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Protein

DNA-binding protein inhibitor ID-3

Gene

ID3

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

Functioni

Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. Implicated in regulating a variety of cellular processes, including cellular growth, senescence, differentiation, apoptosis, angiogenesis, and neoplastic transformation. Involved in myogenesis by inhibiting skeletal muscle and cardiac myocyte differentiation and promoting muscle precursor cells proliferation. Inhibits the binding of E2A-containing protein complexes to muscle creatine kinase E-box enhancer. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Biological rhythms, Myogenesis, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-binding protein inhibitor ID-3
Alternative name(s):
Class B basic helix-loop-helix protein 25
Short name:
bHLHb25
Helix-loop-helix protein HEIR-1
ID-like protein inhibitor HLH 1R21
Inhibitor of DNA binding 3
Inhibitor of differentiation 3
Gene namesi
Name:ID3
Synonyms:1R21, BHLHB25, HEIR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:5362. ID3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: Ensembl
  • microtubule cytoskeleton Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: GDB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29610.

Polymorphism and mutation databases

BioMutaiID3.
DMDMi322510035.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 119119DNA-binding protein inhibitor ID-3PRO_0000127247Add
BLAST

Proteomic databases

MaxQBiQ02535.
PaxDbiQ02535.
PRIDEiQ02535.

PTM databases

PhosphoSiteiQ02535.

Expressioni

Tissue specificityi

Expressed abundantly in lung, kidney and adrenal gland, but not in adult brain.

Inductioni

By phorbol 12-myristate 13-acetate (PMA).

Gene expression databases

BgeeiQ02535.
CleanExiHS_ID3.
GenevisibleiQ02535. HS.

Organism-specific databases

HPAiCAB021353.
HPA024677.

Interactioni

Subunit structurei

Homodimer, and heterodimer with other HLH proteins. Interacts with COPS5 and COPS7A. Interacts with IFI204. Interacts with GATA4 and NKX2-5. Interacts with ANKRD2; both proteins cooperate in myoblast differentiation (By similarity). Interacts with CLOCK and ARNTL/BMAL1.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
FAM74A2Q5RGS33EBI-1387094,EBI-10244822
TCF12Q990813EBI-1387094,EBI-722877
TCF3P159233EBI-1387094,EBI-769630
TCF4P158843EBI-1387094,EBI-533224

Protein-protein interaction databases

BioGridi109625. 32 interactions.
DIPiDIP-713N.
IntActiQ02535. 17 interactions.
STRINGi9606.ENSP00000363689.

Structurei

Secondary structure

1
119
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi40 – 423Combined sources
Helixi43 – 5412Combined sources
Helixi66 – 8116Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LFHNMR-A/B29-83[»]
ProteinModelPortaliQ02535.
SMRiQ02535. Positions 32-83.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 8053bHLHPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG83634.
GeneTreeiENSGT00390000000908.
HOGENOMiHOG000234788.
HOVERGENiHBG009009.
InParanoidiQ02535.
KOiK17694.
OMAiPARGCYE.
OrthoDBiEOG7X9G8G.
PhylomeDBiQ02535.
TreeFamiTF326217.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
IPR026052. DNA-bd_prot-inh.
[Graphical view]
PANTHERiPTHR11723. PTHR11723. 1 hit.
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q02535-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKALSPVRGC YEAVCCLSER SLAIARGRGK GPAAEEPLSL LDDMNHCYSR
60 70 80 90 100
LRELVPGVPR GTQLSQVEIL QRVIDYILDL QVVLAEPAPG PPDGPHLPIQ
110
TAELTPELVI SNDKRSFCH
Length:119
Mass (Da):12,999
Last modified:February 8, 2011 - v2
Checksum:i7FC38B56B4DCEFBC
GO

Sequence cautioni

The sequence CAA47360.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti105 – 1051T → A.7 Publications
Corresponds to variant rs11574 [ dbSNP | Ensembl ].
VAR_016122
Natural varianti111 – 1111S → A.
Corresponds to variant rs11542317 [ dbSNP | Ensembl ].
VAR_030739

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66924 mRNA. Translation: CAA47360.1. Different initiation.
X69111 mRNA. Translation: CAA48862.1.
X73428 Genomic DNA. Translation: CAA51827.1.
BT006791 mRNA. Translation: AAP35437.1.
AK290003 mRNA. Translation: BAF82692.1.
AL021154 Genomic DNA. Translation: CAA15950.1.
CH471134 Genomic DNA. Translation: EAW95060.1.
BC003107 mRNA. Translation: AAH03107.1.
CCDSiCCDS237.1.
PIRiI37092. S28529.
RefSeqiNP_002158.3. NM_002167.4.
UniGeneiHs.76884.

Genome annotation databases

EnsembliENST00000374561; ENSP00000363689; ENSG00000117318.
GeneIDi3399.
KEGGihsa:3399.
UCSCiuc001bhh.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66924 mRNA. Translation: CAA47360.1. Different initiation.
X69111 mRNA. Translation: CAA48862.1.
X73428 Genomic DNA. Translation: CAA51827.1.
BT006791 mRNA. Translation: AAP35437.1.
AK290003 mRNA. Translation: BAF82692.1.
AL021154 Genomic DNA. Translation: CAA15950.1.
CH471134 Genomic DNA. Translation: EAW95060.1.
BC003107 mRNA. Translation: AAH03107.1.
CCDSiCCDS237.1.
PIRiI37092. S28529.
RefSeqiNP_002158.3. NM_002167.4.
UniGeneiHs.76884.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LFHNMR-A/B29-83[»]
ProteinModelPortaliQ02535.
SMRiQ02535. Positions 32-83.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109625. 32 interactions.
DIPiDIP-713N.
IntActiQ02535. 17 interactions.
STRINGi9606.ENSP00000363689.

PTM databases

PhosphoSiteiQ02535.

Polymorphism and mutation databases

BioMutaiID3.
DMDMi322510035.

Proteomic databases

MaxQBiQ02535.
PaxDbiQ02535.
PRIDEiQ02535.

Protocols and materials databases

DNASUi3399.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374561; ENSP00000363689; ENSG00000117318.
GeneIDi3399.
KEGGihsa:3399.
UCSCiuc001bhh.4. human.

Organism-specific databases

CTDi3399.
GeneCardsiGC01M023884.
HGNCiHGNC:5362. ID3.
HPAiCAB021353.
HPA024677.
MIMi600277. gene.
neXtProtiNX_Q02535.
PharmGKBiPA29610.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG83634.
GeneTreeiENSGT00390000000908.
HOGENOMiHOG000234788.
HOVERGENiHBG009009.
InParanoidiQ02535.
KOiK17694.
OMAiPARGCYE.
OrthoDBiEOG7X9G8G.
PhylomeDBiQ02535.
TreeFamiTF326217.

Miscellaneous databases

ChiTaRSiID3. human.
GeneWikiiID3_(gene).
GenomeRNAii3399.
NextBioi13432.
PROiQ02535.
SOURCEiSearch...

Gene expression databases

BgeeiQ02535.
CleanExiHS_ID3.
GenevisibleiQ02535. HS.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
IPR026052. DNA-bd_prot-inh.
[Graphical view]
PANTHERiPTHR11723. PTHR11723. 1 hit.
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mutually exclusive expression of a helix-loop-helix gene and N-myc in human neuroblastomas and in normal development."
    Ellmeier W., Aguzzi A., Kleiner E., Kurzbauer R., Weith A.
    EMBO J. 11:2563-2571(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-105.
  2. "An immediate early human gene encodes an Id-like helix-loop-helix protein and is regulated by protein kinase C activation in diverse cell types."
    Deed R.W., Bianchi S.M., Atherton G.T., Johnston D., Santibanez-Koref M., Murphy J.J., Norton J.D.
    Oncogene 8:599-607(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, VARIANT ALA-105.
  3. "Structural organisation and chromosomal mapping of the human Id-3 gene."
    Deed R.W., Hirose T., Mitchell E.L.D., Santibanez-Koref M.F., Norton J.D.
    Gene 151:309-314(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-105.
    Tissue: Blood.
  4. "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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-105.
  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], VARIANT ALA-105.
    Tissue: Hippocampus.
  6. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ALA-105.
  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], VARIANT ALA-105.
    Tissue: Skin.
  9. "The transcriptional repressor ID2 can interact with the canonical clock components CLOCK and BMAL1 and mediate inhibitory effects on mPer1 expression."
    Ward S.M., Fernando S.J., Hou T.Y., Duffield G.E.
    J. Biol. Chem. 285:38987-39000(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CLOCK AND ARNTL.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiID3_HUMAN
AccessioniPrimary (citable) accession number: Q02535
Secondary accession number(s): A8K1T8, O75641
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 8, 2011
Last modified: June 24, 2015
This is version 149 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.