Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q2VIR3 (IF2GL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative eukaryotic translation initiation factor 2 subunit 3-like protein
Alternative name(s):
Eukaryotic translation initiation factor 2 subunit gamma A
Short name=eIF-2-gamma A
Short name=eIF-2gA
Gene names
Name:EIF2S3L
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length472 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceUncertain

General annotation (Comments)

Function

eIF-2 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 By similarity.

Subunit structure

Heterotrimer composed of an alpha, a beta and a gamma chain By similarity.

Sequence similarities

Belongs to the GTP-binding elongation factor family. EIF2G subfamily.

Caution

Could be the product of a pseudogene. Evidence for transcription scarce. To the best of our knowledge, peptides that have been sequenced so far and that were identical to the canonical sequence displayed in this entry are common to both EIF2S3 and EIF2S3L and thus do not allow to discriminate both proteins. Protein sequence data have been included in EIF2S3 entry.

Sequence caution

The sequence ABB92405.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAA07331.1 differs from that shown. Reason: Frameshift at position 304.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Coding sequence diversityAlternative splicing
   LigandGTP-binding
Nucleotide-binding
   Molecular functionInitiation factor
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from electronic annotation. Source: InterPro

translation initiation factor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q2VIR3-1)

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.
Note: No experimental confirmation available.
Isoform 2 (identifier: Q2VIR3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     437-472: VGEKIALSRRVEKHWRLIGWGQIRRGVTIKPTVDDD → IHLIHLDLIKELEWGPLLTNETQRKSAANF
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 472471Putative eukaryotic translation initiation factor 2 subunit 3-like protein
PRO_0000343941

Regions

Nucleotide binding48 – 558GTP By similarity
Nucleotide binding134 – 1385GTP By similarity
Nucleotide binding190 – 1934GTP By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue161Phosphoserine By similarity

Natural variations

Alternative sequence437 – 47236VGEKI…TVDDD → IHLIHLDLIKELEWGPLLTN ETQRKSAANF in isoform 2.
VSP_034711

Experimental info

Sequence conflict2431I → F in ABB92405. Ref.1
Sequence conflict2581V → G in CAA07331. Ref.4
Sequence conflict2791A → T in CAA07331. Ref.4
Sequence conflict2921Q → H in CAA07331. Ref.4
Sequence conflict3001I → L in CAA07331. Ref.4
Sequence conflict3131S → P in ABB92405. Ref.1
Sequence conflict3131S → P in AAH87847. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 22, 2008. Version 2.
Checksum: 6ECFD47900903ED9

FASTA47251,229
        10         20         30         40         50         60 
MAGGEAGVTL GQPHLSRQDL TTLDVTKLTP LSHEVISRQA TINIGTIGHV AHGKSTVVKA 

        70         80         90        100        110        120 
ISGVHTVRFK NELERNITIK LGYANAKIYQ LDDPSCPRPE CYRSCGSSMP DEFPTDIPGT 

       130        140        150        160        170        180 
KGNFRLVRHV SFVDCPGHDI LMATMLNGAA VMDAALLLIA GNESCPQPQT SEHLAAIEIM 

       190        200        210        220        230        240 
KLKHILILQN KIDLVKERQA KEQYEQILAF VQGTVAEGAP IIPISAQLKY NIEVVCEYIV 

       250        260        270        280        290        300 
KKIPVPPRDF TSEPRLIVIR SFDVNKPGCE VDDLKGGVAG GSILKGVLKV GQETEVRPGI 

       310        320        330        340        350        360 
VSKDSEGKLM CKSIFSKIVS LFAEHNDLQY AAPGGLIGVG TKIDPTLCRA DRMVGQILGA 

       370        380        390        400        410        420 
VGALPEIFTE LEISYFLLRR LLGVRTEGDK KAAKVQKLSK NEVLMVNIGS LSTGGRVSAV 

       430        440        450        460        470 
KADLGKIVLT NPVCTEVGEK IALSRRVEKH WRLIGWGQIR RGVTIKPTVD DD 

« Hide

Isoform 2 [UniParc].

Checksum: 8B418E91C29E7045
Show »

FASTA46650,544

References

« Hide 'large scale' references
[1]"Emergence of young human genes after a burst of retroposition in primates."
Marques A.C., Dupanloup I., Vinckenbosch N., Reymond A., Kaessmann H.
PLoS Biol. 3:E357-E357(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], EVOLUTIONARY ANALYSIS.
[2]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., 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. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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] OF 2-471 (ISOFORM 2).
Tissue: Testis.
[4]"Characterization of genes encoding translation initiation factor eIF-2gamma in mouse and human: sex chromosome localization, escape from X-inactivation and evolution."
Ehrmann I.E., Ellis P.S., Mazeyrat S., Duthie S., Brockdorff N., Mattei M.-G., Gavin M.A., Affara N.A., Brown G.M., Simpson E., Mitchell M.J., Scott D.M.
Hum. Mol. Genet. 7:1725-1737(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 61-309.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ120619 Genomic DNA. Translation: ABB92405.1. Sequence problems.
AC068775 Genomic DNA. No translation available.
BC087847 mRNA. Translation: AAH87847.1.
AJ006932 Genomic DNA. Translation: CAA07331.1. Frameshift.
UniGeneHs.539684.

3D structure databases

ProteinModelPortalQ2VIR3.
SMRQ2VIR3. Positions 37-460.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ2VIR3. 2 interactions.
STRING9606.ENSP00000323063.

PTM databases

PhosphoSiteQ2VIR3.

Polymorphism databases

DMDM205830883.

Proteomic databases

MaxQBQ2VIR3.
PaxDbQ2VIR3.
PRIDEQ2VIR3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GeneCardsGC12P010558.
H-InvDBHIX0036834.
HPACAB012471.
neXtProtNX_Q2VIR3.

Phylogenomic databases

eggNOGCOG5257.
HOGENOMHOG000229292.
HOVERGENHBG006123.
InParanoidQ2VIR3.
OMATEQHEAI.
PhylomeDBQ2VIR3.

Gene expression databases

BgeeQ2VIR3.
GenevestigatorQ2VIR3.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR000795. EF_GTP-bd_dom.
IPR027417. P-loop_NTPase.
IPR015256. TIF2_gsu_C.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004161. Transl_elong_EFTu/EF1A_2.
[Graphical view]
PfamPF09173. eIF2_C. 1 hit.
PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSPR00315. ELONGATNFCT.
SUPFAMSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNetSearch...

Entry information

Entry nameIF2GL_HUMAN
AccessionPrimary (citable) accession number: Q2VIR3
Secondary accession number(s): Q5I0X0, Q6KF84
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: July 22, 2008
Last modified: May 14, 2014
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Translation initiation factors

List of translation initiation factor entries

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM