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Protein

Elongation factor 1-delta

Gene

EEF1D

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.
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).

GO - Molecular functioni

  1. activating transcription factor binding Source: UniProtKB
  2. DNA binding Source: UniProtKB
  3. heat shock protein binding Source: UniProtKB
  4. signal transducer activity Source: UniProtKB
  5. translation elongation factor activity Source: UniProtKB-KW
  6. translation factor activity, nucleic acid binding Source: ProtInc

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. cellular response to ionizing radiation Source: UniProtKB
  3. gene expression Source: Reactome
  4. mRNA transcription Source: UniProtKB
  5. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  6. regulation of cell death Source: UniProtKB
  7. regulation of transcription, DNA-templated Source: UniProtKB-KW
  8. signal transduction Source: GOC
  9. transcription, DNA-templated Source: UniProtKB-KW
  10. translation Source: Reactome
  11. translational elongation Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_1477. Eukaryotic Translation Elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor 1-delta
Short name:
EF-1-delta
Alternative name(s):
Antigen NY-CO-4
Gene namesi
Name:EEF1D
Synonyms:EF1D
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componentsi: Chromosome 8, Unplaced

Organism-specific databases

HGNCiHGNC:3211. EEF1D.

Subcellular locationi

Isoform 2 : Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. eukaryotic translation elongation factor 1 complex Source: ProtInc
  4. nucleolus Source: HPA
  5. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27647.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 281280Elongation factor 1-deltaPRO_0000155046Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei17 – 171N6-acetyllysine1 Publication
Modified residuei60 – 601Phosphoserine1 Publication
Modified residuei73 – 731Phosphothreonine1 Publication
Modified residuei107 – 1071N6-acetyllysine1 Publication
Modified residuei117 – 1171N6-acetyllysine; alternate1 Publication
Modified residuei117 – 1171N6-succinyllysine; alternateBy similarity
Modified residuei129 – 1291Phosphothreonine1 Publication
Modified residuei133 – 1331Phosphoserine10 Publications
Modified residuei147 – 1471Phosphothreonine3 Publications
Modified residuei162 – 1621Phosphoserine; by CK213 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP29692.
PaxDbiP29692.
PRIDEiP29692.

2D gel databases

OGPiP29692.

PTM databases

PhosphoSiteiP29692.

Expressioni

Tissue specificityi

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

Inductioni

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.2 Publications

Gene expression databases

BgeeiP29692.
CleanExiHS_EEF1D.
ExpressionAtlasiP29692. baseline and differential.
GenevestigatoriP29692.

Organism-specific databases

HPAiHPA045101.
HPA051002.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
ARHGAP21Q5T5U32EBI-358607,EBI-1642518
ATG7O953522EBI-358607,EBI-987834
CAMSAP2Q08AD12EBI-358607,EBI-1051869
EEF1GP266413EBI-358607,EBI-351467

Protein-protein interaction databases

BioGridi108256. 76 interactions.
IntActiP29692. 58 interactions.
MINTiMINT-1139610.
STRINGi9606.ENSP00000391944.

Structurei

3D structure databases

SMRiP29692. Positions 192-281.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni80 – 11536Leucine-zipperAdd
BLAST
Regioni173 – 281109Catalytic (GEF)Add
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG2092.
GeneTreeiENSGT00390000011747.
HOGENOMiHOG000207272.
HOVERGENiHBG000787.
InParanoidiP29692.
KOiK15410.
PhylomeDBiP29692.
TreeFamiTF313134.

