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P29692 (EF1D_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 156. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Elongation factor 1-delta

Short name=EF-1-delta
Alternative name(s):
Antigen NY-CO-4
Gene names
Name:EEF1D
Synonyms:EF1D
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length281 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Isoform 1:EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP, regenerating EF-1-alpha for another round of transfer of aminoacyl-tRNAs to the ribosome. Ref.28

Isoform 2:Regulates induction of heat-shock-responsive genes through association with heat shock transcription factors and direct DNA-binding at heat shock promoter elements (HSE). Ref.28

Subunit structure

EF-1 is composed of 4 subunits: alpha, beta, delta isoform 1, and gamma. Isoform 2 interacts with HSF1 and NFE2L2. Ref.28

Subcellular location

Isoform 2: Nucleus Ref.28.

Tissue specificity

Isoform 2 is specifically expressed in brain, cerebellum and testis. Ref.28

Induction

By homocysteine (HC), may mediate accelerated synthesis of free thiol-containing proteins in response to HC-induced oxidative stress. Also induced following exposure to ionizing radiation. Ref.10 Ref.11

Sequence similarities

Belongs to the EF-1-beta/EF-1-delta family.

Ontologies

Keywords
   Biological processProtein biosynthesis
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   LigandDNA-binding
   Molecular functionElongation factor
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular protein metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

signal transduction

Inferred from mutant phenotype PubMed 12761501. Source: GOC

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

translation

Traceable author statement. Source: Reactome

translational elongation

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

eukaryotic translation elongation factor 1 complex

Traceable author statement Ref.1. Source: ProtInc

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 16169070PubMed 16189514PubMed 20195357. Source: IntAct

signal transducer activity

Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB

translation elongation factor activity

Inferred from electronic annotation. Source: UniProtKB-KW

translation factor activity, nucleic acid binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P29692-1)

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.
Isoform 2 (identifier: P29692-2)

Also known as: eEF1BdeltaL;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRSGKASCTL...VSSLRPNRKM
Note: Contains a phosphoserine at position 91. Contains a phosphoserine at position 94.
Isoform 3 (identifier: P29692-3)

The sequence of this isoform differs from the canonical sequence as follows:
     40-63: Missing.
Note: Contains a phosphoserine at position 40.
Isoform 4 (identifier: P29692-4)

The sequence of this isoform differs from the canonical sequence as follows:
     78-96: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 281280Elongation factor 1-delta
PRO_0000155046

Regions

Region80 – 11536Leucine-zipper
Region173 – 281109Catalytic (GEF)

Amino acid modifications

Modified residue21N-acetylalanine Ref.9 Ref.31
Modified residue171N6-acetyllysine Ref.25
Modified residue1071N6-acetyllysine Ref.25
Modified residue1171N6-acetyllysine; alternate Ref.25
Modified residue1171N6-succinyllysine; alternate By similarity
Modified residue1331Phosphoserine Ref.12 Ref.14 Ref.15 Ref.17 Ref.19 Ref.20 Ref.23 Ref.26 Ref.30
Modified residue1471Phosphothreonine Ref.12 Ref.19 Ref.24
Modified residue1621Phosphoserine; by CK2 Ref.12 Ref.13 Ref.14 Ref.16 Ref.18 Ref.19 Ref.21 Ref.23 Ref.24 Ref.26 Ref.29 Ref.30

Natural variations

Alternative sequence11M → MRSGKASCTLETVWEDKHKY EEAERRFYEHEATQAAASAQ QLPAEGPAMNGPGQDDPEDA DEAEAPDGGSRRDPRKSQDS RKPLQKKRKRSPKSGLGPAD LALLGLSAERVWLDKSLFDQ AESSYRQKLADVAAQAAWPP ALAPWGLCTHGNQVACHHVT WGIWVNKSSFDQAERAFVEW SQALLLAPDGSRRQGTPNTG QQVAVPDLAHQPSPPVNGQP PLGSLQALVREVWLEKPRYD AAERGFYEALFDGHPPGKVR LQERAGLAEGARRGRRDRRG RNILGNKRAGLRRADGEAPS ALPYCYFLQKDAEAPWLSKP AYDSAECRHHAAEALRVAWC LEAASLSHRPGPRSGLSVSS LRPNRKM in isoform 2.
VSP_037884
Alternative sequence40 – 6324Missing in isoform 3.
VSP_043812
Alternative sequence78 – 9619Missing in isoform 4.
VSP_045960

Experimental info

Sequence conflict341A → R in CAA79716. Ref.1
Sequence conflict441S → T in CAA79716. Ref.1
Sequence conflict2091T → A in BAG56855. Ref.4
Isoform 2:
Sequence conflict1891D → E in AAP35906. Ref.3
Sequence conflict1891D → E in EAW82228. Ref.4
Sequence conflict1891D → E in AAH07847. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 5.
Checksum: CE778D6D5D09BD6C

