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O60841

- IF2P_HUMAN

UniProt

O60841 - IF2P_HUMAN

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
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 4 (24 Nov 2009)
      Previous versions | rss
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    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. protein binding Source: IntAct
    5. 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

    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

    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

    ArrayExpressiO60841.
    BgeeiO60841.
    CleanExiHS_EIF5B.
    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. 20 interactions.
    IntActiO60841. 14 interactions.
    MINTiMINT-3000520.
    STRINGi9606.ENSP00000289371.

    Structurei

    3D structure databases

    ProteinModelPortaliO60841.
    SMRiO60841. Positions 600-1199.
    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.
    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

    MGKKQKNKSE DSTKDDIDLD ALAAEIEGAG AAKEQEPQKS KGKKKKEKKK     50
    QDFDEDDILK ELEELSLEAQ GIKADRETVA VKPTENNEEE FTSKDKKKKG 100
    QKGKKQSFDD NDSEELEDKD SKSKKTAKPK VEMYSGSDDD DDFNKLPKKA 150
    KGKAQKSNKK WDGSEEDEDN SKKIKERSRI NSSGESGDES DEFLQSRKGQ 200
    KKNQKNKPGP NIESGNEDDD ASFKIKTVAQ KKAEKKERER KKRDEEKAKL 250
    RKLKEKEELE TGKKDQSKQK ESQRKFEEET VKSKVTVDTG VIPASEEKAE 300
    TPTAAEDDNE GDKKKKDKKK KKGEKEEKEK EKKKGPSKAT VKAMQEALAK 350
    LKEEEERQKR EEEERIKRLE ELEAKRKEEE RLEQEKRERK KQKEKERKER 400
    LKKEGKLLTK SQREARARAE ATLKLLQAQG VEVPSKDSLP KKRPIYEDKK 450
    RKKIPQQLES KEVSESMELC AAVEVMEQGV PEKEETPPPV EPEEEEDTED 500
    AGLDDWEAMA SDEETEKVEG NKVHIEVKEN PEEEEEEEEE EEEDEESEEE 550
    EEEEGESEGS EGDEEDEKVS DEKDSGKTLD KKPSKEMSSD SEYDSDDDRT 600
    KEERAYDKAK RRIEKRRLEH SKNVNTEKLR APIICVLGHV DTGKTKILDK 650
    LRHTHVQDGE AGGITQQIGA TNVPLEAINE QTKMIKNFDR ENVRIPGMLI 700
    IDTPGHESFS NLRNRGSSLC DIAILVVDIM HGLEPQTIES INLLKSKKCP 750
    FIVALNKIDR LYDWKKSPDS DVAATLKKQK KNTKDEFEER AKAIIVEFAQ 800
    QGLNAALFYE NKDPRTFVSL VPTSAHTGDG MGSLIYLLVE LTQTMLSKRL 850
    AHCEELRAQV MEVKALPGMG TTIDVILING RLKEGDTIIV PGVEGPIVTQ 900
    IRGLLLPPPM KELRVKNQYE KHKEVEAAQG VKILGKDLEK TLAGLPLLVA 950
    YKEDEIPVLK DELIHELKQT LNAIKLEEKG VYVQASTLGS LEALLEFLKT 1000
    SEVPYAGINI GPVHKKDVMK ASVMLEHDPQ YAVILAFDVR IERDAQEMAD 1050
    SLGVRIFSAE IIYHLFDAFT KYRQDYKKQK QEEFKHIAVF PCKIKILPQY 1100
    IFNSRDPIVM GVTVEAGQVK QGTPMCVPSK NFVDIGIVTS IEINHKQVDV 1150
    AKKGQEVCVK IEPIPGESPK MFGRHFEATD ILVSKISRQS IDALKDWFRD 1200
    EMQKSDWQLI VELKKVFEII 1220
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 600-1199.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115024. 20 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.
    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

    ArrayExpressi O60841.
    Bgeei O60841.
    CleanExi HS_EIF5B.
    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

    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: October 1, 2014
    This is version 142 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