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Q9JMA1

- UBP14_MOUSE

UniProt

Q9JMA1 - UBP14_MOUSE

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Protein

Ubiquitin carboxyl-terminal hydrolase 14

Gene

Usp14

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 ERN1.2 Publications

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 sitei114 – 1141NucleophilePROSITE-ProRule annotation
Active sitei434 – 4341Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  1. endopeptidase inhibitor activity Source: Ensembl
  2. ubiquitin-specific protease activity Source: Ensembl
  3. ubiquitin thiolesterase activity Source: Ensembl

GO - Biological processi

  1. protein deubiquitination Source: Ensembl
  2. regulation of chemotaxis Source: Ensembl
  3. regulation of proteasomal protein catabolic process Source: Ensembl
  4. synaptic transmission Source: MGI
  5. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Protein family/group databases

MEROPSiC19.015.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Usp14
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:1928898. Usp14.

Subcellular locationi

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

GO - Cellular componenti

  1. cell surface Source: Ensembl
  2. cytoplasmic membrane-bounded vesicle Source: Ensembl
  3. plasma membrane Source: UniProtKB-KW
  4. proteasome complex Source: UniProtKB-KW
  5. synapse Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 493493Ubiquitin carboxyl-terminal hydrolase 14PRO_0000080637Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei143 – 1431Phosphoserine1 Publication
Modified residuei235 – 2351PhosphothreonineBy similarity
Modified residuei448 – 4481N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9JMA1.
PaxDbiQ9JMA1.
PRIDEiQ9JMA1.

PTM databases

PhosphoSiteiQ9JMA1.

Expressioni

Gene expression databases

BgeeiQ9JMA1.
CleanExiMM_USP14.
ExpressionAtlasiQ9JMA1. baseline and differential.
GenevestigatoriQ9JMA1.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi208492. 6 interactions.
IntActiQ9JMA1. 1 interaction.
MINTiMINT-4139172.

Structurei

Secondary structure

1
493
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107
Beta strandi13 – 2412
Helixi26 – 3611
Turni41 – 433
Beta strandi68 – 703

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WGGNMR-A4-86[»]
ProteinModelPortaliQ9JMA1.
SMRiQ9JMA1. Positions 6-86, 98-482.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JMA1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 8077Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST
Domaini105 – 482378USPAdd
BLAST

Sequence similaritiesi

Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation
Contains 1 USP domain.Curated

Phylogenomic databases

eggNOGiNOG286607.
GeneTreeiENSGT00390000009615.
HOGENOMiHOG000202292.
HOVERGENiHBG054185.
InParanoidiQ9JMA1.
KOiK11843.
OMAiDWGNLKI.
OrthoDBiEOG7F7W8H.
PhylomeDBiQ9JMA1.
TreeFamiTF314494.

Family and domain databases

InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
IPR028889. UCH/PAN2.
[Graphical view]
PfamiPF00443. UCH. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS00299. 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]

Sequencei

Sequence statusi: Complete.

Q9JMA1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPLYSVTVKW GKEKFEGVEL NTDEPPMVFK AQLFALTGVQ PARQKVMVKG
60 70 80 90 100
GTLKDDDWGN IKMKNGMTVL MMGSADALPE EPSAKTVFVE DMTEEQLATA
110 120 130 140 150
MELPCGLTNL GNTCYMNATV QCIRSVPELK DALKRYAGAL RASGEMASAQ
160 170 180 190 200
YITAALRDLF DSMDKTSSSI PPIILLQFLH MAFPQFAEKG EQGQYLQQDA
210 220 230 240 250
NECWIQMMRV LQQKLEAIED DSGRETDSSS APAVTPSKKK SLIDQYFGVE
260 270 280 290 300
FETTMKCTES EEEEVTKGKE NQLQLSCFIN QEVKYLFTGL KLRLQEEITK
310 320 330 340 350
QSPTLQRNAL YIKSSKISRL PAYLTIQMVR FFYKEKESVN AKVLKDVKFP
360 370 380 390 400
LMLDVYELCT PELQEKMVSF RSKFKDLEDK KVNQQPNAND KNSPPKEIKY
410 420 430 440 450
EPFSFADDIG SNNCGYYDLQ AVLTHQGRSS SSGHYVSWVR RKQDEWIKFD
460 470 480 490
DDKVSIVTPE DILRLSGGGD WHIAYVLLYG PRRVEIMEEE SEQ
Length:493
Mass (Da):56,002
Last modified:January 23, 2007 - v3
Checksum:i4E5F5DCB86057FF9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti185 – 1851Q → R in BAA93551. 1 PublicationCurated
Sequence conflicti310 – 3101L → S in BAA93551. 1 PublicationCurated
Sequence conflicti385 – 3851Q → E in BAB27544. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS37735.1.
RefSeqiNP_067497.2. NM_021522.4.
UniGeneiMm.329277.
Mm.447089.

Genome annotation databases

EnsembliENSMUST00000092096; ENSMUSP00000089728; ENSMUSG00000047879.
GeneIDi59025.
KEGGimmu:59025.
UCSCiuc008ean.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS37735.1.
RefSeqi NP_067497.2. NM_021522.4.
UniGenei Mm.329277.
Mm.447089.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WGG NMR - A 4-86 [» ]
ProteinModelPortali Q9JMA1.
SMRi Q9JMA1. Positions 6-86, 98-482.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 208492. 6 interactions.
IntActi Q9JMA1. 1 interaction.
MINTi MINT-4139172.

Protein family/group databases

MEROPSi C19.015.

PTM databases

PhosphoSitei Q9JMA1.

Proteomic databases

MaxQBi Q9JMA1.
PaxDbi Q9JMA1.
PRIDEi Q9JMA1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000092096 ; ENSMUSP00000089728 ; ENSMUSG00000047879 .
GeneIDi 59025.
KEGGi mmu:59025.
UCSCi uc008ean.1. mouse.

Organism-specific databases

CTDi 9097.
MGIi MGI:1928898. Usp14.

Phylogenomic databases

eggNOGi NOG286607.
GeneTreei ENSGT00390000009615.
HOGENOMi HOG000202292.
HOVERGENi HBG054185.
InParanoidi Q9JMA1.
KOi K11843.
OMAi DWGNLKI.
OrthoDBi EOG7F7W8H.
PhylomeDBi Q9JMA1.
TreeFami TF314494.

Miscellaneous databases

EvolutionaryTracei Q9JMA1.
NextBioi 314596.
PROi Q9JMA1.
SOURCEi Search...

Gene expression databases

Bgeei Q9JMA1.
CleanExi MM_USP14.
ExpressionAtlasi Q9JMA1. baseline and differential.
Genevestigatori Q9JMA1.

Family and domain databases

InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
IPR028889. UCH/PAN2.
[Graphical view ]
Pfami PF00443. UCH. 1 hit.
[Graphical view ]
SMARTi SM00213. UBQ. 1 hit.
[Graphical view ]
SUPFAMi SSF54236. SSF54236. 1 hit.
PROSITEi PS00299. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiUBP14_MOUSE
AccessioniPrimary (citable) accession number: Q9JMA1
Secondary accession number(s): Q543U5, Q923F2, Q9D0L0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3