SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P55010

- IF5_HUMAN

UniProt

P55010 - IF5_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Eukaryotic translation initiation factor 5
Gene
EIF5
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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]).

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi27 – 348GTP Reviewed prediction

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-KW
  2. GTPase activity Source: ProtInc
  3. poly(A) RNA binding Source: UniProtKB
  4. translation factor activity, nucleic acid binding Source: ProtInc
  5. translation initiation factor activity Source: UniProtKB

GO - Biological processi

  1. GTP catabolic process Source: GOC
  2. cellular protein metabolic process Source: Reactome
  3. gene expression Source: Reactome
  4. regulation of translational initiation Source: ProtInc
  5. translation Source: Reactome
  6. translational initiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_931. Ribosomal scanning and start codon recognition.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 5
Short name:
eIF-5
Gene namesi
Name:EIF5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:3299. EIF5.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: UniProtKB
  3. plasma membrane Source: HPA
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27725.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 431431Eukaryotic translation initiation factor 5
PRO_0000212516Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei10 – 101Phosphoserine2 Publications
Modified residuei229 – 2291Phosphoserine1 Publication
Modified residuei389 – 3891Phosphoserine4 Publications
Modified residuei390 – 3901Phosphoserine4 Publications
Modified residuei419 – 4191Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP55010.
PaxDbiP55010.
PeptideAtlasiP55010.
PRIDEiP55010.

PTM databases

PhosphoSiteiP55010.

Expressioni

Gene expression databases

ArrayExpressiP55010.
BgeeiP55010.
CleanExiHS_EIF5.
GenevestigatoriP55010.

Organism-specific databases

HPAiCAB004226.
HPA000867.

Interactioni

Protein-protein interaction databases

BioGridi108298. 39 interactions.
IntActiP55010. 5 interactions.
MINTiMINT-5004352.
STRINGi9606.ENSP00000216554.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65
Beta strandi17 – 193
Beta strandi23 – 253
Beta strandi27 – 315
Beta strandi33 – 364
Helixi39 – 457
Helixi51 – 6111
Beta strandi65 – 684
Turni69 – 724
Beta strandi73 – 786
Helixi82 – 9514
Turni100 – 1023
Beta strandi103 – 1053
Beta strandi108 – 1125
Turni113 – 1164
Beta strandi117 – 1215
Beta strandi123 – 1253
Beta strandi128 – 1303
Beta strandi133 – 1364
Helixi137 – 1437
Helixi236 – 25217
Helixi256 – 2583
Helixi260 – 26910
Helixi273 – 2753
Helixi276 – 2849
Helixi289 – 2957
Helixi297 – 3048
Helixi308 – 32417
Helixi326 – 3294
Helixi330 – 3323
Helixi333 – 34210
Helixi348 – 3569
Beta strandi361 – 3633
Helixi365 – 38319
Helixi400 – 4089

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E9HNMR-A1-150[»]
2G2KNMR-A2-170[»]
2IU1X-ray1.80A232-431[»]
ProteinModelPortaliP55010.
SMRiP55010. Positions 3-150, 232-407.

Miscellaneous databases

EvolutionaryTraceiP55010.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini233 – 392160W2
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi196 – 2027Asp/Glu-rich (highly acidic)
Compositional biasi384 – 40219Asp/Glu-rich (highly acidic)
Add
BLAST
Compositional biasi423 – 4297Asp-rich (acidic)

Sequence similaritiesi

Belongs to the eIF-2-beta/eIF-5 family.
Contains 1 W2 domain.

Phylogenomic databases

eggNOGiCOG1601.
HOGENOMiHOG000214327.
HOVERGENiHBG006132.
InParanoidiP55010.
KOiK03262.
OMAiMHQAQLL.
OrthoDBiEOG7FV3QF.
PhylomeDBiP55010.
TreeFamiTF101533.

Family and domain databases

Gene3Di1.25.40.180. 1 hit.
3.30.30.50. 1 hit.
InterProiIPR016024. 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]
PfamiPF01873. eIF-5_eIF-2B. 1 hit.
PF02020. W2. 1 hit.
[Graphical view]
SMARTiSM00653. eIF2B_5. 1 hit.
SM00515. eIF5C. 1 hit.
[Graphical view]
SUPFAMiSSF100966. SSF100966. 1 hit.
SSF48371. SSF48371. 1 hit.
SSF75689. SSF75689. 1 hit.
PROSITEiPS51363. W2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P55010-1 [UniParc]FASTAAdd to Basket

« Hide

MSVNVNRSVS DQFYRYKMPR LIAKVEGKGN GIKTVIVNMV DVAKALNRPP    50
TYPTKYFGCE LGAQTQFDVK NDRYIVNGSH EANKLQDMLD GFIKKFVLCP 100
ECENPETDLH VNPKKQTIGN SCKACGYRGM LDTHHKLCTF ILKNPPENSD 150
SGTGKKEKEK KNRKGKDKEN GSVSSSETPP PPPPPNEINP PPHTMEEEED 200
DDWGEDTTEE AQRRRMDEIS DHAKVLTLSD DLERTIEERV NILFDFVKKK 250
KEEGVIDSSD KEIVAEAERL DVKAMGPLVL TEVLFNEKIR EQIKKYRRHF 300
LRFCHNNKKA QRYLLHGLEC VVAMHQAQLI SKIPHILKEM YDADLLEEEV 350
IISWSEKASK KYVSKELAKE IRVKAEPFIK WLKEAEEESS GGEEEDEDEN 400
IEVVYSKAAS VPKVETVKSD NKDDDIDIDA I 431
Length:431
Mass (Da):49,223
Last modified:January 10, 2003 - v2
Checksum:iC6CCC3A255F9B9BC
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti418 – 4181K → M in a breast cancer sample; somatic mutation. 1 Publication
VAR_036467

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 601E → G in CAB45711. 1 Publication
Sequence conflicti203 – 2031W → S in AAC50572. 1 Publication
Sequence conflicti295 – 2951K → E in CAB45711. 1 Publication
Sequence conflicti311 – 3111Q → K in AAH32866. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS9980.1.
PIRiT12450.
RefSeqiNP_001960.2. NM_001969.4.
NP_892116.2. NM_183004.4.
UniGeneiHs.433702.
Hs.741278.

Genome annotation databases

EnsembliENST00000216554; ENSP00000216554; ENSG00000100664.
ENST00000392715; ENSP00000376477; ENSG00000100664.
ENST00000558506; ENSP00000453743; ENSG00000100664.
GeneIDi1983.
KEGGihsa:1983.
UCSCiuc001ymq.4. human.

Polymorphism databases

DMDMi27735202.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS9980.1.
PIRi T12450.
RefSeqi NP_001960.2. NM_001969.4.
NP_892116.2. NM_183004.4.
UniGenei Hs.433702.
Hs.741278.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P55010.
SMRi P55010. Positions 3-150, 232-407.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108298. 39 interactions.
IntActi P55010. 5 interactions.
MINTi MINT-5004352.
STRINGi 9606.ENSP00000216554.

PTM databases

PhosphoSitei P55010.

Polymorphism databases

DMDMi 27735202.

Proteomic databases

MaxQBi P55010.
PaxDbi P55010.
PeptideAtlasi P55010.
PRIDEi P55010.

Protocols and materials databases

DNASUi 1983.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000216554 ; ENSP00000216554 ; ENSG00000100664 .
ENST00000392715 ; ENSP00000376477 ; ENSG00000100664 .
ENST00000558506 ; ENSP00000453743 ; ENSG00000100664 .
GeneIDi 1983.
KEGGi hsa:1983.
UCSCi uc001ymq.4. human.

Organism-specific databases

CTDi 1983.
GeneCardsi GC14P103800.
HGNCi HGNC:3299. EIF5.
HPAi CAB004226.
HPA000867.
MIMi 601710. gene.
neXtProti NX_P55010.
PharmGKBi PA27725.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1601.
HOGENOMi HOG000214327.
HOVERGENi HBG006132.
InParanoidi P55010.
KOi K03262.
OMAi MHQAQLL.
OrthoDBi EOG7FV3QF.
PhylomeDBi P55010.
TreeFami TF101533.

Enzyme and pathway databases

Reactomei REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_931. Ribosomal scanning and start codon recognition.

Miscellaneous databases

ChiTaRSi eIF5. human.
EvolutionaryTracei P55010.
GeneWikii EIF5.
GenomeRNAii 1983.
NextBioi 8031.
PROi P55010.
SOURCEi Search...

Gene expression databases

ArrayExpressi P55010.
Bgeei P55010.
CleanExi HS_EIF5.
Genevestigatori P55010.

Family and domain databases

Gene3Di 1.25.40.180. 1 hit.
3.30.30.50. 1 hit.
InterProi 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 ]
Pfami PF01873. eIF-5_eIF-2B. 1 hit.
PF02020. W2. 1 hit.
[Graphical view ]
SMARTi SM00653. eIF2B_5. 1 hit.
SM00515. eIF5C. 1 hit.
[Graphical view ]
SUPFAMi SSF100966. SSF100966. 1 hit.
SSF48371. SSF48371. 1 hit.
SSF75689. SSF75689. 1 hit.
PROSITEi PS51363. W2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  5. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-229; SER-389; SER-390 AND SER-419, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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.
  15. Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-418.

Entry informationi

Entry nameiIF5_HUMAN
AccessioniPrimary (citable) accession number: P55010
Secondary accession number(s): Q53XB3, Q9H5N2, Q9UG48
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 10, 2003
Last modified: September 3, 2014
This is version 142 of the entry and version 2 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 14
    Human chromosome 14: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi