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Protein Page:
eIF2-alpha (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
eIF2-alpha a translation initiation factor that functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40s ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B. Phosphorylated by at least 4 kinases: PERK, GCN2, HRI and PKR. Phosphorylation stabilizes the eIF-2/GDP/eIF-2B complex and prevents GDP/GTP exchange reaction, thus impairing the recycling of eIF-2 between successive rounds of initiation and leading to global inhibition of translation. Upregulated in some thyroid cancers and bronchiolo-alveolar adenocarcinomas; aberrant phosphorylation correlates with Alzheimer disease and Epstein-Barr virus infections. Note: This description may include information from UniProtKB.
Protein type: Translation initiation; Translation
Chromosomal Location of Human Ortholog: 14q23.3
Cellular Component: eukaryotic translation initiation factor 2B complex; polysome; membrane; stress granule; cytosol; nucleus; eukaryotic translation initiation factor 2 complex
Molecular Function: protein binding; translation initiation factor activity; ribosome binding
Biological Process: regulation of translation initiation in response to stress; cellular protein metabolic process; unfolded protein response, activation of signaling protein activity; translation; unfolded protein response; protein amino acid autophosphorylation; translational initiation; gene expression
Reference #:  P05198 (UniProtKB)
Alt. Names/Synonyms: EIF-2; eIF-2-alpha; eIF-2A; eIF-2alpha; EIF2; EIF2A; EIF2S1; Eukaryotic translation initiation factor 2 subunit 1; Eukaryotic translation initiation factor 2 subunit alpha; eukaryotic translation initiation factor 2, subunit 1 alpha, 35kDa; IF2A
Gene Symbols: EIF2S1
Molecular weight: 36,112 Da
Basal Isoelectric point: 5.02  Predict pI for various phosphorylation states
CST Pathways:  Translation: eIF2  |  Translational Control
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

eIF2-alpha

Protein Structure Not Found.


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Sites Implicated In
apoptosis, induced: S52‑p
apoptosis, inhibited: S52‑p
cell growth, altered: S52‑p
translation, altered: S49‑p, S52‑p
activity, induced: S52‑p
activity, inhibited: S52‑p
molecular association, regulation: S49‑p, S52‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 S26-p VVMVNVRsIAEMGAY
4 1 S49-p IEGMILLsELsRRRI
67 3 S52-p MILLsELsRRRIRsI
0 1 R54 LLsELsRRRIRsINk
0 1 R55 LsELsRRRIRsINkL
0 1 S58-p LsRRRIRsINkLIRI
0 2 K61-ub RRIRsINkLIRIGRN
0 61 Y82-p RVDKEKGyIDLSkRR
0 1 K87-ub KGyIDLSkRRVSPEE
0 2 K101-ac EAIKCEDkFTkSkTV
0 1 K101 EAIKCEDKFTkSkTV
0 7 K104-ub KCEDkFTkSkTVYSI
0 3 K106-ub EDkFTkSkTVYSILR
0 1 K123 AEVLEYTKDEQLESL
0 2 K123-ub AEVLEYTkDEQLESL
0 2 K141-ac TAWVFDDkYkRPGyG
0 4 K141-ub TAWVFDDkYkRPGyG
0 4 K143-ub WVFDDkYkRPGyGAy
0 13 Y147-p DkYkRPGyGAyDAFk
0 87 Y150-p kRPGyGAyDAFkHAV
0 1 K154-ub yGAyDAFkHAVsDPS
0 2 S158-p DAFkHAVsDPSILDS
0 1 S165 sDPSILDSLDLNEDE
0 4 T185-p NNINRRLtPQAVkIR
0 1 K190-ub RLtPQAVkIRADIEV
0 3 Y200-p ADIEVACyGyEGIDA
0 12 Y202-p IEVACyGyEGIDAVK
0 1 S219-p LRAGLNCsTENMPIK
0 1 Y235-p NLIAPPRyVMTTTTL
0 1 T245-p TTTTLERtEGLSVLS
0 2 K259-ub SQAMAVIkEKIEEKR
0 1 K276-ub FNVQMEPkVVtDtDE
0 21 T279-p QMEPkVVtDtDEtEL
0 2 T281-p EPkVVtDtDEtELAR
0 1 T284-p VVtDtDEtELARQME
3398 : Phospho-eIF2alpha (Ser51) (D9G8) XP(R) Rabbit mAb
3597 : Phospho-eIF2alpha (Ser51) (119A11) Rabbit mAb
5199 : Phospho-eIF2 alpha (Ser51) (D9G8) XP(R) Rabbit mAb (Biotinylated)
9721 : Phospho-eIF2alpha (Ser51) Antibody
  mouse

