P46734 (MP2K3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dual specificity mitogen-activated protein kinase kinase 3
Short name=MAP kinase kinase 3
Short name=MAPKK 3
EC=2.7.12.2

Alternative name(s):
MAPK/ERK kinase 3
Short name=MEK 3
Stress-activated protein kinase kinase 2
Short name=SAPK kinase 2
Short name=SAPKK-2
Short name=SAPKK2

Gene names

Name:	MAP2K3
Synonyms:	MEK3, MKK3, PRKMK3, SKK2

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	347 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Dual specificity kinase. Is activated by cytokines and environmental stress in vivo. Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in the MAP kinase p38.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Activated by dual phosphorylation on Ser-218 and Thr-222.
Subunit structure	Binds to DYRK1B/MIRK and increases its kinase activity. Part of a complex with MAP3K3, RAC1 and CCM2. Interacts with ARRB1. Interacts with Yersinia yopJ. Ref.8 Ref.9 Ref.10
Tissue specificity	Abundant expression is seen in the skeletal muscle. It is also widely expressed in other tissues.
Post-translational modification	Autophosphorylated. Phosphorylation on Ser-218 and Thr-222 by MAP kinase kinase kinases regulates positively the kinase activity. Phosphorylated by TAOK2. Ref.6 Ref.7 Yersinia yopJ may acetylate Ser/Thr residues, preventing phosphorylation and activation, thus blocking the MAPK signaling pathway.
Involvement in disease	Defects in MAP2K3 may be involved in colon cancer.
Sequence similarities	Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase Tyrosine-protein kinase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	MyD88-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome TRIF-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome Toll signaling pathway Traceable author statement. Source: Reactome cardiac muscle contraction Inferred from electronic annotation. Source: Compara inflammatory response Inferred from electronic annotation. Source: Compara innate immune response Traceable author statement. Source: Reactome positive regulation of transcription, DNA-dependent Inferred from direct assay Ref.8. Source: UniProtKB regulation of cytokine biosynthetic process Inferred from electronic annotation. Source: Compara stress-activated MAPK cascade Traceable author statement. Source: Reactome toll-like receptor 1 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 2 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 3 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 4 signaling pathway Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase kinase activity Traceable author statement Ref.1. Source: ProtInc protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW protein tyrosine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DYRK1B	Q9Y463	2	EBI-602462,EBI-634187
LRRK2	Q5S007	3	EBI-602462,EBI-5323863
MAP3K5	Q99683	2	EBI-602462,EBI-476263

Alternative products

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

Isoform 3 (identifier: P46734-1)

Also known as: 3b;

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 1 (identifier: P46734-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: Missing.

Isoform 2 (identifier: P46734-3)

Also known as: 3c;

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: MESPASSQPASMPQSK → MGVQGTLMSRDSQTPHLLSIL

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 347	347	Dual specificity mitogen-activated protein kinase kinase 3		PRO_0000086378
Regions
	Domain	64 – 325	262	Protein kinase
	Nucleotide binding	70 – 78	9	ATP By similarity
Sites
	Active site	190	1	Proton acceptor By similarity
	Binding site	93	1	ATP By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Ref.11
	Modified residue	3	1	Phosphoserine Ref.11
	Modified residue	15	1	Phosphoserine Ref.11
	Modified residue	218	1	Phosphoserine Ref.6
	Modified residue	222	1	Phosphothreonine Ref.6
Natural variations
	Alternative sequence	1 – 29	29	Missing in isoform 1.		VSP_004878
	Alternative sequence	1 – 16	16	MESPA…MPQSK → MGVQGTLMSRDSQTPHLLSI L in isoform 2.		VSP_004877
	Natural variant	26	1	R → T. Ref.14		VAR_040817
	Natural variant	40	1	P → T. Corresponds to variant rs33911218 [ dbSNP | Ensembl ].		VAR_046062
	Natural variant	55	1	R → T. Corresponds to variant rs36047035 [ dbSNP | Ensembl ].		VAR_061742
	Natural variant	68	1	S → P. Ref.14 Corresponds to variant rs34105301 [ dbSNP | Ensembl ].		VAR_046063
	Natural variant	84	1	A → T. Ref.14 Corresponds to variant rs2305873 [ dbSNP | Ensembl ].		VAR_046064
	Natural variant	90	1	M → I. Ref.14 Corresponds to variant rs36076766 [ dbSNP | Ensembl ].		VAR_046065
	Natural variant	94	1	R → L. Ref.14 Corresponds to variant rs56067280 [ dbSNP | Ensembl ].		VAR_046066
	Natural variant	96	1	R → W. Ref.14 Corresponds to variant rs56216806 [ dbSNP | Ensembl ].		VAR_046067
	Natural variant	175	1	R → W in colon cancer. Ref.13		VAR_014208
	Natural variant	215	1	L → V in colon cancer. Ref.13		VAR_014209
	Natural variant	293	1	R → H. Ref.14 Corresponds to variant rs35206134 [ dbSNP | Ensembl ].		VAR_046068
	Natural variant	339	1	V → M. Ref.14 Corresponds to variant rs2363198 [ dbSNP | Ensembl ].		VAR_046069
Experimental info
	Mutagenesis	218	1	S → A: Inactivation. Ref.6
	Mutagenesis	218	1	S → E: Constitutive activation. Ref.6
	Mutagenesis	222	1	T → A: Inactivation. Ref.6
	Mutagenesis	222	1	T → E: Constitutive activation. Ref.6
	Sequence conflict	341	1	E → K Ref.1
	Sequence conflict	341	1	E → K Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 3 (3b) [UniParc]. Last modified November 1, 2002. Version 2. Checksum: A80BA4FDFF8F75A2	FASTA	347	39,318
	10 20 30 40 50 60 MESPASSQPA SMPQSKGKSK RKKDLRISCM SKPPAPNPTP PRNLDSRTFI TIGDRNFEVE 70 80 90 100 110 120 ADDLVTISEL GRGAYGVVEK VRHAQSGTIM AVKRIRATVN SQEQKRLLMD LDINMRTVDC 130 140 150 160 170 180 FYTVTFYGAL FREGDVWICM ELMDTSLDKF YRKVLDKNMT IPEDILGEIA VSIVRALEHL 190 200 210 220 230 240 HSKLSVIHRD VKPSNVLINK EGHVKMCDFG ISGYLVDSVA KTMDAGCKPY MAPERINPEL 250 260 270 280 290 300 NQKGYNVKSD VWSLGITMIE MAILRFPYES WGTPFQQLKQ VVEEPSPQLP ADRFSPEFVD 310 320 330 340 FTAQCLRKNP AERMSYLELM EHPFFTLHKT KKTDIAAFVK EILGEDS
	Isoform 1 [UniParc]. Checksum: 966821BE4B76E8FA	FASTA	318	36,173
	10 20 30 40 50 60 MSKPPAPNPT PPRNLDSRTF ITIGDRNFEV EADDLVTISE LGRGAYGVVE KVRHAQSGTI 70 80 90 100 110 120 MAVKRIRATV NSQEQKRLLM DLDINMRTVD CFYTVTFYGA LFREGDVWIC MELMDTSLDK 130 140 150 160 170 180 FYRKVLDKNM TIPEDILGEI AVSIVRALEH LHSKLSVIHR DVKPSNVLIN KEGHVKMCDF 190 200 210 220 230 240 GISGYLVDSV AKTMDAGCKP YMAPERINPE LNQKGYNVKS DVWSLGITMI EMAILRFPYE 250 260 270 280 290 300 SWGTPFQQLK QVVEEPSPQL PADRFSPEFV DFTAQCLRKN PAERMSYLEL MEHPFFTLHK 310 TKKTDIAAFV KEILGEDS
	Isoform 2 (3c) [UniParc]. Checksum: F59612D9001EA9C5	FASTA	352	39,940
	10 20 30 40 50 60 MGVQGTLMSR DSQTPHLLSI LGKSKRKKDL RISCMSKPPA PNPTPPRNLD SRTFITIGDR 70 80 90 100 110 120 NFEVEADDLV TISELGRGAY GVVEKVRHAQ SGTIMAVKRI RATVNSQEQK RLLMDLDINM 130 140 150 160 170 180 RTVDCFYTVT FYGALFREGD VWICMELMDT SLDKFYRKVL DKNMTIPEDI LGEIAVSIVR 190 200 210 220 230 240 ALEHLHSKLS VIHRDVKPSN VLINKEGHVK MCDFGISGYL VDSVAKTMDA GCKPYMAPER 250 260 270 280 290 300 INPELNQKGY NVKSDVWSLG ITMIEMAILR FPYESWGTPF QQLKQVVEEP SPQLPADRFS 310 320 330 340 350 PEFVDFTAQC LRKNPAERMS YLELMEHPFF TLHKTKKTDI AAFVKEILGE DS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms." Derijard B., Raingeaud J., Barrett T., Wu I.-H., Han J., Ulevitch R.J., Davis R.J. Science 267:682-685(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[2]	"Purification and identification of a major activator for p38 from osmotically shocked cells: activation of mitogen-activated protein kinase kinase 6 by osmotic shock, tumor necrosis factor-alpha, and H2O2." Moriguchi T., Toyoshima F., Gotoh Y., Iwamatsu A., Irie K., Mori E., Kuroyanagi N., Hagiwara M., Matsumoto K., Nishida E. J. Biol. Chem. 271:26981-26988(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[3]	Han J. Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS 2 AND 3).
