SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O60869

- EDF1_HUMAN

UniProt

O60869 - EDF1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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 motif Reviewed prediction
Add
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
Complete GO annotation...

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
Complete GO annotation...

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.3 Publications

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
Complete GO annotation...

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 – 11Removed1 Publication
Chaini2 – 148147Endothelial differentiation-related factor 1
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiO60869.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini81 – 13555HTH cro/C1-type
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni37 – 11377Interaction with NR5A2, PPARG and NR1H3
Add
BLAST
Regioni69 – 10840Interaction with TBP and NR5A1
Add
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.

Sequence similaritiesi

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.
VSP_054701Add
BLAST
Alternative sequencei130 – 14819LKLRG…GPRAK → ECPSTLRRVR in isoform 2.
VSP_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]
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...

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 ]
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 125 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

Similar proteinsi