 
S26 VVMVNVRSIAEMGAY
S49 IEGMILLSELsRrrI
S52-p MILLSELsRrrIRSI
R54-m1 LLSELsRrrIRSINK
R55-m1 LSELsRrrIRSINKL
S58 LsRrrIRSINKLIRI
K61 rrIRSINKLIRIGRN
Y82-p RVDKEKGyIDLSKRR
K87 KGyIDLSKRRVSPEE
K101 EAIKCEDKFTkSkTV
K101-ub EAIKCEDkFTkSkTV
K104-ub KCEDkFTkSkTVYSI
K106-ub EDkFTkSkTVYSILR
K123-ac AEVLEYTkDEQLESL
K123 AEVLEYTKDEQLESL
K141-ac TAWVFDDkYKRPGyG
K141-ub TAWVFDDkYKRPGyG
K143 WVFDDkYKRPGyGAy
Y147-p DkYKRPGyGAyDAFK
Y150-p KRPGyGAyDAFKHAV
K154 yGAyDAFKHAVsDPS
S158-p DAFKHAVsDPSILDs
S165-p sDPSILDsLDLNEDE
T185-p NNINRRLtPQAVKIR
K190 RLtPQAVKIRADIEV
Y200 ADIEVACYGYEGIDA
Y202 IEVACYGYEGIDAVK
S219 LRAGLNCSTETMPIK
Y235 NLIAPPRYVMTTTTL
T245 TTTTLERTEGLSVLN
K259-ub NQAMAVIkEKIEEKR
K276 FNVQMEPKVVtDTDE
T279-p QMEPKVVtDTDETEL
T281 EPKVVtDTDETELAR
T284 VVtDTDETELARQLE
3398 : Phospho-eIF2alpha (Ser51) (D9G8) XP(R) Rabbit mAb
3597 : Phospho-eIF2alpha (Ser51) (119A11) Rabbit mAb
5199 : Phospho-eIF2 alpha (Ser51) (D9G8) XP(R) Rabbit mAb (Biotinylated)
9721 : Phospho-eIF2alpha (Ser51) Antibody
  rat

 
S26 VVMVNVRSIAEMGAY
S49 IEGMILLSELsRRRI
S52-p MILLSELsRRRIRSI
R54 LLSELsRRRIRSINK
R55 LSELsRRRIRSINKL
S58 LsRRRIRSINKLIRI
K61 RRIRSINKLIRIGRN
Y82 RVDKEKGYIDLSKRR
K87 KGYIDLSKRRVSPEE
K101 EAIKCEDKFTKSKTV
K101 EAIKCEDKFTKSKTV
K104 KCEDKFTKSKTVYSI
K106 EDKFTKSKTVYSILR
K123 AEVLEYTKDEQLESL
K123 AEVLEYTKDEQLESL
K141-ac TAWVFDDkYKRPGYG
K141 TAWVFDDKYKRPGYG
K143 WVFDDkYKRPGYGAY
Y147 DkYKRPGYGAYDAFK
Y150 KRPGYGAYDAFKHAV
K154 YGAYDAFKHAVSDPS
S158 DAFKHAVSDPSILDS
S165 SDPSILDSLDLNEDE
T185 NNINRRLTPQAVKIR
K190 RLTPQAVKIRADIEV
Y200 ADIEVACYGYEGIDA
Y202 IEVACYGYEGIDAVK
S219 LRAGLNCSTETMPIK
Y235 NLIAPPRYVMTTTTL
T245 TTTTLERTEGLSVLN
K259 NQAMAVIKEKIEEKR
K276 FNVQMEPKVVTDTDE
T279 QMEPKVVTDTDETEL
T281 EPKVVTDTDETELAR
T284 VVTDTDETELARQLE
3398 : Phospho-eIF2alpha (Ser51) (D9G8) XP(R) Rabbit mAb
3597 : Phospho-eIF2alpha (Ser51) (119A11) Rabbit mAb
5199 : Phospho-eIF2 alpha (Ser51) (D9G8) XP(R) Rabbit mAb (Biotinylated)
9721 : Phospho-eIF2alpha (Ser51) Antibody
  rabbit

 
S25 VVMVNVRSIAEMGAY
S48-p IEGRILLsELsR___
S51-p RILLsELsR______
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
3398 : Phospho-eIF2alpha (Ser51) (D9G8) XP(R) Rabbit mAb
5199 : Phospho-eIF2 alpha (Ser51) (D9G8) XP(R) Rabbit mAb (Biotinylated)
  fruit fly

 
S25 VVMVNVLSIAEMGAY
S48 IEGMILLSELSRRRI
S51 MILLSELSRRRIRSI
R53 LLSELSRRRIRSINK
R54 LSELSRRRIRSINKL
S57 LSRRRIRSINKLIRV
K60 RRIRSINKLIRVGKT
Y81 RVDKEKGYIDLSKRR
K86 KGYIDLSKRRVSPED
R100 DVEKCTERFAKAKAI
R100 DVEKCTERFAKAKAI
K103 KCTERFAKAKAINSL
K105 TERFAKAKAINSLLR
K125 LGFEGNEKLEDLYQK
K125 LGFEGNEKLEDLYQK
K140 TAWHFEKKYNNKTVA
K140 TAWHFEKKYNNKTVA
N142 WHFEKKYNNKTVAYD
T145 EKKYNNKTVAYDIFK
Y148 YNNKTVAYDIFKQSV
K152 TVAYDIFKQSVTDPT
T156 DIFKQSVTDPTVFDE
E163 TDPTVFDECNLEPET
V183 SNIKRKLVSPTVKIR
K188 KLVSPTVKIRADIEC
Y198 ADIECSCYGYEGIDA
Y200 IECSCYGYEGIDAVK
S217 LTKGLELSTEELPIR
Y233 NLIAPPLYVMTTSTT
T243 TTSTTKKTDGLKALE
R257 EVAIEHIRAKTSEYD
K274 FKVIMAPKLVTAIDE
T277 IMAPKLVTAIDEADL
I279 APKLVTAIDEADLAR
A282 LVTAIDEADLARRLE
3398 : Phospho-eIF2alpha (Ser51) (D9G8) XP(R) Rabbit mAb
3597 : Phospho-eIF2alpha (Ser51) (119A11) Rabbit mAb
5199 : Phospho-eIF2 alpha (Ser51) (D9G8) XP(R) Rabbit mAb (Biotinylated)
9721 : Phospho-eIF2alpha (Ser51) Antibody
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