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

 UBP27_MOUSE             Reviewed;         438 AA.
Q8CEG8; B1ATV2; Q8BSW2; Q9JIG5;
24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
24-MAR-2009, sequence version 2.
20-JUN-2018, entry version 112.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase 27;
EC=3.4.19.12;
AltName: Full=Deubiquitinating enzyme 27;
AltName: Full=Ubiquitin thioesterase 27;
AltName: Full=Ubiquitin-specific-processing protease 27;
AltName: Full=X-linked ubiquitin carboxyl-terminal hydrolase 27;
Name=Usp27; Synonyms=Usp27x;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10857745; DOI=10.1006/geno.2000.6173;
Means G.D., Toy D.Y., Baum P.R., Derry J.M.J.;
"A transcript map of a 2-Mb BAC contig in the proximal portion of the
mouse X chromosome and regional mapping of the scurfy mutation.";
Genomics 65:213-223(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Head, and Pituitary;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
FUNCTION, INTERACTION WITH BCL2L11 ISOFORM BIMEL, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF CYS-87.
PubMed=27013495; DOI=10.15252/embr.201541392;
Weber A., Heinlein M., Dengjel J., Alber C., Singh P.K., Haecker G.;
"The deubiquitinase Usp27x stabilizes the BH3-only protein Bim and
enhances apoptosis.";
EMBO Rep. 17:724-738(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:0000269|PubMed:27013495}.
-!- 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:0000269|PubMed:27013495}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:27013495}. Nucleus
{ECO:0000269|PubMed:27013495}.
-!- 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}.
-!- SEQUENCE CAUTION:
Sequence=AAF66953.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAC25840.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAC25840.1; Type=Frameshift; Positions=369; Evidence={ECO:0000305};
Sequence=BAC26935.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF229643; AAF66953.1; ALT_INIT; mRNA.
EMBL; AK028249; BAC25840.1; ALT_SEQ; mRNA.
EMBL; AK030383; BAC26935.1; ALT_INIT; mRNA.
EMBL; AL663104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS52983.1; -.
RefSeq; NP_062334.2; NM_019461.4.
UniGene; Mm.483107; -.
UniGene; Mm.491689; -.
ProteinModelPortal; Q8CEG8; -.
STRING; 10090.ENSMUSP00000111409; -.
iPTMnet; Q8CEG8; -.
PhosphoSitePlus; Q8CEG8; -.
MaxQB; Q8CEG8; -.
PaxDb; Q8CEG8; -.
PRIDE; Q8CEG8; -.
Ensembl; ENSMUST00000115744; ENSMUSP00000111409; ENSMUSG00000046269.
Ensembl; ENSMUST00000178293; ENSMUSP00000137509; ENSMUSG00000046269.
Ensembl; ENSMUST00000191497; ENSMUSP00000139402; ENSMUSG00000046269.
GeneID; 54651; -.
KEGG; mmu:54651; -.
UCSC; uc012hee.1; mouse.
CTD; 389856; -.
MGI; MGI:1859645; Usp27x.
eggNOG; KOG1867; Eukaryota.
eggNOG; ENOG410XQQ0; LUCA.
GeneTree; ENSGT00890000139343; -.
HOVERGEN; HBG058014; -.
InParanoid; Q8CEG8; -.
KO; K11366; -.
OMA; TEKHIHE; -.
OrthoDB; EOG091G09GI; -.
TreeFam; TF323554; -.
PRO; PR:Q8CEG8; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000046269; -.
Genevisible; Q8CEG8; MM.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:1990380; F:Lys48-specific deubiquitinase activity; IDA:UniProtKB.
GO; GO:0061578; F:Lys63-specific deubiquitinase activity; IDA:UniProtKB.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
GO; GO:0071108; P:protein K48-linked deubiquitination; IDA:UniProtKB.
GO; GO:0070536; P:protein K63-linked deubiquitination; IDA:UniProtKB.
GO; GO:0050821; P:protein stabilization; IDA: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; Hydrolase; Nucleus; Protease;
Reference proteome; Thiol protease; Ubl conjugation pathway.
CHAIN 1 438 Ubiquitin carboxyl-terminal hydrolase 27.
/FTId=PRO_0000367515.
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}.
MUTAGEN 87 87 C->A: Loss of catalytic activity. No
effect on BCL2L11-binding, BCL2L11
stabilization, nor on apoptosis.
{ECO:0000269|PubMed:27013495}.
CONFLICT 74 74 T -> A (in Ref. 1; AAF66953).
{ECO:0000305}.
CONFLICT 192 192 P -> H (in Ref. 1; AAF66953).
{ECO:0000305}.
CONFLICT 251 252 LN -> VD (in Ref. 1; AAF66953).
{ECO:0000305}.
CONFLICT 324 324 T -> A (in Ref. 1; AAF66953).
{ECO:0000305}.
SEQUENCE 438 AA; 49599 MW; 159B156E0E00FEB9 CRC64;
MCKDYVYDID IEQIAKEEQG EALKLQASTS TEVSQQQCSV PGLGEKYPTW ETTKPELELL
GHNPRRRRIA SSFTIGLRGL INLGNTCFMN CIVQALTHTP ILRDFFLSDR HRCEMPSPEL
CLVCEMSSLF RELYSGNPSP HVPYKLLHLV WIHARHLAGY RQQDAHEFLI AALDVLHRHC
KGDDVGKVAS NPNHCNCIID QIFTGGLQSD VTCQACHGVS TTIDPCWDIS LDLPGSCTSF
WPMSPGRESS LNGESHIPGI TTLTDCLRRF TRPEHLGSSA KIKCGSCQSY QESTKQLTMK
KLPVVACFHF KRFEHSAKQR RKITTYISFP LELDMTPFMA SSKETRVNGQ LQLPTNSANN
ENKYSLFAVV NHQGTLESGH YTSFIRHHRD QWFKCDDAVI TKASIKDVLD SEGYLLFYHK
QVLEPEPEKV KEMTPQAY


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