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O60841

- IF2P_HUMAN

UniProt

O60841 - IF2P_HUMAN

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Protein

Eukaryotic translation initiation factor 5B

Gene

EIF5B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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 bindingi638 – 6458GTPBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. gene expression Source: Reactome
  3. regulation of translational initiation Source: UniProtKB
  4. translation Source: Reactome
  5. translational initiation Source: Reactome
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.

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, KIAA0741
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:30793. EIF5B.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi640 – 6401V → G: Loss of activity in vivo. Retains full activity in vitro. 1 Publication
Mutagenesisi706 – 7061H → E: Loss of activity; both in vivo and in vitro. 1 Publication
Mutagenesisi706 – 7061H → Q: Loss of activity in vivo. Partial activity in vitro. 1 Publication
Mutagenesisi759 – 7591D → N: Loss of activity; both in vivo and in vitro. 1 Publication

Organism-specific databases

PharmGKBiPA134864457.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12201220Eukaryotic translation initiation factor 5BPRO_0000137294Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei107 – 1071Phosphoserine4 Publications
Modified residuei113 – 1131Phosphoserine6 Publications
Modified residuei134 – 1341Phosphotyrosine3 Publications
Modified residuei135 – 1351Phosphoserine4 Publications
Modified residuei137 – 1371Phosphoserine4 Publications
Modified residuei164 – 1641Phosphoserine6 Publications
Modified residuei171 – 1711Phosphoserine1 Publication
Modified residuei182 – 1821Phosphoserine3 Publications
Modified residuei183 – 1831Phosphoserine2 Publications
Modified residuei186 – 1861Phosphoserine3 Publications
Modified residuei190 – 1901Phosphoserine4 Publications
Modified residuei214 – 2141Phosphoserine7 Publications
Modified residuei301 – 3011Phosphothreonine2 Publications
Modified residuei498 – 4981Phosphothreonine1 Publication
Modified residuei547 – 5471Phosphoserine1 Publication
Modified residuei560 – 5601Phosphoserine1 Publication
Modified residuei588 – 5881Phosphoserine2 Publications
Modified residuei589 – 5891Phosphoserine1 Publication
Modified residuei591 – 5911Phosphoserine1 Publication
Modified residuei595 – 5951Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO60841.
PaxDbiO60841.
PRIDEiO60841.

PTM databases

PhosphoSiteiO60841.

Miscellaneous databases

PMAP-CutDBO60841.

Expressioni

Gene expression databases

BgeeiO60841.
CleanExiHS_EIF5B.
ExpressionAtlasiO60841. baseline and differential.
GenevestigatoriO60841.

Organism-specific databases

HPAiHPA034648.
HPA040095.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
EIF1AYO146022EBI-928530,EBI-286439
ETS1P149212EBI-928530,EBI-913209

Protein-protein interaction databases

BioGridi115024. 25 interactions.
IntActiO60841. 14 interactions.
MINTiMINT-3000520.
STRINGi9606.ENSP00000289371.

Structurei

3D structure databases

ProteinModelPortaliO60841.
SMRiO60841. Positions 594-1219.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini629 – 846218tr-type GPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni638 – 6458G1PROSITE-ProRule annotation
Regioni663 – 6675G2PROSITE-ProRule annotation
Regioni702 – 7054G3PROSITE-ProRule annotation
Regioni756 – 7594G4PROSITE-ProRule annotation
Regioni824 – 8263G5PROSITE-ProRule annotation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi39 – 5012Poly-LysAdd
BLAST
Compositional biasi94 – 996Poly-Lys
Compositional biasi138 – 1425Poly-Asp
Compositional biasi313 – 32210Poly-Lys
Compositional biasi353 – 3564Poly-Glu
Compositional biasi361 – 3644Poly-Glu
Compositional biasi491 – 4966Poly-Glu
Compositional biasi529 – 56739Asp/Glu-rich (acidic)Add
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.
HOGENOMiHOG000105770.
HOVERGENiHBG019036.
InParanoidiO60841.
KOiK03243.
OMAiGSLRMHT.
OrthoDBiEOG7034GC.
PhylomeDBiO60841.
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.

O60841-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGKKQKNKSE DSTKDDIDLD ALAAEIEGAG AAKEQEPQKS KGKKKKEKKK
60 70 80 90 100
QDFDEDDILK ELEELSLEAQ GIKADRETVA VKPTENNEEE FTSKDKKKKG
110 120 130 140 150
QKGKKQSFDD NDSEELEDKD SKSKKTAKPK VEMYSGSDDD DDFNKLPKKA
160 170 180 190 200
KGKAQKSNKK WDGSEEDEDN SKKIKERSRI NSSGESGDES DEFLQSRKGQ
210 220 230 240 250
KKNQKNKPGP NIESGNEDDD ASFKIKTVAQ KKAEKKERER KKRDEEKAKL
260 270 280 290 300
RKLKEKEELE TGKKDQSKQK ESQRKFEEET VKSKVTVDTG VIPASEEKAE
310 320 330 340 350
TPTAAEDDNE GDKKKKDKKK KKGEKEEKEK EKKKGPSKAT VKAMQEALAK
360 370 380 390 400
LKEEEERQKR EEEERIKRLE ELEAKRKEEE RLEQEKRERK KQKEKERKER
410 420 430 440 450
LKKEGKLLTK SQREARARAE ATLKLLQAQG VEVPSKDSLP KKRPIYEDKK
460 470 480 490 500
RKKIPQQLES KEVSESMELC AAVEVMEQGV PEKEETPPPV EPEEEEDTED
510 520 530 540 550
AGLDDWEAMA SDEETEKVEG NKVHIEVKEN PEEEEEEEEE EEEDEESEEE
560 570 580 590 600
EEEEGESEGS EGDEEDEKVS DEKDSGKTLD KKPSKEMSSD SEYDSDDDRT
610 620 630 640 650
KEERAYDKAK RRIEKRRLEH SKNVNTEKLR APIICVLGHV DTGKTKILDK
660 670 680 690 700
LRHTHVQDGE AGGITQQIGA TNVPLEAINE QTKMIKNFDR ENVRIPGMLI
710 720 730 740 750
IDTPGHESFS NLRNRGSSLC DIAILVVDIM HGLEPQTIES INLLKSKKCP
760 770 780 790 800
FIVALNKIDR LYDWKKSPDS DVAATLKKQK KNTKDEFEER AKAIIVEFAQ
810 820 830 840 850
QGLNAALFYE NKDPRTFVSL VPTSAHTGDG MGSLIYLLVE LTQTMLSKRL
860 870 880 890 900
AHCEELRAQV MEVKALPGMG TTIDVILING RLKEGDTIIV PGVEGPIVTQ
910 920 930 940 950
IRGLLLPPPM KELRVKNQYE KHKEVEAAQG VKILGKDLEK TLAGLPLLVA
960 970 980 990 1000
YKEDEIPVLK DELIHELKQT LNAIKLEEKG VYVQASTLGS LEALLEFLKT
1010 1020 1030 1040 1050
SEVPYAGINI GPVHKKDVMK ASVMLEHDPQ YAVILAFDVR IERDAQEMAD
1060 1070 1080 1090 1100
SLGVRIFSAE IIYHLFDAFT KYRQDYKKQK QEEFKHIAVF PCKIKILPQY
1110 1120 1130 1140 1150
IFNSRDPIVM GVTVEAGQVK QGTPMCVPSK NFVDIGIVTS IEINHKQVDV
1160 1170 1180 1190 1200
AKKGQEVCVK IEPIPGESPK MFGRHFEATD ILVSKISRQS IDALKDWFRD
1210 1220
EMQKSDWQLI VELKKVFEII
Length:1,220
Mass (Da):138,827
Last modified:November 24, 2009 - v4
Checksum:i454C29FB90AA768E
GO

Sequence cautioni

The sequence BAA34461.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641E → G in BAA34461. (PubMed:9872452)Curated
Sequence conflicti92 – 921T → I in CAB44357. (PubMed:10432305)Curated
Sequence conflicti180 – 1801I → M in AAD16006. (PubMed:10200264)Curated
Sequence conflicti256 – 2561K → R in AAD16006. (PubMed:10200264)Curated
Sequence conflicti549 – 5491E → V in AAD16006. (PubMed:10200264)Curated
Sequence conflicti669 – 6691G → W in AAD16006. (PubMed:10200264)Curated
Sequence conflicti894 – 8941E → K in CAB44357. (PubMed:10432305)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti337 – 3371S → G.
Corresponds to variant rs10642 [ dbSNP | Ensembl ].
VAR_055954
Natural varianti360 – 3601R → G.
Corresponds to variant rs3205296 [ dbSNP | Ensembl ].
VAR_055955
Natural varianti522 – 5221K → T.3 Publications
Corresponds to variant rs7558074 [ dbSNP | Ensembl ].
VAR_060587

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS42721.1.
PIRiT43483.
RefSeqiNP_056988.3. NM_015904.3.
UniGeneiHs.158688.

Genome annotation databases

EnsembliENST00000289371; ENSP00000289371; ENSG00000158417.
GeneIDi9669.
KEGGihsa:9669.
UCSCiuc002tab.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS42721.1.
PIRi T43483.
RefSeqi NP_056988.3. NM_015904.3.
UniGenei Hs.158688.

3D structure databases

ProteinModelPortali O60841.
SMRi O60841. Positions 594-1219.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115024. 25 interactions.
IntActi O60841. 14 interactions.
MINTi MINT-3000520.
STRINGi 9606.ENSP00000289371.

PTM databases

PhosphoSitei O60841.

Proteomic databases

MaxQBi O60841.
PaxDbi O60841.
PRIDEi O60841.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000289371 ; ENSP00000289371 ; ENSG00000158417 .
GeneIDi 9669.
KEGGi hsa:9669.
UCSCi uc002tab.3. human.

Organism-specific databases

CTDi 9669.
GeneCardsi GC02P099953.
H-InvDB HIX0002308.
HGNCi HGNC:30793. EIF5B.
HPAi HPA034648.
HPA040095.
MIMi 606086. gene.
neXtProti NX_O60841.
PharmGKBi PA134864457.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0532.
GeneTreei ENSGT00730000111064.
HOGENOMi HOG000105770.
HOVERGENi HBG019036.
InParanoidi O60841.
KOi K03243.
OMAi GSLRMHT.
OrthoDBi EOG7034GC.
PhylomeDBi O60841.
TreeFami TF101535.

Enzyme and pathway databases

Reactomei REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.

Miscellaneous databases

ChiTaRSi EIF5B. human.
GeneWikii EIF5B.
GenomeRNAii 9669.
NextBioi 36307.
PMAP-CutDB O60841.
PROi O60841.
SOURCEi Search...

Gene expression databases

Bgeei O60841.
CleanExi HS_EIF5B.
ExpressionAtlasi O60841. baseline and differential.
Genevestigatori O60841.

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. "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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma.
  6. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  13. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "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].
  16. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-522, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiIF2P_HUMAN
AccessioniPrimary (citable) accession number: O60841
Secondary accession number(s): O95805
, Q53RV7, Q53SI8, Q9UF81, Q9UMN7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 24, 2009
Last modified: November 26, 2014
This is version 144 of the entry and version 4 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3