Q9NSU2 (TREX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Three prime repair exonuclease 1
EC=3.1.11.2

Alternative name(s):
3'-5' exonuclease TREX1
DNase III

Gene names

Name:

TREX1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	369 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Exonuclease with a preference for double stranded DNA with mismatched 3' termini. May play a role in DNA repair. Ref.1 Ref.2
Catalytic activity	Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Cofactor	Magnesium. Required for activity. Substitution with Mn2+ results in partial activity By similarity.
Subunit structure	Homodimer.
Subcellular location	Nucleus By similarity Ref.1.
Tissue specificity	Detected in thymus, spleen, liver, brain, heart, small intestine and colon. Ref.1 Ref.3
Involvement in disease	Defects in TREX1 are the cause of Aicardi-Goutieres syndrome type 1 (AGS1) [MIM:225750]. A form of Aicardi-Goutieres syndrome, a genetically heterogeneous disease characterized by cerebral atrophy, leukoencephalopathy, intracranial calcifications, chronic cerebrospinal fluid (CSF) lymphocytosis, increased CSF alpha-interferon, and negative serologic investigations for common prenatal infection. Clinical features as thrombocytopenia, hepatosplenomegaly and elevated hepatic transaminases along with intermittent fever may erroneously suggest an infective process. Severe neurological dysfunctions manifest in infancy as progressive microcephaly, spasticity, dystonic posturing and profound psychomotor retardation. Death often occurs in early childhood. AGS1 inheritance can be autosomal recessive or dominant. Ref.11 Ref.12 Ref.16 Defects in TREX1 are a cause of susceptibility to systemic lupus erythematosus (SLE) [MIM:152700]. SLE is a chronic, inflammatory and often febrile multisystemic disorder of connective tissue. It affects principally the skin, joints, kidneys and serosal membranes. It is thought to represent a failure of the regulatory mechanisms of the autoimmune system. Ref.14 Defects in TREX1 are the cause of chilblain lupus (CHBL) [MIM:610448]. Chilblain lupus, a rare cutaneous form of systemic lupus erythematosus. Affected individuals present with painful bluish-red papular or nodular lesions of the skin in acral locations precipitated by cold and wet exposure at temperatures less than 10 degrees centigrade. Ref.12 Ref.13 Defects in TREX1 are the cause of cerebro-retinal vasculopathy (CRV) [MIM:192315]. CRV is a microvascular endotheliopathy with middle-age onset. This retinal vasculopathy is characterized by telangiectasias, microaneurysms and retinal capillary obliteration starting in the macula. Diseased cerebral white matter has prominent small infarcts that often coalesce to pseudotumors. Ref.15
Sequence similarities	Belongs to the exonuclease superfamily. TREX family.
Caution	The gene for this protein is either identical to or adjacent to that of ATRIP. Some of the mRNAs that encode ATRIP also encode TREX1 in another reading frame.
Sequence caution	The sequence AAD48774.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Disease	Aicardi-Goutieres syndrome Disease mutation Neurodegeneration Systemic lupus erythematosus
Ligand	Magnesium
Molecular function	Exonuclease Hydrolase Nuclease
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA recombination Non-traceable author statement Ref.2Ref.3. Source: UniProtKB DNA replication Non-traceable author statement Ref.2Ref.3. Source: UniProtKB cell death Inferred from electronic annotation. Source: UniProtKB-KW mismatch repair Non-traceable author statement Ref.2Ref.3. Source: UniProtKB
Cellular component	nuclear envelope Non-traceable author statement Ref.2. Source: UniProtKB
Molecular function	3'-5'-exodeoxyribonuclease activity Traceable author statement. Source: ProtInc MutLalpha complex binding Inferred from direct assay. Source: MGI MutSalpha complex binding Inferred from direct assay. Source: MGI exodeoxyribonuclease III activity Inferred from electronic annotation. Source: EC metal ion binding Non-traceable author statement Ref.2. Source: UniProtKB protein homodimerization activity Non-traceable author statement Ref.2. Source: UniProtKB single-stranded DNA binding Traceable author statement Ref.2. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NSU2-1)

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.

Isoform 2 (identifier: Q9NSU2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-65: Missing.

Isoform 3 (identifier: Q9NSU2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-55: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 369	369	Three prime repair exonuclease 1		PRO_0000109868
Amino acid modifications
	Modified residue	133	1	Phosphoserine Ref.10
	Modified residue	222	1	Phosphoserine Ref.8
	Modified residue	316	1	Phosphoserine Ref.9 Ref.10
Natural variations
	Alternative sequence	1 – 65	65	Missing in isoform 2.		VSP_010445
	Alternative sequence	1 – 55	55	Missing in isoform 3.		VSP_010446
	Natural variant	73	1	D → N in CHBL and AGS1; loss of function. Ref.13 Ref.16		VAR_037948
	Natural variant	169	1	R → H in AGS1 and SLE. Ref.11 Ref.14		VAR_028319
	Natural variant	213	1	A → V in SLE. Ref.14		VAR_037949
	Natural variant	255	1	D → DD in AGS1; heterozygous compound with H-169. Ref.11		VAR_028320
	Natural variant	255	1	D → N in AGS1; autosomal dominant form; does not affect activity. Ref.12		VAR_032940
	Natural variant	256	1	V → D in AGS1. Ref.11		VAR_028321
	Natural variant	282	1	G → S in SLE; associated in cis with P-302. Ref.14		VAR_037950
	Natural variant	295	1	R → S in SLE. Ref.14		VAR_037951
	Natural variant	302	1	A → P in SLE; associated in cis with S-282. Ref.14		VAR_037952
	Natural variant	321	1	E → G. Ref.14 Corresponds to variant rs55999987 [ dbSNP | Ensembl ].		VAR_037953
	Natural variant	345	1	P → L in SLE. Ref.14		VAR_037954
	Natural variant	360	1	Y → C in SLE. Ref.14		VAR_037955
	Natural variant	361	1	G → A in SLE. Ref.14		VAR_037956
Experimental info
	Sequence conflict	320	1	G → R in CAB50866. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 42B79047A9AD9837	FASTA	369	38,923
	10 20 30 40 50 60 MGPGARRQGR IVQGRPEMCF CPPPTPLPPL RILTLGTHTP TPCSSPGSAA GTYPTMGSQA 70 80 90 100 110 120 LPPGPMQTLI FFDMEATGLP FSQPKVTELC LLAVHRCALE SPPTSQGPPP TVPPPPRVVD 130 140 150 160 170 180 KLSLCVAPGK ACSPAASEIT GLSTAVLAAH GRQCFDDNLA NLLLAFLRRQ PQPWCLVAHN 190 200 210 220 230 240 GDRYDFPLLQ AELAMLGLTS ALDGAFCVDS ITALKALERA SSPSEHGPRK SYSLGSIYTR 250 260 270 280 290 300 LYGQSPPDSH TAEGDVLALL SICQWRPQAL LRWVDAHARP FGTIRPMYGV TASARTKPRP 310 320 330 340 350 360 SAVTTTAHLA TTRNTSPSLG ESRGTKDLPP VKDPGALSRE GLLAPLGLLA ILTLAVATLY GLSLATPGE
	Isoform 2 [UniParc]. Checksum: 922048DCC4122124	FASTA	304	32,276
	10 20 30 40 50 60 MQTLIFFDME ATGLPFSQPK VTELCLLAVH RCALESPPTS QGPPPTVPPP PRVVDKLSLC 70 80 90 100 110 120 VAPGKACSPA ASEITGLSTA VLAAHGRQCF DDNLANLLLA FLRRQPQPWC LVAHNGDRYD 130 140 150 160 170 180 FPLLQAELAM LGLTSALDGA FCVDSITALK ALERASSPSE HGPRKSYSLG SIYTRLYGQS 190 200 210 220 230 240 PPDSHTAEGD VLALLSICQW RPQALLRWVD AHARPFGTIR PMYGVTASAR TKPRPSAVTT 250 260 270 280 290 300 TAHLATTRNT SPSLGESRGT KDLPPVKDPG ALSREGLLAP LGLLAILTLA VATLYGLSLA TPGE
	Isoform 3 [UniParc]. Checksum: EE8F63B6496D72F4	FASTA	314	33,212
	10 20 30 40 50 60 MGSQALPPGP MQTLIFFDME ATGLPFSQPK VTELCLLAVH RCALESPPTS QGPPPTVPPP 70 80 90 100 110 120 PRVVDKLSLC VAPGKACSPA ASEITGLSTA VLAAHGRQCF DDNLANLLLA FLRRQPQPWC 130 140 150 160 170 180 LVAHNGDRYD FPLLQAELAM LGLTSALDGA FCVDSITALK ALERASSPSE HGPRKSYSLG 190 200 210 220 230 240 SIYTRLYGQS PPDSHTAEGD VLALLSICQW RPQALLRWVD AHARPFGTIR PMYGVTASAR 250 260 270 280 290 300 TKPRPSAVTT TAHLATTRNT SPSLGESRGT KDLPPVKDPG ALSREGLLAP LGLLAILTLA 310 VATLYGLSLA TPGE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A human DNA editing enzyme homologous to the Escherichia coli DnaQ/MutD protein." Hoess M., Robins P., Naven T.J.P., Pappin D.J.C., Sgouros J., Lindahl T. EMBO J. 18:3868-3875(1999) [PubMed: 10393201] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[2]	"Identification and expression of the TREX1 and TREX2 cDNA sequences encoding mammalian 3'-->5' exonucleases." Mazur D.J., Perrino F.W. J. Biol. Chem. 274:19655-19660(1999) [PubMed: 10391904] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION.
[3]	"Structure and expression of the TREX1 and TREX2 3'-->5' exonuclease genes." Mazur D.J., Perrino F.W. J. Biol. Chem. 276:14718-14727(2001) [PubMed: 11278605] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Thymus.
[5]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Testis.
[6]	NIEHS SNPs program Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Eye.
[8]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND SER-316, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Mutations in the gene encoding the 3'-5' DNA exonuclease TREX1 cause Aicardi-Goutieres syndrome at the AGS1 locus." Crow Y.J., Hayward B.E., Parmar R., Robins P., Leitch A., Ali M., Black D.N., van Bokhoven H., Brunner H.G., Hamel B.C.J., Corry P.C., Cowan F.M., Frints S.G., Klepper J., Livingston J.H., Lynch S.A., Massey R.F., Meritet J.F. , Michaud J.L., Ponsot G., Voit T., Lebon P., Bonthron D.T., Jackson A.P., Barnes D.E., Lindahl T. Nat. Genet. 38:917-920(2006) [PubMed: 16845398] [Abstract] Cited for: VARIANTS AGS1 HIS-169; ASP-255 INS AND ASP-256.
[12]	"Heterozygous mutations in TREX1 cause familial chilblain lupus and dominant Aicardi-Goutieres syndrome." Rice G., Newman W.G., Dean J., Patrick T., Parmar R., Flintoff K., Robins P., Harvey S., Hollis T., O'Hara A., Herrick A.L., Bowden A.P., Perrino F.W., Lindahl T., Barnes D.E., Crow Y.J. Am. J. Hum. Genet. 80:811-815(2007) [PubMed: 17357087] [Abstract] Cited for: INVOLVEMENT IN CHBL, VARIANT AGS1 ASN-255, CHARACTERIZATION OF VARIANT AGS1 ASN-255.
[13]	"A mutation in TREX1 that impairs susceptibility to granzyme A-mediated cell death underlies familial chilblain lupus." Lee-Kirsch M.A., Chowdhury D., Harvey S., Gong M., Senenko L., Engel K., Pfeiffer C., Hollis T., Gahr M., Perrino F.W., Lieberman J., Hubner N. J. Mol. Med. 85:531-537(2007) [PubMed: 17440703] [Abstract] Cited for: VARIANT CHBL ASN-73, CHARACTERIZATION OF VARIANT CHBL ASN-73.
[14]	"Mutations in the gene encoding the 3'-5' DNA exonuclease TREX1 are associated with systemic lupus erythematosus." Lee-Kirsch M.A., Gong M., Chowdhury D., Senenko L., Engel K., Lee Y.A., de Silva U., Bailey S.L., Witte T., Vyse T.J., Kere J., Pfeiffer C., Harvey S., Wong A., Koskenmies S., Hummel O., Rohde K., Schmidt R.E. , Dominiczak A.F., Gahr M., Hollis T., Perrino F.W., Lieberman J., Huebner N. Nat. Genet. 39:1065-1067(2007) [PubMed: 17660818] [Abstract] Cited for: VARIANTS SLE HIS-169; VAL-213; SER-282; SER-295; PRO-302; LEU-345; CYS-360 AND ALA-361, VARIANT GLY-321.
[15]	"C-terminal truncations in human 3'-5' DNA exonuclease TREX1 cause autosomal dominant retinal vasculopathy with cerebral leukodystrophy." Richards A., van den Maagdenberg A.M.J.M., Jen J.C., Kavanagh D., Bertram P., Spitzer D., Liszewski M.K., Barilla-Labarca M.-L., Terwindt G.M., Kasai Y., McLellan M., Grand M.G., Vanmolkot K.R.J., de Vries B., Wan J., Kane M.J., Mamsa H., Schaefer R. , Stam A.H., Haan J., de Jong P.T.V.M., Storimans C.W., van Schooneveld M.J., Oosterhuis J.A., Gschwendter A., Dichgans M., Kotschet K.E., Hodgkinson S., Hardy T.A., Delatycki M.B., Hajj-Ali R.A., Kothari P.H., Nelson S.F., Frants R.R., Baloh R.W., Ferrari M.D., Atkinson J.P. Nat. Genet. 39:1068-1070(2007) [PubMed: 17660820] [Abstract] Cited for: INVOLVEMENT IN CRV.
[16]	"A de novo p.Asp18Asn mutation in TREX1 in a patient with Aicardi-Goutieres syndrome." Haaxma C.A., Crow Y.J., van Steensel M.A., Lammens M.M., Rice G.I., Verbeek M.M., Willemsen M.A. Am. J. Med. Genet. A 152:2612-2617(2010) [PubMed: 20799324] [Abstract] Cited for: VARIANT AGS1 ASN-73.
+	Additional computationally mapped references.

