Q9Y463 (DYR1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dual specificity tyrosine-phosphorylation-regulated kinase 1B
EC=2.7.12.1

Alternative name(s):
Minibrain-related kinase
Mirk protein kinase

Gene names

Name:	DYRK1B
Synonyms:	MIRK

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

General annotation (Comments)

Function	Dual-specificity kinase which possesses both serine/ threonine and tyrosine kinase activities. Enhances the transcriptional activity of TCF1/HNF1A and FOXO1. Inhibits epithelial cell migration. Mediates colon carcinoma cell survival in mitogen-poor environments. Ref.2 Ref.5 Ref.6
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Inhibited by RANBP9.
Subunit structure	Dimer. Interacts with DCOHM, MAP2K3/MKK3, RANBP9 and TCF1/HNF1A. Part of a complex consisting of RANBP9, RAN, DYRK1B and COPS5. Interatcs with DCAF7. Ref.5 Ref.6 Ref.7
Subcellular location	Nucleus.
Tissue specificity	Highest expression in skeletal muscle, testis, heart and brain with little expression in colon or lung. Expressed in a variety of tumor cell lines. Ref.2
Post-translational modification	Autophosphorylated on tyrosine residues. Phosphorylated by MAP kinase. Tyrosine phosphorylation may be required for dimerization. Ref.2 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MNB/DYRK subfamily. Contains 1 protein kinase domain.
Sequence caution	The sequence AAC28914.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
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	positive regulation of transcription, DNA-dependent Inferred from direct assay Ref.5. Source: UniProtKB
Cellular component	nucleus Inferred from direct assay. Source: HPA
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.5Ref.7. Source: UniProtKB protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine/tyrosine kinase activity Inferred from electronic annotation. Source: EC protein tyrosine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW transcription coactivator activity Inferred from direct assay Ref.5. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HNF1A	P20823	4	EBI-634187,EBI-636034
MAP2K3	P46734	2	EBI-634187,EBI-602462
PCBD2	Q9H0N5	2	EBI-634187,EBI-634289
RANBP9	Q96S59	4	EBI-634187,EBI-636085

Alternative products

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

Isoform 1 (identifier: Q9Y463-1)

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: Q9Y463-2)

The sequence of this isoform differs from the canonical sequence as follows:
     366-405: Missing.

Isoform 3 (identifier: Q9Y463-3)

The sequence of this isoform differs from the canonical sequence as follows:
     378-405: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 629	629	Dual specificity tyrosine-phosphorylation-regulated kinase 1B		PRO_0000085934
Regions
	Domain	111 – 431	321	Protein kinase
	Nucleotide binding	117 – 125	9	ATP By similarity
	Region	480 – 520	41	Interaction with RANBP9
	Motif	69 – 86	18	Bipartite nuclear localization signal Potential
	Compositional bias	558 – 561	4	Poly-Pro
Sites
	Active site	239	1	Proton acceptor By similarity
	Binding site	140	1	ATP By similarity
Amino acid modifications
	Modified residue	57	1	N6-acetyllysine Ref.14
	Modified residue	271	1	Phosphotyrosine; by autocatalysis Ref.11
	Modified residue	273	1	Phosphotyrosine; by autocatalysis Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
Natural variations
	Alternative sequence	366 – 405	40	Missing in isoform 2.		VSP_004925
	Alternative sequence	378 – 405	28	Missing in isoform 3.		VSP_004926
	Natural variant	28	1	L → P. Ref.15 Corresponds to variant rs34587974 [ dbSNP | Ensembl ].		VAR_040454
	Natural variant	102	1	R → H. Ref.15 Corresponds to variant rs55687541 [ dbSNP | Ensembl ].		VAR_040455
	Natural variant	234	1	S → G. Ref.15 Corresponds to variant rs35858874 [ dbSNP | Ensembl ].		VAR_040456
	Natural variant	275	1	Q → R in a metastatic melanoma sample; somatic mutation. Ref.15		VAR_040457
Experimental info
	Mutagenesis	140	1	K → R: Abolishes kinase activity. Ref.2
	Mutagenesis	271	1	Y → F: Abolishes kinase activity; when associated with F-273. Ref.2
	Mutagenesis	273	1	Y → F: Abolishes kinase activity; when associated with F-271. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: D7C354AC55943A8B	FASTA	629	69,198
	10 20 30 40 50 60 MAVPPGHGPF SGFPGPQEHT QVLPDVRLLP RRLPLAFRDA TSAPLRKLSV DLIKTYKHIN 70 80 90 100 110 120 EVYYAKKKRR AQQAPPQDSS NKKEKKVLNH GYDDDNHDYI VRSGERWLER YEIDSLIGKG 130 140 150 160 170 180 SFGQVVKAYD HQTQELVAIK IIKNKKAFLN QAQIELRLLE LMNQHDTEMK YYIVHLKRHF 190 200 210 220 230 240 MFRNHLCLVF ELLSYNLYDL LRNTHFRGVS LNLTRKLAQQ LCTALLFLAT PELSIIHCDL 250 260 270 280 290 300 KPENILLCNP KRSAIKIVDF GSSCQLGQRI YQYIQSRFYR SPEVLLGTPY DLAIDMWSLG 310 320 330 340 350 360 CILVEMHTGE PLFSGSNEVD QMNRIVEVLG IPPAAMLDQA PKARKYFERL PGGGWTLRRT 370 380 390 400 410 420 KELRKDYQGP GTRRLQEVLG VQTGGPGGRR AGEPGHSPAD YLRFQDLVLR MLEYEPAARI 430 440 450 460 470 480 SPLGALQHGF FRRTADEATN TGPAGSSAST SPAPLDTCPS SSTASSISSS GGSSGSSSDN 490 500 510 520 530 540 RTYRYSNRYC GGPGPPITDC EMNSPQVPPS QPLRPWAGGD VPHKTHQAPA SASSLPGTGA 550 560 570 580 590 600 QLPPQPRYLG RPPSPTSPPP PELMDVSLVG GPADCSPPHP APAPQHPAAS ALRTRMTGGR 610 620 PPLPPPDDPA TLGPHLGLRG VPQSTAASS
	Isoform 2 [UniParc]. Checksum: E98BF9B257237A9D	FASTA	589	64,934
	10 20 30 40 50 60 MAVPPGHGPF SGFPGPQEHT QVLPDVRLLP RRLPLAFRDA TSAPLRKLSV DLIKTYKHIN 70 80 90 100 110 120 EVYYAKKKRR AQQAPPQDSS NKKEKKVLNH GYDDDNHDYI VRSGERWLER YEIDSLIGKG 130 140 150 160 170 180 SFGQVVKAYD HQTQELVAIK IIKNKKAFLN QAQIELRLLE LMNQHDTEMK YYIVHLKRHF 190 200 210 220 230 240 MFRNHLCLVF ELLSYNLYDL LRNTHFRGVS LNLTRKLAQQ LCTALLFLAT PELSIIHCDL 250 260 270 280 290 300 KPENILLCNP KRSAIKIVDF GSSCQLGQRI YQYIQSRFYR SPEVLLGTPY DLAIDMWSLG 310 320 330 340 350 360 CILVEMHTGE PLFSGSNEVD QMNRIVEVLG IPPAAMLDQA PKARKYFERL PGGGWTLRRT 370 380 390 400 410 420 KELRKDLVLR MLEYEPAARI SPLGALQHGF FRRTADEATN TGPAGSSAST SPAPLDTCPS 430 440 450 460 470 480 SSTASSISSS GGSSGSSSDN RTYRYSNRYC GGPGPPITDC EMNSPQVPPS QPLRPWAGGD 490 500 510 520 530 540 VPHKTHQAPA SASSLPGTGA QLPPQPRYLG RPPSPTSPPP PELMDVSLVG GPADCSPPHP 550 560 570 580 APAPQHPAAS ALRTRMTGGR PPLPPPDDPA TLGPHLGLRG VPQSTAASS
	Isoform 3 [UniParc]. Checksum: 8601907D9652274B	FASTA	601	66,336
	10 20 30 40 50 60 MAVPPGHGPF SGFPGPQEHT QVLPDVRLLP RRLPLAFRDA TSAPLRKLSV DLIKTYKHIN 70 80 90 100 110 120 EVYYAKKKRR AQQAPPQDSS NKKEKKVLNH GYDDDNHDYI VRSGERWLER YEIDSLIGKG 130 140 150 160 170 180 SFGQVVKAYD HQTQELVAIK IIKNKKAFLN QAQIELRLLE LMNQHDTEMK YYIVHLKRHF 190 200 210 220 230 240 MFRNHLCLVF ELLSYNLYDL LRNTHFRGVS LNLTRKLAQQ LCTALLFLAT PELSIIHCDL 250 260 270 280 290 300 KPENILLCNP KRSAIKIVDF GSSCQLGQRI YQYIQSRFYR SPEVLLGTPY DLAIDMWSLG 310 320 330 340 350 360 CILVEMHTGE PLFSGSNEVD QMNRIVEVLG IPPAAMLDQA PKARKYFERL PGGGWTLRRT 370 380 390 400 410 420 KELRKDYQGP GTRRLQEDLV LRMLEYEPAA RISPLGALQH GFFRRTADEA TNTGPAGSSA 430 440 450 460 470 480 STSPAPLDTC PSSSTASSIS SSGGSSGSSS DNRTYRYSNR YCGGPGPPIT DCEMNSPQVP 490 500 510 520 530 540 PSQPLRPWAG GDVPHKTHQA PASASSLPGT GAQLPPQPRY LGRPPSPTSP PPPELMDVSL 550 560 570 580 590 600 VGGPADCSPP HPAPAPQHPA ASALRTRMTG GRPPLPPPDD PATLGPHLGL RGVPQSTAAS S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of DYRK1B, a novel member of the DYRK family of protein kinases." Leder S., Weber Y., Altafaj X., Estivill X., Joost H.-G., Becker W. Biochem. Biophys. Res. Commun. 254:474-479(1999) [PubMed: 9918863] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3). Tissue: Testis.
[2]	"Mirk protein kinase is a mitogen-activated protein kinase substrate that mediates survival of colon cancer cells." Lee K., Deng X., Friedman E. Cancer Res. 60:3631-3637(2000) [PubMed: 10910078] [Abstract] Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, MUTAGENESIS OF LYS-140; TYR-271 AND TYR-273. Tissue: Colon carcinoma.
[3]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed: 15057824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Pancreas.
[5]	"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: 11980910] [Abstract] Cited for: FUNCTION, INTERACTION WITH DCOHM; MAP2K3 AND TCF1. Tissue: Muscle.
[6]	"Serine/threonine kinase Mirk/Dyrk1B is an inhibitor of epithelial cell migration and is negatively regulated by the Met adaptor Ran-binding protein M." Zou Y., Lim S., Lee K., Deng X., Friedman E. J. Biol. Chem. 278:49573-49581(2003) [PubMed: 14500717] [Abstract] Cited for: FUNCTION, DIMERIZATION, INTERACTION WITH RANBP9, IDENTIFICATION IN A COMPLEX WITH RAN; RANBP9 AND COPS5.
[7]	"Phosphorylation of Ser640 in muscle glycogen synthase by DYRK family protein kinases." Skurat A.V., Dietrich A.D. J. Biol. Chem. 279:2490-2498(2004) [PubMed: 14593110] [Abstract] Cited for: INTERACTION WITH DCAF7.
[8]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-273, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[9]	"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks." Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M. Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-273, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[10]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-273, MASS SPECTROMETRY. Tissue: Platelet.
[11]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-271 AND TYR-273, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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 TYR-273, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-273, MASS SPECTROMETRY.
[14]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-57, MASS SPECTROMETRY.
[15]	"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: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] PRO-28; HIS-102; GLY-234 AND ARG-275.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y17999 mRNA. Translation: CAA76991.1. Y17999 mRNA. Translation: CAA76990.1. Y17999 mRNA. Translation: CAA76989.1. AF205861 mRNA. Translation: AAF15893.1. AC005393 Genomic DNA. Translation: AAC28914.1. Sequence problems. BC018751 mRNA. Translation: AAH18751.1. BC025291 mRNA. Translation: AAH25291.1.
IPI	IPI00000352. IPI00215873. IPI00332215.
PIR	JG0195.
RefSeq	NP_004705.1. NM_004714.1. NP_006474.1. NM_006483.1. NP_006475.1. NM_006484.1.
UniGene	Hs.130988.
3D structure databases
ProteinModelPortal	Q9Y463.
SMR	Q9Y463. Positions 100-433.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y463. 5 interactions.
MINT	MINT-2790122.
STRING	Q9Y463.
PTM databases
PhosphoSite	Q9Y463.
Polymorphism databases
DMDM	9296963.
Proteomic databases
PRIDE	Q9Y463.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000323039; ENSP00000312789; ENSG00000105204.
GeneID	9149.
KEGG	hsa:9149.
UCSC	uc002omi.1. human. uc002omj.1. human. uc002omk.1. human.
Organism-specific databases
CTD	9149.
GeneCards	GC19M040316.
H-InvDB	HIX0202834.
HGNC	HGNC:3092. DYRK1B.
HPA	HPA028786.
MIM	604556. gene.
neXtProt	NX_Q9Y463.
PharmGKB	PA27549.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG14617.
GeneTree	ENSGT00550000074148.
HOGENOM	HBG755340.
HOVERGEN	HBG051425.
InParanoid	Q9Y463.
OMA	PAPMLEQ.
OrthoDB	EOG42NJ05.
PhylomeDB	Q9Y463.
Enzyme and pathway databases
BRENDA	2.7.12.1. 2681.
Gene expression databases
ArrayExpress	Q9Y463.
Bgee	Q9Y463.
CleanEx	HS_DYRK1B.
Genevestigator	Q9Y463.
GermOnline	ENSG00000105204. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. [Graphical view]
KO	K08825.
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
NextBio	34319.
SOURCE	Search...

Entry information

Entry name

DYR1B_HUMAN

Accession

Primary (citable) accession number: Q9Y463
Secondary accession number(s): O75258, O75788, O75789

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1999
Last modified:	January 25, 2012
This is version 120 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.