P16858 (G3P_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glyceraldehyde-3-phosphate dehydrogenase
Short name=GAPDH
EC=1.2.1.12

Alternative name(s):
Peptidyl-cysteine S-nitrosylase GAPDH
EC=2.6.99.-

Gene names

Name:	Gapdh
Synonyms:	Gapd

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	333 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Modulates the organization and assembly of the cytoskeleton. Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules. Also participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation. Ref.11
Catalytic activity	D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH. Ref.10
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
Subunit structure	Homotetramer. Interacts with EIF1AD, USP25, PRKCI and WARS. Interacts with TPPP; the interaction is direct. Interacts (when S-nitrosylated) with SIAH1; leading to nuclear translocation. Interacts with RILPL1/GOSPEL, leading to prevent the interaction between GAPDH and SIAH1 and prevent nuclear translocation. Interacts with CHP1; the interaction increases the binding of CHP1 with microtubules. Associates with microtubules By similarity. Component of the GAIT complex. Ref.11
Subcellular location	Cytoplasm › cytosol By similarity. Nucleus By similarity. Cytoplasm › cytoskeleton By similarity. Note: Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal By similarity.
Post-translational modification	ISGylated By similarity. S-nitrosylation of Cys-150 leads to interaction with SIAH1, followed by translocation to the nucleus By similarity. Sulfhydration at Cys-150 increases catalytic activity.
Sequence similarities	Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords
Biological process	Apoptosis Glycolysis Translation regulation
Cellular component	Cytoplasm Cytoskeleton Nucleus
Ligand	NAD
Molecular function	Oxidoreductase Transferase
PTM	ADP-ribosylation Acetylation Methylation Phosphoprotein S-nitrosylation Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway microtubule cytoskeleton organization Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of translation Inferred from direct assay Ref.11. Source: UniProtKB neuron apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB peptidyl-cysteine S-trans-nitrosylation Inferred from sequence or structural similarity. Source: UniProtKB protein stabilization Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytosol Inferred from sequence or structural similarity. Source: UniProtKB microtubule cytoskeleton Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	NAD binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred from electronic annotation. Source: InterPro glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity Inferred from direct assay Ref.10. Source: UniProtKB microtubule binding Inferred from sequence or structural similarity. Source: UniProtKB peptidyl-cysteine S-nitrosylase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Kcnma1	Q08460	3	EBI-444871,EBI-1633915

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 333	332	Glyceraldehyde-3-phosphate dehydrogenase		PRO_0000145490
Regions
	Nucleotide binding	11 – 12	2	NAD By similarity
	Region	2 – 146	145	Interaction with WARS By similarity
	Region	149 – 151	3	Glyceraldehyde 3-phosphate binding By similarity
	Region	209 – 210	2	Glyceraldehyde 3-phosphate binding By similarity
Sites
	Active site	150	1	Nucleophile By similarity
	Binding site	33	1	NAD By similarity
	Binding site	78	1	NAD; via carbonyl oxygen By similarity
	Binding site	120	1	NAD By similarity
	Binding site	180	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	232	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	314	1	NAD By similarity
	Site	177	1	Activates thiol group during catalysis By similarity
Amino acid modifications
	Modified residue	3	1	N6,N6-dimethyllysine By similarity
	Modified residue	7	1	Deamidated asparagine By similarity
	Modified residue	40	1	Phosphotyrosine By similarity
	Modified residue	59	1	N6-acetyllysine By similarity
	Modified residue	62	1	Deamidated asparagine By similarity
	Modified residue	64	1	N6,N6-dimethyllysine By similarity
	Modified residue	68	1	Deamidated asparagine By similarity
	Modified residue	73	1	Phosphothreonine By similarity
	Modified residue	120	1	Phosphoserine By similarity
	Modified residue	146	1	Phosphoserine By similarity
	Modified residue	147	1	Deamidated asparagine By similarity
	Modified residue	149	1	Phosphoserine By similarity
	Modified residue	150	1	ADP-ribosylcysteine; by autocatalysis; in irreversibly inhibited form By similarity
	Modified residue	150	1	Cysteine persulfide Ref.10
	Modified residue	150	1	S-nitrosocysteine; in reversibly inhibited form By similarity
	Modified residue	153	1	Deamidated asparagine By similarity
	Modified residue	182	1	Phosphothreonine By similarity
	Modified residue	192	1	N6,N6-dimethyllysine; alternate By similarity
	Modified residue	192	1	N6-acetyllysine By similarity
	Modified residue	192	1	N6-malonyllysine; alternate By similarity
	Modified residue	209	1	Phosphothreonine Ref.9
	Modified residue	213	1	N6,N6-dimethyllysine; alternate By similarity
	Modified residue	213	1	N6-malonyllysine; alternate By similarity
	Modified residue	217	1	N6-acetyllysine By similarity
	Modified residue	223	1	Deamidated asparagine By similarity
	Modified residue	225	1	N6,N6-dimethyllysine; alternate By similarity
	Modified residue	225	1	N6-acetyllysine; alternate By similarity
	Modified residue	227	1	Phosphothreonine By similarity
	Modified residue	235	1	Phosphothreonine By similarity
	Modified residue	252	1	N6-acetyllysine By similarity
	Modified residue	258	1	N6,N6-dimethyllysine By similarity
	Modified residue	261	1	N6,N6-dimethyllysine By similarity
	Modified residue	310	1	Phosphoserine By similarity
	Modified residue	312	1	Phosphotyrosine Ref.8
	Modified residue	314	1	Deamidated asparagine By similarity
	Modified residue	316	1	Phosphotyrosine Ref.7 Ref.8
	Modified residue	318	1	Phosphotyrosine Ref.7 Ref.8
	Modified residue	328	1	Phosphotyrosine Ref.8
	Modified residue	332	1	N6,N6-dimethyllysine By similarity
Experimental info
	Mutagenesis	150	1	C → S: Abolishes sulfhydration and induces impaired enzyme activity. Ref.10
	Sequence conflict	3	1	K → E in BAE40174. Ref.2
	Sequence conflict	30	1	A → V in AAH92267. Ref.4
	Sequence conflict	82	1	N → S in BAE35989. Ref.2
	Sequence conflict	84	1	K → E in BAE40174. Ref.2
	Sequence conflict	89	1	G → S in BAE26016. Ref.2
	Sequence conflict	91	1	E → K in BAE35989. Ref.2
	Sequence conflict	134	1	N → D in AAH85315. Ref.4
	Sequence conflict	195	1	R → C in AAH85315. Ref.4
	Sequence conflict	300	1	A → S in AAH85315. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P16858 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: F25131EFFA9F2BD6	FASTA	333	35,810
	10 20 30 40 50 60 MVKVGVNGFG RIGRLVTRAA ICSGKVEIVA INDPFIDLNY MVYMFQYDST HGKFNGTVKA 70 80 90 100 110 120 ENGKLVINGK PITIFQERDP TNIKWGEAGA EYVVESTGVF TTMEKAGAHL KGGAKRVIIS 130 140 150 160 170 180 APSADAPMFV MGVNHEKYDN SLKIVSNASC TTNCLAPLAK VIHDNFGIVE GLMTTVHAIT 190 200 210 220 230 240 ATQKTVDGPS GKLWRDGRGA AQNIIPASTG AAKAVGKVIP ELNGKLTGMA FRVPTPNVSV 250 260 270 280 290 300 VDLTCRLEKP AKYDDIKKVV KQASEGPLKG ILGYTEDQVV SCDFNSNSHS STFDAGAGIA 310 320 330 LNDNFVKLIS WYDNEYGYSN RVVDLMAYMA SKE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Glyceraldehyde-3-phosphate dehydrogenase mRNA is a major interleukin 2-induced transcript in a cloned T-helper lymphocyte." Sabath D.E., Broome H.E., Prystowsky M.B. Gene 91:185-191(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: BALB/c, C57BL/6J and DBA/2. Tissue: Cerebellum, Eye, Head, Kidney and Lung.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	"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]. Strain: 129, C57BL/6, C57BL/6J, Czech II, FVB/N and FVB/N-3. Tissue: Brain, Colon, Embryo, Eye, Mammary gland and Mammary tumor.