Web resources

GeneReviews

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ243797 mRNA. Translation: CAB50866.1. AF319566 mRNA. Translation: AAK07613.1. AF319567 mRNA. Translation: AAK07614.1. AF319568 mRNA. Translation: AAK07615.1. AF319569 mRNA. Translation: AAK07616.1. AF151105 mRNA. Translation: AAD48774.2. Different initiation. AK315196 mRNA. Translation: BAG37636.1. AL137745 mRNA. No translation available. AF483777 Genomic DNA. Translation: AAL82504.1. BC023630 mRNA. Translation: AAH23630.1.
IPI	IPI00085084. IPI00220019. IPI00411455.
PIR	T46299.
RefSeq	NP_057465.1. NM_016381.3. NP_338599.1. NM_033629.2.
UniGene	Hs.707026. Hs.713742.
3D structure databases
ProteinModelPortal	Q9NSU2.
SMR	Q9NSU2. Positions 61-289.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1466830.
STRING	Q9NSU2.
PTM databases
PhosphoSite	Q9NSU2.
Polymorphism databases
DMDM	47606216.
Proteomic databases
PRIDE	Q9NSU2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000422277; ENSP00000390478; ENSG00000213689.
GeneID	11277.
KEGG	hsa:11277.
UCSC	uc003ctj.2. human. uc003ctk.2. human.
Organism-specific databases
CTD	11277.
GeneCards	GC03P048482.
HGNC	HGNC:12269. TREX1.
HPA	HPA035437.
MIM	152700. phenotype. 192315. phenotype. 225750. phenotype. 606609. gene. 610448. phenotype.
neXtProt	NX_Q9NSU2.
Orphanet	51. Aicardi-Goutieres syndrome. 3421. Cerebroretinal vasculopathy. 90280. Chilblain lupus. 71291. Hereditary vascular retinopathy. 63261. HERNS syndrome.
PharmGKB	PA36949.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG13412.
GeneTree	ENSGT00390000012715.
HOGENOM	HBG282070.
HOVERGEN	HBG079278.
InParanoid	Q9NSU2.
OMA	WVDAHAR.
PhylomeDB	Q9NSU2.
Gene expression databases
ArrayExpress	Q9NSU2.
Bgee	Q9NSU2.
CleanEx	HS_TREX1.
Genevestigator	Q9NSU2.
GermOnline	ENSG00000164053. Homo sapiens.
Family and domain databases
InterPro	IPR012337. RNaseH-like_dom. [Graphical view]
KO	K10790.
SUPFAM	SSF53098. RNaseH_fold. 1 hit.
ProtoNet	Search...
Other
NextBio	42927.
SOURCE	Search...

Entry information

Entry name

TREX1_HUMAN

Accession

Primary (citable) accession number: Q9NSU2
Secondary accession number(s): B2RCN9 , Q8TEU2, Q9BPW1, Q9Y4X2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2004
Last sequence update:	October 1, 2000
Last modified:	December 14, 2011
This is version 102 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.