HUMAN:EF1A1

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	EEF1A1 (synonyms: EEF1A, EF1A, LENG7)
Protein Name(s)	Elongation factor 1-alpha 1 EF-1-alpha-1 Elongation factor Tu EF-Tu Eukaryotic elongation factor 1 A-1 eEF1A-1 Leukocyte receptor cluster member 7
External Links
UniProt	P68104
EMBL	X03558 J04617 X16869 AY043301 BC008587 BC009733 BC009875 BC010735 BC012891 BC014224 BC018150 BC018641 BC021686 BC028674 BC038339 BC057391 BC066893 BC071619 BC072385 BC082268 X03689 M29548
CCDS	CCDS4980.1
PIR	B24977
RefSeq	NP_001393.1
UniGene	Hs.535192 Hs.586423 Hs.745122
PDB	1SYW
PDBsum	1SYW
ProteinModelPortal	P68104
SMR	P68104
BioGrid	108237
IntAct	P68104
MINT	MINT-1180846
STRING	9606.ENSP00000330054
BindingDB	P68104
ChEMBL	CHEMBL1795120
PhosphoSite	P68104
DMDM	55584035
OGP	P68104
SWISS-2DPAGE	P68104
UCD-2DPAGE	P68104
MaxQB	P68104
PaxDb	P68104
PRIDE	P68104
DNASU	1915
Ensembl	ENST00000309268 ENST00000316292 ENST00000331523
GeneID	1915
KEGG	hsa:1915
UCSC	uc003phi.3
CTD	1915
GeneCards	GC06M074225
H-InvDB	HIX0020005 HIX0032108 HIX0033669 HIX0169110
HGNC	HGNC:3189
HPA	HPA051759 HPA053862 HPA056990
MIM	130590
neXtProt	NX_P68104
PharmGKB	PA27625
eggNOG	COG5256
HOGENOM	HOG000229291
HOVERGEN	HBG000179
InParanoid	P68104
KO	K03231
OMA	AIRDMGM
OrthoDB	EOG7NKKK3
PhylomeDB	P68104
TreeFam	TF300304
Reactome	REACT_1404 REACT_1477 REACT_200744
SignaLink	P68104
ChiTaRS	EEF1A1
GeneWiki	Eukaryotic_translation_elongation_factor_1_alpha_1
GenomeRNAi	1915
NextBio	7799
PMAP-CutDB	P68104
PRO	PR:P68104
Proteomes	UP000005640
Bgee	P68104
CleanEx	HS_EEF1A1
ExpressionAtlas	P68104
Genevestigator	P68104
GO	GO:0005737 GO:0005829 GO:0005853 GO:0005615 GO:0070062 GO:0016020 GO:0005730 GO:0005634 GO:0005886 GO:0005525 GO:0003924 GO:0044822 GO:0019901 GO:0003746 GO:0044267 GO:0071364 GO:0010467 GO:0006355 GO:0006351 GO:0006412 GO:0006414
Gene3D	3.40.50.300
HAMAP	MF_00118_A
InterPro	IPR000795 IPR027417 IPR009000 IPR009001 IPR004539 IPR004161 IPR004160
Pfam	PF00009 PF03144 PF03143
PRINTS	PR00315
SUPFAM	SSF50447 SSF50465 SSF52540
TIGRFAMs	TIGR00483
PROSITE	PS00301 PS51722

