P29692 (EF1D_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Elongation factor 1-delta
Short name=EF-1-delta

Alternative name(s):
Antigen NY-CO-4

Gene names

Name:	EEF1D
Synonyms:	EF1D

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	281 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.27 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.27
Subunit structure	EF-1 is composed of 4 subunits: alpha, beta, delta isoform 1, and gamma. Isoform 2 interacts with HSF1 and NFE2L2. Ref.27
Subcellular location	Isoform 2: Nucleus Ref.27.
Tissue specificity	Isoform 2 is specifically expressed in brain, cerebellum and testis. Ref.27
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 process	Protein biosynthesis Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	DNA-binding
Molecular function	Elongation factor
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW translational elongation Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome eukaryotic translation elongation factor 1 complex Traceable author statement Ref.1. Source: ProtInc nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARHGAP21	Q5T5U3	2	EBI-358607,EBI-1642518
ATG7	O95352	2	EBI-358607,EBI-987834
CAMSAP2	Q08AD1	2	EBI-358607,EBI-1051869
EEF1G	P26641	3	EBI-358607,EBI-351467

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.9
	Chain	2 – 281	280	Elongation factor 1-delta		PRO_0000155046
Regions
	Region	80 – 115	36	Leucine-zipper
	Region	173 – 281	109	Catalytic (GEF)
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.9
	Modified residue	17	1	N6-acetyllysine Ref.24
	Modified residue	107	1	N6-acetyllysine Ref.24
	Modified residue	117	1	N6-acetyllysine Ref.24
	Modified residue	129	1	Phosphothreonine By similarity
	Modified residue	133	1	Phosphoserine Ref.12 Ref.14 Ref.15 Ref.17 Ref.19 Ref.20 Ref.22 Ref.25 Ref.29
	Modified residue	147	1	Phosphothreonine Ref.12 Ref.19 Ref.23
	Modified residue	162	1	Phosphoserine; by CK2 Ref.12 Ref.13 Ref.14 Ref.16 Ref.18 Ref.19 Ref.21 Ref.22 Ref.23 Ref.25 Ref.28 Ref.29
Natural variations
	Alternative sequence	1	1	M → 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 sequence	40 – 63	24	Missing in isoform 3.		VSP_043812
	Alternative sequence	78 – 96	19	Missing in isoform 4.		VSP_045960
Experimental info
	Sequence conflict	34	1	A → R in CAA79716. Ref.1
	Sequence conflict	44	1	S → T in CAA79716. Ref.1
	Sequence conflict	209	1	T → A in BAG56855. Ref.4
Isoform 2:
	Sequence conflict	189	1	D → E in AAP35906. Ref.3
	Sequence conflict	189	1	D → E in EAW82228. Ref.4
	Sequence conflict	189	1	D → E in AAH07847. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 5. Checksum: CE778D6D5D09BD6C	FASTA	281	31,122
	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
	Isoform 2 (eEF1BdeltaL) [UniParc]. Checksum: A4CADBF40FCFCC09	FASTA	647	71,408
	10 20 30 40 50 60 MRSGKASCTL ETVWEDKHKY EEAERRFYEH EATQAAASAQ QLPAEGPAMN GPGQDDPEDA 70 80 90 100 110 120 DEAEAPDGGS RRDPRKSQDS RKPLQKKRKR SPKSGLGPAD LALLGLSAER VWLDKSLFDQ 130 140 150 160 170 180 AESSYRQKLA DVAAQAAWPP ALAPWGLCTH GNQVACHHVT WGIWVNKSSF DQAERAFVEW 190 200 210 220 230 240 SQALLLAPDG SRRQGTPNTG QQVAVPDLAH QPSPPVNGQP PLGSLQALVR EVWLEKPRYD 250 260 270 280 290 300 AAERGFYEAL FDGHPPGKVR LQERAGLAEG ARRGRRDRRG RNILGNKRAG LRRADGEAPS 310 320 330 340 350 360 ALPYCYFLQK DAEAPWLSKP AYDSAECRHH AAEALRVAWC LEAASLSHRP GPRSGLSVSS 370 380 390 400 410 420 LRPNRKMATN FLAHEKIWFD KFKYDDAERR FYEQMNGPVA GASRQENGAS VILRDIARAR 430 440 450 460 470 480 ENIQKSLAGS SGPGASSGTS GDHGELVVRI ASLEVENQSL RGVVQELQQA ISKLEARLNV 490 500 510 520 530 540 LEKSSPGHRA TAPQTQHVSP MRQVEPPAKK PATPAEDDED DDIDLFGSDN EEEDKEAAQL 550 560 570 580 590 600 REERLRQYAE KKAKKPALVA KSSILLDVKP WDDETDMAQL EACVRSIQLD GLVWGASKLV 610 620 630 640 PVGYGIRKLQ IQCVVEDDKV GTDLLEEEIT KFEEHVQSVD IAAFNKI
	Isoform 3 [UniParc]. Checksum: E38BA673BE18FBE5	FASTA	257	28,558
	10 20 30 40 50 60 MATNFLAHEK IWFDKFKYDD AERRFYEQMN GPVAGASRQS SGPGASSGTS GDHGELVVRI 70 80 90 100 110 120 ASLEVENQSL RGVVQELQQA ISKLEARLNV LEKSSPGHRA TAPQTQHVSP MRQVEPPAKK 130 140 150 160 170 180 PATPAEDDED DDIDLFGSDN EEEDKEAAQL REERLRQYAE KKAKKPALVA KSSILLDVKP 190 200 210 220 230 240 WDDETDMAQL EACVRSIQLD GLVWGASKLV PVGYGIRKLQ IQCVVEDDKV GTDLLEEEIT 250 KFEEHVQSVD IAAFNKI
	Isoform 4 [UniParc]. Checksum: 7F9682E53B69BC17	FASTA	262	29,071
	10 20 30 40 50 60 MATNFLAHEK IWFDKFKYDD AERRFYEQMN GPVAGASRQE NGASVILRDI ARARENIQKS 70 80 90 100 110 120 LAGSSGPGAS SGTSGDHVVQ ELQQAISKLE ARLNVLEKSS PGHRATAPQT QHVSPMRQVE 130 140 150 160 170 180 PPAKKPATPA EDDEDDDIDL FGSDNEEEDK EAAQLREERL RQYAEKKAKK PALVAKSSIL 190 200 210 220 230 240 LDVKPWDDET DMAQLEACVR SIQLDGLVWG ASKLVPVGYG IRKLQIQCVV EDDKVGTDLL 250 260 EEEITKFEEH VQSVDIAAFN KI