[5]	Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 4-11; 27-50; 65-78; 85-105; 116-137; 144-189; 199-213; 218-246 AND 262-333, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
[6]	"Housekeeping genes for phylogenetic analysis of eutherian relationships." Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A. Mol. Biol. Evol. 23:1493-1503(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-249.
[7]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-316 AND TYR-318, MASS SPECTROMETRY. Tissue: Mast cell.
[8]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-312; TYR-316; TYR-318 AND TYR-328, MASS SPECTROMETRY. Tissue: Brain.
[9]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-209, MASS SPECTROMETRY. Tissue: Liver.
[10]	"H2S signals through protein S-sulfhydration." Mustafa A.K., Gadalla M.M., Sen N., Kim S., Mu W., Gazi S.K., Barrow R.K., Yang G., Wang R., Snyder S.H. Sci. Signal. 2:RA72-RA72(2009) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, SULFHYDRATION AT CYS-150, MUTAGENESIS OF CYS-150.
[11]	"Heterotrimeric GAIT complex drives transcript-selective translation inhibition in murine macrophages." Arif A., Chatterjee P., Moodt R.A., Fox P.L. Mol. Cell. Biol. 32:5046-5055(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, RECONSTITUTION OF THE GAIT COMPLEX.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M32599 mRNA. Translation: AAA37659.1. AK002273 mRNA. Translation: BAB21979.1. AK081405 mRNA. Translation: BAC38211.1. AK140794 mRNA. Translation: BAE24481.1. AK144690 mRNA. Translation: BAE26016.1. AK146435 mRNA. Translation: BAE27169.1. AK147738 mRNA. Translation: BAE28105.1. AK147891 mRNA. Translation: BAE28208.1. AK160399 mRNA. Translation: BAE35768.1. AK160753 mRNA. Translation: BAE35989.1. AK164415 mRNA. Translation: BAE37778.1. AK168217 mRNA. Translation: BAE40174.1. AL662926 Genomic DNA. Translation: CAI25599.1. BC082592 mRNA. Translation: AAH82592.1. BC083065 mRNA. Translation: AAH83065.1. BC083079 mRNA. Translation: AAH83079.1. BC083080 mRNA. Translation: AAH83080.1. BC083149 mRNA. Translation: AAH83149.1. BC085274 mRNA. Translation: AAH85274.1. BC085275 mRNA. Translation: AAH85275.1. BC085315 mRNA. Translation: AAH85315.1. BC091768 mRNA. Translation: AAH91768.1. BC092252 mRNA. Translation: AAH92252.1. BC092264 mRNA. Translation: AAH92264.1. BC092267 mRNA. Translation: AAH92267.1. BC092294 mRNA. Translation: AAH92294.1. BC093508 mRNA. Translation: AAH93508.1. BC094037 mRNA. Translation: AAH94037.1. BC095932 mRNA. Translation: AAH95932.1. BC096440 mRNA. Translation: AAH96440.1. BC096590 mRNA. Translation: AAH96590.1. BC110311 mRNA. Translation: AAI10312.1. BC145810 mRNA. Translation: AAI45811.1. BC145812 mRNA. Translation: AAI45813.1. DQ403054 mRNA. Translation: ABD77187.1.
IPI	IPI00273646.
PIR	DEMSG. JT0553.
RefSeq	NP_032110.1. NM_008084.2. XP_001476757.1. XM_001476707.3.
UniGene	Mm.304088. Mm.309092. Mm.317779. Mm.343110. Mm.392463. Mm.458138. Mm.458416.
3D structure databases
ProteinModelPortal	P16858.
SMR	P16858. Positions 2-333.
ModBase	Search...
Protein-protein interaction databases
IntAct	P16858. 8 interactions.
MINT	MINT-1869564.
PTM databases
PhosphoSite	P16858.
2D gel databases
REPRODUCTION-2DPAGE	P16858. Q5U410.
SWISS-2DPAGE	P16858.
Proteomic databases
PaxDb	P16858.
PRIDE	P16858.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000117757; ENSMUSP00000113942; ENSMUSG00000057666. ENSMUST00000118875; ENSMUSP00000113213; ENSMUSG00000057666.
GeneID	100042025. 14433.
KEGG	mmu:100042025. mmu:14433.
UCSC	uc007igj.1. mouse.
Organism-specific databases
CTD	2597.
MGI	MGI:95640. Gapdh.
Phylogenomic databases
eggNOG	COG0057.
GeneTree	ENSGT00690000101860.
HOVERGEN	HBG000227.
InParanoid	A6H6A8.
KO	K00134.
OMA	ASENEYK.
OrthoDB	EOG4Q84XS.
Enzyme and pathway databases
SABIO-RK	P16858.
UniPathway	UPA00109; UER00184.
Gene expression databases
ArrayExpress	P16858.
Bgee	P16858.
CleanEx	MM_GAPDH.
Genevestigator	P16858.
GermOnline	ENSMUSG00000057666. Mus musculus.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR020831. GlycerAld/Erythrose_P_DH. IPR020830. GlycerAld_3-P_DH_AS. IPR020829. GlycerAld_3-P_DH_cat. IPR020828. GlycerAld_3-P_DH_NAD(P)-bd. IPR006424. Glyceraldehyde-3-P_DH_1. IPR016040. NAD(P)-bd_dom. [Graphical view]
PANTHER	PTHR10836. PTHR10836. 1 hit.
Pfam	PF02800. Gp_dh_C. 1 hit. PF00044. Gp_dh_N. 1 hit. [Graphical view]
PIRSF	PIRSF000149. GAP_DH. 1 hit.
PRINTS	PR00078. G3PDHDRGNASE.
SMART	SM00846. Gp_dh_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR01534. GAPDH-I. 1 hit.
PROSITE	PS00071. GAPDH. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	286057.
SOURCE	Search...

Entry information

Entry name

G3P_MOUSE

Accession

Primary (citable) accession number: P16858
Secondary accession number(s): A6H6A8 , Q0QEU0, Q3THM2, Q3TUI2, Q3UMT2, Q4V783, Q569X2, Q569X5, Q5U410

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 139 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program