Reviewed, UniProtKB/Swiss-Prot Q9Z188 (DYR1B_MOUSE)

Names and origin

Protein names

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

Gene names

Name:

Dyrk1b

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	629 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Dual-specificity kinase which possesses both serine/ threonine and tyrosine kinase activity. Enhances the transcriptional activity of TCF1/HNF1A and FOXO1. Inhibits epithelial cell migration. Mediates colon carcinoma cell survival in mitogen-poor environments. Ref.2
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.2
Enzyme regulation	Inhibited by RANBP9 By similarity.
Subunit structure	Dimer. Interacts with DCOHM, MAP2K3/MKK3 and TCF1/HNF1A. Part of a complex consisting of RANBP9, RAN, DYRK1B and COPS5 By similarity. Interatcs with WDR68 By similarity.
Subcellular location	Nucleus.
Tissue specificity	Isoform 1 and isoform 2 are broadly expressed. Isoform 3 seems specific for skeletal muscle (at protein level). Ref.2
Developmental stage	Isoform 1 is present from 14 dpc. Isoform 3 is present from 18 dpc (at protein level). Ref.2
Post-translational modification	Phosphorylated by MAP kinase. Tyrosine phosphorylation may be required for dimerization By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MNB/DYRK subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase Tyrosine-protein kinase
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	myoblast fusion Inferred from mutant phenotype. Source: MGI protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW 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...

Alternative products

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

Isoform 1 (identifier: Q9Z188-1)

Also known as: p69;

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: Q9Z188-2)

Also known as: p65;

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

Note: Inactive.

Isoform 3 (identifier: Q9Z188-3)

Also known as: p75;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLAARPPHWGPHRAPAPRGPSAIPDPGLSGGGSRGAGCEKAPPGRAPAPGLTPLRPSEPTM

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_0000085935
Regions
	Domain	111 – 431	321	Protein kinase
	Nucleotide binding	117 – 125	9	ATP By similarity
	Region	480 – 520	41	Interaction with RANBP9 By similarity
	Motif	69 – 86	18	Bipartite nuclear localization signal Potential
	Compositional bias	558 – 561	4	Poly-Pro
	Compositional bias	577 – 584	8	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 By similarity
	Modified residue	271	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	273	1	Phosphotyrosine Ref.5 Ref.6 Ref.7 Ref.8 Ref.9
Natural variations
	Alternative sequence	1	1	M → MLAARPPHWGPHRAPAPRGP SAIPDPGLSGGGSRGAGCEK APPGRAPAPGLTPLRPSEPT M in isoform 3.		VSP_022954
	Alternative sequence	366 – 405	40	Missing in isoform 2.		VSP_022955
Experimental info
	Sequence conflict	459	1	P → H in BAE28495. Ref.4
	Sequence conflict	531	1	S → P in BAE28495. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (p69) [UniParc]. Last modified February 6, 2007. Version 3. Checksum: 54FCE6DBD3918D1C	FASTA	629	69,178
	10 20 30 40 50 60 MAVPPGHGPF SGFPGPQEHT QVLPDVRLLP RRLPLAFRDA ASAPLRKLSV DLIKTYKHIN 70 80 90 100 110 120 EVYYAKKKRR AQQAPPQDSS TKKEKKVLNH 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 QMSRIVEVLG IPPAPMLEQA 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 GGSSGSSNDN 490 500 510 520 530 540 RAYRYSNRYC GGPGPPITDC EMNSPQVLPS QPLRPWAGGD VPHKTHQAPI SASTLPGTGA 550 560 570 580 590 600 QLPPLPRCLG RPPSPTSPPP PELMDVSLVG SPPDCSPPPP APAPQHPAAS ALRTRMTGGR 610 620 PPLPPPDDPA TLGPRLGLHG VPQSTAASS
	Isoform 2 (p65). Checksum: 48B4242AD6E8401E	FASTA	589	64,914
	10 20 30 40 50 60 MAVPPGHGPF SGFPGPQEHT QVLPDVRLLP RRLPLAFRDA ASAPLRKLSV DLIKTYKHIN 70 80 90 100 110 120 EVYYAKKKRR AQQAPPQDSS TKKEKKVLNH 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 QMSRIVEVLG IPPAPMLEQA PKARKYFERL PGGGWTLRRT 370 380 390 400 410 420 KELRKDLVLR MLEYEPAARI SPLGALQHGF FRRTADEATN TGPAGSSAST SPAPLDTCPS 430 440 450 460 470 480 SSTASSISSS GGSSGSSNDN RAYRYSNRYC GGPGPPITDC EMNSPQVLPS QPLRPWAGGD 490 500 510 520 530 540 VPHKTHQAPI SASTLPGTGA QLPPLPRCLG RPPSPTSPPP PELMDVSLVG SPPDCSPPPP 550 560 570 580 APAPQHPAAS ALRTRMTGGR PPLPPPDDPA TLGPRLGLHG VPQSTAASS
	Isoform 3 (p75). Checksum: 8A1437EF65C65B50	FASTA	689	75,095
	10 20 30 40 50 60 MLAARPPHWG PHRAPAPRGP SAIPDPGLSG GGSRGAGCEK APPGRAPAPG LTPLRPSEPT 70 80 90 100 110 120 MAVPPGHGPF SGFPGPQEHT QVLPDVRLLP RRLPLAFRDA ASAPLRKLSV DLIKTYKHIN 130 140 150 160 170 180 EVYYAKKKRR AQQAPPQDSS TKKEKKVLNH GYDDDNHDYI VRSGERWLER YEIDSLIGKG 190 200 210 220 230 240 SFGQVVKAYD HQTQELVAIK IIKNKKAFLN QAQIELRLLE LMNQHDTEMK YYIVHLKRHF 250 260 270 280 290 300 MFRNHLCLVF ELLSYNLYDL LRNTHFRGVS LNLTRKLAQQ LCTALLFLAT PELSIIHCDL 310 320 330 340 350 360 KPENILLCNP KRSAIKIVDF GSSCQLGQRI YQYIQSRFYR SPEVLLGTPY DLAIDMWSLG 370 380 390 400 410 420 CILVEMHTGE PLFSGSNEVD QMSRIVEVLG IPPAPMLEQA PKARKYFERL PGGGWTLRRT 430 440 450 460 470 480 KELRKDYQGP GTRRLQEVLG VQTGGPGGRR AGEPGHSPAD YLRFQDLVLR MLEYEPAARI 490 500 510 520 530 540 SPLGALQHGF FRRTADEATN TGPAGSSAST SPAPLDTCPS SSTASSISSS GGSSGSSNDN 550 560 570 580 590 600 RAYRYSNRYC GGPGPPITDC EMNSPQVLPS QPLRPWAGGD VPHKTHQAPI SASTLPGTGA 610 620 630 640 650 660 QLPPLPRCLG RPPSPTSPPP PELMDVSLVG SPPDCSPPPP APAPQHPAAS ALRTRMTGGR 670 680 PPLPPPDDPA TLGPRLGLHG VPQSTAASS

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 [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2). Strain: 129/SvJ and NMRI. Tissue: Liver and Testis.
[2]	"Alternative splicing variants of dual specificity tyrosine phosphorylated and regulated kinase 1B exhibit distinct patterns of expression and functional properties." Leder S., Czajkowska H., Maenz B., De Graaf K., Barthel A., Joost H.-G., Becker W. Biochem. J. 372:881-888(2003) [PubMed: 12633499] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, CATALYTIC ACTIVITY, FUNCTION. Strain: NMRI.
[3]	"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: Eye.
[4]	"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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-533 (ISOFORM 2). Strain: C57BL/6J.
[5]	"Proteomic analysis of in vivo phosphorylated synaptic proteins." Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I., Blackstock W.P., Choudhary J.S., Grant S.G. J. Biol. Chem. 280:5972-5982(2005) [PubMed: 15572359] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-273, MASS SPECTROMETRY. Tissue: Brain.
[6]	"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: 17947660] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-273, MASS SPECTROMETRY. Tissue: Mast cell.
[7]	"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.
[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: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-273, MASS SPECTROMETRY. Tissue: Brain.
[9]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-273, MASS SPECTROMETRY. Tissue: Brain cortex.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Y18280 mRNA. Translation: CAA77101.2. AJ252172 Genomic DNA. Translation: CAC20675.1. AJ537610 mRNA. Translation: CAD61290.1. BC019545 mRNA. Translation: AAH19545.1. AK148342 mRNA. Translation: BAE28495.1.
IPI	IPI00323385. IPI00460677. IPI00761738.
PIR	JG0196.
RefSeq	NP_001033046.1. NP_034222.1.
UniGene	Mm.57249
3D structure databases
HSSP	HSSP built from PDB template 1JOW based on UniProtKB Q00534.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9Z188.
PTM databases
PhosphoSite	Q9Z188.
Proteomic databases
PRIDE	Q9Z188.
Genome annotation databases
Ensembl	ENSMUST00000002483; ENSMUSP00000002483; ENSMUSG00000002409; Mus musculus. [Genome view] ENSMUST00000085901; ENSMUSP00000083064; ENSMUSG00000002409; Mus musculus. [Genome view]
GeneID	13549.
KEGG	mmu:13549.
UCSC	uc009fxz.1. mouse. uc009fya.1. mouse. uc009fyb.1. mouse.
Organism-specific databases
CTD	13549.
MGI	MGI:1330302. Dyrk1b.
Phylogenomic databases
HOVERGEN	Q9Z188.
OMA	LVGGPPD.
Gene expression databases
ArrayExpress	Q9Z188.
Bgee	Q9Z188.
Genevestigator	Q9Z188.
Family and domain databases
InterPro	IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	284162.
SOURCE	Search...

Entry information

Entry name

DYR1B_MOUSE

Accession

Primary (citable) accession number: Q9Z188
Secondary accession number(s): Q3UFR5, Q70UR5, Q9EPM2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	February 6, 2007
Last modified:	November 3, 2009
This is version 81 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)