Eukaryotic translation initiation factor 1

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P41567 (EIF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 113. History...

Clusters with 100%, 90%, 50% identity |

Documents (6) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Eukaryotic translation initiation factor 1
Short name=eIF1

Alternative name(s):
A121
Protein translation factor SUI1 homolog
Sui1iso1

Gene names

Name:	EIF1
Synonyms:	SUI1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	113 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	Interacts with RENT2. Ref.5
Sequence similarities	Belongs to the SUI1 family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Coding sequence diversity	Polymorphism
Molecular function	Initiation factor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	regulation of translational initiation Traceable author statement Ref.3. Source: ProtInc response to stress Non-traceable author statement Ref.3. Source: UniProtKB
Cellular_component	cytoplasm Traceable author statement Ref.3. Source: ProtInc
Molecular_function	translation initiation factor activity Non-traceable author statement Ref.3. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.6

Chain

2 – 113

112

Eukaryotic translation initiation factor 1

PRO_0000130554

Amino acid modifications

Modified residue

N-acetylserine Ref.6 Ref.7

Modified residue

Phosphoserine Ref.7

Natural variations

Natural variant

L → P.
Corresponds to variant rs3390 [ dbSNP | Ensembl ].

VAR_052505

Natural variant

R → G.
Corresponds to variant rs3387 [ dbSNP | Ensembl ].

VAR_052506

Experimental info

Sequence conflict

I → V in AAD19900. Ref.3

Sequence conflict

A → P in AAD19900. Ref.3

Secondary structure

113

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P41567 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: A7BC7F9B53FFEB2C
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FASTA

113

12,732

        10         20         30         40         50         60 
MSAIQNLHSF DPFADASKGD DLLPAGTEDY IHIRIQQRNG RKTLTTVQGI ADDYDKKKLV 

        70         80         90        100        110 
KAFKKKFACN GTVIEHPEYG EVIQLQGDQR KNICQFLVEI GLAKDDQLKV HGF

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"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, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE. Tissue: Cervix carcinoma.
[7]	"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, MASS SPECTROMETRY.
[8]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00015077.

PIR

JC2042.

RefSeq

NP_005792.1. NM_005801.3.

UniGene

Hs.150580.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IF1	NMR	-	A	1-113	[»]

ProteinModelPortal

P41567.

ModBase

Search...

Protein-protein interaction databases

IntAct

P41567. 2 interactions.

MINT

MINT-1432975.

STRING

9606.ENSP00000419449.

PTM databases

PhosphoSite

P41567.

Polymorphism databases

DMDM

1174483.

Proteomic databases

PaxDb

P41567.

PeptideAtlas

P41567.

PRIDE

P41567.

Protocols and materials databases

DNASU

10209.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000469257; ENSP00000419449; ENSG00000173812.

GeneID

10209.

KEGG

hsa:10209.

UCSC

uc002hxj.3. human.

Organism-specific databases

CTD

10209.

GeneCards

GC17P039845.

HGNC

HGNC:3249. EIF1.

HPA

HPA043003.

neXtProt

NX_P41567.

PharmGKB

PA27683.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0023.

HOGENOM

HOG000279813.

HOVERGEN

HBG000295.

InParanoid

P41567.

K03113.

OMA

DANIPTT.

OrthoDB

EOG4XH01M.

PhylomeDB

P41567.

Gene expression databases

ArrayExpress

P41567.

Bgee

P41567.

CleanEx

HS_EIF1.

Genevestigator

P41567.

GermOnline

ENSG00000173812. Homo sapiens.

Family and domain databases

InterPro

IPR005874. SUI1_euk.
IPR001950. TIF_SUI1.
[Graphical view]

Pfam

PF01253. SUI1. 1 hit.
[Graphical view]

PIRSF

PIRSF004499. SUI1_euk. 1 hit.

SUPFAM

SSF55159. TIF_SUI1. 1 hit.

TIGRFAMs

TIGR01160. SUI1_MOF2. 1 hit.

PROSITE

PS50296. SUI1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P41567.

GenomeRNAi

10209.

NextBio

38652.

Entry information

Entry name

EIF1_HUMAN

Accession

Primary (citable) accession number: P41567
Secondary accession number(s): Q9UNQ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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

Translation initiation factors

List of translation initiation factor entries

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents