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O60869

- EDF1_HUMAN

UniProt

O60869 - EDF1_HUMAN

Protein

Endothelial differentiation-related factor 1

Gene

EDF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Transcriptional coactivator stimulating NR5A1 and ligand-dependent NR1H3/LXRA and PPARG transcriptional activities. Enhances the DNA-binding activity of ATF1, ATF2, CREB1 and NR5A1. Regulates nitric oxid synthase activity probably by sequestering calmodulin in the cytoplasm. May function in endothelial cells differentiation, hormone-induced cardiomyocytes hypertrophy and lipid metabolism.4 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi92 – 11120H-T-H motifPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. sequence-specific DNA binding Source: InterPro
    4. transcription coactivator activity Source: UniProtKB

    GO - Biological processi

    1. endothelial cell differentiation Source: UniProtKB
    2. multicellular organismal development Source: ProtInc
    3. positive regulation of DNA binding Source: UniProtKB
    4. positive regulation of transcription, DNA-templated Source: UniProtKB
    5. regulation of lipid metabolic process Source: UniProtKB
    6. regulation of transcription, DNA-templated Source: UniProtKB
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Developmental protein

    Keywords - Biological processi

    Differentiation, Transcription, Transcription regulation

    Keywords - Ligandi

    Calmodulin-binding, DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endothelial differentiation-related factor 1
    Short name:
    EDF-1
    Alternative name(s):
    Multiprotein-bridging factor 1
    Short name:
    MBF1
    Gene namesi
    Name:EDF1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:3164. EDF1.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Also nuclear upon binding to NR5A1 and treatment of cells with TPA or forskolin.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt
    3. intracellular Source: ProtInc
    4. nucleolus Source: HPA
    5. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi40 – 401T → D: Loss of interaction with CALM; when associated with D-58; D-91 and D-111. 1 Publication
    Mutagenesisi58 – 581T → D: Loss of interaction with CALM; when associated with D-40; D-91 and D-111. 1 Publication
    Mutagenesisi65 – 651T → D: No effect on CALM-binding. No effect; when associated with D-74. 1 Publication
    Mutagenesisi74 – 741T → D: No effect on CALM-binding. No effect; when associated with D-65. 1 Publication
    Mutagenesisi87 – 871S → A: No effect on CALM-binding. 1 Publication
    Mutagenesisi87 – 871S → D: Loss of interaction with CALM and higher affinity for TBP. Same effect; when associated with D-65 and D-74. 1 Publication
    Mutagenesisi91 – 911T → A: No effect on CALM-binding. 1 Publication
    Mutagenesisi91 – 911T → D: Partial loss of interaction with CALM. Complete loss of interaction; when associated with D-40; D-58 and D-111. 1 Publication
    Mutagenesisi111 – 1111S → D: Loss of interaction with CALM; when associated with D-40; D-58 and D-91. 1 Publication

    Organism-specific databases

    PharmGKBiPA27604.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 148147Endothelial differentiation-related factor 1PRO_0000149795Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications

    Post-translational modificationi

    Phosphorylated (by PKA and PKC).2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO60869.
    PaxDbiO60869.
    PeptideAtlasiO60869.
    PRIDEiO60869.

    PTM databases

    PhosphoSiteiO60869.

    Expressioni

    Tissue specificityi

    Expressed in brain, liver, lung, kidney and heart (at protein level). Ubiquitously expressed. More abundant in heart, pancreas, liver, intestine and adipose tissues.3 Publications

    Developmental stagei

    Expressed in fetal tissues. More abundant in kidney.1 Publication

    Inductioni

    Down-regulated by HIV-1 Tat or phorbol ester (TPA) treatment in endothelial cells (at mRNA and protein levels).1 Publication

    Gene expression databases

    BgeeiO60869.
    CleanExiHS_EDF1.
    GenevestigatoriO60869.

    Organism-specific databases

    HPAiHPA035642.

    Interactioni

    Subunit structurei

    Interacts with TBP and the transcription factor IID (TFIID) complex, NR5A2, NR1H3 and PPARG. Interaction with TBP is regulated by phosphorylation. Binds NR5A1, ATF1, FOS and JUN via their conserved basic region. Binding to calmodulin is regulated by calcium and phosphorylation of the IQ motif.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NR1H3Q131334EBI-781301,EBI-781356
    NR5A1Q047524EBI-781310,EBI-850837From a different organism.
    NR5A2O004822EBI-781301,EBI-781320
    NSP034952EBI-781301,EBI-2548993From a different organism.
    PPARGP372314EBI-781301,EBI-781384
    TBPP202262EBI-781310,EBI-355371

    Protein-protein interaction databases

    BioGridi114260. 13 interactions.
    IntActiO60869. 14 interactions.
    MINTiMINT-3000548.
    STRINGi9606.ENSP00000224073.

    Structurei

    Secondary structure

    1
    148
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi76 – 8611
    Turni87 – 893
    Helixi92 – 998
    Helixi103 – 1119
    Helixi118 – 12811
    Turni135 – 1384
    Beta strandi140 – 1434

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X57NMR-A71-148[»]
    ProteinModelPortaliO60869.
    SMRiO60869. Positions 71-148.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO60869.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini81 – 13555HTH cro/C1-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni37 – 11377Interaction with NR5A2, PPARG and NR1H3Add
    BLAST
    Regioni69 – 10840Interaction with TBP and NR5A1Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi81 – 888IQ motif

    Domaini

    The IQ motif, which is involved in calmodulin binding, overlaps with the binding domain for nuclear receptors and transcription factors. Its phosphorylation probably allows a switch between the two activities of the protein By similarity.By similarity

    Sequence similaritiesi

    Contains 1 HTH cro/C1-type DNA-binding domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1813.
    HOGENOMiHOG000195726.
    HOVERGENiHBG051440.
    InParanoidiO60869.
    KOiK03627.
    OMAiTKVNEKP.
    OrthoDBiEOG7RFTJZ.
    PhylomeDBiO60869.
    TreeFamiTF300064.

    Family and domain databases

    Gene3Di1.10.260.40. 1 hit.
    InterProiIPR001387. Cro/C1-type_HTH.
    IPR010982. Lambda_DNA-bd_dom.
    IPR013729. MBF1_N.
    [Graphical view]
    PfamiPF01381. HTH_3. 1 hit.
    PF08523. MBF1. 1 hit.
    [Graphical view]
    SMARTiSM00530. HTH_XRE. 1 hit.
    [Graphical view]
    SUPFAMiSSF47413. SSF47413. 1 hit.
    PROSITEiPS50943. HTH_CROC1. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O60869-1) [UniParc]FASTAAdd to Basket

    Also known as: Alpha

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAESDWDTVT VLRKKGPTAA QAKSKQAILA AQRRGEDVET SKKWAAGQNK    50
    QHSITKNTAK LDRETEELHH DRVTLEVGKV IQQGRQSKGL TQKDLATKIN 100
    EKPQVIADYE SGRAIPNNQV LGKIERAIGL KLRGKDIGKP IEKGPRAK 148
    Length:148
    Mass (Da):16,369
    Last modified:August 1, 1998 - v1
    Checksum:iADC2C5384BF85C11
    GO
    Isoform 2 (identifier: O60869-2) [UniParc]FASTAAdd to Basket

    Also known as: Beta

    The sequence of this isoform differs from the canonical sequence as follows:
         130-148: LKLRGKDIGKPIEKGPRAK → ECPSTLRRVR

    Show »
    Length:139
    Mass (Da):15,481
    Checksum:i9F30DE6890D7E801
    GO
    Isoform 3 (identifier: O60869-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         129-148: GLKLRGKDIGKPIEKGPRAK → DVGTRSARVLRAQ

    Note: No experimental confirmation available. Gene prediction based on EST data.

    Show »
    Length:141
    Mass (Da):15,636
    Checksum:iE31C8E26A4679A23
    GO

    Sequence cautioni

    The sequence CAI12698.1 differs from that shown. Reason: Erroneous gene model prediction.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei129 – 14820GLKLR…GPRAK → DVGTRSARVLRAQ in isoform 3. CuratedVSP_054701Add
    BLAST
    Alternative sequencei130 – 14819LKLRG…GPRAK → ECPSTLRRVR in isoform 2. 1 PublicationVSP_013336Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ005259 mRNA. Translation: CAA06446.1.
    AB002282 mRNA. Translation: BAA88073.1.
    AB002283 mRNA. Translation: BAA88074.1.
    CR541914 mRNA. Translation: CAG46712.1.
    BT009863 mRNA. Translation: AAP88865.1.
    AL355987 Genomic DNA. Translation: CAI12697.1.
    AL355987 Genomic DNA. Translation: CAI12698.1. Sequence problems.
    AL355987 Genomic DNA. Translation: CAI12699.1.
    BC015500 mRNA. Translation: AAH15500.1.
    CCDSiCCDS65193.1. [O60869-3]
    CCDS7011.1. [O60869-1]
    CCDS7012.1. [O60869-2]
    RefSeqiNP_001268226.1. NM_001281297.1. [O60869-3]
    NP_001268227.1. NM_001281298.1.
    NP_001268228.1. NM_001281299.1.
    NP_003783.1. NM_003792.3. [O60869-1]
    NP_694880.1. NM_153200.2. [O60869-2]
    UniGeneiHs.174050.

    Genome annotation databases

    EnsembliENST00000224073; ENSP00000224073; ENSG00000107223. [O60869-1]
    ENST00000371648; ENSP00000360711; ENSG00000107223. [O60869-2]
    ENST00000371649; ENSP00000360712; ENSG00000107223. [O60869-3]
    GeneIDi8721.
    KEGGihsa:8721.
    UCSCiuc004cjt.1. human. [O60869-1]
    uc004cju.1. human. [O60869-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ005259 mRNA. Translation: CAA06446.1 .
    AB002282 mRNA. Translation: BAA88073.1 .
    AB002283 mRNA. Translation: BAA88074.1 .
    CR541914 mRNA. Translation: CAG46712.1 .
    BT009863 mRNA. Translation: AAP88865.1 .
    AL355987 Genomic DNA. Translation: CAI12697.1 .
    AL355987 Genomic DNA. Translation: CAI12698.1 . Sequence problems.
    AL355987 Genomic DNA. Translation: CAI12699.1 .
    BC015500 mRNA. Translation: AAH15500.1 .
    CCDSi CCDS65193.1. [O60869-3 ]
    CCDS7011.1. [O60869-1 ]
    CCDS7012.1. [O60869-2 ]
    RefSeqi NP_001268226.1. NM_001281297.1. [O60869-3 ]
    NP_001268227.1. NM_001281298.1.
    NP_001268228.1. NM_001281299.1.
    NP_003783.1. NM_003792.3. [O60869-1 ]
    NP_694880.1. NM_153200.2. [O60869-2 ]
    UniGenei Hs.174050.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X57 NMR - A 71-148 [» ]
    ProteinModelPortali O60869.
    SMRi O60869. Positions 71-148.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114260. 13 interactions.
    IntActi O60869. 14 interactions.
    MINTi MINT-3000548.
    STRINGi 9606.ENSP00000224073.

    PTM databases

    PhosphoSitei O60869.

    Proteomic databases

    MaxQBi O60869.
    PaxDbi O60869.
    PeptideAtlasi O60869.
    PRIDEi O60869.

    Protocols and materials databases

    DNASUi 8721.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000224073 ; ENSP00000224073 ; ENSG00000107223 . [O60869-1 ]
    ENST00000371648 ; ENSP00000360711 ; ENSG00000107223 . [O60869-2 ]
    ENST00000371649 ; ENSP00000360712 ; ENSG00000107223 . [O60869-3 ]
    GeneIDi 8721.
    KEGGi hsa:8721.
    UCSCi uc004cjt.1. human. [O60869-1 ]
    uc004cju.1. human. [O60869-2 ]

    Organism-specific databases

    CTDi 8721.
    GeneCardsi GC09M139756.
    HGNCi HGNC:3164. EDF1.
    HPAi HPA035642.
    MIMi 605107. gene.
    neXtProti NX_O60869.
    PharmGKBi PA27604.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1813.
    HOGENOMi HOG000195726.
    HOVERGENi HBG051440.
    InParanoidi O60869.
    KOi K03627.
    OMAi TKVNEKP.
    OrthoDBi EOG7RFTJZ.
    PhylomeDBi O60869.
    TreeFami TF300064.

    Miscellaneous databases

    EvolutionaryTracei O60869.
    GeneWikii EDF1.
    GenomeRNAii 8721.
    NextBioi 32709.
    PROi O60869.
    SOURCEi Search...

    Gene expression databases

    Bgeei O60869.
    CleanExi HS_EDF1.
    Genevestigatori O60869.

    Family and domain databases

    Gene3Di 1.10.260.40. 1 hit.
    InterProi IPR001387. Cro/C1-type_HTH.
    IPR010982. Lambda_DNA-bd_dom.
    IPR013729. MBF1_N.
    [Graphical view ]
    Pfami PF01381. HTH_3. 1 hit.
    PF08523. MBF1. 1 hit.
    [Graphical view ]
    SMARTi SM00530. HTH_XRE. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47413. SSF47413. 1 hit.
    PROSITEi PS50943. HTH_CROC1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "EDF-1, a novel gene product down-regulated in human endothelial cell differentiation."
      Dragoni I., Mariotti M., Consalez G.G., Soria M.R., Maier J.A.M.
      J. Biol. Chem. 273:31119-31124(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION, FUNCTION.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, INTERACTION WITH TBP; NR5A1; FOS; JUN AND ATF1, SUBCELLULAR LOCATION, FUNCTION.
    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 (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 1).
      Tissue: Pancreas.
    7. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-13 AND 99-113, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma.
    8. "Interaction between endothelial differentiation-related factor-1 and calmodulin in vitro and in vivo."
      Mariotti M., De Benedictis L., Avon E., Maier J.A.M.
      J. Biol. Chem. 275:24047-24051(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CALM AND TBP, MUTAGENESIS OF THR-40; THR-58; THR-91 AND SER-111, PHOSPHORYLATION, SUBCELLULAR LOCATION.
    9. "Multiprotein bridging factor-1 (MBF-1) is a cofactor for nuclear receptors that regulate lipid metabolism."
      Brendel C., Gelman L., Auwerx J.
      Mol. Endocrinol. 16:1367-1377(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NR5A2; NR1H3; PPARG AND TFIID COMPLEX, TISSUE SPECIFICITY, FUNCTION.
    10. "The dual role of endothelial differentiation-related factor-1 in the cytosol and nucleus: modulation by protein kinase A."
      Ballabio E., Mariotti M., De Benedictis L., Maier J.A.M.
      Cell. Mol. Life Sci. 61:1069-1074(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF THR-65; THR-74 AND SER-87, INTERACTION WITH TBP AND CALM, PHOSPHORYLATION, SUBCELLULAR LOCATION, FUNCTION.
    11. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Solution structures of the HTH domain of human EDF-1 protein."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 71-148.

    Entry informationi

    Entry nameiEDF1_HUMAN
    AccessioniPrimary (citable) accession number: O60869
    Secondary accession number(s): Q5T5T2, Q9UIM1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 12, 2005
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 126 of the entry and version 1 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 9
      Human chromosome 9: 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