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Protein

Ubiquitin carboxyl-terminal hydrolase 27

Gene

Usp27

Organism
Mus musculus (Mouse)
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 endopeptidase activity Source: GO_Central
  2. ubiquitin-specific protease activity Source: GO_Central

GO - Biological processi

  1. histone deubiquitination Source: GO_Central
  2. proteasome-mediated ubiquitin-dependent protein catabolic process Source: GO_Central
  3. regulation of proteasomal protein catabolic process Source: GO_Central
  4. regulation of transcription, DNA-templated Source: GO_Central
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 thioesterase 27
Ubiquitin-specific-processing protease 27
X-linked ubiquitin carboxyl-terminal hydrolase 27
Gene namesi
Name:Usp27
Synonyms:Usp27x
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:1859645. Usp27x.

Subcellular locationi

GO - Cellular componenti

  1. SAGA complex Source: GO_Central
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 438438Ubiquitin carboxyl-terminal hydrolase 27PRO_0000367515Add
BLAST

Proteomic databases

PRIDEiQ8CEG8.

PTM databases

PhosphoSiteiQ8CEG8.

Expressioni

Gene expression databases

BgeeiQ8CEG8.
ExpressionAtlasiQ8CEG8. baseline and differential.
GenevestigatoriQ8CEG8.

Structurei

3D structure databases

ProteinModelPortaliQ8CEG8.
SMRiQ8CEG8. 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

eggNOGiCOG5533.
GeneTreeiENSGT00780000121889.
HOVERGENiHBG058014.
InParanoidiQ8CEG8.
KOiK11366.
OMAiTEKHIHE.
OrthoDBiEOG7FR7G7.
TreeFamiTF323554.

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.

Q8CEG8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCKDYVYDID IEQIAKEEQG EALKLQASTS TEVSQQQCSV PGLGEKYPTW
60 70 80 90 100
ETTKPELELL GHNPRRRRIA SSFTIGLRGL INLGNTCFMN CIVQALTHTP
110 120 130 140 150
ILRDFFLSDR HRCEMPSPEL CLVCEMSSLF RELYSGNPSP HVPYKLLHLV
160 170 180 190 200
WIHARHLAGY RQQDAHEFLI AALDVLHRHC KGDDVGKVAS NPNHCNCIID
210 220 230 240 250
QIFTGGLQSD VTCQACHGVS TTIDPCWDIS LDLPGSCTSF WPMSPGRESS
260 270 280 290 300
LNGESHIPGI TTLTDCLRRF TRPEHLGSSA KIKCGSCQSY QESTKQLTMK
310 320 330 340 350
KLPVVACFHF KRFEHSAKQR RKITTYISFP LELDMTPFMA SSKETRVNGQ
360 370 380 390 400
LQLPTNSANN ENKYSLFAVV NHQGTLESGH YTSFIRHHRD QWFKCDDAVI
410 420 430
TKASIKDVLD SEGYLLFYHK QVLEPEPEKV KEMTPQAY
Length:438
Mass (Da):49,599
Last modified:March 24, 2009 - v2
Checksum:i159B156E0E00FEB9
GO

Sequence cautioni

The sequence AAF66953.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC25840.1 differs from that shown. Reason: Frameshift at position 369. Curated
The sequence BAC25840.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAC26935.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741T → A in AAF66953 (PubMed:10857745).Curated
Sequence conflicti192 – 1921P → H in AAF66953 (PubMed:10857745).Curated
Sequence conflicti251 – 2522LN → VD in AAF66953 (PubMed:10857745).Curated
Sequence conflicti324 – 3241T → A in AAF66953 (PubMed:10857745).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS52983.1.
RefSeqiNP_062334.2. NM_019461.4.
UniGeneiMm.483107.
Mm.491689.

Genome annotation databases

EnsembliENSMUST00000115744; ENSMUSP00000111409; ENSMUSG00000046269.
ENSMUST00000178293; ENSMUSP00000137509; ENSMUSG00000046269.
ENSMUST00000191497; ENSMUSP00000139402; ENSMUSG00000046269.
GeneIDi54651.
KEGGimmu:54651.
UCSCiuc012hee.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS52983.1.
RefSeqiNP_062334.2. NM_019461.4.
UniGeneiMm.483107.
Mm.491689.

3D structure databases

ProteinModelPortaliQ8CEG8.
SMRiQ8CEG8. Positions 76-418.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ8CEG8.

Proteomic databases

PRIDEiQ8CEG8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000115744; ENSMUSP00000111409; ENSMUSG00000046269.
ENSMUST00000178293; ENSMUSP00000137509; ENSMUSG00000046269.
ENSMUST00000191497; ENSMUSP00000139402; ENSMUSG00000046269.
GeneIDi54651.
KEGGimmu:54651.
UCSCiuc012hee.1. mouse.

Organism-specific databases

CTDi389856.
MGIiMGI:1859645. Usp27x.

Phylogenomic databases

eggNOGiCOG5533.
GeneTreeiENSGT00780000121889.
HOVERGENiHBG058014.
InParanoidiQ8CEG8.
KOiK11366.
OMAiTEKHIHE.
OrthoDBiEOG7FR7G7.
TreeFamiTF323554.

Miscellaneous databases

NextBioi311508.
PROiQ8CEG8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CEG8.
ExpressionAtlasiQ8CEG8. baseline and differential.
GenevestigatoriQ8CEG8.

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. "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.
    , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.

Entry informationi

Entry nameiUBP27_MOUSE
AccessioniPrimary (citable) accession number: Q8CEG8
Secondary accession number(s): B1ATV2, Q8BSW2, Q9JIG5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 24, 2009
Last modified: March 4, 2015
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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