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Protein

Ubiquitin carboxyl-terminal hydrolase 14

Gene

USP14

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. 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. Indispensable for synaptic development and function at neuromuscular junctions (NMJs).3 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).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei114 – 1141Nucleophile1 Publication
Active sitei435 – 4351Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  • cysteine-type endopeptidase activity Source: ProtInc
  • endopeptidase inhibitor activity Source: UniProtKB
  • proteasome binding Source: UniProtKB
  • tRNA guanylyltransferase activity Source: ProtInc
  • ubiquitin-specific protease activity Source: FlyBase

GO - Biological processi

  • negative regulation of endopeptidase activity Source: GOC
  • negative regulation of ER-associated ubiquitin-dependent protein catabolic process Source: ParkinsonsUK-UCL
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: GO_Central
  • protein deubiquitination Source: FlyBase
  • regulation of chemotaxis Source: UniProtKB
  • regulation of proteasomal protein catabolic process Source: UniProtKB
  • synaptic transmission Source: Ensembl
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
Synonyms:TGT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:12612. USP14.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • cytoplasm Source: HPA
  • cytoplasmic membrane-bounded vesicle Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • nucleus Source: GO_Central
  • plasma membrane Source: UniProtKB-SubCell
  • proteasome complex Source: UniProtKB-KW
  • synapse Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Proteasome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37238.

Polymorphism and mutation databases

BioMutaiUSP14.
DMDMi1729927.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 494494Ubiquitin carboxyl-terminal hydrolase 14PRO_0000080636Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei143 – 1431Phosphoserine5 Publications
Modified residuei235 – 2351Phosphothreonine2 Publications
Modified residuei449 – 4491N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP54578.
PaxDbiP54578.
PeptideAtlasiP54578.
PRIDEiP54578.

2D gel databases

OGPiP54578.

PTM databases

PhosphoSiteiP54578.

Expressioni

Gene expression databases

BgeeiP54578.
CleanExiHS_USP14.
ExpressionAtlasiP54578. baseline and differential.
GenevestigatoriP54578.

Organism-specific databases

HPAiHPA001308.

Interactioni

Subunit structurei

Homodimer (Potential). Associates with the 26S proteasome. Interacts with FANCC, CXCR4 and ERN1.Curated3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PPP3CAQ082093EBI-1048016,EBI-352922

Protein-protein interaction databases

BioGridi114551. 59 interactions.
IntActiP54578. 31 interactions.
MINTiMINT-3020275.
STRINGi9606.ENSP00000261601.

Structurei

Secondary structure

1
494
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi110 – 1123Combined sources
Helixi114 – 12411Combined sources
Helixi127 – 1348Combined sources
Beta strandi144 – 1474Combined sources
Helixi148 – 16619Combined sources
Beta strandi168 – 1703Combined sources
Helixi173 – 18210Combined sources
Helixi184 – 1874Combined sources
Helixi200 – 21213Combined sources
Helixi242 – 2465Combined sources
Beta strandi249 – 26012Combined sources
Beta strandi269 – 27810Combined sources
Beta strandi280 – 2823Combined sources
Helixi286 – 2927Combined sources
Beta strandi297 – 3015Combined sources
Turni303 – 3064Combined sources
Beta strandi311 – 3199Combined sources
Beta strandi322 – 3298Combined sources
Beta strandi336 – 3394Combined sources
Beta strandi351 – 3544Combined sources
Helixi356 – 3583Combined sources
Helixi361 – 3666Combined sources
Turni367 – 3715Combined sources
Helixi372 – 3743Combined sources
Turni409 – 4124Combined sources
Beta strandi416 – 43015Combined sources
Beta strandi433 – 44311Combined sources
Beta strandi446 – 4516Combined sources
Beta strandi454 – 4585Combined sources
Helixi460 – 4634Combined sources
Helixi464 – 4674Combined sources
Beta strandi468 – 4725Combined sources
Beta strandi474 – 4818Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AYNX-ray3.20A/B/C91-494[»]
2AYOX-ray3.50A91-494[»]
ProteinModelPortaliP54578.
SMRiP54578. Positions 6-86, 98-483.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54578.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 8077Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST
Domaini105 – 483379USPAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG286607.
GeneTreeiENSGT00390000009615.
HOGENOMiHOG000202292.
HOVERGENiHBG054185.
InParanoidiP54578.
KOiK11843.
OMAiDWGNLKI.
OrthoDBiEOG7F7W8H.
PhylomeDBiP54578.
TreeFamiTF314494.

Family and domain databases

InterProiIPR001394. Peptidase_C19_UCH.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
IPR018200. USP_CS.
IPR028889. USP_dom.
[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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P54578-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPLYSVTVKW GKEKFEGVEL NTDEPPMVFK AQLFALTGVQ PARQKVMVKG
60 70 80 90 100
GTLKDDDWGN IKIKNGMTLL MMGSADALPE EPSAKTVFVE DMTEEQLASA
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 DSVKETDSSS ASAATPSKKK SLIDQFFGVE
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
LMLDMYELCT PELQEKMVSF RSKFKDLEDK KVNQQPNTSD KKSSPQKEVK
410 420 430 440 450
YEPFSFADDI GSNNCGYYDL QAVLTHQGRS SSSGHYVSWV KRKQDEWIKF
460 470 480 490
DDDKVSIVTP EDILRLSGGG DWHIAYVLLY GPRRVEIMEE ESEQ
Length:494
Mass (Da):56,069
Last modified:January 23, 2007 - v3
Checksum:iE6D4679A86E9DF00
GO
Isoform 2 (identifier: P54578-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     66-100: Missing.

Note: No experimental confirmation available.

Show »
Length:459
Mass (Da):52,386
Checksum:i3EDE73254891B166
GO
Isoform 3 (identifier: P54578-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     55-65: Missing.

Note: No experimental confirmation available.

Show »
Length:483
Mass (Da):54,770
Checksum:iB57991EE5A5CCA4E
GO

Sequence cautioni

The sequence CR976282 differs from that shown. Reason: Frameshift at position 288. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei55 – 6511Missing in isoform 3. 1 PublicationVSP_057292Add
BLAST
Alternative sequencei66 – 10035Missing in isoform 2. 1 PublicationVSP_047343Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30888 mRNA. Translation: AAB60365.1.
BT007183 mRNA. Translation: AAP35847.1.
AK297605 mRNA. Translation: BAH12624.1.
AP000845 Genomic DNA. No translation available.
BC003556 mRNA. Translation: AAH03556.1.
CR976282 mRNA. No translation available.
CCDSiCCDS32780.1. [P54578-1]
CCDS32781.1. [P54578-2]
PIRiG01932.
RefSeqiNP_001032411.1. NM_001037334.1. [P54578-2]
NP_005142.1. NM_005151.3. [P54578-1]
UniGeneiHs.464416.
Hs.707058.

Genome annotation databases

EnsembliENST00000261601; ENSP00000261601; ENSG00000101557. [P54578-1]
ENST00000400266; ENSP00000383125; ENSG00000101557. [P54578-3]
ENST00000582707; ENSP00000464447; ENSG00000101557. [P54578-2]
GeneIDi9097.
KEGGihsa:9097.
UCSCiuc002kkf.1. human. [P54578-1]
uc010wyr.1. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30888 mRNA. Translation: AAB60365.1.
BT007183 mRNA. Translation: AAP35847.1.
AK297605 mRNA. Translation: BAH12624.1.
AP000845 Genomic DNA. No translation available.
BC003556 mRNA. Translation: AAH03556.1.
CR976282 mRNA. No translation available.
CCDSiCCDS32780.1. [P54578-1]
CCDS32781.1. [P54578-2]
PIRiG01932.
RefSeqiNP_001032411.1. NM_001037334.1. [P54578-2]
NP_005142.1. NM_005151.3. [P54578-1]
UniGeneiHs.464416.
Hs.707058.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AYNX-ray3.20A/B/C91-494[»]
2AYOX-ray3.50A91-494[»]
ProteinModelPortaliP54578.
SMRiP54578. Positions 6-86, 98-483.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114551. 59 interactions.
IntActiP54578. 31 interactions.
MINTiMINT-3020275.
STRINGi9606.ENSP00000261601.

Chemistry

BindingDBiP54578.
ChEMBLiCHEMBL1293295.

Protein family/group databases

MEROPSiC19.015.

PTM databases

PhosphoSiteiP54578.

Polymorphism and mutation databases

BioMutaiUSP14.
DMDMi1729927.

2D gel databases

OGPiP54578.

Proteomic databases

MaxQBiP54578.
PaxDbiP54578.
PeptideAtlasiP54578.
PRIDEiP54578.

Protocols and materials databases

DNASUi9097.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261601; ENSP00000261601; ENSG00000101557. [P54578-1]
ENST00000400266; ENSP00000383125; ENSG00000101557. [P54578-3]
ENST00000582707; ENSP00000464447; ENSG00000101557. [P54578-2]
GeneIDi9097.
KEGGihsa:9097.
UCSCiuc002kkf.1. human. [P54578-1]
uc010wyr.1. human.

Organism-specific databases

CTDi9097.
GeneCardsiGC18P000148.
HGNCiHGNC:12612. USP14.
HPAiHPA001308.
MIMi607274. gene.
neXtProtiNX_P54578.
PharmGKBiPA37238.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG286607.
GeneTreeiENSGT00390000009615.
HOGENOMiHOG000202292.
HOVERGENiHBG054185.
InParanoidiP54578.
KOiK11843.
OMAiDWGNLKI.
OrthoDBiEOG7F7W8H.
PhylomeDBiP54578.
TreeFamiTF314494.

Miscellaneous databases

ChiTaRSiUSP14. human.
EvolutionaryTraceiP54578.
GeneWikiiUSP14.
GenomeRNAii9097.
NextBioi34093.
PROiP54578.
SOURCEiSearch...

Gene expression databases

BgeeiP54578.
CleanExiHS_USP14.
ExpressionAtlasiP54578. baseline and differential.
GenevestigatoriP54578.

Family and domain databases

InterProiIPR001394. Peptidase_C19_UCH.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
IPR018200. USP_CS.
IPR028889. USP_dom.
[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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "tRNA-guanine transglycosylase cDNA from human placenta."
    Deshpande K.L., Katze J.R.
    Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1).
    Tissue: Skin.
  6. Heil O., Ebert L., Hennig S., Henze S., Radelof U., Schneider D., Korn B.
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-308 (ISOFORM 2).
    Tissue: T-cell.
  7. "Yeast two-hybrid screens imply involvement of Fanconi anemia proteins in transcription regulation, cell signaling, oxidative metabolism, and cellular transport."
    Reuter T.Y., Medhurst A.L., Waisfisz Q., Zhi Y., Herterich S., Hoehn H., Gross H.J., Joenje H., Hoatlin M.E., Mathew C.G., Huber P.A.
    Exp. Cell Res. 289:211-221(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FANCC.
  8. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  9. "Relative structural and functional roles of multiple deubiquitylating proteins associated with mammalian 26S proteasome."
    Koulich E., Li X., DeMartino G.N.
    Mol. Biol. Cell 19:1072-1082(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH THE 26S PROTEASOME, FUNCTION.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "USP14 inhibits ER-associated degradation via interaction with IRE1alpha."
    Nagai A., Kadowaki H., Maruyama T., Takeda K., Nishitoh H., Ichijo H.
    Biochem. Biophys. Res. Commun. 379:995-1000(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ERN1.
  12. "Deubiquitination of CXCR4 by USP14 is critical for both CXCL12-induced CXCR4 degradation and chemotaxis but not ERK activation."
    Mines M.A., Goodwin J.S., Limbird L.E., Cui F.F., Fan G.H.
    J. Biol. Chem. 284:5742-5752(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CXCR4, FUNCTION, SUBCELLULAR LOCATION.
  13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-449, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143 AND THR-235, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143 AND THR-235, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14."
    Hu M., Li P., Song L., Jeffrey P.D., Chenova T.A., Wilkinson K.D., Cohen R.E., Shi Y.
    EMBO J. 24:3747-3756(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 91-494, CATALYTIC ACTIVITY, ACTIVE SITE.

Entry informationi

Entry nameiUBP14_HUMAN
AccessioniPrimary (citable) accession number: P54578
Secondary accession number(s): B7Z4N8, J3QRZ5, Q53XY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: May 27, 2015
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

Was originally (Ref. 1) thought to be a guanine tRNA-ribosyltransferase.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. 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.