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
involved_in	GO:1900022	regulation of D-erythro-sphingosine kinase activity	PMID:18263879^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0019900	kinase binding	PMID:18263879^[1]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9NRA0 UniProtKB:Q9NYA1	F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:26497934^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0098574	cytoplasmic side of lysosomal membrane	PMID:20797626^[3]	ECO:0000303	author statement without traceable support used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1904714	regulation of chaperone-mediated autophagy	PMID:20797626^[3]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:19158340^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0030864	cortical actin cytoskeleton	PMID:19158340^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0032587	ruffle membrane	PMID:19158340^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:17980171^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:17177976^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:17177976^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0019901	protein kinase binding	PMID:17177976^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P42681	F		Seeded From UniProt	complete
enables	GO:0000049	tRNA binding	PMID:12426392^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:24209753^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:8743958^[9]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:1001608)	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:8743958^[9]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:1001608)	Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:19946888^[10]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19199708^[11]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001831)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19056867^[12]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001088)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:12519789^[13]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	produced_by:(CL:0000236)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[14]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000639)	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21630459^[15]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000019)	Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:23580065^[16]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001827)	Seeded From UniProt	complete
involved_in	GO:0071364	cellular response to epidermal growth factor stimulus	PMID:9852145^[17]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22681889^[18]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22658674^[19]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0019901	protein kinase binding	PMID:17595531^[20]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q96RG2	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:9852145^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P10126	C		Seeded From UniProt	complete
part_of	GO:0005730	nucleolus	PMID:9852145^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:9852145^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006414	translational elongation	PMID:21873635^[21]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1096317 PANTHER:PTN000562490 SGD:S000000322 dictyBase:DDB_G0269134 dictyBase:DDB_G0269136	P		Seeded From UniProt	complete
involved_in	GO:0006412	translation	PMID:21873635^[21]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000561878 dictyBase:DDB_G0269134 dictyBase:DDB_G0269136	P		Seeded From UniProt	complete
enables	GO:0003924	GTPase activity	PMID:21873635^[21]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000561878 SGD:S000001792 WB:WBGene00001168	F		Seeded From UniProt	complete
enables	GO:0003746	translation elongation factor activity	PMID:21873635^[21]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1096317 PANTHER:PTN000562490 SGD:S000000322 dictyBase:DDB_G0269134 dictyBase:DDB_G0269136	F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P10126 ensembl:ENSMUSP00000042457	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P10126 ensembl:ENSMUSP00000042457	C		Seeded From UniProt	complete
enables	GO:0005516	calmodulin binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P10126 ensembl:ENSMUSP00000042457	F		Seeded From UniProt	complete
enables	GO:0003746	translation elongation factor activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004539	F		Seeded From UniProt	complete
enables	GO:0003924	GTPase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000795	F		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000795 InterPro:IPR004161 InterPro:IPR004539	F		Seeded From UniProt	complete
involved_in	GO:0006414	translational elongation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004539	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:12426392^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
NOT\|part_of	GO:0005634	nucleus	PMID:12426392^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