FASTA28131,122
        10         20         30         40         50         60 
MATNFLAHEK IWFDKFKYDD AERRFYEQMN GPVAGASRQE NGASVILRDI ARARENIQKS 

        70         80         90        100        110        120 
LAGSSGPGAS SGTSGDHGEL VVRIASLEVE NQSLRGVVQE LQQAISKLEA RLNVLEKSSP 

       130        140        150        160        170        180 
GHRATAPQTQ HVSPMRQVEP PAKKPATPAE DDEDDDIDLF GSDNEEEDKE AAQLREERLR 

       190        200        210        220        230        240 
QYAEKKAKKP ALVAKSSILL DVKPWDDETD MAQLEACVRS IQLDGLVWGA SKLVPVGYGI 

       250        260        270        280 
RKLQIQCVVE DDKVGTDLLE EEITKFEEHV QSVDIAAFNK I 

« Hide

Isoform 2 (eEF1BdeltaL) [UniParc].

Checksum: A4CADBF40FCFCC09
Show »

FASTA64771,408
Isoform 3 [UniParc].

Checksum: E38BA673BE18FBE5
Show »

FASTA25728,558
Isoform 4 [UniParc].

Checksum: 7F9682E53B69BC17
Show »

FASTA26229,071

References

« Hide 'large scale' references
[1]"The human leucine zipper-containing guanine-nucleotide exchange protein elongation factor-1 delta."
Sanders J.P., Raggiaschi R., Morales J., Moeller W.
Biochim. Biophys. Acta 1174:87-90(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DOMAIN LEUCINE ZIPPER.
Tissue: Skin fibroblast.
[2]"Characterization of human colon cancer antigens recognized by autologous antibodies."
Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E., Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J.
Int. J. Cancer 76:652-658(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Colon carcinoma.
[3]"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 2).
[4]"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. expand/collapse author list , 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 4).
[5]"DNA sequence and analysis of human chromosome 8."
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. expand/collapse author list , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] (ISOFORMS 1; 2 AND 3).
Tissue: Brain, Lung and Muscle.
[9]Bienvenut W.V., Potts A., Barblan J., Quadroni M.
Submitted (JUL-2004) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-10 (ISOFORM 1), ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[10]"Elongation factor 1 delta is enhanced following exposure to ionizing radiation."
Jung M., Kondratyev A.D., Dritschilo A.
Cancer Res. 54:2541-2543(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY IONIZING RADIATION.
[11]"Induction of acute translational response genes by homocysteine. Elongation factors-1alpha, -beta, and -delta."
Chacko G., Ling Q., Hajjar K.A.
J. Biol. Chem. 273:19840-19846(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY HOMOCYSTEINE.
[12]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133; THR-147 AND SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Phosphoproteomic analysis of the human pituitary."
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.
Pituitary 9:109-120(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Pituitary.
[14]"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Prostate cancer.
[15]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[17]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[19]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133; THR-147 AND SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91 AND SER-94 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[22]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"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 THR-147 AND SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[25]"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-17; LYS-107 AND LYS-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"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-133 AND SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[27]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"Transformation of eEF1Bdelta into heat-shock response transcription factor by alternative splicing."
Kaitsuka T., Tomizawa K., Matsushita M.
EMBO Rep. 12:673-681(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION (ISOFORM 2), INTERACTION WITH HSF1 AND NFE2L2 (ISOFORM 2), TISSUE SPECIFICITY (ISOFORM 2), DNA-BINDING (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2).
[29]"Unbiased functional proteomics strategy for protein kinase inhibitor validation and identification of bona fide protein kinase substrates: application to identification of as a substrate for CK2."
Gyenis L., Duncan J.S., Turowec J.P., Bretner M., Litchfield D.W.
J. Proteome Res. 10:4887-4901(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-162 BY CK2.
[30]"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-133 AND SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[32]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z21507 mRNA. Translation: CAA79716.1.
BT007242 mRNA. Translation: AAP35906.1.
AK293339 mRNA. Translation: BAG56855.1.
AC067930 Genomic DNA. No translation available.
CH471162 Genomic DNA. Translation: EAW82227.1.
CH471162 Genomic DNA. Translation: EAW82228.1.
CH471162 Genomic DNA. Translation: EAW82229.1.
CH471162 Genomic DNA. Translation: EAW82230.1.
CH471162 Genomic DNA. Translation: EAW82232.1.
BC007847 mRNA. Translation: AAH07847.1.
BC009907 mRNA. Translation: AAH09907.1.
BC012819 mRNA. Translation: AAH12819.1.
BC062535 mRNA. Translation: AAH62535.1.
BC094806 mRNA. Translation: AAH94806.1.
CCDSCCDS47930.1. [P29692-3]
CCDS56559.1. [P29692-4]
CCDS6404.1. [P29692-2]
CCDS6405.1. [P29692-1]
PIRS34626.
RefSeqNP_001123525.2. NM_001130053.2.
NP_001123527.1. NM_001130055.2. [P29692-1]
NP_001123528.1. NM_001130056.2. [P29692-3]
NP_001123529.1. NM_001130057.2. [P29692-1]
NP_001182132.1. NM_001195203.1. [P29692-4]
NP_001276879.1. NM_001289950.1. [P29692-1]
NP_001951.2. NM_001960.4. [P29692-1]
NP_115754.3. NM_032378.4.
XP_005250880.1. XM_005250823.1. [P29692-2]
XP_005250881.1. XM_005250824.1. [P29692-2]
XP_005250883.1. XM_005250826.1. [P29692-3]
XP_006716584.1. XM_006716521.1. [P29692-2]
XP_006716585.1. XM_006716522.1. [P29692-2]
XP_006716586.1. XM_006716523.1. [P29692-2]
XP_006716587.1. XM_006716524.1. [P29692-2]
XP_006716588.1. XM_006716525.1. [P29692-1]
XP_006725131.1. XM_006725068.1. [P29692-2]
XP_006725132.1. XM_006725069.1. [P29692-2]
XP_006725133.1. XM_006725070.1. [P29692-2]
XP_006725134.1. XM_006725071.1. [P29692-2]
XP_006725135.1. XM_006725072.1. [P29692-2]
XP_006725136.1. XM_006725073.1. [P29692-2]
XP_006725138.1. XM_006725075.1. [P29692-1]
XP_006725139.1. XM_006725076.1. [P29692-3]
UniGeneHs.333388.
Hs.686554.
Hs.703306.

3D structure databases

ProteinModelPortalP29692.
SMRP29692. Positions 192-281.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108256. 69 interactions.
IntActP29692. 57 interactions.
MINTMINT-1139610.
STRING9606.ENSP00000391944.

PTM databases

PhosphoSiteP29692.

Polymorphism databases

DMDM20141357.

2D gel databases

OGPP29692.

Proteomic databases

MaxQBP29692.
PaxDbP29692.
PRIDEP29692.

Protocols and materials databases

DNASU1936.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000317198; ENSP00000317399; ENSG00000104529. [P29692-1]
ENST00000395119; ENSP00000378551; ENSG00000104529. [P29692-1]
ENST00000419152; ENSP00000388261; ENSG00000104529. [P29692-1]
ENST00000423316; ENSP00000410059; ENSG00000104529. [P29692-2]
ENST00000442189; ENSP00000391944; ENSG00000104529. [P29692-2]
ENST00000524624; ENSP00000435697; ENSG00000104529. [P29692-3]
ENST00000526838; ENSP00000436507; ENSG00000104529. [P29692-4]
ENST00000528610; ENSP00000431763; ENSG00000104529. [P29692-3]
ENST00000529272; ENSP00000434872; ENSG00000104529. [P29692-1]
GeneID1936.
KEGGhsa:1936.
UCSCuc003yyp.2. human. [P29692-2]
uc003yys.3. human. [P29692-1]
uc003yyv.3. human. [P29692-3]

Organism-specific databases

CTD1936.
GeneCardsGC08M144661.
H-InvDBHIX0034587.
HGNCHGNC:3211. EEF1D.
HPAHPA045101.
HPA051002.
MIM130592. gene.
neXtProtNX_P29692.
PharmGKBPA27647.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2092.
HOGENOMHOG000207272.
HOVERGENHBG000787.
InParanoidP29692.
KOK15410.
PhylomeDBP29692.
TreeFamTF313134.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP29692.
BgeeP29692.
CleanExHS_EEF1D.
GenevestigatorP29692.

Family and domain databases

Gene3D3.30.70.60. 1 hit.
InterProIPR018940. EF-1_beta_acid_region_euk.
IPR014717. Transl_elong_EF1B/ribosomal_S6.
IPR001326. Transl_elong_EF1B_B/D_CS.
IPR014038. Transl_elong_fac_EF1B_bsu/dsu.
[Graphical view]
PfamPF10587. EF-1_beta_acid. 1 hit.
PF00736. EF1_GNE. 1 hit.
[Graphical view]
SMARTSM00888. EF1_GNE. 1 hit.
[Graphical view]
SUPFAMSSF54984. SSF54984. 1 hit.
PROSITEPS00824. EF1BD_1. 1 hit.
PS00825. EF1BD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEEF1D. human.
GeneWikiEEF1D.
GenomeRNAi1936.
NextBio7841.
PROP29692.
SOURCESearch...

Entry information

Entry nameEF1D_HUMAN
AccessionPrimary (citable) accession number: P29692
Secondary accession number(s): B4DDU4 expand/collapse secondary AC list , D3DWK3, E9PBQ9, Q4VBZ6, Q969J1, Q96I38
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 156 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM