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Reviewed, UniProtKB/Swiss-Prot Q9JMA1 (UBP14_MOUSE)

Last modified January 19, 2010. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ubiquitin carboxyl-terminal hydrolase 14
    EC=3.1.2.15
Alternative name(s):
    Ubiquitin thioesterase 14
    Ubiquitin-specific-processing protease 14
    Deubiquitinating enzyme 14
Gene names
Name: Usp14
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

Ubiquitin C-terminal thioester + H2O = ubiquitin + a thiol.

Subunit structure

Homodimer Potential.

Sequence similarities

Belongs to the peptidase C19 family.

Contains 1 ubiquitin-like domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 493492Ubiquitin carboxyl-terminal hydrolase 14
PRO_0000080637

Regions

Domain4 – 8077Ubiquitin-like

Sites

Active site1141 By similarity
Active site4251 By similarity
Active site4341 By similarity

Amino acid modifications

Modified residue1361Phosphotyrosine Ref.4
Modified residue1431Phosphoserine Ref.4
Modified residue2221Phosphoserine Ref.4
Modified residue2911N6-acetyllysine By similarity
Modified residue3131N6-acetyllysine By similarity
Modified residue4481N6-acetyllysine By similarity

Experimental info

Sequence conflict1851Q → R in BAA93551. Ref.1
Sequence conflict3101L → S in BAA93551. Ref.1
Sequence conflict3851Q → E in BAB27544. Ref.2

Secondary structure

........... 493
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9JMA1-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 4E5F5DCB86057FF9

FASTA49356,002
        10         20         30         40         50         60 
MPLYSVTVKW GKEKFEGVEL NTDEPPMVFK AQLFALTGVQ PARQKVMVKG GTLKDDDWGN 

        70         80         90        100        110        120 
IKMKNGMTVL MMGSADALPE EPSAKTVFVE DMTEEQLATA MELPCGLTNL GNTCYMNATV 

       130        140        150        160        170        180 
QCIRSVPELK DALKRYAGAL RASGEMASAQ YITAALRDLF DSMDKTSSSI PPIILLQFLH 

       190        200        210        220        230        240 
MAFPQFAEKG EQGQYLQQDA NECWIQMMRV LQQKLEAIED DSGRETDSSS APAVTPSKKK 

       250        260        270        280        290        300 
SLIDQYFGVE FETTMKCTES EEEEVTKGKE NQLQLSCFIN QEVKYLFTGL KLRLQEEITK 

       310        320        330        340        350        360 
QSPTLQRNAL YIKSSKISRL PAYLTIQMVR FFYKEKESVN AKVLKDVKFP LMLDVYELCT 

       370        380        390        400        410        420 
PELQEKMVSF RSKFKDLEDK KVNQQPNAND KNSPPKEIKY EPFSFADDIG SNNCGYYDLQ 

       430        440        450        460        470        480 
AVLTHQGRSS SSGHYVSWVR RKQDEWIKFD DDKVSIVTPE DILRLSGGGD WHIAYVLLYG 

       490 
PRRVEIMEEE SEQ 

« Hide

References

« Hide 'large scale' references
[1]"Mouse deubiquitinating enzyme-type TGT."
Hidaka T., Morishita T.
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Corpora quadrigemina, Embryo and Testis.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-136; SER-143 AND SER-222, MASS SPECTROMETRY.
Tissue: Liver.
[5]"Solution structure of the N-terminal ubiquitin-like domain of mouse ubiquitin specific protease 14 (usp14)."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2004) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 4-86.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB034633 mRNA. Translation: BAA93551.1.
AK011322 mRNA. Translation: BAB27544.1.
AK029977 mRNA. Translation: BAC26713.1.
AK045909 mRNA. Translation: BAC32528.1.
BC005571 mRNA. Translation: AAH05571.1.
IPIIPI00270877.
RefSeqNP_067497.2.
UniGeneMm.219648
Mm.329277
Mm.447089

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WGGNMR-A4-85[»]
SMRQ9JMA1. Positions 98-482.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9JMA1.

Protein family/group databases

MEROPSC19.015.

PTM databases

PhosphoSiteQ9JMA1.

Proteomic databases

PRIDEQ9JMA1.

Genome annotation databases

EnsemblENSMUST00000092096; ENSMUSP00000089728; ENSMUSG00000047879; Mus musculus. [Genome view]
GeneID59025.
UCSCuc008ean.1. mouse.

Organism-specific databases

CTD59025.
MGIMGI:1928898. Usp14.

Phylogenomic databases

HOVERGENQ9JMA1.
OMAITHKGRS.
PhylomeDBQ9JMA1.

Enzyme and pathway databases

BRENDA3.1.2.15. 244.

Gene expression databases

ArrayExpressQ9JMA1.
BgeeQ9JMA1.
CleanExMM_USP14.
GenevestigatorQ9JMA1.
GermOnlineENSMUSG00000047879. Mus musculus.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19.
IPR000626. Ubiquitin.
IPR019954. Ubiquitin_CS.
IPR019955. Ubiquitin_supergroup.
[Graphical view]
PfamPF00443. UCH. 1 hit.
[Graphical view]
SMARTSM00213. UBQ. 1 hit.
[Graphical view]
PROSITEPS00299. UBIQUITIN_1. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
PS00972. UCH_2_1. 1 hit.
PS00973. UCH_2_2. 1 hit.
PS50235. UCH_2_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio314596.
SOURCESearch...

Entry information

Entry nameUBP14_MOUSE
AccessionPrimary (citable) accession number: Q9JMA1
Secondary accession number(s): Q543U5, Q923F2, Q9D0L0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: January 23, 2007
Last modified: January 19, 2010
This is version 89 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents