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Q9NX09 (DDIT4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA damage-inducible transcript 4 protein
Alternative name(s):
HIF-1 responsive protein RTP801
Protein regulated in development and DNA damage response 1
Short name=REDD-1
Gene names
Name:DDIT4
Synonyms:REDD1, RTP801
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length232 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulates cell growth, proliferation and survival via inhibition of the activity of the mammalian target of rapamycin complex 1 (mTORC1). Inhibition of mTORC1 is mediated by a pathway that involves DDIT4/REDD1, AKT1, the TSC1-TSC2 complex and the GTPase RHEB. Plays an important role in responses to cellular energy levels and cellular stress, including responses to hypoxia and DNA damage. Regulates p53/TP53-mediated apoptosis in response to DNA damage via its effect on mTORC1 activity. Its role in the response to hypoxia depends on the cell type; it mediates mTORC1 inhibition in fibroblasts and thymocytes, but not in hepatocytes By similarity. Required for mTORC1-mediated defense against viral protein synthesis and virus replication By similarity. Inhibits neuronal differentiation and neurite outgrowth mediated by NGF via its effect on mTORC1 activity. Required for normal neuron migration during embryonic brain development. Plays a role in neuronal cell death. Ref.9 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18

Subunit structure

Monomer. Interacts with BTRC. Identified in a complex with CUL4A, DDB1 and BTRC. Interacts with TXNIP; this inhibits the proteasomal degradation of DDIT4. Ref.16 Ref.17 Ref.18

Subcellular location

Mitochondrion By similarity. Cytoplasmcytosol Ref.1.

Tissue specificity

Broadly expressed, with lowest levels in brain, skeletal muscle and intestine. Up-regulated in substantia nigra neurons from Parkinson disease patients (at protein level). Ref.1 Ref.2 Ref.14 Ref.15

Induction

Up-regulated in fibroblasts upon ionizing radiation, via a TP53-dependent pathway. Up-regulated by TP63 in primary keratinocytes, and down-regulated during keratinocyte differentiation. Up-regulated upon DNA alkylation. Up-regulated by amyloid beta-peptide and retinoic acid. Up-regulated by hypoxia, via a PI3K and HIF1A-dependent but TP53/TP63-independent mechanism (at protein level). Ref.1 Ref.2 Ref.8 Ref.10 Ref.13 Ref.15 Ref.18

Post-translational modification

Phosphorylated by GSK3B; this promotes proteasomal degradation. Ref.16

Polyubiquitinated by a DCX (DDB1-CUL4A-RBX1) E3 ubiquitin-protein ligase complex with BTRC as substrate-recognition component, leading to its proteasomal degradation.

Sequence similarities

Belongs to the DDIT4 family.

Ontologies

Keywords
   Biological processAntiviral defense
Apoptosis
   Cellular componentCytoplasm
Mitochondrion
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbrain development

Inferred from sequence or structural similarity. Source: UniProtKB

cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

defense response to virus

Inferred from electronic annotation. Source: UniProtKB-KW

intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of TOR signaling

Inferred from mutant phenotype Ref.18. Source: UniProtKB

negative regulation of glycolytic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of intracellular signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of peptidyl-serine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of peptidyl-threonine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

neuron differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

neuron migration

Inferred from sequence or structural similarity. Source: UniProtKB

neurotrophin TRK receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of neuron death

Inferred from sequence or structural similarity. Source: UniProtKB

protein complex disassembly

Inferred from electronic annotation. Source: Ensembl

reactive oxygen species metabolic process

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from direct assay Ref.18. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.1. Source: UniProtKB

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

intracellular

Inferred from direct assay. Source: LIFEdb

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 232232DNA damage-inducible transcript 4 protein
PRO_0000307197

Amino acid modifications

Modified residue191Phosphoserine Ref.16
Modified residue231Phosphothreonine Ref.16
Modified residue251Phosphothreonine Ref.16
Modified residue1211Phosphoserine Ref.16

Experimental info

Mutagenesis191S → A: Strongly inhibits proteasomal degradation. Ref.16
Mutagenesis231T → A: Strongly inhibits proteasomal degradation. Strongly inhibits proteasomal degradation; when associated with A-25. Ref.16
Mutagenesis251T → A: Strongly inhibits proteasomal degradation; when associated with A-23. Ref.16
Mutagenesis1031S → L or W: No effect on inhibition of mTORC1. Ref.18
Mutagenesis1331R → A: No effect on inhibition of mTORC1. Ref.18
Mutagenesis1371S → A or D: No effect on inhibition of mTORC1. Ref.18
Mutagenesis1391P → A: Abolishes inhibition of mTORC1. Ref.18
Mutagenesis1401C → S: Mildly reduces inhibition of mTORC1. Ref.18
Mutagenesis2191K → A: Reduces inhibition of mTORC1. Abolishes inhibition of mTORC1; when associated with A-222. Ref.18
Mutagenesis2211L → A: Reduces inhibition of mTORC1. Ref.18
Mutagenesis2221Y → A: Reduces inhibition of mTORC1. Abolishes inhibition of mTORC1; when associated with A-219. Ref.18
Sequence conflict2281L → P in CAB66603. Ref.3

Secondary structure

................ 232
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9NX09 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 774E941EBDD08198

FASTA23225,371
        10         20         30         40         50         60 
MPSLWDRFSS SSTSSSPSSL PRTPTPDRPP RSAWGSATRE EGFDRSTSLE SSDCESLDSS 

        70         80         90        100        110        120 
NSGFGPEEDT AYLDGVSLPD FELLSDPEDE HLCANLMQLL QESLAQARLG SRRPARLLMP 

       130        140        150        160        170        180 
SQLVSQVGKE LLRLAYSEPC GLRGALLDVC VEQGKSCHSV GQLALDPSLV PTFQLTLVLR 

       190        200        210        220        230 
LDSRLWPKIQ GLFSSANSPF LPGFSQSLTL STGFRVIKKK LYSSEQLLIE EC 

« Hide

References

« Hide 'large scale' references
[1]"REDD1, a developmentally regulated transcriptional target of p63 and p53, links p63 to regulation of reactive oxygen species."
Ellisen L.W., Ramsayer K.D., Johannessen C.M., Yang A., Beppu H., Minda K., Oliner J.D., McKeon F., Haber D.A.
Mol. Cell 10:995-1005(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION BY DNA DAMAGE, SUBCELLULAR LOCATION.
Tissue: Fetal brain.
[2]"Identification of a novel hypoxia-inducible factor 1-responsive gene, RTP801, involved in apoptosis."
Shoshani T., Faerman A., Mett I., Zelin E., Tenne T., Gorodin S., Moshel Y., Elbaz S., Budanov A., Chajut A., Kalinski H., Kamer I., Rozen A., Mor O., Keshet E., Leshkowitz D., Einat P., Skaliter R., Feinstein E.
Mol. Cell. Biol. 22:2283-2293(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
[3]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"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. expand/collapse author list , 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].
[5]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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: Kidney and Uterus.
[8]"Identification of amyloid beta-peptide responsive genes by cDNA microarray technology: involvement of RTP801 in amyloid beta-peptide toxicity."
Kim J.-R., Lee S.-R., Chung H.J., Kim S., Baek S.-H., Kim J.H., Kim Y.-S.
Exp. Mol. Med. 35:403-411(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[9]"Regulation of mTOR function in response to hypoxia by REDD1 and the TSC1/TSC2 tumor suppressor complex."
Brugarolas J., Lei K., Hurley R.L., Manning B.D., Reiling J.H., Hafen E., Witters L.A., Ellisen L.W., Kaelin W.G. Jr.
Genes Dev. 18:2893-2904(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Induction of a cell stress response gene RTP801 by DNA damaging agent methyl methanesulfonate through CCAAT/enhancer binding protein."
Lin L., Qian Y., Shi X., Chen Y.
Biochemistry 44:3909-3914(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[11]"The stress-inducted proteins RTP801 and RTP801L are negative regulators of the mammalian target of rapamycin pathway."
Corradetti M.N., Inoki K., Guan K.-L.
J. Biol. Chem. 280:9769-9772(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Regulation of mTOR and cell growth in response to energy stress by REDD1."
Sofer A., Lei K., Johannessen C.M., Ellisen L.W.
Mol. Cell. Biol. 25:5834-5845(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"REDD1 integrates hypoxia-mediated survival signaling downstream of phosphatidylinositol 3-kinase."
Schwarzer R., Tondera D., Arnold W., Giese K., Klippel A., Kaufmann J.
Oncogene 24:1138-1149(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[14]"RTP801 is elevated in Parkinson brain substantia nigral neurons and mediates death in cellular models of Parkinson's disease by a mechanism involving mammalian target of rapamycin inactivation."
Malagelada C., Ryu E.J., Biswas S.C., Jackson-Lewis V., Greene L.A.
J. Neurosci. 26:9996-10005(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[15]"RTP801 is a novel retinoic acid-responsive gene associated with myeloid differentiation."
Gery S., Park D.J., Vuong P.T., Virk R.K., Muller C.I., Hofmann W.-K., Koeffler H.P.
Exp. Hematol. 35:572-578(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
[16]"REDD1, an inhibitor of mTOR signalling, is regulated by the CUL4A-DDB1 ubiquitin ligase."
Katiyar S., Liu E., Knutzen C.A., Lang E.S., Lombardo C.R., Sankar S., Toth J.I., Petroski M.D., Ronai Z., Chiang G.G.
EMBO Rep. 10:866-872(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, UBIQUITINATION, INTERACTION WITH BTRC, IDENTIFICATION IN A COMPLEX WITH CUL4A; DDB1 AND BTRC, IDENTIFICATION BY MASS SPECTROMETRY, PARTIAL PROTEIN SEQUENCE, MUTAGENESIS OF SER-19; THR-23 AND THR-25, PHOSPHORYLATION AT SER-19; THR-23; THR-25 AND SER-121.
[17]"TXNIP potentiates Redd1-induced mTOR suppression through stabilization of Redd1."
Jin H.O., Seo S.K., Kim Y.S., Woo S.H., Lee K.H., Yi J.Y., Lee S.J., Choe T.B., Lee J.H., An S., Hong S.I., Park I.C.
Oncogene 30:3792-3801(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TXNIP, FUNCTION.
[18]"Structural analysis and functional implications of the negative mTORC1 regulator REDD1."
Vega-Rubin-de-Celis S., Abdallah Z., Kinch L., Grishin N.V., Brugarolas J., Zhang X.
Biochemistry 49:2491-2501(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 89-226, FUNCTION, SUBUNIT, INDUCTION, MUTAGENESIS OF SER-103; ARG-133; SER-137; PRO-139; CYS-140; LYS-219; LEU-221 AND TYR-222.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY090097 mRNA. Translation: AAM10442.1.
AF335324 mRNA. Translation: AAL38424.1.
AL136668 mRNA. Translation: CAB66603.1.
AK000507 mRNA. Translation: BAA91214.1.
AL683820 Genomic DNA. Translation: CAH73863.1.
CH471083 Genomic DNA. Translation: EAW54452.1.
BC000708 mRNA. Translation: AAH00708.1.
BC007714 mRNA. Translation: AAH07714.1.
BC015236 mRNA. Translation: AAH15236.1.
CCDSCCDS7315.1.
RefSeqNP_061931.1. NM_019058.2.
UniGeneHs.744875.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LQ9X-ray2.00A/B89-226[»]
ProteinModelPortalQ9NX09.
SMRQ9NX09. Positions 89-222.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120028. 8 interactions.
IntActQ9NX09. 10 interactions.
MINTMINT-1405734.
STRING9606.ENSP00000307305.

PTM databases

PhosphoSiteQ9NX09.

Polymorphism databases

DMDM74753036.

Proteomic databases

MaxQBQ9NX09.
PaxDbQ9NX09.
PRIDEQ9NX09.

Protocols and materials databases

DNASU54541.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000307365; ENSP00000307305; ENSG00000168209.
GeneID54541.
KEGGhsa:54541.
UCSCuc001jsx.1. human.

Organism-specific databases

CTD54541.
GeneCardsGC10P074033.
HGNCHGNC:24944. DDIT4.
HPAHPA034508.
MIM607729. gene.
neXtProtNX_Q9NX09.
PharmGKBPA134977994.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG78982.
HOGENOMHOG000082523.
HOVERGENHBG104439.
InParanoidQ9NX09.
KOK08270.
OMADEHLCAS.
OrthoDBEOG7P2XTF.
PhylomeDBQ9NX09.
TreeFamTF105007.

Gene expression databases

BgeeQ9NX09.
CleanExHS_DDIT4.
GenevestigatorQ9NX09.

Family and domain databases

InterProIPR012918. RTP801-like.
[Graphical view]
PANTHERPTHR12478. PTHR12478. 1 hit.
PfamPF07809. RTP801_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDDIT4. human.
EvolutionaryTraceQ9NX09.
GeneWikiDDIT4.
GenomeRNAi54541.
NextBio56981.
PROQ9NX09.
SOURCESearch...

Entry information

Entry nameDDIT4_HUMAN
AccessionPrimary (citable) accession number: Q9NX09
Secondary accession number(s): Q9H0S3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM