL2L11/BIM
ubiquitination and stabilize BCL2L11 in response to the RAF-MAPK-
degradation signal. By acting on BCL2L11 levels, may counteract
the anti-apoptotic effects of MAPK activity.
{ECO:0000250|UniProtKB:Q8CEG8}.
-!- 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: Interacts with phosphorylated BCL2L11 isoform BIMEL; this
interaction leads to BCL2L11 deubiquitination and stabilization.
{ECO:0000250|UniProtKB:Q8CEG8}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:Q8CEG8}. Nucleus
{ECO:0000250|UniProtKB:Q8CEG8}.
-!- DISEASE: Mental retardation, X-linked 105 (MRX105) [MIM:300984]: A
form of mental retardation, a disorder characterized by
significantly below average general intellectual functioning
associated with impairments in adaptive behavior and manifested
during the developmental period. Intellectual deficiency is the
only primary symptom of non-syndromic X-linked mental retardation,
while syndromic mental retardation presents with associated
physical, neurological and/or psychiatric manifestations.
{ECO:0000269|PubMed:25644381}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
-!- 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.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF238380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; DR004246; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS65260.1; -.
RefSeq; NP_001138545.1; NM_001145073.2.
UniGene; Hs.143587; -.
ProteinModelPortal; A6NNY8; -.
BioGrid; 133302; 7.
IntAct; A6NNY8; 1.
iPTMnet; A6NNY8; -.
PhosphoSitePlus; A6NNY8; -.
EPD; A6NNY8; -.
MaxQB; A6NNY8; -.
PRIDE; A6NNY8; -.
ProteomicsDB; 1647; -.
Ensembl; ENST00000621775; ENSP00000483631; ENSG00000273820.
GeneID; 389856; -.
KEGG; hsa:389856; -.
UCSC; uc033edm.2; human.
CTD; 389856; -.
EuPathDB; HostDB:ENSG00000273820.1; -.
GeneCards; USP27X; -.
H-InvDB; HIX0077135; -.
HGNC; HGNC:13486; USP27X.
HPA; HPA077264; -.
MalaCards; USP27X; -.
MIM; 300975; gene.
MIM; 300984; phenotype.
neXtProt; NX_A6NNY8; -.
OpenTargets; ENSG00000273820; -.
PharmGKB; PA134993614; -.
GeneTree; ENSGT00890000139343; -.
HOVERGEN; HBG058014; -.
InParanoid; A6NNY8; -.
KO; K11366; -.
OMA; TEKHIHE; -.
OrthoDB; EOG091G09GI; -.
PhylomeDB; A6NNY8; -.
GenomeRNAi; 389856; -.
PRO; PR:A6NNY8; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000273820; Expressed in 187 organ(s), highest expression level in chorionic villus.
CleanEx; HS_USP27X; -.
Genevisible; A6NNY8; HS.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:1990380; F:Lys48-specific deubiquitinase activity; ISS:UniProtKB.
GO; GO:0061578; F:Lys63-specific deubiquitinase activity; ISS:UniProtKB.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
GO; GO:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB.
GO; GO:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB.
GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
InterPro; IPR038765; Papain_like_cys_pep_sf.
InterPro; IPR001394; Peptidase_C19_UCH.
InterPro; IPR018200; USP_CS.
InterPro; IPR028889; USP_dom.
Pfam; PF00443; UCH; 1.
SUPFAM; SSF54001; SSF54001; 1.
PROSITE; PS00972; USP_1; 1.
PROSITE; PS00973; USP_2; 1.
PROSITE; PS50235; USP_3; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Disease mutation; Hydrolase;
Mental retardation; Nucleus; Protease; Reference proteome;
Thiol protease; Ubl conjugation pathway.
CHAIN 1 438 Ubiquitin carboxyl-terminal hydrolase 27.
/FTId=PRO_0000306334.
DOMAIN 78 421 USP.
ACT_SITE 87 87 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
ACT_SITE 380 380 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
VARIANT 381 381 Y -> H (in MRX105; dbSNP:rs886038211).
{ECO:0000269|PubMed:25644381}.
/FTId=VAR_077830.
CONFLICT 32 32 E -> D (in Ref. 2; DR004246).
{ECO:0000305}.
CONFLICT 45 45 E -> D (in Ref. 2; DR004246).
{ECO:0000305}.
SEQUENCE 438 AA; 49630 MW; B6BFD18C62B3774C CRC64;
MCKDYVYDKD IEQIAKEEQG EALKLQASTS TEVSHQQCSV PGLGEKFPTW ETTKPELELL
GHNPRRRRIT SSFTIGLRGL INLGNTCFMN CIVQALTHTP ILRDFFLSDR HRCEMPSPEL
CLVCEMSSLF RELYSGNPSP HVPYKLLHLV WIHARHLAGY RQQDAHEFLI AALDVLHRHC
KGDDVGKAAN NPNHCNCIID QIFTGGLQSD VTCQACHGVS TTIDPCWDIS LDLPGSCTSF
WPMSPGRESS VNGESHIPGI TTLTDCLRRF TRPEHLGSSA KIKCGSCQSY QESTKQLTMN
KLPVVACFHF KRFEHSAKQR RKITTYISFP LELDMTPFMA SSKESRMNGQ LQLPTNSGNN
ENKYSLFAVV NHQGTLESGH YTSFIRHHKD QWFKCDDAVI TKASIKDVLD SEGYLLFYHK
QVLEHESEKV KEMNTQAY


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