Family and domain databases

Gene3Di3.30.70.60. 1 hit.
InterProiIPR018940. 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]
PfamiPF10587. EF-1_beta_acid. 1 hit.
PF00736. EF1_GNE. 1 hit.
[Graphical view]
SMARTiSM00888. EF1_GNE. 1 hit.
[Graphical view]
SUPFAMiSSF54984. SSF54984. 1 hit.
PROSITEiPS00824. EF1BD_1. 1 hit.
PS00825. EF1BD_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P29692-1) [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
MATNFLAHEK IWFDKFKYDD AERRFYEQMN GPVAGASRQE NGASVILRDI
60 70 80 90 100
ARARENIQKS LAGSSGPGAS SGTSGDHGEL VVRIASLEVE NQSLRGVVQE
110 120 130 140 150
LQQAISKLEA RLNVLEKSSP GHRATAPQTQ HVSPMRQVEP PAKKPATPAE
160 170 180 190 200
DDEDDDIDLF GSDNEEEDKE AAQLREERLR QYAEKKAKKP ALVAKSSILL
210 220 230 240 250
DVKPWDDETD MAQLEACVRS IQLDGLVWGA SKLVPVGYGI RKLQIQCVVE
260 270 280
DDKVGTDLLE EEITKFEEHV QSVDIAAFNK I
Length:281
Mass (Da):31,122
Last modified:January 22, 2007 - v5
Checksum:iCE778D6D5D09BD6C
GO
Isoform 2 (identifier: P29692-2) [UniParc]FASTAAdd to basket

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.Curated1 Publication

Show »
Length:647
Mass (Da):71,408
Checksum:iA4CADBF40FCFCC09
GO
Isoform 3 (identifier: P29692-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     40-63: Missing.

Note: Contains a phosphoserine at position 40.1 Publication

Show »
Length:257
Mass (Da):28,558
Checksum:iE38BA673BE18FBE5
GO
Isoform 4 (identifier: P29692-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     78-96: Missing.

Note: No experimental confirmation available.

Show »
Length:262
Mass (Da):29,071
Checksum:i7F9682E53B69BC17
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341A → R in CAA79716 (PubMed:8334168).Curated
Sequence conflicti44 – 441S → T in CAA79716 (PubMed:8334168).Curated
Sequence conflicti209 – 2091T → A in BAG56855 (PubMed:14702039).Curated
Isoform 2 (identifier: P29692-2)
Sequence conflicti189 – 1891D → E in AAP35906 (Ref. 3) Curated1 Publication
Sequence conflicti189 – 1891D → E in EAW82228 (PubMed:14702039).Curated1 Publication
Sequence conflicti189 – 1891D → E in AAH07847 (PubMed:16421571).Curated1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MRSGKASCTLETVWEDKHKY EEAERRFYEHEATQAAASAQ QLPAEGPAMNGPGQDDPEDA DEAEAPDGGSRRDPRKSQDS RKPLQKKRKRSPKSGLGPAD LALLGLSAERVWLDKSLFDQ AESSYRQKLADVAAQAAWPP ALAPWGLCTHGNQVACHHVT WGIWVNKSSFDQAERAFVEW SQALLLAPDGSRRQGTPNTG QQVAVPDLAHQPSPPVNGQP PLGSLQALVREVWLEKPRYD AAERGFYEALFDGHPPGKVR LQERAGLAEGARRGRRDRRG RNILGNKRAGLRRADGEAPS ALPYCYFLQKDAEAPWLSKP AYDSAECRHHAAEALRVAWC LEAASLSHRPGPRSGLSVSS LRPNRKM in isoform 2. 2 PublicationsVSP_037884
Alternative sequencei40 – 6324Missing in isoform 3. 1 PublicationVSP_043812Add
BLAST
Alternative sequencei78 – 9619Missing in isoform 4. 1 PublicationVSP_045960Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS47930.1. [P29692-3]
CCDS56559.1. [P29692-4]
CCDS6404.1. [P29692-2]
CCDS6405.1. [P29692-1]
PIRiS34626.
RefSeqiNP_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]
UniGeneiHs.333388.
Hs.686554.
Hs.703306.

