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Q2VIR3

- IF2GL_HUMAN

UniProt

Q2VIR3 - IF2GL_HUMAN

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Protein

Putative eukaryotic translation initiation factor 2 subunit 3-like protein

Gene

EIF2S3L

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 3 out of 5- Protein uncertaini

Functioni

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).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi48 – 558GTPBy similarity
Nucleotide bindingi134 – 1385GTPBy similarity
Nucleotide bindingi190 – 1934GTPBy similarity

GO - Molecular functioni

  1. GTPase activity Source: InterPro
  2. GTP binding Source: UniProtKB-KW
  3. translation initiation factor activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:EIF2S3L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Unplaced

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 472471Putative eukaryotic translation initiation factor 2 subunit 3-like proteinPRO_0000343941Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei16 – 161PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ2VIR3.
PaxDbiQ2VIR3.
PRIDEiQ2VIR3.

PTM databases

PhosphoSiteiQ2VIR3.

Expressioni

Gene expression databases

BgeeiQ2VIR3.
ExpressionAtlasiQ2VIR3. baseline.
GenevestigatoriQ2VIR3.

Organism-specific databases

HPAiCAB012471.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiQ2VIR3. 2 interactions.
STRINGi9606.ENSP00000323063.

Structurei

3D structure databases

ProteinModelPortaliQ2VIR3.
SMRiQ2VIR3. Positions 37-460.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 248210tr-type GPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 558G1PROSITE-ProRule annotation
Regioni76 – 805G2PROSITE-ProRule annotation
Regioni134 – 1374G3PROSITE-ProRule annotation
Regioni190 – 1934G4PROSITE-ProRule annotation
Regioni225 – 2273G5PROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EIF2G subfamily.PROSITE-ProRule annotation
Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5257.
GeneTreeiENSGT00550000074801.
HOGENOMiHOG000229292.
HOVERGENiHBG006123.
InParanoidiQ2VIR3.
OMAiTEQHEAI.
PhylomeDBiQ2VIR3.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR000795. 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]
PfamiPF09173. eIF2_C. 1 hit.
PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51722. G_TR_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q2VIR3-1) [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
MAGGEAGVTL GQPHLSRQDL TTLDVTKLTP LSHEVISRQA TINIGTIGHV
60 70 80 90 100
AHGKSTVVKA ISGVHTVRFK NELERNITIK LGYANAKIYQ LDDPSCPRPE
110 120 130 140 150
CYRSCGSSMP DEFPTDIPGT KGNFRLVRHV SFVDCPGHDI LMATMLNGAA
160 170 180 190 200
VMDAALLLIA GNESCPQPQT SEHLAAIEIM KLKHILILQN KIDLVKERQA
210 220 230 240 250
KEQYEQILAF VQGTVAEGAP IIPISAQLKY NIEVVCEYIV KKIPVPPRDF
260 270 280 290 300
TSEPRLIVIR SFDVNKPGCE VDDLKGGVAG GSILKGVLKV GQETEVRPGI
310 320 330 340 350
VSKDSEGKLM CKSIFSKIVS LFAEHNDLQY AAPGGLIGVG TKIDPTLCRA
360 370 380 390 400
DRMVGQILGA VGALPEIFTE LEISYFLLRR LLGVRTEGDK KAAKVQKLSK
410 420 430 440 450
NEVLMVNIGS LSTGGRVSAV KADLGKIVLT NPVCTEVGEK IALSRRVEKH
460 470
WRLIGWGQIR RGVTIKPTVD DD

Note: No experimental confirmation available.

Length:472
Mass (Da):51,229
Last modified:July 22, 2008 - v2
Checksum:i6ECFD47900903ED9
GO
Isoform 2 (identifier: Q2VIR3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     437-472: VGEKIALSRRVEKHWRLIGWGQIRRGVTIKPTVDDD → IHLIHLDLIKELEWGPLLTNETQRKSAANF

Note: No experimental confirmation available.

Show »
Length:466
Mass (Da):50,544
Checksum:i8B418E91C29E7045
GO

Sequence cautioni

The sequence CAA07331.1 differs from that shown. Reason: Frameshift at position 304.
The sequence ABB92405.1 differs from that shown. Reason: Erroneous gene model prediction.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti243 – 2431I → F in ABB92405. (PubMed:16201836)Curated
Sequence conflicti258 – 2581V → G in CAA07331. (PubMed:9736774)Curated
Sequence conflicti279 – 2791A → T in CAA07331. (PubMed:9736774)Curated
Sequence conflicti292 – 2921Q → H in CAA07331. (PubMed:9736774)Curated
Sequence conflicti300 – 3001I → L in CAA07331. (PubMed:9736774)Curated
Sequence conflicti313 – 3131S → P in ABB92405. (PubMed:16201836)Curated
Sequence conflicti313 – 3131S → P in AAH87847. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei437 – 47236VGEKI…TVDDD → IHLIHLDLIKELEWGPLLTN ETQRKSAANF in isoform 2. 1 PublicationVSP_034711Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
UniGeneiHs.539684.

Polymorphism databases

DMDMi205830883.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
UniGenei Hs.539684.

3D structure databases

ProteinModelPortali Q2VIR3.
SMRi Q2VIR3. Positions 37-460.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q2VIR3. 2 interactions.
STRINGi 9606.ENSP00000323063.

PTM databases

PhosphoSitei Q2VIR3.

Polymorphism databases

DMDMi 205830883.

Proteomic databases

MaxQBi Q2VIR3.
PaxDbi Q2VIR3.
PRIDEi Q2VIR3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

GeneCardsi GC12P010659.
H-InvDB HIX0036834.
HPAi CAB012471.
neXtProti NX_Q2VIR3.

Phylogenomic databases

eggNOGi COG5257.
GeneTreei ENSGT00550000074801.
HOGENOMi HOG000229292.
HOVERGENi HBG006123.
InParanoidi Q2VIR3.
OMAi TEQHEAI.
PhylomeDBi Q2VIR3.

Gene expression databases

Bgeei Q2VIR3.
ExpressionAtlasi Q2VIR3. baseline.
Genevestigatori Q2VIR3.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR000795. 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 ]
Pfami PF09173. eIF2_C. 1 hit.
PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view ]
PRINTSi PR00315. ELONGATNFCT.
SUPFAMi SSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEi PS51722. G_TR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiIF2GL_HUMAN
AccessioniPrimary (citable) accession number: Q2VIR3
Secondary accession number(s): Q5I0X0, Q6KF84
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: July 22, 2008
Last modified: October 29, 2014
This is version 73 of the entry and version 2 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Translation initiation factors
    List of translation initiation factor entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3