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Q8CEG8 (UBP27_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase 27
EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 27
Ubiquitin thioesterase 27
Ubiquitin-specific-processing protease 27
X-linked ubiquitin carboxyl-terminal hydrolase 27
Gene names
Name:Usp27
Synonyms:Usp27x
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length438 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

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).

Sequence similarities

Belongs to the peptidase C19 family.

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.

Sequence caution

The sequence AAF66953.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAC25840.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAC25840.1 differs from that shown. Reason: Frameshift at position 369.

The sequence BAC26935.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 438438Ubiquitin carboxyl-terminal hydrolase 27
PRO_0000367515

Sites

Active site871Nucleophile By similarity
Active site3801Proton acceptor By similarity

Experimental info

Sequence conflict741T → A in AAF66953. Ref.1
Sequence conflict1921P → H in AAF66953. Ref.1
Sequence conflict251 – 2522LN → VD in AAF66953. Ref.1
Sequence conflict3241T → A in AAF66953. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8CEG8 [UniParc].

Last modified March 24, 2009. Version 2.
Checksum: 159B156E0E00FEB9

FASTA43849,599
        10         20         30         40         50         60 
MCKDYVYDID IEQIAKEEQG EALKLQASTS TEVSQQQCSV PGLGEKYPTW ETTKPELELL 

        70         80         90        100        110        120 
GHNPRRRRIA SSFTIGLRGL INLGNTCFMN CIVQALTHTP ILRDFFLSDR HRCEMPSPEL 

       130        140        150        160        170        180 
CLVCEMSSLF RELYSGNPSP HVPYKLLHLV WIHARHLAGY RQQDAHEFLI AALDVLHRHC 

       190        200        210        220        230        240 
KGDDVGKVAS NPNHCNCIID QIFTGGLQSD VTCQACHGVS TTIDPCWDIS LDLPGSCTSF 

       250        260        270        280        290        300 
WPMSPGRESS LNGESHIPGI TTLTDCLRRF TRPEHLGSSA KIKCGSCQSY QESTKQLTMK 

       310        320        330        340        350        360 
KLPVVACFHF KRFEHSAKQR RKITTYISFP LELDMTPFMA SSKETRVNGQ LQLPTNSANN 

       370        380        390        400        410        420 
ENKYSLFAVV NHQGTLESGH YTSFIRHHRD QWFKCDDAVI TKASIKDVLD SEGYLLFYHK 

       430 
QVLEPEPEKV KEMTPQAY

« Hide

References

« Hide 'large scale' references
[1]"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."
Means G.D., Toy D.Y., Baum P.R., Derry J.M.J.
Genomics 65:213-223(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Head and Pituitary.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
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. expand/collapse author list , 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.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF229643 mRNA. Translation: AAF66953.1. Different initiation.
AK028249 mRNA. Translation: BAC25840.1. Sequence problems.
AK030383 mRNA. Translation: BAC26935.1. Different initiation.
AL663104 Genomic DNA. Translation: CAM17475.1.
IPIIPI00224850.
RefSeqNP_062334.2. NM_019461.4.
UniGeneMm.483107.
Mm.488988.

3D structure databases

HSSPHSSP built from PDB template 2AYN based on UniProtKB P54578.
ProteinModelPortalQ8CEG8.
SMRQ8CEG8. Positions 76-418.
ModBaseSearch...

PTM databases

PhosphoSiteQ8CEG8.

Proteomic databases

PRIDEQ8CEG8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000115744; ENSMUSP00000111409; ENSMUSG00000046269.
ENSMUST00000178293; ENSMUSP00000137509; ENSMUSG00000046269.
GeneID54651.
KEGGmmu:54651.

Organism-specific databases

CTD389856.
MGIMGI:1859645. Usp27x.

Phylogenomic databases

eggNOGCOG5533.
GeneTreeENSGT00690000101718.
HOVERGENHBG058014.
InParanoidQ9JIG5.
KOK11366.
OrthoDBEOG4VT5X3.

Gene expression databases

ArrayExpressQ8CEG8.
BgeeQ8CEG8.
GenevestigatorQ8CEG8.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19.
[Graphical view]
PfamPF00443. UCH. 1 hit.
[Graphical view]
PROSITEPS00972. UCH_2_1. 1 hit.
PS00973. UCH_2_2. 1 hit.
PS50235. UCH_2_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio311508.
SOURCESearch...

Entry information

Entry nameUBP27_MOUSE
AccessionPrimary (citable) accession number: Q8CEG8
Secondary accession number(s): B1ATV2, Q8BSW2, Q9JIG5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 24, 2009
Last modified: May 1, 2013
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents