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Protein

Eukaryotic translation initiation factor 2A

Gene

EIF2A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions in the early steps of protein synthesis of a small number of specific mRNAs. Acts by directing the binding of methionyl-tRNAi to 40S ribosomal subunits. In contrast to the eIF-2 complex, it binds methionyl-tRNAi to 40 S subunits in a codon-dependent manner, whereas the eIF-2 complex binds methionyl-tRNAi to 40 S subunits in a GTP-dependent manner. May act by impiging the expression of specific proteins.1 Publication

GO - Molecular functioni

  • ribosome binding Source: UniProtKB
  • translation initiation factor activity Source: UniProtKB
  • tRNA binding Source: UniProtKB

GO - Biological processi

  • positive regulation of signal transduction Source: Ensembl
  • protein phosphorylation Source: Ensembl
  • regulation of translation Source: UniProtKB
  • ribosome assembly Source: UniProtKB
  • SREBP signaling pathway Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis, Translation regulation

Enzyme and pathway databases

SIGNORiQ9BY44.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 2A
Short name:
eIF-2A
Alternative name(s):
65 kDa eukaryotic translation initiation factor 2A
Cleaved into the following chain:
Gene namesi
Name:EIF2A
ORF Names:CDA02, MSTP004, MSTP089
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:3254. EIF2A.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • eukaryotic translation initiation factor 2 complex Source: UniProtKB
  • extracellular space Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA143485453.

Polymorphism and mutation databases

BioMutaiEIF2A.
DMDMi209572747.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 585585Eukaryotic translation initiation factor 2APRO_0000424466Add
BLAST
Initiator methionineiRemoved; alternate1 Publication
Chaini2 – 585584Eukaryotic translation initiation factor 2A, N-terminally processedPRO_0000286076Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei2 – 21N-acetylalanine; in Eukaryotic translation initiation factor 2A, N-terminally processed1 Publication
Modified residuei5 – 51PhosphothreonineCombined sources
Modified residuei503 – 5031PhosphoserineCombined sources
Modified residuei506 – 5061PhosphoserineCombined sources
Modified residuei517 – 5171PhosphoserineCombined sources
Modified residuei518 – 5181PhosphothreonineCombined sources
Modified residuei526 – 5261PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9BY44.
MaxQBiQ9BY44.
PaxDbiQ9BY44.
PeptideAtlasiQ9BY44.
PRIDEiQ9BY44.

PTM databases

iPTMnetiQ9BY44.
PhosphoSiteiQ9BY44.
SwissPalmiQ9BY44.

Expressioni

Tissue specificityi

Widely expressed. Expressed at higher level in pancreas, heart, brain and placenta.1 Publication

Gene expression databases

BgeeiQ9BY44.
CleanExiHS_EIF2A.
ExpressionAtlasiQ9BY44. baseline and differential.
GenevisibleiQ9BY44. HS.

Organism-specific databases

HPAiHPA036256.

Interactioni

Protein-protein interaction databases

BioGridi123822. 49 interactions.
DIPiDIP-40272N.
IntActiQ9BY44. 8 interactions.
MINTiMINT-3063792.
STRINGi9606.ENSP00000417229.

Structurei

3D structure databases

ProteinModelPortaliQ9BY44.
SMRiQ9BY44. Positions 11-415.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati56 – 10045WD 1Add
BLAST
Repeati101 – 15959WD 2Add
BLAST
Repeati160 – 21051WD 3Add
BLAST
Repeati211 – 26454WD 4Add
BLAST
Repeati265 – 30642WD 5Add
BLAST
Repeati307 – 34842WD 6Add
BLAST
Repeati349 – 39143WD 7Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili531 – 58252Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the WD repeat EIF2A family.Curated
Contains 7 WD repeats.Curated

Keywords - Domaini

Coiled coil, Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG2315. Eukaryota.
COG5354. LUCA.
GeneTreeiENSGT00730000111053.
HOGENOMiHOG000193775.
HOVERGENiHBG107842.
InParanoidiQ9BY44.
KOiK15026.
OMAiPIYDVAW.
OrthoDBiEOG7GBFX2.
PhylomeDBiQ9BY44.
TreeFamiTF105866.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR011387. TIF2A.
IPR013979. TIF_beta_prop-like.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF08662. eIF2A. 1 hit.
[Graphical view]
PIRSFiPIRSF017222. eIF2A. 1 hit.
SUPFAMiSSF50978. SSF50978. 2 hits.

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BY44-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAPSTPLLTV RGSEGLYMVN GPPHFTESTV FPRESGKNCK VCIFSKDGTL
60 70 80 90 100
FAWGNGEKVN IISVTNKGLL HSFDLLKAVC LEFSPKNTVL ATWQPYTTSK
110 120 130 140 150
DGTAGIPNLQ LYDVKTGTCL KSFIQKKMQN WCPSWSEDET LCARNVNNEV
160 170 180 190 200
HFFENNNFNT IANKLHLQKI NDFVLSPGPQ PYKVAVYVPG SKGAPSFVRL
210 220 230 240 250
YQYPNFAGPH AALANKSFFK ADKVTMLWNK KATAVLVIAS TDVDKTGASY
260 270 280 290 300
YGEQTLHYIA TNGESAVVQL PKNGPIYDVV WNSSSTEFCA VYGFMPAKAT
310 320 330 340 350
IFNLKCDPVF DFGTGPRNAA YYSPHGHILV LAGFGNLRGQ MEVWDVKNYK
360 370 380 390 400
LISKPVASDS TYFAWCPDGE HILTATCAPR LRVNNGYKIW HYTGSILHKY
410 420 430 440 450
DVPSNAELWQ VSWQPFLDGI FPAKTITYQA VPSEVPNEEP KVATAYRPPA
460 470 480 490 500
LRNKPITNSK LHEEEPPQNM KPQSGNDKPL SKTALKNQRK HEAKKAAKQE
510 520 530 540 550
ARSDKSPDLA PTPAPQSTPR NTVSQSISGD PEIDKKIKNL KKKLKAIEQL
560 570 580
KEQAATGKQL EKNQLEKIQK ETALLQELED LELGI
Length:585
Mass (Da):64,990
Last modified:October 14, 2008 - v3
Checksum:i63D63C0676F232C9
GO
Isoform 2 (identifier: Q9BY44-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-213: Missing.
     214-219: ANKSFF → MFQEV

Note: No experimental confirmation available.
Show »
Length:371
Mass (Da):41,339
Checksum:i0D4454F18732DBD2
GO
Isoform 3 (identifier: Q9BY44-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     34-58: Missing.

Note: No experimental confirmation available.
Show »
Length:560
Mass (Da):62,289
Checksum:iAE5E408990B0CC21
GO
Isoform 4 (identifier: Q9BY44-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     98-158: Missing.

Note: No experimental confirmation available.
Show »
Length:524
Mass (Da):57,994
Checksum:iE6F35813714656EF
GO

Sequence cautioni

The sequence AAK14926.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAM83402.1 differs from that shown. Reason: Frameshift at positions 82 and 90. Curated
The sequence AAQ13506.1 differs from that shown. Reason: Frameshift at position 513. Curated
The sequence AAQ13612.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71L → F in AAQ13612 (Ref. 4) Curated
Sequence conflicti14 – 163EGL → LRT in AAQ13612 (Ref. 4) Curated
Sequence conflicti54 – 541G → A in AAM83402 (PubMed:12133843).Curated
Sequence conflicti55 – 551N → I in AAM83402 (PubMed:12133843).Curated
Sequence conflicti84 – 841S → P in BAB55058 (PubMed:14702039).Curated
Sequence conflicti150 – 1501V → A in AAQ13612 (Ref. 4) Curated
Sequence conflicti173 – 1731F → S in AAQ13612 (Ref. 4) Curated
Sequence conflicti261 – 2611T → P in AAM83402 (PubMed:12133843).Curated
Sequence conflicti263 – 2631G → F in AAM83402 (PubMed:12133843).Curated
Sequence conflicti268 – 2681V → L in AAM83402 (PubMed:12133843).Curated
Sequence conflicti292 – 2921Y → S in AAM83402 (PubMed:12133843).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti97 – 971T → S.5 Publications
Corresponds to variant rs1132979 [ dbSNP | Ensembl ].
VAR_032066
Natural varianti582 – 5821E → K.1 Publication
Corresponds to variant rs17850813 [ dbSNP | Ensembl ].
VAR_032067

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 213213Missing in isoform 2. 1 PublicationVSP_024975Add
BLAST
Alternative sequencei34 – 5825Missing in isoform 3. 1 PublicationVSP_056047Add
BLAST
Alternative sequencei98 – 15861Missing in isoform 4. 1 PublicationVSP_056048Add
BLAST
Alternative sequencei214 – 2196ANKSFF → MFQEV in isoform 2. 1 PublicationVSP_024976

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF497978 mRNA. Translation: AAM83402.1. Frameshift.
AK027356 mRNA. Translation: BAB55058.1.
AK298586 mRNA. Translation: BAG60776.1.
AK293993 mRNA. Translation: BAG57357.1.
AF212241 mRNA. Translation: AAK14926.1. Different initiation.
AF109358 mRNA. Translation: AAQ13506.1. Frameshift.
AF172818 mRNA. Translation: AAQ13612.1. Different initiation.
AC107426 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78830.1.
CH471052 Genomic DNA. Translation: EAW78831.1.
BC011885 mRNA. Translation: AAH11885.1.
CCDSiCCDS46935.1. [Q9BY44-1]
RefSeqiNP_001305972.1. NM_001319043.1. [Q9BY44-3]
NP_001305973.1. NM_001319044.1. [Q9BY44-4]
NP_001305974.1. NM_001319045.1.
NP_001305975.1. NM_001319046.1. [Q9BY44-2]
NP_114414.2. NM_032025.4. [Q9BY44-1]
UniGeneiHs.655782.

Genome annotation databases

EnsembliENST00000406576; ENSP00000385292; ENSG00000144895. [Q9BY44-4]
ENST00000460851; ENSP00000417229; ENSG00000144895. [Q9BY44-1]
ENST00000487799; ENSP00000420537; ENSG00000144895. [Q9BY44-3]
GeneIDi83939.
KEGGihsa:83939.
UCSCiuc003eya.4. human. [Q9BY44-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF497978 mRNA. Translation: AAM83402.1. Frameshift.
AK027356 mRNA. Translation: BAB55058.1.
AK298586 mRNA. Translation: BAG60776.1.
AK293993 mRNA. Translation: BAG57357.1.
AF212241 mRNA. Translation: AAK14926.1. Different initiation.
AF109358 mRNA. Translation: AAQ13506.1. Frameshift.
AF172818 mRNA. Translation: AAQ13612.1. Different initiation.
AC107426 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78830.1.
CH471052 Genomic DNA. Translation: EAW78831.1.
BC011885 mRNA. Translation: AAH11885.1.
CCDSiCCDS46935.1. [Q9BY44-1]
RefSeqiNP_001305972.1. NM_001319043.1. [Q9BY44-3]
NP_001305973.1. NM_001319044.1. [Q9BY44-4]
NP_001305974.1. NM_001319045.1.
NP_001305975.1. NM_001319046.1. [Q9BY44-2]
NP_114414.2. NM_032025.4. [Q9BY44-1]
UniGeneiHs.655782.

3D structure databases

ProteinModelPortaliQ9BY44.
SMRiQ9BY44. Positions 11-415.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123822. 49 interactions.
DIPiDIP-40272N.
IntActiQ9BY44. 8 interactions.
MINTiMINT-3063792.
STRINGi9606.ENSP00000417229.

PTM databases

iPTMnetiQ9BY44.
PhosphoSiteiQ9BY44.
SwissPalmiQ9BY44.

Polymorphism and mutation databases

BioMutaiEIF2A.
DMDMi209572747.

Proteomic databases

EPDiQ9BY44.
MaxQBiQ9BY44.
PaxDbiQ9BY44.
PeptideAtlasiQ9BY44.
PRIDEiQ9BY44.

Protocols and materials databases

DNASUi83939.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000406576; ENSP00000385292; ENSG00000144895. [Q9BY44-4]
ENST00000460851; ENSP00000417229; ENSG00000144895. [Q9BY44-1]
ENST00000487799; ENSP00000420537; ENSG00000144895. [Q9BY44-3]
GeneIDi83939.
KEGGihsa:83939.
UCSCiuc003eya.4. human. [Q9BY44-1]

Organism-specific databases

CTDi83939.
GeneCardsiEIF2A.
H-InvDBHIX0200477.
HGNCiHGNC:3254. EIF2A.
HPAiHPA036256.
MIMi609234. gene.
neXtProtiNX_Q9BY44.
PharmGKBiPA143485453.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2315. Eukaryota.
COG5354. LUCA.
GeneTreeiENSGT00730000111053.
HOGENOMiHOG000193775.
HOVERGENiHBG107842.
InParanoidiQ9BY44.
KOiK15026.
OMAiPIYDVAW.
OrthoDBiEOG7GBFX2.
PhylomeDBiQ9BY44.
TreeFamiTF105866.

Enzyme and pathway databases

SIGNORiQ9BY44.

Miscellaneous databases

GeneWikiiEIF2A.
GenomeRNAii83939.
PROiQ9BY44.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BY44.
CleanExiHS_EIF2A.
ExpressionAtlasiQ9BY44. baseline and differential.
GenevisibleiQ9BY44. HS.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR011387. TIF2A.
IPR013979. TIF_beta_prop-like.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF08662. eIF2A. 1 hit.
[Graphical view]
PIRSFiPIRSF017222. eIF2A. 1 hit.
SUPFAMiSSF50978. SSF50978. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of mammalian eIF2A and identification of the yeast homolog."
    Zoll W.L., Horton L.E., Komar A.A., Hensold J.O., Merrick W.C.
    J. Biol. Chem. 277:37079-37087(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, VARIANT SER-97.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4), VARIANT SER-97.
    Tissue: Cerebellum and Embryo.
  3. "A novel gene expressed in human pheochromocytoma."
    Li Y., Huang Q., Peng Y., Song H., Yu Y., Xu S., Ren S., Chen Z., Han Z.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT SER-97.
    Tissue: Pheochromocytoma.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-585 (ISOFORM 1), VARIANT SER-97.
    Tissue: Aorta and Heart.
  5. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-97.
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LYS-582.
    Tissue: Lymph.
  8. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-11; 184-192 AND 506-520, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506; SER-517 AND THR-518, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503 AND THR-518, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5; SER-506 AND SER-526, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiEIF2A_HUMAN
AccessioniPrimary (citable) accession number: Q9BY44
Secondary accession number(s): A8MPS6
, B4DF96, B4DQ14, D3DNI9, Q5QTR2, Q7Z4E9, Q8NFM1, Q96EW9, Q96K81
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: October 14, 2008
Last modified: July 6, 2016
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

Was initially thought to constitute the ortholog of prokaryotic IF-2 (infB) protein.Curated

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.