Tag | Content |
---|---|
UniProt Accession | EF1A1_HUMAN; P68104; |
Entrez ID | 1915 |
GenBank Protein ID | NM_001402.5; XM_011535514.2; |
GenBank Nucleotide ID | NP_001393.1; XP_011533816.1; |
Protein Name | 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) |
Gene Name | EEF1A1; EEF1A; EF1A; LENG7 |
Organism | Homo sapiens |
NCBI Taxa ID | 9606 |
Functional Description | This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. With PARP1 and TXK, forms a complex that acts as a T helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production. |
Sequence (Fasta) | MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL 60 DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV 120 GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP PYSQKRYEEI VKEVSTYIKK 180 IGYNPDTVAF VPISGWNGDN MLEPSANMPW FKGWKVTRKD GNASGTTLLE ALDCILPPTR 240 PTDKPLRLPL QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APVNVTTEVK SVEMHHEALS 300 EALPGDNVGF NVKNVSVKDV RRGNVAGDSK NDPPMEAAGF TAQVIILNHP GQISAGYAPV 360 LDCHTAHIAC KFAELKEKID RRSGKKLEDG PKFLKSGDAA IVDMVPGKPM CVESFSDYPP 420 LGRFAVRDMR QTVAVGVIKA VDKKAAGAGK VTKSAQKAQK AK 463 |
|
Database | Annotation |
---|---|
CTD (Curated) (count: 4) | MESH:D002277
; Carcinoma MESH:D015674 ; Mammary Neoplasms, Animal MESH:D008325 ; Mammary Neoplasms, Experimental MESH:D013274 ; Stomach Neoplasms |
DisGeNet (Curated) (count: 3) | C0024667; Animal Mammary Neoplasms
C0024668; Mammary Neoplasms, Experimental C0038356; Stomach Neoplasms |
GWASdb (count: 3) | rs11755449; Blood Pressure; hypertension
rs2073466; Hypertension; hypertension rs2073465; Blood Pressure; hypertension |
PTM | Modification Sites |
---|---|
Phosphorylation (count: 44) (view all) | 106 IKNMITGTSQADCAV dbPAF
128 GEFEAGISKNGQTRE dbPAF 133 GISKNGQTREHALLA dbPAF 141 REHALLAYTLGVKQL dbPAF 142 EHALLAYTLGVKQLI dbPAF 157 VGVNKMDSTEPPYSQ dbPAF |
Acetylation (count: 26) (view all) | 146 LAYTLGVKQLIVGVN PLMD
154 QLIVGVNKMDSTEPP PLMD 165 TEPPYSQKRYEEIVK PLMD 172 KRYEEIVKEVSTYIK PLMD 179 KEVSTYIKKIGYNPD PLMD 219 KGWKVTRKDGNASGT PLMD |
Ubiquitination (count: 34) (view all) | 129 EFEAGISKNGQTREH PLMD
146 LAYTLGVKQLIVGVN PLMD 154 QLIVGVNKMDSTEPP PLMD 165 TEPPYSQKRYEEIVK PLMD 172 KRYEEIVKEVSTYIK PLMD 179 KEVSTYIKKIGYNPD PLMD |
Sumoylation (count: 7) (view all) | 219 KGWKVTRKDGNASGT PLMD
255 LPLQDVYKIGGIGTV PLMD 273 RVETGVLKPGMVVTF PLMD 290 VNVTTEVKSVEMHHE PLMD 318 NVKNVSVKDVRRGNV PLMD 392 KKLEDGPKFLKSGDA PLMD |
Glycation (count: 1) | 129 EFEAGISKNGQTREH PLMD |
Malonylation (count: 11) (view all) | 172 KRYEEIVKEVSTYIK PLMD
179 KEVSTYIKKIGYNPD PLMD 180 EVSTYIKKIGYNPDT PLMD 244 PPTRPTDKPLRLPLQ PLMD 255 LPLQDVYKIGGIGTV PLMD 273 RVETGVLKPGMVVTF PLMD |
Methylation (count: 10) (view all) | 154 QLIVGVNKMDSTEPP PLMD
165 TEPPYSQKRYEEIVK PLMD 318 NVKNVSVKDVRRGNV PLMD 36 YKCGGIDKRTIEKFE PLMD 5 ***MGKEKTHINIVV PLMD 51 KEAAEMGKGSFKYAW PLMD |
Phosphoglycerylation (count: 1) | 330 GNVAGDSKNDPPMEA PLMD |
Succinylation (count: 9) (view all) | 172 KRYEEIVKEVSTYIK PLMD
179 KEVSTYIKKIGYNPD PLMD 255 LPLQDVYKIGGIGTV PLMD 273 RVETGVLKPGMVVTF PLMD 318 NVKNVSVKDVRRGNV PLMD 392 KKLEDGPKFLKSGDA PLMD |
Network | Interaction | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
A | B | Source | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
|