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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), MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Liver.
[22]	"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, MASS SPECTROMETRY.
[23]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[24]	"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, MASS SPECTROMETRY.
[25]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[26]	"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].
[27]	"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).
[28]	"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.
[29]	"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, MASS SPECTROMETRY.
+	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.
IPI	IPI00023048. IPI00642971. IPI01013278.
PIR	S34626.
RefSeq	NP_001123525.2. NM_001130053.2. NP_001123527.1. NM_001130055.2. NP_001123528.1. NM_001130056.2. NP_001123529.1. NM_001130057.2. NP_001182132.1. NM_001195203.1. NP_001951.2. NM_001960.4. NP_115754.3. NM_032378.4.
UniGene	Hs.333388. Hs.686554. Hs.703306.
3D structure databases
ProteinModelPortal	P29692.
ModBase	Search...
Protein-protein interaction databases
IntAct	P29692. 55 interactions.
MINT	MINT-1139610.
STRING	9606.ENSP00000391944.
PTM databases
PhosphoSite	P29692.
Polymorphism databases
DMDM	20141357.
2D gel databases
OGP	P29692.
Proteomic databases
PaxDb	P29692.
PRIDE	P29692.
Protocols and materials databases
DNASU	1936.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000317198; ENSP00000317399; ENSG00000104529. ENST00000395119; ENSP00000378551; ENSG00000104529. ENST00000419152; ENSP00000388261; ENSG00000104529. ENST00000423316; ENSP00000410059; ENSG00000104529. ENST00000442189; ENSP00000391944; ENSG00000104529. ENST00000524624; ENSP00000435697; ENSG00000104529. ENST00000526838; ENSP00000436507; ENSG00000104529. ENST00000528610; ENSP00000431763; ENSG00000104529. ENST00000529272; ENSP00000434872; ENSG00000104529.
GeneID	1936.
KEGG	hsa:1936.
UCSC	uc003yyp.2. human. uc003yys.3. human.
Organism-specific databases
CTD	1936.
GeneCards	GC08M144661.
H-InvDB	HIX0034587.
HGNC	HGNC:3211. EEF1D.
HPA	HPA045101.
MIM	130592. gene.
neXtProt	NX_P29692.
PharmGKB	PA27647.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2092.
HOGENOM	HOG000207272.
HOVERGEN	HBG000787.
InParanoid	P29692.
KO	K15410.
OrthoDB	EOG4CJVGT.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	P29692.
Bgee	P29692.
CleanEx	HS_EEF1D.
Genevestigator	P29692.
GermOnline	ENSG00000104529. Homo sapiens.
Family and domain databases
Gene3D	3.30.70.60. 1 hit.
InterPro	IPR018940. 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]
Pfam	PF10587. EF-1_beta_acid. 1 hit. PF00736. EF1_GNE. 1 hit. [Graphical view]
SMART	SM00888. EF1_GNE. 1 hit. [Graphical view]
SUPFAM	SSF54984. Transl_elong_EF1B_B/D_G_exch. 1 hit.
PROSITE	PS00824. EF1BD_1. 1 hit. PS00825. EF1BD_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	EEF1D. human.
GenomeRNAi	1936.
NextBio	7841.
SOURCE	Search...

Entry information

Entry name

EF1D_HUMAN

Accession

Primary (citable) accession number: P29692
Secondary accession number(s): B4DDU4 , D3DWK3, E9PBQ9, Q4VBZ6, Q969J1, Q96I38

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 145 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.