NOT\|part_of	GO:0005634	nucleus	PMID:12426392^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:12426392^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006414	translational elongation	PMID:8812466^[22]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005853	eukaryotic translation elongation factor 1 complex	PMID:2564392^[23]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:3512269^[24]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	PMID:3512269^[24]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003746	translation elongation factor activity	PMID:17595531^[20]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:1904813	ficolin-1-rich granule lumen	Reactome:R-HSA-6800434	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0043312	neutrophil degranulation	Reactome:R-HSA-6798695	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0034774	secretory granule lumen	Reactome:R-HSA-6798748	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-8932413 Reactome:R-HSA-8931974 Reactome:R-HSA-156913	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	Reactome:R-HSA-6800434 Reactome:R-HSA-6798748	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006414	translational elongation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0251	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
enables	GO:0003746	translation elongation factor activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0251	F		Seeded From UniProt	complete
involved_in	GO:0006412	translation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0648	P		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0342	F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0039	C		Seeded From UniProt	complete
part_of	GO:0005730	nucleolus	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0188	C		Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Leclercq, TM et al. (2008) Eukaryotic elongation factor 1A interacts with sphingosine kinase and directly enhances its catalytic activity. J. Biol. Chem. 283 9606-14 PubMed GONUTS page
↑ Boratkó, A et al. (2015) Elongation factor-1A1 is a novel substrate of the protein phosphatase 1-TIMAP complex. Int. J. Biochem. Cell Biol. 69 105-13 PubMed GONUTS page
↑ ^3.0 ^3.1 Bandyopadhyay, U et al. (2010) Identification of regulators of chaperone-mediated autophagy. Mol. Cell 39 535-47 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Zhong, D et al. (2009) The SAM domain of the RhoGAP DLC1 binds EF1A1 to regulate cell migration. J. Cell. Sci. 122 414-24 PubMed GONUTS page
↑ Yang, YF et al. (2008) The possible interaction of CDA14 and protein elongation factor 1alpha. Biochim. Biophys. Acta 1784 312-8 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Maruyama, T et al. (2007) Txk, a member of the non-receptor tyrosine kinase of the Tec family, forms a complex with poly(ADP-ribose) polymerase 1 and elongation factor 1alpha and regulates interferon-gamma gene transcription in Th1 cells. Clin. Exp. Immunol. 147 164-75 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 ^7.4 Bohnsack, MT et al. (2002) Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm. EMBO J. 21 6205-15 PubMed GONUTS page
↑ Mingot, JM et al. (2013) eEF1A mediates the nuclear export of SNAG-containing proteins via the Exportin5-aminoacyl-tRNA complex. Cell Rep 5 727-37 PubMed GONUTS page
↑ ^9.0 ^9.1 Sanders, J et al. (1996) Immunofluorescence studies of human fibroblasts demonstrate the presence of the complex of elongation factor-1 beta gamma delta in the endoplasmic reticulum. J. Cell. Sci. 109 ( Pt 5) 1113-7 PubMed GONUTS page
↑ Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page
↑ Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page
↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
↑ Wubbolts, R et al. (2003) Proteomic and biochemical analyses of human B cell-derived exosomes. Potential implications for their function and multivesicular body formation. J. Biol. Chem. 278 10963-72 PubMed GONUTS page
↑ Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page
↑ de Mateo, S et al. (2011) Proteomic characterization of the human sperm nucleus. Proteomics 11 2714-26 PubMed GONUTS page
↑ Pieragostino, D et al. (2013) Shotgun proteomics reveals specific modulated protein patterns in tears of patients with primary open angle glaucoma naïve to therapy. Mol Biosyst 9 1108-16 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 ^17.3 Gangwani, L et al. (1998) Interaction of ZPR1 with translation elongation factor-1alpha in proliferating cells. J. Cell Biol. 143 1471-84 PubMed GONUTS page
↑ Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page
↑ Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page
↑ ^20.0 ^20.1 Eckhardt, K et al. (2007) Male germ cell expression of the PAS domain kinase PASKIN and its novel target eukaryotic translation elongation factor eEF1A1. Cell. Physiol. Biochem. 20 227-40 PubMed GONUTS page
↑ ^21.0 ^21.1 ^21.2 ^21.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Lund, A et al. (1996) Assignment of human elongation factor 1alpha genes: EEF1A maps to chromosome 6q14 and EEF1A2 to 20q13.3. Genomics 36 359-61 PubMed GONUTS page
↑ Uetsuki, T et al. (1989) Isolation and characterization of the human chromosomal gene for polypeptide chain elongation factor-1 alpha. J. Biol. Chem. 264 5791-8 PubMed GONUTS page
↑ ^24.0 ^24.1 Brands, JH et al. (1986) The primary structure of the alpha subunit of human elongation factor 1. Structural aspects of guanine-nucleotide-binding sites. Eur. J. Biochem. 155 167-71 PubMed GONUTS page

[PMID:18263879-1] 1.0 ^1.1 Leclercq, TM et al. (2008) Eukaryotic elongation factor 1A interacts with sphingosine kinase and directly enhances its catalytic activity. J. Biol. Chem. 283 9606-14 PubMed GONUTS page

[PMID:26497934-2] Boratkó, A et al. (2015) Elongation factor-1A1 is a novel substrate of the protein phosphatase 1-TIMAP complex. Int. J. Biochem. Cell Biol. 69 105-13 PubMed GONUTS page

[PMID:20797626-3] 3.0 ^3.1 Bandyopadhyay, U et al. (2010) Identification of regulators of chaperone-mediated autophagy. Mol. Cell 39 535-47 PubMed GONUTS page

[PMID:19158340-4] 4.0 ^4.1 ^4.2 Zhong, D et al. (2009) The SAM domain of the RhoGAP DLC1 binds EF1A1 to regulate cell migration. J. Cell. Sci. 122 414-24 PubMed GONUTS page

[PMID:17980171-5] Yang, YF et al. (2008) The possible interaction of CDA14 and protein elongation factor 1alpha. Biochim. Biophys. Acta 1784 312-8 PubMed GONUTS page

[PMID:17177976-6] 6.0 ^6.1 ^6.2 Maruyama, T et al. (2007) Txk, a member of the non-receptor tyrosine kinase of the Tec family, forms a complex with poly(ADP-ribose) polymerase 1 and elongation factor 1alpha and regulates interferon-gamma gene transcription in Th1 cells. Clin. Exp. Immunol. 147 164-75 PubMed GONUTS page

[PMID:12426392-7] 7.0 ^7.1 ^7.2 ^7.3 ^7.4 Bohnsack, MT et al. (2002) Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm. EMBO J. 21 6205-15 PubMed GONUTS page

[PMID:24209753-8] Mingot, JM et al. (2013) eEF1A mediates the nuclear export of SNAG-containing proteins via the Exportin5-aminoacyl-tRNA complex. Cell Rep 5 727-37 PubMed GONUTS page

[PMID:8743958-9] 9.0 ^9.1 Sanders, J et al. (1996) Immunofluorescence studies of human fibroblasts demonstrate the presence of the complex of elongation factor-1 beta gamma delta in the endoplasmic reticulum. J. Cell. Sci. 109 ( Pt 5) 1113-7 PubMed GONUTS page

[PMID:19946888-10] Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page

[PMID:19199708-11] Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page

[PMID:19056867-12] Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page

[PMID:12519789-13] Wubbolts, R et al. (2003) Proteomic and biochemical analyses of human B cell-derived exosomes. Potential implications for their function and multivesicular body formation. J. Biol. Chem. 278 10963-72 PubMed GONUTS page

[PMID:20458337-14] Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page

[PMID:21630459-15] Mateo, S et al. (2011) Proteomic characterization of the human sperm nucleus. Proteomics 11 2714-26 PubMed GONUTS page

[PMID:23580065-16] Pieragostino, D et al. (2013) Shotgun proteomics reveals specific modulated protein patterns in tears of patients with primary open angle glaucoma naïve to therapy. Mol Biosyst 9 1108-16 PubMed GONUTS page

[PMID:9852145-17] 17.0 ^17.1 ^17.2 ^17.3 Gangwani, L et al. (1998) Interaction of ZPR1 with translation elongation factor-1alpha in proliferating cells. J. Cell Biol. 143 1471-84 PubMed GONUTS page

[PMID:22681889-18] Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page

[PMID:22658674-19] Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page

[PMID:17595531-20] 20.0 ^20.1 Eckhardt, K et al. (2007) Male germ cell expression of the PAS domain kinase PASKIN and its novel target eukaryotic translation elongation factor eEF1A1. Cell. Physiol. Biochem. 20 227-40 PubMed GONUTS page

[PMID:21873635-21] 21.0 ^21.1 ^21.2 ^21.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:8812466-22] Lund, A et al. (1996) Assignment of human elongation factor 1alpha genes: EEF1A maps to chromosome 6q14 and EEF1A2 to 20q13.3. Genomics 36 359-61 PubMed GONUTS page

[PMID:2564392-23] Uetsuki, T et al. (1989) Isolation and characterization of the human chromosomal gene for polypeptide chain elongation factor-1 alpha. J. Biol. Chem. 264 5791-8 PubMed GONUTS page

[PMID:3512269-24] 24.0 ^24.1 Brands, JH et al. (1986) The primary structure of the alpha subunit of human elongation factor 1. Structural aspects of guanine-nucleotide-binding sites. Eur. J. Biochem. 155 167-71 PubMed GONUTS page

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