P55010 (IF5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Eukaryotic translation initiation factor 5
Short name=eIF-5

Gene names

Name:

EIF5

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	431 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the release of eIF-2 and the guanine nucleotide. The subsequent joining of a 60S ribosomal subunit results in the formation of a functional 80S initiation complex (80S.mRNA.Met-tRNA[F]).
Sequence similarities	Belongs to the eIF-2-beta/eIF-5 family. Contains 1 W2 domain.

Ontologies

Keywords
Biological process	Protein biosynthesis
Coding sequence diversity	Polymorphism
Ligand	GTP-binding Nucleotide-binding
Molecular function	Initiation factor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA metabolic process Inferred from electronic annotation. Source: InterPro regulation of translational initiation Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytosol Non-traceable author statement Ref.1. Source: UniProtKB
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Traceable author statement Ref.1. Source: ProtInc translation initiation factor activity Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 431

431

Eukaryotic translation initiation factor 5

PRO_0000212516

Regions

Domain

233 – 392

160

W2

Nucleotide binding

27 – 34

8

GTP Potential

Compositional bias

196 – 202

7

Asp/Glu-rich (highly acidic)

Compositional bias

384 – 402

19

Asp/Glu-rich (highly acidic)

Compositional bias

423 – 429

7

Asp-rich (acidic)

Amino acid modifications

Modified residue

10

1

Phosphoserine Ref.8 Ref.10

Modified residue

229

1

Phosphoserine Ref.8

Modified residue

389

1

Phosphoserine Ref.8 Ref.9 Ref.10 Ref.12

Modified residue

390

1

Phosphoserine Ref.8 Ref.9 Ref.10 Ref.12

Modified residue

419

1

Phosphoserine Ref.8 Ref.10

Natural variations

Natural variant

418

1

K → M in a breast cancer sample; somatic mutation. Ref.14

VAR_036467

Experimental info

Sequence conflict

60

1

E → G in CAB45711. Ref.2

Sequence conflict

203

1

W → S in AAC50572. Ref.1

Sequence conflict

295

1

K → E in CAB45711. Ref.2

Sequence conflict

311

1

Q → K in AAH32866. Ref.6

Secondary structure

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431

Helix Strand Turn

Details...

Beta strand

2 – 6

5

Beta strand

17 – 19

3

Beta strand

23 – 25

3

Beta strand

27 – 31

5

Beta strand

33 – 36

4

Helix

39 – 45

7

Helix

51 – 61

11

Beta strand

65 – 68

4

Turn

69 – 72

4

Beta strand

73 – 78

6

Helix

82 – 95

14

Turn

100 – 102

3

Beta strand

103 – 105

3

Beta strand

108 – 112

5

Turn

113 – 116

4

Beta strand

117 – 121

5

Beta strand

123 – 125

3

Beta strand

128 – 130

3

Beta strand

133 – 136

4

Helix

137 – 143

7

Helix

236 – 252

17

Helix

256 – 258

3

Helix

260 – 269

10

Helix

273 – 275

3

Helix

276 – 284

9

Helix

289 – 295

7

Helix

297 – 304

8

Helix

308 – 324

17

Helix

326 – 329

4

Helix

330 – 332

3

Helix

333 – 342

10

Helix

348 – 356

9

Beta strand

361 – 363

3

Helix

365 – 383

19

Helix

400 – 408

9

Sequences

	Sequence		Length	Mass (Da)
	P55010 [UniParc]. Last modified January 10, 2003. Version 2. Checksum: C6CCC3A255F9B9BC	FASTA	431	49,223
	10 20 30 40 50 60 MSVNVNRSVS DQFYRYKMPR LIAKVEGKGN GIKTVIVNMV DVAKALNRPP TYPTKYFGCE 70 80 90 100 110 120 LGAQTQFDVK NDRYIVNGSH EANKLQDMLD GFIKKFVLCP ECENPETDLH VNPKKQTIGN 130 140 150 160 170 180 SCKACGYRGM LDTHHKLCTF ILKNPPENSD SGTGKKEKEK KNRKGKDKEN GSVSSSETPP 190 200 210 220 230 240 PPPPPNEINP PPHTMEEEED DDWGEDTTEE AQRRRMDEIS DHAKVLTLSD DLERTIEERV 250 260 270 280 290 300 NILFDFVKKK KEEGVIDSSD KEIVAEAERL DVKAMGPLVL TEVLFNEKIR EQIKKYRRHF 310 320 330 340 350 360 LRFCHNNKKA QRYLLHGLEC VVAMHQAQLI SKIPHILKEM YDADLLEEEV IISWSEKASK 370 380 390 400 410 420 KYVSKELAKE IRVKAEPFIK WLKEAEEESS GGEEEDEDEN IEVVYSKAAS VPKVETVKSD 430 NKDDDIDIDA I

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of multiple mRNAs that encode mammalian translation initiation factor 5 (eIF-5)." Si K., Das K., Maitra U. J. Biol. Chem. 271:16934-16938(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: Brain and Uterus.
[7]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-229; SER-389; SER-390 AND SER-419, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389 AND SER-390, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-389; SER-390 AND SER-419, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389 AND SER-390, MASS SPECTROMETRY.
[13]	"Solution structure of the EIF-5_EIF-2B domain from human eukaryotic translation initiation factor 5." RIKEN structural genomics initiative (RSGI) Submitted (JAN-2008) to the PDB data bank Cited for: STRUCTURE BY NMR OF 1-150.
[14]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-418.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U49436 mRNA. Translation: AAC50572.1.
AL080102 mRNA. Translation: CAB45711.1.
AK026933 mRNA. Translation: BAB15593.1.
BX537367 mRNA. Translation: CAD97610.1.
CH471061 Genomic DNA. Translation: EAW81809.1.
BC007728 mRNA. Translation: AAH07728.1.
BC032866 mRNA. Translation: AAH32866.1.

IPI

IPI00022648.

PIR

T12450.

RefSeq

NP_001960.2. NM_001969.4.
NP_892116.2. NM_183004.4.

UniGene

Hs.433702.
Hs.741278.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2E9H	NMR	-	A	1-150	[»]
2G2K	NMR	-	A	2-170	[»]
2IU1	X-ray	1.80	A	232-431	[»]

ProteinModelPortal

P55010.

ModBase

Search...

Protein-protein interaction databases

IntAct

P55010. 5 interactions.

MINT

MINT-5004352.

STRING

9606.ENSP00000216554.

PTM databases

PhosphoSite

P55010.

Polymorphism databases

DMDM

27735202.

Proteomic databases

PaxDb

P55010.

PeptideAtlas

P55010.

PRIDE

P55010.

Protocols and materials databases

DNASU

1983.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000216554; ENSP00000216554; ENSG00000100664.
ENST00000392715; ENSP00000376477; ENSG00000100664.
ENST00000558506; ENSP00000453743; ENSG00000100664.

GeneID

1983.

KEGG

hsa:1983.

UCSC

uc001ymq.3. human.

Organism-specific databases

CTD

1983.

GeneCards

GC14P103800.

HGNC

HGNC:3299. EIF5.

HPA

CAB004226.
HPA000867.

MIM

601710. gene.

neXtProt

NX_P55010.

PharmGKB

PA27725.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1601.

HOGENOM

HOG000214327.

HOVERGEN

HBG006132.

InParanoid

P55010.

KO

K03262.

OMA

MHQAQLL.

OrthoDB

EOG47D9GG.

PhylomeDB

P55010.

Enzyme and pathway databases

Reactome

REACT_17015. Metabolism of proteins.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P55010.

Bgee

P55010.

CleanEx

HS_EIF5.

Genevestigator

P55010.

GermOnline

ENSG00000100664. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.180. 1 hit.
3.30.30.50. 1 hit.

InterPro

IPR016024. ARM-type_fold.
IPR016021. MIF4-like_typ_1/2/3.
IPR002735. Transl_init_fac_IF2/IF5.
IPR016189. Transl_init_fac_IF2/IF5_N.
IPR016190. Transl_init_fac_IF2/IF5_Zn-bd.
IPR003307. W2_domain.
[Graphical view]

Pfam

PF01873. eIF-5_eIF-2B. 1 hit.
PF02020. W2. 1 hit.
[Graphical view]

SMART

SM00653. eIF2B_5. 1 hit.
SM00515. eIF5C. 1 hit.
[Graphical view]

SUPFAM

SSF48371. ARM-type_fold. 1 hit.
SSF100966. Transl_init_fac_IF2/IF5_N. 1 hit.
SSF75689. Transl_init_fac_IF2/IF5_Zn-bd. 1 hit.

PROSITE

PS51363. W2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

eIF5. human.

EvolutionaryTrace

P55010.

GenomeRNAi

1983.

NextBio

8031.

SOURCE

Search...

Entry information

Entry name

IF5_HUMAN

Accession

Primary (citable) accession number: P55010
Secondary accession number(s): Q53XB3, Q9H5N2, Q9UG48

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 10, 2003
Last modified:	May 1, 2013
This is version 129 of the entry and version 2 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.