P10081 (IF4A_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP-dependent RNA helicase eIF4A
EC=3.6.4.13

Alternative name(s):
Eukaryotic initiation factor 4A
Short name=eIF-4A
Stimulator factor I 37 kDa component
Translation initiation factor 1/2
p37

Gene names

Name:	TIF1
Synonyms:	TIF41A
Ordered Locus Names:	YKR059W
AND
Name:	TIF2
Synonyms:	TIF41B
Ordered Locus Names:	YJL138C
ORF Names:	J0660

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	395 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	ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon. Ref.10 Ref.11 Ref.13 Ref.15 Ref.16 Ref.17
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	Component of the eIF4F complex, which composition varies with external and internal environmental conditions. It is composed of at least eIF4A (TIF1/TIF2), eIF4E (TIF45) and eIF4G (TIF4631 or TIF4632) By similarity. Interacts with eIF4G1/TIF4631 and eIF4G2/TIF4632. Ref.15 Ref.16
Subcellular location	Cytoplasm Ref.18.
Domain	The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis. Ref.17
Miscellaneous	TIF1 and TIF2 code for the same protein. Present with 106000 molecules/cell in log phase SD medium. Ref.19
Sequence similarities	Belongs to the DEAD box helicase family. eIF4A subfamily. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain.
Biophysicochemical properties	Kinetic parameters: KM=470 µM for ATP Ref.13 Ref.17 Vmax=2.6 pmol/sec/µg enzyme for ATP pH dependence: Optimum pH is 6.0.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Helicase Hydrolase Initiation factor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	eukaryotic translation initiation factor 4F complex Inferred from genetic interaction Ref.15Ref.2. Source: SGD plasma membrane enriched fraction Inferred from direct assay. Source: SGD ribosome Traceable author statement. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent RNA helicase activity Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct translation initiation factor activity Inferred from direct assay Ref.13. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TIF4631	P39935	8	EBI-9017,EBI-9002

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 395

394

ATP-dependent RNA helicase eIF4A

PRO_0000054968

Regions

Domain

53 – 222

170

Helicase ATP-binding

Domain

233 – 394

162

Helicase C-terminal

Nucleotide binding

66 – 73

8

ATP

Motif

22 – 50

29

Q motif

Motif

170 – 173

4

DEAD box

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.14

Modified residue

2

1

Phosphoserine Ref.20

Modified residue

128

1

Phosphothreonine Ref.22

Modified residue

129

1

Phosphoserine Ref.22

Modified residue

146

1

Phosphothreonine Ref.21 Ref.22

Experimental info

Mutagenesis

24

1

F → A: Lethal in vivo and reduces ATP binding and ATPase activity in vitro. Ref.17

Mutagenesis

42

1

F → A: Slow growth in vivo and reduces ATP binding and ATPase activity in vitro. Ref.17

Mutagenesis

46

1

S → A: Reduces ATP binding and ATPase activity in vitro. Ref.17

Mutagenesis

49

1

Q → A: Reduces ATP binding and ATPase activity in vitro. Ref.17

Mutagenesis

49

1

Q → E: Increases about 3-fold ATP binding but reduces about 2-fold ATPase activity in vitro. Ref.17

Mutagenesis

66

1

A → D: Slow growth. Ref.12 Ref.13

Mutagenesis

66

1

A → V: Lethal and dominant negative if overexpressed in vivo. Impairs ATP hydrolysis, RNA-helicase and translation activity in vitro. Ref.12 Ref.13

Mutagenesis

72

1

K → A: Lethal in vivo and reduces ATP binding and ATPase activity in vitro. Ref.17

Mutagenesis

79

1

A → V in TIF1-1; no growth at 36 degrees Celsius. Ref.12

Mutagenesis

126

1

G → D: Lethal. Ref.12

Mutagenesis

127

1

G → D: Slow growth. Ref.12

Mutagenesis

145

1

G → D: Lethal. Ref.12

Mutagenesis

145

1

G → S: Slow growth. Ref.12

Mutagenesis

170

1

D → E: Lethal. Ref.12

Mutagenesis

173

1

D → H: Lethal. Ref.12

Mutagenesis

311

1

S → F: Slow growth. Ref.12

Mutagenesis

347

1

R → E, G, I, S or T: Lethal and dominant negative if overexpressed. Ref.12

Secondary structure

1

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395

Helix Strand Turn

Details...

Helix

24 – 27

4

Helix

31 – 40

10

Helix

47 – 57

11

Beta strand

62 – 65

4

Helix

72 – 83

12

Beta strand

93 – 96

4

Helix

100 – 113

14

Turn

114 – 116

3

Beta strand

121 – 124

4

Beta strand

141 – 145

5

Helix

147 – 155

9

Beta strand

166 – 170

5

Helix

172 – 177

6

Helix

181 – 190

10

Beta strand

196 – 203

8

Helix

206 – 215

10

Beta strand

220 – 222

3

Beta strand

235 – 243

9

Helix

244 – 246

3

Helix

247 – 257

11

Beta strand

263 – 269

7

Helix

270 – 282

13

Beta strand

287 – 290

4

Helix

296 – 307

12

Beta strand

312 – 317

6

Helix

318 – 320

3

Turn

321 – 323

3

Beta strand

330 – 336

7

Helix

341 – 346

6

Beta strand

359 – 365

7

Turn

366 – 368

3

Helix

369 – 378

10

Turn

391 – 394

4

Sequences

	Sequence		Length	Mass (Da)
	P10081 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 19D8C133C815DD48	FASTA	395	44,697
	10 20 30 40 50 60 MSEGITDIEE SQIQTNYDKV VYKFDDMELD ENLLRGVFGY GFEEPSAIQQ RAIMPIIEGH 70 80 90 100 110 120 DVLAQAQSGT GKTGTFSIAA LQRIDTSVKA PQALMLAPTR ELALQIQKVV MALAFHMDIK 130 140 150 160 170 180 VHACIGGTSF VEDAEGLRDA QIVVGTPGRV FDNIQRRRFR TDKIKMFILD EADEMLSSGF 190 200 210 220 230 240 KEQIYQIFTL LPPTTQVVLL SATMPNDVLE VTTKFMRNPV RILVKKDELT LEGIKQFYVN 250 260 270 280 290 300 VEEEEYKYEC LTDLYDSISV TQAVIFCNTR RKVEELTTKL RNDKFTVSAI YSDLPQQERD 310 320 330 340 350 360 TIMKEFRSGS SRILISTDLL ARGIDVQQVS LVINYDLPAN KENYIHRIGR GGRFGRKGVA 370 380 390 INFVTNEDVG AMRELEKFYS TQIEELPSDI ATLLN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of the genes TIF1 and TIF2 from Saccharomyces cerevisiae coding for a translation initiation factor." Linder P., Slonimski P.P. Nucleic Acids Res. 16:10359-10359(1988) [PubMed: 3057442] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TIF1 AND TIF2). Strain: CD11/B1830/50.
[2]	"An essential yeast protein, encoded by duplicated genes TIF1 and TIF2 and homologous to the mammalian translation initiation factor eIF-4A, can suppress a mitochondrial missense mutation." Linder P., Slonimski P.P. Proc. Natl. Acad. Sci. U.S.A. 86:2286-2290(1989) [PubMed: 2648398] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TIF1 AND TIF2). Strain: CD11/B1830/50.
[3]	"Complete DNA sequence of yeast chromosome XI." Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W. Nature 369:371-378(1994) [PubMed: 8196765] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TIF1). Strain: ATCC 96604 / S288c / FY1679.
[4]	"Sequence analysis of a 40.7 kb segment from the left arm of yeast chromosome X reveals 14 known genes and 13 new open reading frames including homologues of genes clustered on the right arm of chromosome XI." Katsoulou C., Tzermia M., Tavernarakis N., Alexandraki D. Yeast 12:787-797(1996) [PubMed: 8813765] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TIF2). Strain: ATCC 96604 / S288c / FY1679.
[5]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L. EMBO J. 15:2031-2049(1996) [PubMed: 8641269] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TIF2). Strain: ATCC 96604 / S288c / FY1679.
[6]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION (TIF1 AND TIF2). Strain: ATCC 204508 / S288c.
[7]	"Requirement of the self-glucosylating initiator proteins Glg1p and Glg2p for glycogen accumulation in Saccharomyces cerevisiae." Cheng C., Mu J., Farkas I., Huang D., Goebl M.G., Roach P.J. Mol. Cell. Biol. 15:6632-6640(1995) [PubMed: 8524228] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-93 (TIF2).
[8]	"The Saccharomyces cerevisiae RPB4 gene is tightly linked to the TIF2 gene." Foreman P.K., Davis R.W., Sachs A.B. Nucleic Acids Res. 19:2781-2781(1991) [PubMed: 2041753] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 307-395 (TIF2).
[9]	"The 66 kDa component of yeast SFI, stimulatory factor I, is hsp60." Smiley J.K., Brown W.C., Campbell J.L. Nucleic Acids Res. 20:4913-4918(1992) [PubMed: 1408806] [Abstract] Cited for: PROTEIN SEQUENCE OF 332-340; 342-347 AND 378-391.
[10]	"Translation in Saccharomyces cerevisiae: initiation factor 4A-dependent cell-free system." Blum S., Mueller M., Schmid S.R., Linder P., Trachsel H. Proc. Natl. Acad. Sci. U.S.A. 86:6043-6046(1989) [PubMed: 2668952] [Abstract] Cited for: FUNCTION.
[11]	"Translation initiation factor-dependent extracts from Saccharomyces cerevisiae." Altmann M., Blum S., Pelletier J., Sonenberg N., Wilson T.M., Trachsel H. Biochim. Biophys. Acta 1050:155-159(1990) [PubMed: 2169890] [Abstract] Cited for: FUNCTION.
[12]	"Translation initiation factor 4A from Saccharomyces cerevisiae: analysis of residues conserved in the D-E-A-D family of RNA helicases." Schmid S.R., Linder P. Mol. Cell. Biol. 11:3463-3471(1991) [PubMed: 2046664] [Abstract] Cited for: CHARACTERIZATION, MUTAGENESIS OF ALA-66; ALA-79; GLY-126; GLY-127; GLY-145; ASP-170; ASP-173; SER-311 AND ARG-347.
[13]	"ATP hydrolysis by initiation factor 4A is required for translation initiation in Saccharomyces cerevisiae." Blum S., Schmid S.R., Pause A., Buser P., Linder P., Sonenberg N., Trachsel H. Proc. Natl. Acad. Sci. U.S.A. 89:7664-7668(1992) [PubMed: 1502180] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ALA-66.
[14]	"Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins." Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., Payne W.E. Electrophoresis 18:1347-1360(1997) [PubMed: 9298649] [Abstract] Cited for: ACETYLATION AT SER-2.
[15]	"Eukaryotic translation initiation factors 4G and 4A from Saccharomyces cerevisiae interact physically and functionally." Neff C.L., Sachs A.B. Mol. Cell. Biol. 19:5557-5564(1999) [PubMed: 10409745] [Abstract] Cited for: FUNCTION, INTERACTION WITH TIF4631 AND TIF4632.
[16]	"Interaction of translation initiation factor eIF4G with eIF4A in the yeast Saccharomyces cerevisiae." Dominguez D., Altmann M., Benz J., Baumann U., Trachsel H. J. Biol. Chem. 274:26720-26726(1999) [PubMed: 10480875] [Abstract] Cited for: FUNCTION, INTERACTION WITH TIF4631.
[17]	"The Q motif: a newly identified motif in DEAD box helicases may regulate ATP binding and hydrolysis." Tanner N.K., Cordin O., Banroques J., Doere M., Linder P. Mol. Cell 11:127-138(2003) [PubMed: 12535527] [Abstract] Cited for: FUNCTION, DOMAIN, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF PHE-24; PHE-42; SER-46; GLN-49 AND LYS-72.
[18]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[19]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[20]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY. Strain: YAL6B.
[21]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-146, MASS SPECTROMETRY. Strain: ADR376.
[22]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-128; SER-129 AND THR-146, MASS SPECTROMETRY.
[23]	"Crystallographic structure of the amino terminal domain of yeast initiation factor 4A, a representative DEAD-box RNA helicase." Johnson E.R., McKay D.B. RNA 5:1526-1534(1999) [PubMed: 10606264] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 3-225.
[24]	"Crystal structure of the ATPase domain of translation initiation factor 4A from Saccharomyces cerevisiae -- the prototype of the DEAD box protein family." Benz J., Trachsel H., Baumann U. Structure 7:671-679(1999) [PubMed: 10404596] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 10-233.
[25]	"Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase." Caruthers J.M., Johnson E.R., McKay D.B. Proc. Natl. Acad. Sci. U.S.A. 97:13080-13085(2000) [PubMed: 11087862] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 231-395.
+	Additional computationally mapped references.

Web resources

RNA helicases from the baker's yeast Saccharomyces cerevisiae

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X12813 Genomic DNA. Translation: CAA31301.1.
X12814 Genomic DNA. Translation: CAA31302.1.
X58099 Genomic DNA. Translation: CAA41110.1.
X87371 Genomic DNA. Translation: CAA60817.1.
Z49413 Genomic DNA. Translation: CAA89433.1.
U25436 Genomic DNA. Translation: AAA91645.1.
Z28284 Genomic DNA. Translation: CAA82138.1.
BK006943 Genomic DNA. Translation: DAA08662.1.
BK006944 Genomic DNA. Translation: DAA09210.1.

PIR

FIBY1. S05835.

RefSeq

NP_012397.1. NM_001181571.1.
NP_012985.1. NM_001179849.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FUK	X-ray	1.75	A	231-395	[»]
1FUU	X-ray	2.50	A/B	2-395	[»]
1QDE	X-ray	2.00	A	9-232	[»]
1QVA	X-ray	2.50	A	2-224	[»]
2VSO	X-ray	2.60	A/B	1-395	[»]
2VSX	X-ray	2.80	A/B	1-395	[»]

ProteinModelPortal

P10081.

SMR

P10081. Positions 12-395.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4571N.

IntAct

P10081. 69 interactions.

MINT

MINT-546056.

STRING

P10081.

2D gel databases

SWISS-2DPAGE

P10081.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YJL138C; YJL138C; YJL138C.
YKR059W; YKR059W; YKR059W.

GeneID

853303.
853933.

KEGG

sce:YJL138C.
sce:YKR059W.

Organism-specific databases

SGD

S000001767. TIF1.
S000003674. TIF2.

Phylogenomic databases

eggNOG

fuNOG04518.

GeneTree

EFGT00050000000529.

HOGENOM

HBG737336.

OMA

DIKVHAC.

OrthoDB

EOG4PG98F.

Gene expression databases

Genevestigator

P10081.

GermOnline

YJL138C. Saccharomyces cerevisiae.
YKR059W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR014001. DEAD-like_helicase.
IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR001650. Helicase_C.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]

KO

K03257.

Pfam

PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]

SMART

SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]

PROSITE

PS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

973627.

Entry information

Entry name

IF4A_YEAST

Accession

Primary (citable) accession number: P10081
Secondary accession number(s): D6VW46

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 150 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program