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Protein Page:
EIF5 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
EIF5 eukaryotic translation initiation factor 5. Catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the release of eIF-2 and the guanine nucleotide. The subsequent joining of a 60S ribosomal subunit results in the formation of a functional 80S initiation complex. Note: This description may include information from UniProtKB.
Protein type: Translation initiation; Translation
Chromosomal Location of Human Ortholog: 14q32.32
Cellular Component: cytoplasm; cytosol; nucleus; plasma membrane
Molecular Function: GTPase activity; protein binding; translation factor activity, nucleic acid binding
Biological Process: regulation of translational initiation
Reference #:  P55010 (UniProtKB)
Alt. Names/Synonyms: eIF-5; EIF-5A; EIF5; Eukaryotic translation initiation factor 5; IF5
Gene Symbols: EIF5
Molecular weight: 49,223 Da
Basal Isoelectric point: 5.41  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

EIF5

Protein Structure Not Found.
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Sites Implicated In
cell cycle regulation: S389‑p, S390‑p
translation, altered: S389‑p, S390‑p
molecular association, regulation: S389‑p, S390‑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



 LTP 

LTP: 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.


 HTP 

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


       human

 
0 1 S2‑p ______MsVNVNRsV
0 2 S8‑p MsVNVNRsVsDQFyR
0 18 S10‑p VNVNRsVsDQFyRyK
0 1 Y14‑p RsVsDQFyRyKMPRL
0 1 Y16‑p VsDQFyRyKMPRLIA
0 2 K24‑ac KMPRLIAkVEGkGNG
0 2 K28‑ac LIAkVEGkGNGIkTV
0 3 K33‑ac EGkGNGIkTVIVNMV
0 17 K55‑ac RPPTYPTkYFGCELG
0 4 K55‑ub RPPTYPTkYFGCELG
0 1 K143 KLCTFILKNPPENsD
0 1 S149‑p LKNPPENsDsGTGKK
0 1 S151‑p NPPENsDsGTGKKEK
0 1 T153 PENsDsGTGKKEKEK
1 0 S174 DKENGSVSssETPPP
0 1 S175‑p KENGSVSssETPPPP
0 1 S176‑p ENGSVSssETPPPPP
1 0 T207‑p DDDWGEDttEEAQRR
1 0 T208‑p DDWGEDttEEAQRRR
0 1 S220‑p RRRMDEIsDHAKVLt
0 5 T227‑p sDHAKVLtLsDDLER
0 21 S229‑p HAKVLtLsDDLERTI
0 2 K288‑ub TEVLFNEkIREQIKK
0 2 Y362‑p SEKASKKyVSKELAK
3 90 S389‑p LKEAEEEssGGEEED
3 91 S390‑p KEAEEEssGGEEEDE
0 36 Y405‑p DENIEVVysKAAsVP
0 3 S406‑p ENIEVVysKAAsVPK
0 8 S410‑p VVysKAAsVPKVETV
0 17 S419‑p PKVETVKsDNKDDDI
  mouse

 
S2‑p ______MsVNVNRSV
S8 MsVNVNRSVsDQFYR
S10‑p VNVNRSVsDQFYRYK
Y14 RSVsDQFYRYKMPRL
Y16 VsDQFYRYKMPRLIA
K24 KMPRLIAKVEGkGNG
K28‑ac LIAKVEGkGNGIkTV
K33‑ac EGkGNGIkTVIVNMV
K55 RPPTYPTKYFGCELG
K55‑ub RPPTYPTkYFGCELG
K143‑ub KLCTFILkNPPENSD
S149 LkNPPENSDIGtGKK
I151 NPPENSDIGtGKKEK
T153‑p PENSDIGtGKKEKEK
S174 DKENGSVSTSETPPP
T175 KENGSVSTSETPPPP
S176 ENGSVSTSETPPPPP
T205 DDDWGEDTTEEAQRR
T206 DDWGEDTTEEAQRRR
S218‑p RRRMDEIsDHAKGLT
T225 sDHAKGLTLsDDLER
S227‑p HAKGLTLsDDLERTV
K286 TEVLFDEKIREQIKK
Y360‑p SEKASKKyVSKELAK
S387‑p LKEAEEEssGGEEED
S388‑p KEAEEEssGGEEEDE
Y403‑p DENIEVVysKTAsVP
S404‑p ENIEVVysKTAsVPK
S408‑p VVysKTAsVPKVETV
S417‑p PKVETVKsDNKDDDI
  rat

 
S2 ______MSVNVNRSV
S8 MSVNVNRSVsDQFYR
S10‑p VNVNRSVsDQFYRYK
Y14 RSVsDQFYRYKMPRL
Y16 VsDQFYRYKMPRLIA
K24‑ac KMPRLIAkVEGKGNG
K28 LIAkVEGKGNGIKTV
K33 EGKGNGIKTVIVNMV
K55 RPPTYPTKYFGCELG
K55 RPPTYPTKYFGCELG
K143 KLCTFILKNPPENSD
S149 LKNPPENSDIGTGKK
I151 NPPENSDIGTGKKEK
T153 PENSDIGTGKKEKEK
S174‑p DKENGSVsTSETPPP
T175 KENGSVsTSETPPPP
S176 ENGSVsTSETPPPPP
T205 DDDWGEDTTEEAQRR
T206 DDWGEDTTEEAQRRR
S218 RRRMDEISDHAKGLT
T225 SDHAKGLTLsDDLER
S227‑p HAKGLTLsDDLERTV
K286 TEVLFDEKIREQIKK
Y360 SEKASKKYVSKELAK
S387‑p LKEAEEEssGGEEED
S388‑p KEAEEEssGGEEEDE
Y403 DENIEVVYSKTASVP
S404 ENIEVVYSKTASVPK
S408 VVYSKTASVPKVETV
S417‑p PKVETVKsDNKDDDI
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