[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] (ISOFORM 1). Tissue: Trachea.
[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 3). Tissue: Leukocyte.
[6]	"MKK3- and MKK6-regulated gene expression is mediated by the p38 mitogen-activated protein kinase signal transduction pathway." Raingeaud J., Whitmarsh A.J., Barrett T., Derijard B., Davis R.J. Mol. Cell. Biol. 16:1247-1255(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-218 AND THR-222, MUTAGENESIS OF SER-218 AND THR-222.
[7]	"Regulation of stress-responsive mitogen-activated protein (MAP) kinase pathways by TAO2." Chen Z., Cobb M.H. J. Biol. Chem. 276:16070-16075(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY TAOK2.
[8]	"Mirk protein kinase is activated by MKK3 and functions as a transcriptional activator of HNF1alpha." Lim S., Jin K., Friedman E. J. Biol. Chem. 277:25040-25046(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DYRK1B. Tissue: Muscle.
[9]	"Platelet-activating factor-induced clathrin-mediated endocytosis requires beta-arrestin-1 recruitment and activation of the p38 MAPK signalosome at the plasma membrane for actin bundle formation." McLaughlin N.J., Banerjee A., Kelher M.R., Gamboni-Robertson F., Hamiel C., Sheppard F.R., Moore E.E., Silliman C.C. J. Immunol. 176:7039-7050(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ARRB1.
[10]	"Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation." Mukherjee S., Keitany G., Li Y., Wang Y., Ball H.L., Goldsmith E.J., Orth K. Science 312:1211-1214(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH YOPJ, ACETYLATION.
[11]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-15, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"Mutation analyses of 268 candidate genes in human tumor cell lines." Teng D.-H., Chen Y., Lian L., Ha P.C., Tavtigian S.V., Wong A.K.C. Genomics 74:352-364(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS COLON CANCER TRP-175 AND VAL-215.
[14]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] THR-26; PRO-68; THR-84; ILE-90; LEU-94; TRP-96; HIS-293 AND MET-339.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L36719 mRNA. Translation: AAC41718.1. D87116 mRNA. Translation: BAA13248.1. U66839 mRNA. Translation: AAB40652.1. U66840 Genomic DNA. Translation: AAB40653.1. AK093838 mRNA. Translation: BAG52769.1. BC032478 mRNA. Translation: AAH32478.1.
IPI	IPI00218857. IPI00218858. IPI00220438.
RefSeq	NP_002747.2. NM_002756.4. NP_659731.1. NM_145109.2.
UniGene	Hs.514012.
3D structure databases
ProteinModelPortal	P46734.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-34242N.
IntAct	P46734. 5 interactions.
MINT	MINT-4300215.
STRING	9606.ENSP00000345083.
PTM databases
PhosphoSite	P46734.
Polymorphism databases
DMDM	24638466.
Proteomic databases
PaxDb	P46734.
PRIDE	P46734.
Protocols and materials databases
DNASU	5606.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000316920; ENSP00000319139; ENSG00000034152. ENST00000342679; ENSP00000345083; ENSG00000034152. ENST00000361818; ENSP00000355081; ENSG00000034152.
GeneID	5606.
KEGG	hsa:5606.
UCSC	uc002gys.3. human.
Organism-specific databases
CTD	5606.
GeneCards	GC17P021187.
HGNC	HGNC:6843. MAP2K3.
HPA	CAB018548. HPA044497.
MIM	602315. gene.
neXtProt	NX_P46734.
PharmGKB	PA30588.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000234206.
HOVERGEN	HBG108518.
KO	K04432.
OrthoDB	EOG4P2Q2M.
Enzyme and pathway databases
BRENDA	2.7.12.2. 2681.
Pathway_Interaction_DB	anthraxpathway. Cellular roles of Anthrax toxin. il12_2pathway. IL12-mediated signaling events. p38_mkk3_6pathway. p38 MAPK signaling pathway. p38alphabetapathway. Regulation of p38-alpha and p38-beta. vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2. p38gammadeltapathway. Signaling mediated by p38-gamma and p38-delta. tnfpathway. TNF receptor signaling pathway. mapktrkpathway. Trk receptor signaling mediated by the MAPK pathway.
Reactome	REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines. REACT_6900. Immune System.
Gene expression databases
ArrayExpress	P46734.
Bgee	P46734.
CleanEx	HS_MAP2K3.
Genevestigator	P46734.
GermOnline	ENSG00000034152. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P46734.
ChEMBL	CHEMBL2109.
ChiTaRS	MAP2K3. human.
GenomeRNAi	5606.
NextBio	21784.
PMAP-CutDB	P46734.
SOURCE	Search...

Entry information

Entry name

MP2K3_HUMAN

Accession

Primary (citable) accession number: P46734
Secondary accession number(s): B3KSK7 , Q99441, Q9UE71, Q9UE72

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 2002
Last modified:	May 1, 2013
This is version 138 of the entry and version 2 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.