Q16644 (MAPK3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
MAP kinase-activated protein kinase 3
Short name=MAPK-activated protein kinase 3
Short name=MAPKAP kinase 3
Short name=MAPKAP-K3
Short name=MAPKAPK-3
Short name=MK-3
EC=2.7.11.1

Alternative name(s):
Chromosome 3p kinase
Short name=3pK

Gene names

Name:

MAPKAPK3

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

General annotation (Comments)

Function	Stress-activated serine/threonine-protein kinase involved in cytokines production, endocytosis, cell migration, chromatin remodeling and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. MAPKAPK2 and MAPKAPK3, share the same function and substrate specificity, but MAPKAPK3 kinase activity and level in protein expression are lower compared to MAPKAPK2. Phosphorylates HSP27/HSPB1, KRT18, KRT20, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to dissociate HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impair their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins, such as TTP/ZFP36, leading to regulate the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity leading to inhibition of dependent degradation of ARE-containing transcript. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3. Also acts as a modulator of Polycomb-mediated repression. Ref.1 Ref.7 Ref.8 Ref.11 Ref.12 Ref.13
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.7
Enzyme regulation	Activated following phosphorylation by p38-alpha/MAPK14 following various stresses. Inhibited by ligand 5B (2'-[2-(1,3-benzodioxol-5-yl)pyrimidin-4-yl]-5',6'-dihydrospiro[piperidine-4,7'-pyrrolo[3,2-c]pyridin]- 4'(1'h)-one) and ligand P4O (2-[2-(2-fluorophenyl)pyridin-4-yl]-1,5,6,7-tetrahydro- 4h-pyrrolo[3,2-c]pyridin-4-one), 2 ATP-competitive inhibitors.
Subunit structure	Heterodimer with p38-alpha/MAPK14. The heterodimer with p38-alpha/MAPK14 forms a stable complex: molecules are positioned 'face to face' so that the ATP-binding sites of both kinases are at the heterodimer interface By similarity. Interacts with TCF3 and with polycomb proteins, such as PCH2 and BMI1/PCGF4. Ref.9 Ref.11
Subcellular location	Nucleus. Cytoplasm. Note: Predominantly located in the nucleus, when activated it translocates to the cytoplasm. Ref.10
Tissue specificity	Widely expressed, with a higher expression level observed in heart and skeletal muscle. No expression in brain. Ref.1 Ref.2
Post-translational modification	Phosphorylated and activated by MAPK1/ERK2 and MAPK3/ERK1. Phosphorylated and activated by MAP kinase p38-alpha/MAPK14 at Thr-201, Ser-251 and Thr-313 By similarity. Ref.1 Ref.2
Sequence similarities	Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	MyD88-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome Ras protein signal transduction 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 innate immune response Traceable author statement. Source: Reactome macropinocytosis Inferred from sequence or structural similarity. Source: UniProtKB nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome peptidyl-serine phosphorylation Inferred from direct assay PubMed 15850461. Source: BHF-UCL response to lipopolysaccharide Inferred from sequence or structural similarity. Source: UniProtKB 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.9. Source: ProtInc protein serine/threonine kinase activity Inferred from direct assay Ref.7. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HSPB1	P04792	2	EBI-1384657,EBI-352682

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 382

382

MAP kinase-activated protein kinase 3

PRO_0000086293

Regions

Domain

44 – 304

261

Protein kinase

Nucleotide binding

50 – 58

9

ATP By similarity

Region

307 – 343

37

Autoinhibitory helix By similarity

Region

345 – 369

25

p38 MAPK-binding site By similarity

Motif

335 – 344

10

Nuclear export signal (NES) By similarity

Motif

350 – 353

4

Bipartite nuclear localization signal 1 By similarity

Motif

364 – 368

5

Bipartite nuclear localization signal 2 By similarity

Sites

Active site

166

1

Proton acceptor By similarity

Binding site

73

1

ATP By similarity

Amino acid modifications

Modified residue

201

1

Phosphothreonine; by MAPK14 By similarity

Modified residue

251

1

Phosphoserine; by MAPK14 By similarity

Modified residue

307

1

Phosphoserine; by autocatalysis By similarity

Modified residue

313

1

Phosphothreonine; by MAPK14 By similarity

Natural variations

Natural variant

28

1

P → S in a glioblastoma multiforme sample; somatic mutation. Ref.18

VAR_040755

Natural variant

105

1

E → A in an ovarian endometrioid sample; somatic mutation. Ref.18

VAR_040756

Natural variant

276

1

D → Y. Ref.18
Corresponds to variant rs56107897 [ dbSNP | Ensembl ].

VAR_040757

Experimental info

Mutagenesis

73

1

K → M: Higher affinity toward PCH2. Ref.11

Secondary structure

1

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382

Helix Strand Turn

Details...

Helix

39 – 41

3

Beta strand

43 – 53

11

Beta strand

56 – 63

8

Turn

64 – 66

3

Beta strand

69 – 78

10

Helix

79 – 91

13

Beta strand

100 – 108

9

Beta strand

111 – 119

9

Helix

126 – 131

6

Helix

140 – 159

20

Helix

169 – 171

3

Beta strand

172 – 175

4

Beta strand

183 – 185

3

Helix

218 – 237

20

Turn

267 – 269

3

Beta strand

271 – 273

3

Helix

275 – 284

10

Helix

289 – 291

3

Helix

295 – 300

6

Helix

302 – 305

4

Helix

307 – 309

3

Helix

317 – 323

7

Helix

325 – 327

3

Helix

328 – 343

16

Beta strand

344 – 346

3

Sequences

	Sequence		Length	Mass (Da)
	Q16644 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 405F958B7F54E6F3	FASTA	382	42,987
	10 20 30 40 50 60 MDGETAEEQG GPVPPPVAPG GPGLGGAPGG RREPKKYAVT DDYQLSKQVL GLGVNGKVLE 70 80 90 100 110 120 CFHRRTGQKC ALKLLYDSPK ARQEVDHHWQ ASGGPHIVCI LDVYENMHHG KRCLLIIMEC 130 140 150 160 170 180 MEGGELFSRI QERGDQAFTE REAAEIMRDI GTAIQFLHSH NIAHRDVKPE NLLYTSKEKD 190 200 210 220 230 240 AVLKLTDFGF AKETTQNALQ TPCYTPYYVA PEVLGPEKYD KSCDMWSLGV IMYILLCGFP 250 260 270 280 290 300 PFYSNTGQAI SPGMKRRIRL GQYGFPNPEW SEVSEDAKQL IRLLLKTDPT ERLTITQFMN 310 320 330 340 350 360 HPWINQSMVV PQTPLHTARV LQEDKDHWDE VKEEMTSALA TMRVDYDQVK IKDLKTSNNR 370 380 LLNKRRKKQA GSSSASQGCN NQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of mitogen-activated protein (MAP) kinase-activated protein kinase-3, a novel substrate of CSBP p38 MAP kinase." McLaughlin M.M., Kumar S., McDonnell P.C., Van Horn S., Lee J.C., Livi G.P., Young P.R. J. Biol. Chem. 271:8488-8492(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION.
[2]	"3pK, a new mitogen-activated protein kinase-activated protein kinase located in the small cell lung cancer tumor suppressor gene region." Sithanandam G., Latif F., Duh F.-M., Bernal R., Smola U., Li H., Kuzmin I., Wixler V., Geil L., Shrestha S., Lloyd P.A., Bader S., Sekido Y., Tartof K.D., Kashuba V.I., Zabarovsky E.R., Dean M., Klein G. , Lerman M.I., Minna J.D., Rapp U.R., Allikmets R. Mol. Cell. Biol. 16:868-876(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, PHOSPHORYLATION BY MAPK1/ERK2 AND MAPK3/ERK1. Tissue: Heart.
[3]	Erratum Sithanandam G., Latif F., Duh F.-M., Bernal R., Smola U., Li H., Kuzmin I., Wixler V., Geil L., Shrestha S., Lloyd P.A., Bader S., Sekido Y., Tartof K.D., Kashuba V.I., Zabarovsky E.R., Dean M., Klein G. , Lerman M.I., Minna J.D., Rapp U.R., Allikmets R. Mol. Cell. Biol. 16:1880-1880(1996)
[4]	"Human protein factory for converting the transcriptome into an in vitro-expressed proteome." Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N. Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	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].
[6]	"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: Colon and Skin.
[7]	"A comparison of the substrate specificity of MAPKAP kinase-2 and MAPKAP kinase-3 and their activation by cytokines and cellular stress." Clifton A.D., Young P.R., Cohen P. FEBS Lett. 392:209-214(1996) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, FUNCTION IN PHOSPHORYLATION OF HSPB1.
[8]	"Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation." Rogalla T., Ehrnsperger M., Preville X., Kotlyarov A., Lutsch G., Ducasse C., Paul C., Wieske M., Arrigo A.P., Buchner J., Gaestel M. J. Biol. Chem. 274:18947-18956(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF HSPB1.
[9]	"Serine/Threonine kinases 3pK and MAPK-activated protein kinase 2 interact with the basic helix-loop-helix transcription factor E47 and repress its transcriptional activity." Neufeld B., Grosse-Wilde A., Hoffmeyer A., Jordan B.W., Chen P., Dinev D., Ludwig S., Rapp U.R. J. Biol. Chem. 275:20239-20242(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TCF3.
[10]	"Mitogen-activated 3p kinase is active in the nucleus." Zakowski V., Keramas G., Kilian K., Rapp U.R., Ludwig S. Exp. Cell Res. 299:101-109(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[11]	"MAPKAP kinase 3pK phosphorylates and regulates chromatin association of the polycomb group protein Bmi1." Voncken J.W., Niessen H., Neufeld B., Rennefahrt U., Dahlmans V., Kubben N., Holzer B., Ludwig S., Rapp U.R. J. Biol. Chem. 280:5178-5187(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF LYS-73, INTERACTION WITH PHC2 AND BMI1.
[12]	"Roles for TAB1 in regulating the IL-1-dependent phosphorylation of the TAB3 regulatory subunit and activity of the TAK1 complex." Mendoza H., Campbell D.G., Burness K., Hastie J., Ronkina N., Shim J.H., Arthur J.S., Davis R.J., Gaestel M., Johnson G.L., Ghosh S., Cohen P. Biochem. J. 409:711-722(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF TAB3.
[13]	"MAPKAP kinases MK2 and MK3 in inflammation: complex regulation of TNF biosynthesis via expression and phosphorylation of tristetraprolin." Ronkina N., Menon M.B., Schwermann J., Tiedje C., Hitti E., Kotlyarov A., Gaestel M. Biochem. Pharmacol. 80:1915-1920(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"MK2 and MK3--a pair of isoenzymes?" Ronkina N., Kotlyarov A., Gaestel M. Front. Biosci. 13:5511-5521(2008) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[15]	"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].
[16]	"High-resolution crystal structure of human Mapkap kinase 3 in complex with a high affinity ligand." Cheng R., Felicetti B., Palan S., Toogood-Johnson I., Scheich C., Barker J., Whittaker M., Hesterkamp T. Protein Sci. 19:168-173(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 33-349 IN COMPLEX WITH INHIBITOR P4O.
[17]	"Structure-based lead identification of ATP-competitive MK2 inhibitors." Barf T., Kaptein A., de Wilde S., van der Heijden R., van Someren R., Demont D., Schultz-Fademrecht C., Versteegh J., van Zeeland M., Seegers N., Kazemier B., van de Kar B., van Hoek M., de Roos J., Klop H., Smeets R., Hofstra C., Hornberg J., Oubrie A. Bioorg. Med. Chem. Lett. 21:3818-3822(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 33-349 IN COMPLEX WITH INHIBITOR 5B.
[18]	"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] SER-28; ALA-105 AND TYR-276.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U43784 mRNA. Translation: AAC50428.1.
U09578 mRNA. Translation: AAD09136.1.
AB451303 mRNA. Translation: BAG70117.1.
CH471055 Genomic DNA. Translation: EAW65131.1.
BC001662 mRNA. Translation: AAH01662.1.
BC007591 mRNA. Translation: AAH07591.1.
BC010407 mRNA. Translation: AAH10407.1.

IPI

IPI00005777.

PIR

JC6094.

RefSeq

NP_001230854.1. NM_001243925.1.
NP_001230855.1. NM_001243926.1.
NP_004626.1. NM_004635.4.

UniGene

Hs.234521.
Hs.735013.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3FHR	X-ray	1.90	A	33-349	[»]
3FXW	X-ray	2.00	A	33-349	[»]
3R1N	X-ray	2.09	A	33-349	[»]
3SHE	X-ray	2.25	A	33-349	[»]

ProteinModelPortal

Q16644.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q16644. 3 interactions.

STRING

9606.ENSP00000350639.

PTM databases

PhosphoSite

Q16644.

Polymorphism databases

DMDM

74762148.

Proteomic databases

PaxDb

Q16644.

PeptideAtlas

Q16644.

PRIDE

Q16644.

Protocols and materials databases

DNASU

7867.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000357955; ENSP00000350639; ENSG00000114738.
ENST00000446044; ENSP00000396467; ENSG00000114738.

GeneID

7867.

KEGG

hsa:7867.

UCSC

uc003day.2. human.

Organism-specific databases

CTD

7867.

GeneCards

GC03P050648.

HGNC

HGNC:6888. MAPKAPK3.

MIM

602130. gene.

neXtProt

NX_Q16644.

PharmGKB

PA30632.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233031.

HOVERGEN

HBG106948.

InParanoid

Q16644.

KO

K04444.

OMA

IRMGQYG.

OrthoDB

EOG4HQDJP.

PhylomeDB

Q16644.

Enzyme and pathway databases

Pathway_Interaction_DB

p38_mk2pathway. p38 signaling mediated by MAPKAP kinases.
p38alphabetadownstreampathway. Signaling mediated by p38-alpha and p38-beta.

Reactome

REACT_111102. Signal Transduction.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q16644.

Bgee

Q16644.

CleanEx

HS_MAPKAPK3.

Genevestigator

Q16644.

GermOnline

ENSG00000114738. 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

Q16644.

ChEMBL

CHEMBL4670.

ChiTaRS

MAPKAPK3. human.

EvolutionaryTrace

Q16644.

GenomeRNAi

7867.

NextBio

30313.

SOURCE

Search...

Entry information

Entry name

MAPK3_HUMAN

Accession

Primary (citable) accession number: Q16644
Secondary accession number(s): B5BU67

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 112 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.