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Q9JMA1 (UBP14_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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 14

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 14
Ubiquitin thioesterase 14
Ubiquitin-specific-processing protease 14
Gene names
Name:Usp14
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. Ensures the regeneration of ubiquitin at the proteasome. Maintains the cellular levels of monomeric ubiquitin in cells. Indispensable for synaptic development and function at neuromuscular junctions (NMJs). Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell. Required for the degradation of the chemokine receptor cxcr4 which is critical for CXCL12-induced cell chemotaxis. Serves also as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1. Ref.5 Ref.7

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 structure

Homodimer Potential. Interacts with FANCC, CXCR4 and ERN1 By similarity. Associates with the 26S proteasome.

Subcellular location

Cytoplasm By similarity. Cell membrane; Peripheral membrane protein By similarity.

Sequence similarities

Belongs to the peptidase C19 family. USP14/UBP6 subfamily.

Contains 1 ubiquitin-like domain.

Contains 1 USP domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 493493Ubiquitin carboxyl-terminal hydrolase 14
PRO_0000080637

Regions

Domain4 – 8077Ubiquitin-like
Domain105 – 482378USP

Sites

Active site1141Nucleophile By similarity
Active site4341Proton acceptor By similarity

Amino acid modifications

Modified residue1431Phosphoserine Ref.6
Modified residue2351Phosphothreonine 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 [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14."
Borodovsky A., Kessler B.M., Casagrande R., Overkleeft H.S., Wilkinson K.D., Ploegh H.L.
EMBO J. 20:5187-5196(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION, ASSOCIATION WITH THE 26S PROTEASOME.
[5]"Loss of Usp14 results in reduced levels of ubiquitin in ataxia mice."
Anderson C., Crimmins S., Wilson J.A., Korbel G.A., Ploegh H.L., Wilson S.M.
J. Neurochem. 95:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ASSOCIATION WITH THE 26S PROTEASOME.
[6]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[7]"The proteasome-associated deubiquitinating enzyme Usp14 is essential for the maintenance of synaptic ubiquitin levels and the development of neuromuscular junctions."
Chen P.C., Qin L.N., Li X.M., Walters B.J., Wilson J.A., Mei L., Wilson S.M.
J. Neurosci. 29:10909-10919(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"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.
RefSeqNP_067497.2. NM_021522.4.
UniGeneMm.329277.
Mm.447089.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WGGNMR-A4-85[»]
ProteinModelPortalQ9JMA1.
SMRQ9JMA1. Positions 6-86, 98-482.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid208492. 4 interactions.
IntActQ9JMA1. 1 interaction.
MINTMINT-4139172.

Protein family/group databases

MEROPSC19.015.

PTM databases

PhosphoSiteQ9JMA1.

Proteomic databases

PaxDbQ9JMA1.
PRIDEQ9JMA1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000092096; ENSMUSP00000089728; ENSMUSG00000047879.
GeneID59025.
KEGGmmu:59025.
UCSCuc008ean.1. mouse.

Organism-specific databases

CTD9097.
MGIMGI:1928898. Usp14.

Phylogenomic databases

eggNOGNOG286607.
GeneTreeENSGT00390000009615.
HOGENOMHOG000202292.
HOVERGENHBG054185.
KOK11843.
OMAMRRELKC.
OrthoDBEOG7F7W8H.
TreeFamTF314494.

Gene expression databases

ArrayExpressQ9JMA1.
BgeeQ9JMA1.
CleanExMM_USP14.
GenevestigatorQ9JMA1.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR019954. Ubiquitin_CS.
IPR000626. Ubiquitin_dom.
IPR028889. UCH/PAN2.
[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. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9JMA1.
NextBio314596.
PROQ9JMA1.
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: March 19, 2014
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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