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Protein

Eukaryotic translation initiation factor 1

Gene

EIF1

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

Functioni

Necessary for scanning and involved in initiation site selection. Promotes the assembly of 48S ribosomal complexes at the authentic initiation codon of a conventional capped mRNA.

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. translation factor activity, nucleic acid binding Source: ProtInc
  3. translation initiation factor activity Source: UniProtKB

GO - Biological processi

  1. dosage compensation by inactivation of X chromosome Source: Ensembl
  2. regulation of translational initiation Source: ProtInc
  3. response to stress Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 1
Short name:
eIF1
Alternative name(s):
A121
Protein translation factor SUI1 homolog
Sui1iso1
Gene namesi
Name:EIF1
Synonyms:SUI1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:3249. EIF1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27683.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 113112Eukaryotic translation initiation factor 1PRO_0000130554Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine3 Publications
Modified residuei9 – 91Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP41567.
PaxDbiP41567.
PeptideAtlasiP41567.
PRIDEiP41567.

PTM databases

PhosphoSiteiP41567.

Expressioni

Gene expression databases

BgeeiP41567.
CleanExiHS_EIF1.
ExpressionAtlasiP41567. baseline and differential.
GenevestigatoriP41567.

Organism-specific databases

HPAiHPA043003.

Interactioni

Subunit structurei

Interacts with RENT2.1 Publication

Protein-protein interaction databases

BioGridi115504. 5 interactions.
DIPiDIP-50783N.
IntActiP41567. 5 interactions.
MINTiMINT-1432975.
STRINGi9606.ENSP00000419449.

Structurei

Secondary structure

1
113
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi38 – 414Combined sources
Beta strandi46 – 494Combined sources
Helixi56 – 605Combined sources
Helixi63 – 664Combined sources
Beta strandi71 – 744Combined sources
Turni77 – 793Combined sources
Beta strandi80 – 878Combined sources
Helixi90 – 10011Combined sources
Turni105 – 1073Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IF1NMR-A1-113[»]
4KZXX-ray7.81l1-113[»]
4KZYX-ray7.01l1-113[»]
ProteinModelPortaliP41567.
SMRiP41567. Positions 1-113.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41567.

Family & Domainsi

Sequence similaritiesi

Belongs to the SUI1 family.Curated

Phylogenomic databases

eggNOGiCOG0023.
HOGENOMiHOG000279813.
HOVERGENiHBG000295.
InParanoidiP41567.
KOiK03113.
PhylomeDBiP41567.
TreeFamiTF314417.

Family and domain databases

Gene3Di3.30.780.10. 1 hit.
InterProiIPR005874. SUI1_euk.
IPR001950. TIF_SUI1.
[Graphical view]
PfamiPF01253. SUI1. 1 hit.
[Graphical view]
PIRSFiPIRSF004499. SUI1_euk. 1 hit.
SUPFAMiSSF55159. SSF55159. 1 hit.
TIGRFAMsiTIGR01160. SUI1_MOF2. 1 hit.
PROSITEiPS50296. SUI1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P41567-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSAIQNLHSF DPFADASKGD DLLPAGTEDY IHIRIQQRNG RKTLTTVQGI
60 70 80 90 100
ADDYDKKKLV KAFKKKFACN GTVIEHPEYG EVIQLQGDQR KNICQFLVEI
110
GLAKDDQLKV HGF
Length:113
Mass (Da):12,732
Last modified:November 1, 1995 - v1
Checksum:iA7BC7F9B53FFEB2C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311I → V in AAD19900. (PubMed:10347211)Curated
Sequence conflicti62 – 621A → P in AAD19900. (PubMed:10347211)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti59 – 591L → P.
Corresponds to variant rs3390 [ dbSNP | Ensembl ].
VAR_052505
Natural varianti90 – 901R → G.
Corresponds to variant rs3387 [ dbSNP | Ensembl ].
VAR_052506

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26247 mRNA. Translation: AAA60602.1.
AF083441 mRNA. Translation: AAD52028.1.
AF100737 mRNA. Translation: AAD19900.1.
BC005118 mRNA. Translation: AAH05118.1.
BC008710 mRNA. Translation: AAH08710.1.
CCDSiCCDS11403.1.
PIRiJC2042.
RefSeqiNP_005792.1. NM_005801.3.
UniGeneiHs.150580.

Genome annotation databases

EnsembliENST00000469257; ENSP00000419449; ENSG00000173812.
GeneIDi10209.
KEGGihsa:10209.
UCSCiuc002hxj.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26247 mRNA. Translation: AAA60602.1.
AF083441 mRNA. Translation: AAD52028.1.
AF100737 mRNA. Translation: AAD19900.1.
BC005118 mRNA. Translation: AAH05118.1.
BC008710 mRNA. Translation: AAH08710.1.
CCDSiCCDS11403.1.
PIRiJC2042.
RefSeqiNP_005792.1. NM_005801.3.
UniGeneiHs.150580.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IF1NMR-A1-113[»]
4KZXX-ray7.81l1-113[»]
4KZYX-ray7.01l1-113[»]
ProteinModelPortaliP41567.
SMRiP41567. Positions 1-113.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115504. 5 interactions.
DIPiDIP-50783N.
IntActiP41567. 5 interactions.
MINTiMINT-1432975.
STRINGi9606.ENSP00000419449.

PTM databases

PhosphoSiteiP41567.

Proteomic databases

MaxQBiP41567.
PaxDbiP41567.
PeptideAtlasiP41567.
PRIDEiP41567.

Protocols and materials databases

DNASUi10209.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000469257; ENSP00000419449; ENSG00000173812.
GeneIDi10209.
KEGGihsa:10209.
UCSCiuc002hxj.3. human.

Organism-specific databases

CTDi10209.
GeneCardsiGC17P039845.
HGNCiHGNC:3249. EIF1.
HPAiHPA043003.
neXtProtiNX_P41567.
PharmGKBiPA27683.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0023.
HOGENOMiHOG000279813.
HOVERGENiHBG000295.
InParanoidiP41567.
KOiK03113.
PhylomeDBiP41567.
TreeFamiTF314417.

Miscellaneous databases

EvolutionaryTraceiP41567.
GeneWikiiEIF1.
GenomeRNAii10209.
NextBioi38652.
PROiP41567.

Gene expression databases

BgeeiP41567.
CleanExiHS_EIF1.
ExpressionAtlasiP41567. baseline and differential.
GenevestigatoriP41567.

Family and domain databases

Gene3Di3.30.780.10. 1 hit.
InterProiIPR005874. SUI1_euk.
IPR001950. TIF_SUI1.
[Graphical view]
PfamiPF01253. SUI1. 1 hit.
[Graphical view]
PIRSFiPIRSF004499. SUI1_euk. 1 hit.
SUPFAMiSSF55159. SSF55159. 1 hit.
TIGRFAMsiTIGR01160. SUI1_MOF2. 1 hit.
PROSITEiPS50296. SUI1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Expressed sequence tags identify a human isolog of the suil translation initiation factor."
    Fields C.A., Adams M.D.
    Biochem. Biophys. Res. Commun. 198:288-291(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Okadaic acid-responsive genes in malignant glioma cells identified by mRNA differential display."
    Singh S.K., Murray S.F., Chin L.S.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "Cloning and characterization of a human genotoxic and endoplasmic reticulum stress-inducible cDNA that encodes translation initiation factor 1 (eIF1(A121/SUI1))."
    Sheikh M.S., Fernandez-Salas E., Yu M., Hussain A., Dinman J.D., Peltz S.W., Huang Y., Fornace A.J. Jr.
    J. Biol. Chem. 274:16487-16493(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "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].
    Tissue: Eye and Lung.
  5. "Novel Upf2p orthologues suggest a functional link between translation initiation and nonsense surveillance complexes."
    Mendell J.T., Medghalchi S.M., Lake R.G., Noensie E.N., Dietz H.C.
    Mol. Cell. Biol. 20:8944-8957(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RENT2.
  6. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  7. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Structure and interactions of the translation initiation factor eIF1."
    Fletcher C.M., Pestova T.V., Hellen C.U., Wagner G.
    EMBO J. 18:2631-2637(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiEIF1_HUMAN
AccessioniPrimary (citable) accession number: P41567
Secondary accession number(s): Q9UNQ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 7, 2015
This is version 128 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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. Translation initiation factors
    List of translation initiation factor entries
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.