P68104

PTMD Annotation Information


※ Protein Information

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 DescriptionThis 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

※ PTM-Disease Association

NumPTMDiseaseCell TypeTypePTM SitePMID
1Serine PhosphorylationBreast cancer/tumor/carcinomaDS30020832312
[Reference]: Phosphorylation of eEF1A1 at Ser300 by T?R-I results in inhibition of mRNA translation.

※ Disease Cross-ref Annotation

DatabaseAnnotation
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 Sites

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

※ Protein-Protein Interaction

NetworkInteraction
ABSource