P52480 (KPYM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pyruvate kinase isozymes M1/M2
EC=2.7.1.40

Alternative name(s):
Pyruvate kinase muscle isozyme

Gene names

Name:	Pkm
Synonyms:	Pk3, Pkm2, Pykm

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	531 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	Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation By similarity.
Catalytic activity	ATP + pyruvate = ADP + phosphoenolpyruvate.
Cofactor	Magnesium. Potassium.
Enzyme regulation	Allosterically activated by D-fructose 1,6-bisphosphate (FBP). Inhibited by oxalate and 3,3',5-triiodo-L-thyronine (T3). The activity of the tetrameric form is inhibited by PML. Selective binding to tyrosine-phosphorylated peptides releases the allosteric activator FBP, leading to inhibition of PKM enzymatic activity, this diverts glucose metabolites from energy production to anabolic processes when cells are stimulated by certain growth factors. Glycolytic flux are highly dependent on de novo biosynthesis of serine and glycine, and serine is a natural ligand and allosteric activator By similarity.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
Subunit structure	Monomer and homotetramer. Exists as a monomer in the absence of fructose 1,6 bi-phosphate (FBP), and reversibly associates to form a homotetramer in the presence of FBP. The monomeric form binds T3. Tetramer formation induces pyruvate kinase activity. Interacts with HERC1, POU5F1 and PML. Interacts (isoform M2) with EGLN3; the interaction hydroxylates PKM under hypoxia and enhances binding to HIF1A. Interacts (isoform M2) with HIF1A; the interaction is enhanced by binding of EGLN3, promoting enhanced transcription activity under hypoxia By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Tissue specificity	Embryonic stem cells and embryonal carcinoma cells. Ref.8
Post-translational modification	ISGylated. Ref.7 Under hypoxia, hydroxylated by EGLN3 By similarity. Acetylation at Lys-305 is stimulated by high glucose concentration, it decreases enzyme activity and promotes its lysosomal-dependent degradation via chaperone-mediated autophagy By similarity.
Miscellaneous	There are 4 isozymes of pyruvate kinase in mammals (L, R, M1, M2) encoded by 2 different genes: PKLR and PKM. The L and R isozymes are generated from the PKLR by differential splicing of RNA; the M1 and M2 forms are produced from the PKM gene by differential splicing. L type is major isozyme in the liver, R is found in red cells, M1 is the main form in muscle, heart and brain, and M2 is found in early fetal tissues as well as in most cancer cells.
Sequence similarities	Belongs to the pyruvate kinase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Potassium Pyruvate
Molecular function	Kinase Transferase
PTM	Acetylation Hydroxylation Phosphoprotein Ubl conjugation
Technical term	Allosteric enzyme Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from direct assay PubMed 7262549PubMed 7295297. Source: MGI programmed cell death Inferred from electronic annotation. Source: Compara
Cellular_component	cilium Inferred from direct assay PubMed 16687649. Source: MGI mitochondrion Inferred from direct assay PubMed 14651853. Source: MGI nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: InterPro potassium ion binding Inferred from electronic annotation. Source: InterPro pyruvate kinase activity Inferred from direct assay PubMed 7262549PubMed 7295297. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Pou5f1	P20263	6	EBI-647785,EBI-1606219

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform M2 (identifier: P52480-1)

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 M1 (identifier: P52480-2)

The sequence of this isoform differs from the canonical sequence as follows:
     389-433: IYHLQLFEEL...CSGAIIVLTK → MFHRLLFEEL...LAAALIVLTE

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 531	530	Pyruvate kinase isozymes M1/M2		PRO_0000112089
Regions
	Region	307 – 531	225	Interaction with POU5F1 By similarity
	Region	389 – 433	45	Intersubunit contact
	Region	432 – 437	6	D-fructose 1,6-bisphosphate binding; part of allosteric site By similarity
	Region	514 – 521	8	D-fructose 1,6-bisphosphate binding; part of allosteric site By similarity
Sites
	Metal binding	75	1	Potassium By similarity
	Metal binding	77	1	Potassium By similarity
	Metal binding	113	1	Potassium By similarity
	Metal binding	114	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	272	1	Magnesium By similarity
	Metal binding	296	1	Magnesium By similarity
	Binding site	70	1	Serine By similarity
	Binding site	73	1	Substrate By similarity
	Binding site	106	1	Serine By similarity
	Binding site	295	1	Substrate; via amide nitrogen By similarity
	Binding site	296	1	Substrate; via amide nitrogen By similarity
	Binding site	328	1	Substrate By similarity
	Binding site	464	1	Serine By similarity
	Binding site	482	1	D-fructose 1,6-bisphosphate; part of allosteric site By similarity
	Binding site	489	1	D-fructose 1,6-bisphosphate; part of allosteric site By similarity
	Site	270	1	Transition state stabilizer By similarity
	Site	433	1	Crucial for phosphotyrosine binding By similarity
Amino acid modifications
	Modified residue	37	1	Phosphoserine By similarity
	Modified residue	62	1	N6-acetyllysine By similarity
	Modified residue	89	1	N6-acetyllysine By similarity
	Modified residue	105	1	Phosphotyrosine Ref.9
	Modified residue	148	1	Phosphotyrosine Ref.9
	Modified residue	166	1	N6-acetyllysine By similarity
	Modified residue	175	1	Phosphotyrosine By similarity
	Modified residue	195	1	Phosphothreonine By similarity
	Modified residue	266	1	N6-acetyllysine By similarity
	Modified residue	305	1	N6-acetyllysine By similarity
	Modified residue	403	1	4-hydroxyproline By similarity
	Modified residue	408	1	4-hydroxyproline By similarity
	Modified residue	433	1	N6-acetyllysine By similarity
Natural variations
	Alternative sequence	389 – 433	45	IYHLQ…IVLTK → MFHRLLFEELVRASSHSTDL MEAMAMGSVEASYKCLAAAL IVLTE in isoform M1.		VSP_025057
Experimental info
	Sequence conflict	8	1	A → V in CAA65761. Ref.2
	Sequence conflict	121	1	T → A in BAE30642. Ref.3
	Sequence conflict	121	1	T → A in BAE32031. Ref.3
	Sequence conflict	158	1	W → R in BAA07457. Ref.1
	Sequence conflict	166	1	K → E in BAE42098. Ref.3
	Sequence conflict	170	1	V → L in BAE30642. Ref.3
	Sequence conflict	170	1	V → L in BAE32031. Ref.3
	Sequence conflict	177	1	D → G in BAE42199. Ref.3
	Sequence conflict	230	1	K → R in BAE30642. Ref.3
	Sequence conflict	230	1	K → R in BAE32031. Ref.3
	Sequence conflict	299	1	I → T in BAA07457. Ref.1
	Sequence conflict	309	1	A → S in BAA07457. Ref.1
	Sequence conflict	327	1	A → S in BAA07457. Ref.1
	Sequence conflict	327	1	A → S in CAA65761. Ref.2
	Sequence conflict	333	1	S → I in BAA07457. Ref.1
	Sequence conflict	333	1	S → I in CAA65761. Ref.2
	Sequence conflict	485	1	D → N in BAE33055. Ref.3
	Sequence conflict	485	1	D → N in BAE42192. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform M2 [UniParc]. Last modified May 1, 2007. Version 4. Checksum: 34CBBC01BC0C047D	FASTA	531	57,845
	10 20 30 40 50 60 MPKPHSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSAPI TARNTGIICT IGPASRSVEM 70 80 90 100 110 120 LKEMIKSGMN VARLNFSHGT HEYHAETIKN VREATESFAS DPILYRPVAV ALDTKGPEIR 130 140 150 160 170 180 TGLIKGSGTA EVELKKGATL KITLDNAYME KCDENILWLD YKNICKVVEV GSKIYVDDGL 190 200 210 220 230 240 ISLQVKEKGA DFLVTEVENG GSLGSKKGVN LPGAAVDLPA VSEKDIQDLK FGVEQDVDMV 250 260 270 280 290 300 FASFIRKAAD VHEVRKVLGE KGKNIKIISK IENHEGVRRF DEILEASDGI MVARGDLGIE 310 320 330 340 350 360 IPAEKVFLAQ KMMIGRCNRA GKPVICATQM LESMIKKPRP TRAEGSDVAN AVLDGADCIM 370 380 390 400 410 420 LSGETAKGDY PLEAVRMQHL IAREAEAAIY HLQLFEELRR LAPITSDPTE AAAVGAVEAS 430 440 450 460 470 480 FKCCSGAIIV LTKSGRSAHQ VARYRPRAPI IAVTRNPQTA RQAHLYRGIF PVLCKDAVLN 490 500 510 520 530 AWAEDVDLRV NLAMDVGKAR GFFKKGDVVI VLTGWRPGSG FTNTMRVVPV P
	Isoform M1 [UniParc]. Checksum: D0D163786CC6D4A6	FASTA	531	57,985
	10 20 30 40 50 60 MPKPHSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSAPI TARNTGIICT IGPASRSVEM 70 80 90 100 110 120 LKEMIKSGMN VARLNFSHGT HEYHAETIKN VREATESFAS DPILYRPVAV ALDTKGPEIR 130 140 150 160 170 180 TGLIKGSGTA EVELKKGATL KITLDNAYME KCDENILWLD YKNICKVVEV GSKIYVDDGL 190 200 210 220 230 240 ISLQVKEKGA DFLVTEVENG GSLGSKKGVN LPGAAVDLPA VSEKDIQDLK FGVEQDVDMV 250 260 270 280 290 300 FASFIRKAAD VHEVRKVLGE KGKNIKIISK IENHEGVRRF DEILEASDGI MVARGDLGIE 310 320 330 340 350 360 IPAEKVFLAQ KMMIGRCNRA GKPVICATQM LESMIKKPRP TRAEGSDVAN AVLDGADCIM 370 380 390 400 410 420 LSGETAKGDY PLEAVRMQHL IAREAEAAMF HRLLFEELVR ASSHSTDLME AMAMGSVEAS 430 440 450 460 470 480 YKCLAAALIV LTESGRSAHQ VARYRPRAPI IAVTRNPQTA RQAHLYRGIF PVLCKDAVLN 490 500 510 520 530 AWAEDVDLRV NLAMDVGKAR GFFKKGDVVI VLTGWRPGSG FTNTMRVVPV P

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of the complementary DNA for the mouse pyruvate kinase M-2 gene whose expression is dependent upon cell differentiation." Izumi S., Manabe A., Tomoyasu A., Kihara-Negishi F., Ariga H. Biochim. Biophys. Acta 1267:135-138(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM M2).
[2]	"Gene expression of mouse M1 and M2 pyruvate kinase isoenzymes correlates with differential poly(A) tract extension of their mRNAs during the development of spermatogenesis." de Luis O., del Mazo J. Biochim. Biophys. Acta 1396:294-305(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM M2). Strain: Swiss.
[3]	"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] (ISOFORM M2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-395 (ISOFORM M1). Strain: C57BL/6J and NOD. Tissue: Bone marrow, Kidney and Muellerian duct.
[4]	"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.
[5]	"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] (ISOFORM M2). Strain: C57BL/6 and FVB/N. Tissue: Brain and Mammary tumor.
[6]	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 33-56; 67-89; 93-115; 126-136; 142-162; 167-224; 231-246; 248-255; 279-305; 320-336; 343-399; 401-433; 468-498 AND 506-526, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
[7]	"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells." Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E. Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract] Cited for: ISGYLATION.
[8]	"Pyruvate kinase isozyme type M2 (PKM2) interacts and cooperates with Oct-4 in regulating transcription." Lee J., Kim H.K., Han Y.-M., Kim J. Int. J. Biochem. Cell Biol. 40:1043-1054(2008) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[9]	"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-105 AND TYR-148, MASS SPECTROMETRY. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D38379 mRNA. Translation: BAA07457.1. X97047 mRNA. Translation: CAA65761.1. AK002341 mRNA. Translation: BAB22025.1. AK135397 mRNA. Translation: BAE22519.1. AK151724 mRNA. Translation: BAE30642.1. AK153483 mRNA. Translation: BAE32031.1. AK155110 mRNA. Translation: BAE33055.1. AK155655 mRNA. Translation: BAE33370.1. AK170892 mRNA. Translation: BAE42098.1. AK168943 mRNA. Translation: BAE40751.1. AK171023 mRNA. Translation: BAE42192.1. AK171033 mRNA. Translation: BAE42199.1. AC160637 Genomic DNA. No translation available. BC016619 mRNA. Translation: AAH16619.1. BC094663 mRNA. Translation: AAH94663.1.
IPI	IPI00407130. IPI00845840.
PIR	S55921.
RefSeq	NP_001240812.1. NM_001253883.1. NP_035229.2. NM_011099.3.
UniGene	Mm.326167. Mm.488724.
3D structure databases
ProteinModelPortal	P52480.
SMR	P52480. Positions 13-531.
ModBase	Search...
Protein-protein interaction databases
IntAct	P52480. 8 interactions.
MINT	MINT-1850796.
PTM databases
PhosphoSite	P52480.
2D gel databases
REPRODUCTION-2DPAGE	IPI00407130. P52480.
SWISS-2DPAGE	P52480.
Proteomic databases
PaxDb	P52480.
PRIDE	P52480.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000034834; ENSMUSP00000034834; ENSMUSG00000032294. ENSMUST00000163694; ENSMUSP00000128770; ENSMUSG00000032294.
GeneID	18746.
KEGG	mmu:18746.
UCSC	uc009pyf.1. mouse. uc009pyi.1. mouse.
Organism-specific databases
CTD	5315.
MGI	MGI:97591. Pkm.
Phylogenomic databases
eggNOG	COG0469.
GeneTree	ENSGT00390000008859.
HOVERGEN	HBG000941.
InParanoid	P52480.
KO	K00873.
OMA	VKMMATI.
OrthoDB	EOG40GCQJ.
Enzyme and pathway databases
SABIO-RK	P52480.
UniPathway	UPA00109; UER00188.
Gene expression databases
Bgee	P52480.
CleanEx	MM_PKM2.
Genevestigator	P52480.
GermOnline	ENSMUSG00000032294. Mus musculus.
Family and domain databases
Gene3D	2.40.33.10. 1 hit. 3.20.20.60. 2 hits. 3.40.1380.20. 1 hit.
InterPro	IPR001697. Pyr_Knase. IPR015813. Pyrv/PenolPyrv_Kinase. IPR011037. Pyrv_Knase-like_insert_dom. IPR015794. Pyrv_Knase_a/b. IPR018209. Pyrv_Knase_AS. IPR015793. Pyrv_Knase_brl. IPR015795. Pyrv_Knase_C. IPR015806. Pyrv_Knase_insert_dom. [Graphical view]
PANTHER	PTHR11817. PTHR11817. 1 hit.
Pfam	PF00224. PK. 1 hit. PF02887. PK_C. 1 hit. [Graphical view]
PRINTS	PR01050. PYRUVTKNASE.
SUPFAM	SSF50800. PK_B_barrel_like. 1 hit. SSF52935. Pyruvate_kinase. 1 hit. SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMs	TIGR01064. pyruv_kin. 1 hit.
PROSITE	PS00110. PYRUVATE_KINASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PKM2. mouse.
NextBio	294905.
SOURCE	Search...

Entry information

Entry name

KPYM_MOUSE

Accession

Primary (citable) accession number: P52480
Secondary accession number(s): Q3TBV8 , Q3TBW5, Q3TC59, Q3U1X3, Q3U5P6, Q4VC20, Q64484, Q91YI8, Q9CWB1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	May 1, 2007
Last modified:	April 3, 2013
This is version 139 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program