Genome annotation databases

EnsembliENST00000317198; 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]
ENST00000614575; ENSP00000478340; ENSG00000273594. [P29692-3]
ENST00000615067; ENSP00000479653; ENSG00000273594. [P29692-1]
ENST00000615698; ENSP00000483527; ENSG00000273594. [P29692-1]
ENST00000619144; ENSP00000477608; ENSG00000273594. [P29692-2]
ENST00000620155; ENSP00000480505; ENSG00000273594. [P29692-2]
GeneIDi1936.
KEGGihsa:1936.
UCSCiuc003yyp.2. human. [P29692-2]
uc003yys.3. human. [P29692-1]
uc003yyv.3. human. [P29692-3]

Polymorphism databases

DMDMi20141357.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS47930.1. [P29692-3]
CCDS56559.1. [P29692-4]
CCDS6404.1. [P29692-2]
CCDS6405.1. [P29692-1]
PIRiS34626.
RefSeqiNP_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]
UniGeneiHs.333388.
Hs.686554.
Hs.703306.

3D structure databases

SMRiP29692. Positions 192-281.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108256. 76 interactions.
IntActiP29692. 58 interactions.
MINTiMINT-1139610.
STRINGi9606.ENSP00000391944.

PTM databases

PhosphoSiteiP29692.

Polymorphism databases

DMDMi20141357.

2D gel databases

OGPiP29692.

Proteomic databases

MaxQBiP29692.
PaxDbiP29692.
PRIDEiP29692.

Protocols and materials databases

DNASUi1936.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000317198; 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]
ENST00000614575; ENSP00000478340; ENSG00000273594. [P29692-3]
ENST00000615067; ENSP00000479653; ENSG00000273594. [P29692-1]
ENST00000615698; ENSP00000483527; ENSG00000273594. [P29692-1]
ENST00000619144; ENSP00000477608; ENSG00000273594. [P29692-2]
ENST00000620155; ENSP00000480505; ENSG00000273594. [P29692-2]
GeneIDi1936.
KEGGihsa:1936.
UCSCiuc003yyp.2. human. [P29692-2]
uc003yys.3. human. [P29692-1]
uc003yyv.3. human. [P29692-3]

Organism-specific databases

CTDi1936.
GeneCardsiGC08M144661.
H-InvDBHIX0034587.
HGNCiHGNC:3211. EEF1D.
HPAiHPA045101.
HPA051002.
MIMi130592. gene.
neXtProtiNX_P29692.
PharmGKBiPA27647.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2092.
GeneTreeiENSGT00390000011747.
HOGENOMiHOG000207272.
HOVERGENiHBG000787.
InParanoidiP29692.
KOiK15410.
PhylomeDBiP29692.
TreeFamiTF313134.

Enzyme and pathway databases

ReactomeiREACT_1477. Eukaryotic Translation Elongation.

Miscellaneous databases

ChiTaRSiEEF1D. human.
GeneWikiiEEF1D.
GenomeRNAii1936.
NextBioi7841.
PROiP29692.
SOURCEiSearch...

Gene expression databases

BgeeiP29692.
CleanExiHS_EEF1D.
ExpressionAtlasiP29692. baseline and differential.
GenevestigatoriP29692.

Family and domain databases

Gene3Di3.30.70.60. 1 hit.
InterProiIPR018940. 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]
PfamiPF10587. EF-1_beta_acid. 1 hit.
PF00736. EF1_GNE. 1 hit.
[Graphical view]
SMARTiSM00888. EF1_GNE. 1 hit.
[Graphical view]
SUPFAMiSSF54984. SSF54984. 1 hit.
PROSITEiPS00824. EF1BD_1. 1 hit.
PS00825. EF1BD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1992) [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(1997) [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 (APR-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.
    , 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(2003) [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.
    , 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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. 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(2003) [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 (JUN-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(1993) [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(1997) [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(2005) [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. 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(2006) [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(2006) [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(2006) [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(2007) [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(2007) [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(2007) [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. 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(2007) [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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. 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(2008) [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(2008) [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(2009) [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. 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(2010) [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(2010) [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(2010) [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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  32. "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(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; THR-73; THR-129; SER-133 AND SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiEF1D_HUMAN
AccessioniPrimary (citable) accession number: P29692
Secondary accession number(s): B4DDU4
, D3DWK3, E9PBQ9, Q4VBZ6, Q969J1, Q96I38
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 31, 1993
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 164 of the entry and version 5 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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: 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. 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.