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Q05D44

- IF2P_MOUSE

UniProt

Q05D44 - IF2P_MOUSE

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Protein

Eukaryotic translation initiation factor 5B

Gene

Eif5b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Function in general translation initiation by promoting the binding of the formylmethionine-tRNA to ribosomes. Seems to function along with eIF-2 By similarity.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi634 – 6418GTPBy similarity

GO - Molecular functioni

  1. GTPase activity Source: InterPro
  2. GTP binding Source: UniProtKB-KW
  3. poly(A) RNA binding Source: Ensembl
  4. translation initiation factor activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 5B
Short name:
eIF-5B
Alternative name(s):
Translation initiation factor IF-2
Gene namesi
Name:Eif5b
Synonyms:If2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:2441772. Eif5b.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12161216Eukaryotic translation initiation factor 5BPRO_0000354071Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei108 – 1081PhosphoserineBy similarity
Modified residuei114 – 1141Phosphoserine2 Publications
Modified residuei137 – 1371Phosphoserine3 Publications
Modified residuei139 – 1391Phosphoserine3 Publications
Modified residuei165 – 1651Phosphoserine1 Publication
Modified residuei172 – 1721PhosphoserineBy similarity
Modified residuei183 – 1831PhosphoserineBy similarity
Modified residuei184 – 1841PhosphoserineBy similarity
Modified residuei187 – 1871Phosphoserine2 Publications
Modified residuei191 – 1911Phosphoserine2 Publications
Modified residuei215 – 2151Phosphoserine4 Publications
Modified residuei300 – 3001PhosphothreonineBy similarity
Modified residuei497 – 4971PhosphothreonineBy similarity
Modified residuei556 – 5561PhosphoserineBy similarity
Modified residuei584 – 5841PhosphoserineBy similarity
Modified residuei585 – 5851PhosphoserineBy similarity
Modified residuei587 – 5871PhosphoserineBy similarity
Modified residuei591 – 5911PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ05D44.
PaxDbiQ05D44.
PRIDEiQ05D44.

PTM databases

PhosphoSiteiQ05D44.

Expressioni

Gene expression databases

BgeeiQ05D44.
ExpressionAtlasiQ05D44. baseline and differential.
GenevestigatoriQ05D44.

Interactioni

Subunit structurei

Interacts with ANXA5 in a calcium and phospholipid-dependent manner.By similarity

Protein-protein interaction databases

BioGridi230580. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ05D44.
SMRiQ05D44. Positions 624-1211.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini625 – 842218tr-type GPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni634 – 6418G1PROSITE-ProRule annotation
Regioni659 – 6635G2PROSITE-ProRule annotation
Regioni698 – 7014G3PROSITE-ProRule annotation
Regioni752 – 7554G4PROSITE-ProRule annotation
Regioni820 – 8223G5PROSITE-ProRule annotation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi39 – 452414Lys-richAdd
BLAST
Compositional biasi235 – 561327Glu-richAdd
BLAST

Sequence similaritiesi

Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily.PROSITE-ProRule annotation
Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0532.
GeneTreeiENSGT00730000111064.
HOVERGENiHBG019036.
InParanoidiQ05D44.
KOiK03243.
OMAiGSLRMHT.
OrthoDBiEOG7034GC.
PhylomeDBiQ05D44.
TreeFamiTF101535.

Family and domain databases

Gene3Di3.40.50.10050. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR000795. EF_GTP-bd_dom.
IPR029459. EFTU-type.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR023115. TIF_IF2_dom3.
IPR009000. Transl_B-barrel.
IPR004161. Transl_elong_EFTu/EF1A_2.
[Graphical view]
PfamiPF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF14578. GTP_EFTU_D4. 1 hit.
PF11987. IF-2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF52156. SSF52156. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51722. G_TR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q05D44-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGKKQKNKSE DSTKDDTDLG ALAAEIEGAG AAKEQEPQKS KGKKKKEKKK
60 70 80 90 100
QDFDENDILR ELEELSLEAQ GIRADRDAAA VKPTENNEEE SASKQDKKKK
110 120 130 140 150
GQKGKKTSFD ENDSEELEDK DSKSKKTARP NSEAPLSGSE DADDSNKLSK
160 170 180 190 200
KGKKAQKSTK KRDGSEEDED NSKRSKERSR VNSSGESGGE SDEFLQSRKG
210 220 230 240 250
QKKNQKNKSV PTVDSGNEDD DSSFKIKTVA QKKAEKKERE KKKRDEEKAK
260 270 280 290 300
LRKMKEKEEL EKGKKEQSKQ REPQKRPEEE VLTLRGTPDT GAASEEKGDT
310 320 330 340 350
AAALEDDNEG DKKKKDKKKK KTEKDEKEKE KKKGPSKSTV KAIQEALAKL
360 370 380 390 400
KEEEERQKRE EEERIKRLEE LEAKRKEEER LEQEKRERKK QKEKERKERL
410 420 430 440 450
KKEGKLLTKS QREARARAEV TLRHLQAQGV EVPSKDSLPK KRPVYEDKKK
460 470 480 490 500
KKTPQQLESK EVSETLEISA PVEAVDQGGP EKEETPPSVE PEEEEDTEDA
510 520 530 540 550
GLDDWEAMAS DEEREKEGNM IHIEVEENPE EEEEEEEEEE EEESEDEEEE
560 570 580 590 600
GDSEGSDGDE EDCKLSDEKD SGKAGDTKPS KDASSDSEYD SDDDRTKEER
610 620 630 640 650
AYDKAKRRIE KRRLEHGKNV NTEKLRAPII CVLGHVDTGK TKILDKLRHT
660 670 680 690 700
HVQDGEAGGI TQQIGATNVP LEAINEQTKM IKNFDRENVR IPGMLIIDTP
710 720 730 740 750
GHESFSNLRN RGSSLCDIAI LVVDIMHGLE PQTIESINIL KSKKCPFIVA
760 770 780 790 800
LNKIDRLYDW KKSPDSDVAV TLKKQKKNTK DEFEERAKAI IVEFAQQGLN
810 820 830 840 850
AALFYENKDP RTFVSLVPTS AHTGDGMGSL IYLLVELTQT MLSKRLAHCE
860 870 880 890 900
ELRAQVMEVK ALPGMGTTID VILINGRLKE GDTIIVPGVE GPIVTQIRGL
910 920 930 940 950
LLPPPMKELR VKNQYEKHKE VEAAQGVKIL GKDLEKTLAG LPLLVAYKDD
960 970 980 990 1000
EIPVLKDELI HELKQTLNAI KLEEKGVYVQ ASTLGSLEAL LEFLKTSEVP
1010 1020 1030 1040 1050
YAGINIGPVH KKDVMKASVM LEHDPQYAVI LAFDVRIERD AQEMADSLGV
1060 1070 1080 1090 1100
RIFSAEIIYH LFDAFTKYRQ DYKKQKQEEF KHIAVFPCKM KILPQYIFNS
1110 1120 1130 1140 1150
RDPIVIGVTV EAGQVKQGTP MCVPSKNFVD IGIVTSIEIN HKQVDVAKKG
1160 1170 1180 1190 1200
QEVCVKIEPI PGESPKMFGR HFEATDILVS KISRQSIDAL KDWFRDEMQK
1210
SDWQLIVELK KVFEII
Length:1,216
Mass (Da):137,616
Last modified:November 25, 2008 - v2
Checksum:i38D1C21648E4EAEC
GO

Sequence cautioni

The sequence AAH18347.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence AAH37150.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence AAH40746.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence AAH60288.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti121 – 1211D → N in BAE26259. (PubMed:16141072)Curated
Sequence conflicti188 – 1881G → C in BAE26259. (PubMed:16141072)Curated
Sequence conflicti254 – 2541M → L in BAE26259. (PubMed:16141072)Curated
Sequence conflicti302 – 3021A → V in BAE26259. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC114583 Genomic DNA. No translation available.
AK145146 mRNA. Translation: BAE26259.1.
AK145732 mRNA. Translation: BAE26614.1.
AK163527 mRNA. Translation: BAE37384.1.
BC018347 mRNA. Translation: AAH18347.1. Sequence problems.
BC037150 mRNA. Translation: AAH37150.1. Sequence problems.
BC040746 mRNA. Translation: AAH40746.1. Sequence problems.
BC060288 mRNA. Translation: AAH60288.1. Sequence problems.
CCDSiCCDS35544.1.
RefSeqiNP_938045.2. NM_198303.2.
UniGeneiMm.260943.

Genome annotation databases

EnsembliENSMUST00000027252; ENSMUSP00000027252; ENSMUSG00000026083.
GeneIDi226982.
KEGGimmu:226982.
UCSCiuc007aso.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC114583 Genomic DNA. No translation available.
AK145146 mRNA. Translation: BAE26259.1 .
AK145732 mRNA. Translation: BAE26614.1 .
AK163527 mRNA. Translation: BAE37384.1 .
BC018347 mRNA. Translation: AAH18347.1 . Sequence problems.
BC037150 mRNA. Translation: AAH37150.1 . Sequence problems.
BC040746 mRNA. Translation: AAH40746.1 . Sequence problems.
BC060288 mRNA. Translation: AAH60288.1 . Sequence problems.
CCDSi CCDS35544.1.
RefSeqi NP_938045.2. NM_198303.2.
UniGenei Mm.260943.

3D structure databases

ProteinModelPortali Q05D44.
SMRi Q05D44. Positions 624-1211.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 230580. 1 interaction.

PTM databases

PhosphoSitei Q05D44.

Proteomic databases

MaxQBi Q05D44.
PaxDbi Q05D44.
PRIDEi Q05D44.

Protocols and materials databases

DNASUi 226982.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000027252 ; ENSMUSP00000027252 ; ENSMUSG00000026083 .
GeneIDi 226982.
KEGGi mmu:226982.
UCSCi uc007aso.1. mouse.

Organism-specific databases

CTDi 9669.
MGIi MGI:2441772. Eif5b.

Phylogenomic databases

eggNOGi COG0532.
GeneTreei ENSGT00730000111064.
HOVERGENi HBG019036.
InParanoidi Q05D44.
KOi K03243.
OMAi GSLRMHT.
OrthoDBi EOG7034GC.
PhylomeDBi Q05D44.
TreeFami TF101535.

Miscellaneous databases

ChiTaRSi EIF5B. mouse.
NextBioi 378430.
PROi Q05D44.
SOURCEi Search...

Gene expression databases

Bgeei Q05D44.
ExpressionAtlasi Q05D44. baseline and differential.
Genevestigatori Q05D44.

Family and domain databases

Gene3Di 3.40.50.10050. 1 hit.
3.40.50.300. 1 hit.
InterProi IPR000795. EF_GTP-bd_dom.
IPR029459. EFTU-type.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR023115. TIF_IF2_dom3.
IPR009000. Transl_B-barrel.
IPR004161. Transl_elong_EFTu/EF1A_2.
[Graphical view ]
Pfami PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF14578. GTP_EFTU_D4. 1 hit.
PF11987. IF-2. 1 hit.
[Graphical view ]
PRINTSi PR00315. ELONGATNFCT.
SUPFAMi SSF50447. SSF50447. 1 hit.
SSF52156. SSF52156. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00231. small_GTP. 1 hit.
PROSITEi PS51722. G_TR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-771.
    Strain: C57BL/6J.
    Tissue: Corpora quadrigemina and Mammary gland.
  3. "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] OF 1-402.
    Strain: FVB/N.
    Tissue: Limb and Mammary tumor.
  4. "Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm."
    Bohnsack M.T., Regener K., Schwappach B., Saffrich R., Paraskeva E., Hartmann E., Goerlich D.
    EMBO J. 21:6205-6215(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  6. "A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
    Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
    J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187 AND SER-191, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Teratocarcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-137; SER-139; SER-187; SER-191 AND SER-215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 AND SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-137; SER-139 AND SER-215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiIF2P_MOUSE
AccessioniPrimary (citable) accession number: Q05D44
Secondary accession number(s): Q3SYI4
, Q3TQJ8, Q3UL37, Q3UM39, Q6PAI0, Q8CFF4, Q8CGD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: November 25, 2008
Last modified: October 29, 2014
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3