O60841 (IF2P_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Translation initiation factor IF-2

Gene names

Name:	EIF5B
Synonyms:	IF2, KIAA0741

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	1220 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Function in general translation initiation by promoting the binding of the formylmethionine-tRNA to ribosomes. Seems to function along with eIF-2 By similarity.
Subunit structure	Interacts with ANXA5 in a calcium and phospholipid-dependent manner By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the IF-2 family.
Sequence caution	The sequence BAA34461.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	GTP-binding Nucleotide-binding
Molecular function	Initiation factor
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	GTP catabolic process Inferred from electronic annotation. Source: GOC regulation of translational initiation Inferred from direct assay Ref.1. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro translation initiation factor activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF1AY	O14602	2	EBI-928530,EBI-286439
ETS1	P14921	2	EBI-928530,EBI-913209

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1220	1220	Eukaryotic translation initiation factor 5B		PRO_0000137294
Regions
	Nucleotide binding	638 – 645	8	GTP By similarity
	Compositional bias	39 – 50	12	Poly-Lys
	Compositional bias	94 – 99	6	Poly-Lys
	Compositional bias	138 – 142	5	Poly-Asp
	Compositional bias	313 – 322	10	Poly-Lys
	Compositional bias	353 – 356	4	Poly-Glu
	Compositional bias	361 – 364	4	Poly-Glu
	Compositional bias	491 – 496	6	Poly-Glu
	Compositional bias	529 – 567	39	Asp/Glu-rich (acidic)
Amino acid modifications
	Modified residue	107	1	Phosphoserine Ref.8 Ref.13 Ref.14 Ref.17
	Modified residue	113	1	Phosphoserine Ref.8 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17
	Modified residue	134	1	Phosphotyrosine Ref.13 Ref.15 Ref.17
	Modified residue	135	1	Phosphoserine Ref.13 Ref.15 Ref.16 Ref.17
	Modified residue	137	1	Phosphoserine Ref.13 Ref.15 Ref.16 Ref.17
	Modified residue	164	1	Phosphoserine Ref.8 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17
	Modified residue	171	1	Phosphoserine Ref.17
	Modified residue	178	1	Phosphoserine By similarity
	Modified residue	182	1	Phosphoserine Ref.13 Ref.15 Ref.16
	Modified residue	183	1	Phosphoserine Ref.13 Ref.15
	Modified residue	186	1	Phosphoserine Ref.13 Ref.15 Ref.16
	Modified residue	190	1	Phosphoserine Ref.5 Ref.13 Ref.15 Ref.16
	Modified residue	214	1	Phosphoserine Ref.8 Ref.9 Ref.10 Ref.11 Ref.15 Ref.16 Ref.17
	Modified residue	301	1	Phosphothreonine Ref.13 Ref.16
	Modified residue	498	1	Phosphothreonine Ref.17
	Modified residue	547	1	Phosphoserine Ref.13
	Modified residue	560	1	Phosphoserine Ref.13
	Modified residue	588	1	Phosphoserine Ref.13 Ref.16
	Modified residue	589	1	Phosphoserine Ref.16
	Modified residue	591	1	Phosphoserine Ref.16
	Modified residue	595	1	Phosphoserine Ref.13 Ref.16
Natural variations
	Natural variant	337	1	S → G. Corresponds to variant rs10642 [ dbSNP | Ensembl ].		VAR_055954
	Natural variant	360	1	R → G. Corresponds to variant rs3205296 [ dbSNP | Ensembl ].		VAR_055955
	Natural variant	522	1	K → T. Ref.1 Ref.2 Ref.18 Corresponds to variant rs7558074 [ dbSNP | Ensembl ].		VAR_060587
Experimental info
	Mutagenesis	640	1	V → G: Loss of activity in vivo. Retains full activity in vitro. Ref.2
	Mutagenesis	706	1	H → E: Loss of activity; both in vivo and in vitro. Ref.2
	Mutagenesis	706	1	H → Q: Loss of activity in vivo. Partial activity in vitro. Ref.2
	Mutagenesis	759	1	D → N: Loss of activity; both in vivo and in vitro. Ref.2
	Sequence conflict	64	1	E → G in BAA34461. Ref.3
	Sequence conflict	92	1	T → I in CAB44357. Ref.1
	Sequence conflict	180	1	I → M in AAD16006. Ref.2
	Sequence conflict	256	1	K → R in AAD16006. Ref.2
	Sequence conflict	549	1	E → V in AAD16006. Ref.2
	Sequence conflict	669	1	G → W in AAD16006. Ref.2
	Sequence conflict	894	1	E → K in CAB44357. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O60841 [UniParc]. Last modified November 24, 2009. Version 4. Checksum: 454C29FB90AA768E	FASTA	1,220	138,827
	10 20 30 40 50 60 MGKKQKNKSE DSTKDDIDLD ALAAEIEGAG AAKEQEPQKS KGKKKKEKKK QDFDEDDILK 70 80 90 100 110 120 ELEELSLEAQ GIKADRETVA VKPTENNEEE FTSKDKKKKG QKGKKQSFDD NDSEELEDKD 130 140 150 160 170 180 SKSKKTAKPK VEMYSGSDDD DDFNKLPKKA KGKAQKSNKK WDGSEEDEDN SKKIKERSRI 190 200 210 220 230 240 NSSGESGDES DEFLQSRKGQ KKNQKNKPGP NIESGNEDDD ASFKIKTVAQ KKAEKKERER 250 260 270 280 290 300 KKRDEEKAKL RKLKEKEELE TGKKDQSKQK ESQRKFEEET VKSKVTVDTG VIPASEEKAE 310 320 330 340 350 360 TPTAAEDDNE GDKKKKDKKK KKGEKEEKEK EKKKGPSKAT VKAMQEALAK LKEEEERQKR 370 380 390 400 410 420 EEEERIKRLE ELEAKRKEEE RLEQEKRERK KQKEKERKER LKKEGKLLTK SQREARARAE 430 440 450 460 470 480 ATLKLLQAQG VEVPSKDSLP KKRPIYEDKK RKKIPQQLES KEVSESMELC AAVEVMEQGV 490 500 510 520 530 540 PEKEETPPPV EPEEEEDTED AGLDDWEAMA SDEETEKVEG NKVHIEVKEN PEEEEEEEEE 550 560 570 580 590 600 EEEDEESEEE EEEEGESEGS EGDEEDEKVS DEKDSGKTLD KKPSKEMSSD SEYDSDDDRT 610 620 630 640 650 660 KEERAYDKAK RRIEKRRLEH SKNVNTEKLR APIICVLGHV DTGKTKILDK LRHTHVQDGE 670 680 690 700 710 720 AGGITQQIGA TNVPLEAINE QTKMIKNFDR ENVRIPGMLI IDTPGHESFS NLRNRGSSLC 730 740 750 760 770 780 DIAILVVDIM HGLEPQTIES INLLKSKKCP FIVALNKIDR LYDWKKSPDS DVAATLKKQK 790 800 810 820 830 840 KNTKDEFEER AKAIIVEFAQ QGLNAALFYE NKDPRTFVSL VPTSAHTGDG MGSLIYLLVE 850 860 870 880 890 900 LTQTMLSKRL AHCEELRAQV MEVKALPGMG TTIDVILING RLKEGDTIIV PGVEGPIVTQ 910 920 930 940 950 960 IRGLLLPPPM KELRVKNQYE KHKEVEAAQG VKILGKDLEK TLAGLPLLVA YKEDEIPVLK 970 980 990 1000 1010 1020 DELIHELKQT LNAIKLEEKG VYVQASTLGS LEALLEFLKT SEVPYAGINI GPVHKKDVMK 1030 1040 1050 1060 1070 1080 ASVMLEHDPQ YAVILAFDVR IERDAQEMAD SLGVRIFSAE IIYHLFDAFT KYRQDYKKQK 1090 1100 1110 1120 1130 1140 QEEFKHIAVF PCKIKILPQY IFNSRDPIVM GVTVEAGQVK QGTPMCVPSK NFVDIGIVTS 1150 1160 1170 1180 1190 1200 IEINHKQVDV AKKGQEVCVK IEPIPGESPK MFGRHFEATD ILVSKISRQS IDALKDWFRD 1210 1220 EMQKSDWQLI VELKKVFEII

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of hIF2, a human homologue of bacterial translation initiation factor 2 and its interaction with HIV-1 matrix." Wilson S.A., Sieiro-Vazquez C., Edwards N.J., Iourin O., Byles E.D., Kotsopoulou E., Adamson C.S., Kingsman S.M., Kingsman A.J., Martin-Rendon E. Biochem. J. 342:97-103(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-522. Tissue: Cervix carcinoma.
[2]	"Universal conservation in translation initiation revealed by human and archaeal homologs of bacterial translation initiation factor IF2." Lee J.H., Choi S.K., Roll-Mecak A., Burley S.K., Dever T.E. Proc. Natl. Acad. Sci. U.S.A. 96:4342-4347(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF VAL-640; HIS-706 AND ASP-759, CHARACTERIZATION, VARIANT THR-522. Tissue: Testis.
[3]	"Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Bienvenut W.V., Waridel P., Quadroni M. Submitted (MAR-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 9-33; 77-94; 106-122; 180-197; 206-224; 285-298; 425-436; 629-644; 653-683; 695-713; 749-757; 766-777; 882-902; 1000-1015; 1044-1055; 1096-1120 AND 1175-1185, PHOSPHORYLATION AT SER-190, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"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] OF 89-1220. Tissue: Testis.
[7]	"Characterization of 16 novel human genes showing high similarity to yeast sequences." Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B., Cannata N., Zimbello R., Lanfranchi G., Valle G. Yeast 18:69-80(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 833-1220.
[8]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; SER-113; SER-164 AND SER-214, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line." Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S. Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, MASS SPECTROMETRY. Tissue: Prostate cancer.
[10]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, MASS SPECTROMETRY. Tissue: T-cell.
[12]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Platelet.
[13]	"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-107; SER-113; TYR-134; SER-135; SER-137; SER-164; SER-182; SER-183; SER-186; SER-190; THR-301; SER-547; SER-560; SER-588 AND SER-595, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; SER-113 AND SER-164, MASS SPECTROMETRY. Tissue: Liver.
[15]	"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-113; TYR-134; SER-135; SER-137; SER-164; SER-182; SER-183; SER-186; SER-190 AND SER-214, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"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-113; SER-135; SER-137; SER-164; SER-182; SER-186; SER-190; SER-214; THR-301; SER-588; SER-589; SER-591 AND SER-595, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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-107; SER-113; TYR-134; SER-135; SER-137; SER-164; SER-171; SER-214 AND THR-498, MASS SPECTROMETRY.
[18]	"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: VARIANT [LARGE SCALE ANALYSIS] THR-522, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ006776 mRNA. Translation: CAB44357.1. AF078035 mRNA. Translation: AAD16006.1. AC018690 Genomic DNA. Translation: AAY24313.1. AC079447 Genomic DNA. Translation: AAX93258.1. AB018284 mRNA. Translation: BAA34461.2. Different initiation. AL133563 mRNA. Translation: CAB63717.1. AJ006412 mRNA. Translation: CAA07018.1.
IPI	IPI00299254.
PIR	T43483.
RefSeq	NP_056988.3. NM_015904.3.
UniGene	Hs.158688.
3D structure databases
ProteinModelPortal	O60841.
SMR	O60841. Positions 628-1215.
ModBase	Search...
Protein-protein interaction databases
IntAct	O60841. 11 interactions.
STRING	9606.ENSP00000289371.
PTM databases
PhosphoSite	O60841.
Proteomic databases
PaxDb	O60841.
PRIDE	O60841.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000289371; ENSP00000289371; ENSG00000158417.
GeneID	9669.
KEGG	hsa:9669.
UCSC	uc002tab.3. human.
Organism-specific databases
CTD	9669.
GeneCards	GC02P099953.
H-InvDB	HIX0002308.
HGNC	HGNC:30793. EIF5B.
HPA	HPA034648.
MIM	606086. gene.
neXtProt	NX_O60841.
PharmGKB	PA134864457.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0532.
HOGENOM	HOG000105770.
HOVERGEN	HBG019036.
InParanoid	O60841.
KO	K03243.
OMA	VMGVIVE.
OrthoDB	EOG44BB1J.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	O60841.
Bgee	O60841.
CleanEx	HS_EIF5B.
Genevestigator	O60841.
GermOnline	ENSG00000158417. Homo sapiens.
Family and domain databases
Gene3D	3.40.50.10050. 1 hit.
InterPro	IPR000795. EF_GTP-bd_dom. IPR005225. Small_GTP-bd_dom. IPR015760. TIF_IF2. IPR023115. TIF_IF2_dom3. IPR004161. Transl_elong_EFTu/EF1A_2. IPR009000. Transl_elong_init/rib_B-barrel. [Graphical view]
PANTHER	PTHR23115:SF41. PTHR23115:SF41. 1 hit.
Pfam	PF00009. GTP_EFTU. 1 hit. PF03144. GTP_EFTU_D2. 1 hit. PF11987. IF-2. 1 hit. [Graphical view]
PRINTS	PR00315. ELONGATNFCT.
SUPFAM	SSF52156. TIF_IF2_dom3. 1 hit. SSF50447. Translat_factor. 1 hit.
TIGRFAMs	TIGR00231. small_GTP. 1 hit.
PROSITE	PS01176. IF2. False negative. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	EIF5B. human.
GenomeRNAi	9669.
NextBio	36307.
PMAP-CutDB	O60841.
SOURCE	Search...

Entry information

Entry name

IF2P_HUMAN

Accession

Primary (citable) accession number: O60841
Secondary accession number(s): O95805 , Q53RV7, Q53SI8, Q9UF81, Q9UMN7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 24, 2009
Last modified:	May 1, 2013
This is version 129 of the entry and version 4 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.