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P24534

- EF1B_HUMAN

UniProt

P24534 - EF1B_HUMAN

Protein

Elongation factor 1-beta

Gene

EEF1B2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP.

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. translation elongation factor activity Source: UniProtKB

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. gene expression Source: Reactome
    3. translation Source: Reactome
    4. translational elongation Source: UniProtKB

    Keywords - Molecular functioni

    Elongation factor

    Keywords - Biological processi

    Protein biosynthesis

    Enzyme and pathway databases

    ReactomeiREACT_1477. Eukaryotic Translation Elongation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elongation factor 1-beta
    Short name:
    EF-1-beta
    Gene namesi
    Name:EEF1B2
    Synonyms:EEF1B, EF1B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:3208. EEF1B2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. eukaryotic translation elongation factor 1 complex Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27644.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 225224Elongation factor 1-betaPRO_0000155021Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei7 – 71N6-acetyllysine1 Publication
    Modified residuei8 – 81Phosphoserine3 Publications
    Modified residuei93 – 931Phosphothreonine1 Publication
    Modified residuei95 – 951Phosphoserine4 Publications
    Modified residuei106 – 1061Phosphoserine10 Publications

    Post-translational modificationi

    Phosphorylation affects the GDP/GTP exchange rate.10 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP24534.
    PaxDbiP24534.
    PeptideAtlasiP24534.
    PRIDEiP24534.

    2D gel databases

    DOSAC-COBS-2DPAGEP24534.
    OGPiP24534.
    SWISS-2DPAGEP24534.

    PTM databases

    PhosphoSiteiP24534.

    Miscellaneous databases

    PMAP-CutDBP24534.

    Expressioni

    Inductioni

    By homocysteine (HC), may mediate accelerated synthesis of free thiol-containing proteins in response to HC-induced oxidative stress.1 Publication

    Gene expression databases

    ArrayExpressiP24534.
    BgeeiP24534.
    CleanExiHS_EEF1B2.
    GenevestigatoriP24534.

    Organism-specific databases

    HPAiCAB012477.
    HPA035029.

    Interactioni

    Subunit structurei

    EF-1 is composed of 4 subunits: alpha, beta, delta, and gamma.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EEF1GP266413EBI-354334,EBI-351467

    Protein-protein interaction databases

    BioGridi108253. 46 interactions.
    IntActiP24534. 22 interactions.
    MINTiMINT-4999956.
    STRINGi9606.ENSP00000236957.

    Structurei

    Secondary structure

    1
    225
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi140 – 15011
    Helixi155 – 16410
    Beta strandi171 – 18313
    Beta strandi185 – 1939
    Helixi200 – 2078
    Turni211 – 2133
    Beta strandi214 – 2207

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B64NMR-A136-225[»]
    ProteinModelPortaliP24534.
    SMRiP24534. Positions 10-69, 136-225.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP24534.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 8483GST C-terminalAdd
    BLAST

    Sequence similaritiesi

    Belongs to the EF-1-beta/EF-1-delta family.Curated
    Contains 1 GST C-terminal domain.Curated

    Phylogenomic databases

    eggNOGiCOG2092.
    HOGENOMiHOG000207273.
    HOVERGENiHBG000787.
    InParanoidiP24534.
    KOiK03232.
    OMAiVRAIEMD.
    OrthoDBiEOG7RZ5QW.
    PhylomeDBiP24534.
    TreeFamiTF313134.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.30.70.60. 1 hit.
    InterProiIPR018940. EF-1_beta_acid_region_euk.
    IPR010987. Glutathione-S-Trfase_C-like.
    IPR014717. Transl_elong_EF1B/ribosomal_S6.
    IPR001326. Transl_elong_EF1B_B/D_CS.
    IPR014038. Transl_elong_fac_EF1B_bsu/dsu.
    [Graphical view]
    PfamiPF10587. EF-1_beta_acid. 1 hit.
    PF00736. EF1_GNE. 1 hit.
    [Graphical view]
    SMARTiSM00888. EF1_GNE. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF54984. SSF54984. 1 hit.
    PROSITEiPS00824. EF1BD_1. 1 hit.
    PS00825. EF1BD_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P24534-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGFGDLKSPA GLQVLNDYLA DKSYIEGYVP SQADVAVFEA VSSPPPADLC    50
    HALRWYNHIK SYEKEKASLP GVKKALGKYG PADVEDTTGS GATDSKDDDD 100
    IDLFGSDDEE ESEEAKRLRE ERLAQYESKK AKKPALVAKS SILLDVKPWD 150
    DETDMAKLEE CVRSIQADGL VWGSSKLVPV GYGIKKLQIQ CVVEDDKVGT 200
    DMLEEQITAF EDYVQSMDVA AFNKI 225
    Length:225
    Mass (Da):24,764
    Last modified:January 23, 2007 - v3
    Checksum:iCDE763ADBF127822
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60489 mRNA. Translation: CAA43019.1.
    X60656 mRNA. Translation: CAA43063.1.
    BT007079 mRNA. Translation: AAP35742.1.
    CR456825 mRNA. Translation: CAG33106.1.
    AK291910 mRNA. Translation: BAF84599.1.
    AC007383 Genomic DNA. Translation: AAY15062.1.
    CH471063 Genomic DNA. Translation: EAW70381.1.
    BC000211 mRNA. Translation: AAH00211.1.
    BC004931 mRNA. Translation: AAH04931.1.
    BC067787 mRNA. Translation: AAH67787.1.
    CCDSiCCDS2367.1.
    PIRiS25432.
    RefSeqiNP_001032752.1. NM_001037663.1.
    NP_001950.1. NM_001959.3.
    NP_066944.1. NM_021121.3.
    UniGeneiHs.421608.

    Genome annotation databases

    EnsembliENST00000236957; ENSP00000236957; ENSG00000114942.
    ENST00000392221; ENSP00000376055; ENSG00000114942.
    ENST00000392222; ENSP00000376056; ENSG00000114942.
    GeneIDi1933.
    KEGGihsa:1933.
    UCSCiuc002vbf.1. human.

    Polymorphism databases

    DMDMi119163.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60489 mRNA. Translation: CAA43019.1 .
    X60656 mRNA. Translation: CAA43063.1 .
    BT007079 mRNA. Translation: AAP35742.1 .
    CR456825 mRNA. Translation: CAG33106.1 .
    AK291910 mRNA. Translation: BAF84599.1 .
    AC007383 Genomic DNA. Translation: AAY15062.1 .
    CH471063 Genomic DNA. Translation: EAW70381.1 .
    BC000211 mRNA. Translation: AAH00211.1 .
    BC004931 mRNA. Translation: AAH04931.1 .
    BC067787 mRNA. Translation: AAH67787.1 .
    CCDSi CCDS2367.1.
    PIRi S25432.
    RefSeqi NP_001032752.1. NM_001037663.1.
    NP_001950.1. NM_001959.3.
    NP_066944.1. NM_021121.3.
    UniGenei Hs.421608.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B64 NMR - A 136-225 [» ]
    ProteinModelPortali P24534.
    SMRi P24534. Positions 10-69, 136-225.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108253. 46 interactions.
    IntActi P24534. 22 interactions.
    MINTi MINT-4999956.
    STRINGi 9606.ENSP00000236957.

    PTM databases

    PhosphoSitei P24534.

    Polymorphism databases

    DMDMi 119163.

    2D gel databases

    DOSAC-COBS-2DPAGE P24534.
    OGPi P24534.
    SWISS-2DPAGE P24534.

    Proteomic databases

    MaxQBi P24534.
    PaxDbi P24534.
    PeptideAtlasi P24534.
    PRIDEi P24534.

    Protocols and materials databases

    DNASUi 1933.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000236957 ; ENSP00000236957 ; ENSG00000114942 .
    ENST00000392221 ; ENSP00000376055 ; ENSG00000114942 .
    ENST00000392222 ; ENSP00000376056 ; ENSG00000114942 .
    GeneIDi 1933.
    KEGGi hsa:1933.
    UCSCi uc002vbf.1. human.

    Organism-specific databases

    CTDi 1933.
    GeneCardsi GC02P207024.
    HGNCi HGNC:3208. EEF1B2.
    HPAi CAB012477.
    HPA035029.
    MIMi 600655. gene.
    neXtProti NX_P24534.
    PharmGKBi PA27644.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2092.
    HOGENOMi HOG000207273.
    HOVERGENi HBG000787.
    InParanoidi P24534.
    KOi K03232.
    OMAi VRAIEMD.
    OrthoDBi EOG7RZ5QW.
    PhylomeDBi P24534.
    TreeFami TF313134.

    Enzyme and pathway databases

    Reactomei REACT_1477. Eukaryotic Translation Elongation.

    Miscellaneous databases

    ChiTaRSi EEF1B2. human.
    EvolutionaryTracei P24534.
    GeneWikii EEF1B2.
    GenomeRNAii 1933.
    NextBioi 7829.
    PMAP-CutDB P24534.
    PROi P24534.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P24534.
    Bgeei P24534.
    CleanExi HS_EEF1B2.
    Genevestigatori P24534.

    Family and domain databases

    Gene3Di 1.20.1050.10. 1 hit.
    3.30.70.60. 1 hit.
    InterProi IPR018940. EF-1_beta_acid_region_euk.
    IPR010987. Glutathione-S-Trfase_C-like.
    IPR014717. Transl_elong_EF1B/ribosomal_S6.
    IPR001326. Transl_elong_EF1B_B/D_CS.
    IPR014038. Transl_elong_fac_EF1B_bsu/dsu.
    [Graphical view ]
    Pfami PF10587. EF-1_beta_acid. 1 hit.
    PF00736. EF1_GNE. 1 hit.
    [Graphical view ]
    SMARTi SM00888. EF1_GNE. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47616. SSF47616. 1 hit.
    SSF54984. SSF54984. 1 hit.
    PROSITEi PS00824. EF1BD_1. 1 hit.
    PS00825. EF1BD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of human elongation factor-1 beta cDNA."
      Sanders J., Maassen J.A., Amons R., Moeller W.
      Nucleic Acids Res. 19:4551-4551(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Skin fibroblast.
    2. "Human elongation factor 1 beta: cDNA and derived amino acid sequence."
      von der Kammer H., Klaudiny J., Zimmer M., Scheit K.H.
      Biochem. Biophys. Res. Commun. 177:312-317(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Ovarian granulosa cell.
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "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].
    6. "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].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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, Eye and Pancreas.
    9. "Human liver protein map: a reference database established by microsequencing and gel comparison."
      Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
      Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-11.
      Tissue: Liver.
    10. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 8-22; 140-157 AND 164-176, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain cortex.
    11. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
      Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
      Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 55-60; 79-85; 123-127 AND 164-175.
      Tissue: Keratinocyte.
    12. "Induction of acute translational response genes by homocysteine. Elongation factors-1alpha, -beta, and -delta."
      Chacko G., Ling Q., Hajjar K.A.
      J. Biol. Chem. 273:19840-19846(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY HOMOCYSTEINE.
    13. "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-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Prostate cancer.
    15. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
      Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
      Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    16. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-95 AND SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "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-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    19. "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].
    20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "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-8; SER-95 AND SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    22. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-7, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "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-95 AND SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "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-8; THR-93; SER-95 AND SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiEF1B_HUMAN
    AccessioniPrimary (citable) accession number: P24534
    Secondary accession number(s): A8K795, Q6IBH9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 167 of the entry and version 3 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3