Q9NX09 (DDIT4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	232 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Cytoplasm › cytosol 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 process	Antiviral defense Apoptosis
Cellular component	Cytoplasm Mitochondrion
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	brain 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 cascade Inferred from mutant phenotype Ref.18. Source: UniProtKB negative regulation of glycolysis Inferred from electronic annotation. Source: Compara negative regulation of intracellular protein kinase cascade 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 nerve growth factor receptor signaling pathway 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 positive regulation of neuron death Inferred from sequence or structural similarity. Source: UniProtKB protein complex disassembly Inferred from electronic annotation. Source: Compara reactive oxygen species metabolic process Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from direct assay Ref.18. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay Ref.1. Source: UniProtKB cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 232

232

DNA damage-inducible transcript 4 protein

PRO_0000307197

Amino acid modifications

Modified residue

19

1

Phosphoserine Ref.16

Modified residue

23

1

Phosphothreonine Ref.16

Modified residue

25

1

Phosphothreonine Ref.16

Modified residue

121

1

Phosphoserine Ref.16

Experimental info

Mutagenesis

19

1

S → A: Strongly inhibits proteasomal degradation. Ref.16

Mutagenesis

23

1

T → A: Strongly inhibits proteasomal degradation. Strongly inhibits proteasomal degradation; when associated with A-25. Ref.16

Mutagenesis

25

1

T → A: Strongly inhibits proteasomal degradation; when associated with A-23. Ref.16

Mutagenesis

103

1

S → L or W: No effect on inhibition of mTORC1. Ref.18

Mutagenesis

133

1

R → A: No effect on inhibition of mTORC1. Ref.18

Mutagenesis

137

1

S → A or D: No effect on inhibition of mTORC1. Ref.18

Mutagenesis

139

1

P → A: Abolishes inhibition of mTORC1. Ref.18

Mutagenesis

140

1

C → S: Mildly reduces inhibition of mTORC1. Ref.18

Mutagenesis

219

1

K → A: Reduces inhibition of mTORC1. Abolishes inhibition of mTORC1; when associated with A-222. Ref.18

Mutagenesis

221

1

L → A: Reduces inhibition of mTORC1. Ref.18

Mutagenesis

222

1

Y → A: Reduces inhibition of mTORC1. Abolishes inhibition of mTORC1; when associated with A-219. Ref.18

Sequence conflict

228

1

L → P in CAB66603. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

232

Helix Strand Turn

Details...

Helix

90 – 104

15

Beta strand

107 – 112

6

Helix

121 – 135

15

Helix

141 – 144

4

Beta strand

145 – 153

9

Beta strand

156 – 165

10

Beta strand

173 – 180

8

Beta strand

214 – 220

7

Sequences

	Sequence		Length	Mass (Da)
	Q9NX09 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 774E941EBDD08198	FASTA	232	25,371
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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, 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.

IPI

IPI00550489.

RefSeq

NP_061931.1. NM_019058.2.

UniGene

Hs.723254.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3LQ9	X-ray	2.00	A/B	89-226	[»]

ProteinModelPortal

Q9NX09.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NX09. 3 interactions.

MINT

MINT-1405734.

STRING

9606.ENSP00000307305.

PTM databases

PhosphoSite

Q9NX09.

Polymorphism databases

DMDM

74753036.

Proteomic databases

PaxDb

Q9NX09.

PRIDE

Q9NX09.

Protocols and materials databases

DNASU

54541.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000307365; ENSP00000307305; ENSG00000168209.

GeneID

54541.

KEGG

hsa:54541.

UCSC

uc001jsx.1. human.

Organism-specific databases

CTD

54541.

GeneCards

GC10P074033.

HGNC

HGNC:24944. DDIT4.

HPA

HPA034508.

MIM

607729. gene.

neXtProt

NX_Q9NX09.

PharmGKB

PA134977994.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG78982.

HOGENOM

HOG000082523.

HOVERGEN

HBG104439.

InParanoid

Q9NX09.

KO

K08270.

OMA

DEHLCAS.

OrthoDB

EOG4TXBT0.

PhylomeDB

Q9NX09.

Gene expression databases

Bgee

Q9NX09.

CleanEx

HS_DDIT4.

Genevestigator

Q9NX09.

Family and domain databases

InterPro

IPR012918. RTP801-like.
[Graphical view]

PANTHER

PTHR12478. PTHR12478. 1 hit.

Pfam

PF07809. RTP801_C. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

DDIT4. human.

EvolutionaryTrace

Q9NX09.

GenomeRNAi

54541.

NextBio

56981.

SOURCE

Search...

Entry information

Entry name

DDIT4_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.