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Protein

Dual specificity tyrosine-phosphorylation-regulated kinase 1B

Gene

Dyrk1b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Inhibits the SHH and WNT1 pathways, thereby enhancing adipogenesis. In addition, promotes expression of the gluconeogenic enzyme glucose-6-phosphatase (G6PC).By similarity1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Enzyme regulationi

Inhibited by RANBP9.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei140 – 1401ATPPROSITE-ProRule annotation
Active sitei239 – 2391Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi117 – 1259ATPPROSITE-ProRule annotation
Nucleotide bindingi190 – 1934ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • adipose tissue development Source: UniProtKB
  • myoblast fusion Source: MGI
  • positive regulation of transcription, DNA-templated Source: MGI
  • protein phosphorylation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.12.1. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity tyrosine-phosphorylation-regulated kinase 1B (EC:2.7.12.1)
Gene namesi
Name:Dyrk1b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1330302. Dyrk1b.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 629629Dual specificity tyrosine-phosphorylation-regulated kinase 1BPRO_0000085935Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei63 – 631PhosphotyrosineBy similarity
Modified residuei92 – 921PhosphotyrosineBy similarity
Modified residuei111 – 1111PhosphotyrosineBy similarity
Modified residuei129 – 1291PhosphotyrosineBy similarity
Modified residuei171 – 1711PhosphotyrosineBy similarity
Modified residuei262 – 2621PhosphoserineBy similarity
Modified residuei271 – 2711Phosphotyrosine; by autocatalysisBy similarity
Modified residuei273 – 2731PhosphotyrosineBy similarity
Modified residuei401 – 4011PhosphotyrosineBy similarity
Modified residuei624 – 6241PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by MAP kinase. Tyrosine phosphorylation may be required for dimerization (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9Z188.
MaxQBiQ9Z188.
PaxDbiQ9Z188.
PRIDEiQ9Z188.

PTM databases

iPTMnetiQ9Z188.
PhosphoSiteiQ9Z188.

Expressioni

Tissue specificityi

Isoform 1 and isoform 2 are broadly expressed. Isoform 3 seems specific for skeletal muscle (at protein level).1 Publication

Developmental stagei

Isoform 1 is present from 14 dpc. Isoform 3 is present from 18 dpc (at protein level).1 Publication

Gene expression databases

BgeeiQ9Z188.
GenevisibleiQ9Z188. MM.

Interactioni

Subunit structurei

Dimer. Interacts with DCOHM, MAP2K3/MKK3 and TCF1/HNF1A. Part of a complex consisting of RANBP9, RAN, DYRK1B and COPS5 (By similarity). Interacts with DCAF7 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000083064.

Structurei

3D structure databases

ProteinModelPortaliQ9Z188.
SMRiQ9Z188. Positions 100-459.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini111 – 431321Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni480 – 52041Interaction with RANBP9By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi69 – 8618Bipartite nuclear localization signalSequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi558 – 5614Poly-Pro
Compositional biasi577 – 5848Poly-Pro

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0667. Eukaryota.
ENOG410XPET. LUCA.
GeneTreeiENSGT00760000119032.
HOGENOMiHOG000220863.
HOVERGENiHBG051425.
InParanoidiQ9Z188.
KOiK08825.
OMAiRAYRYSN.
OrthoDBiEOG77127N.
PhylomeDBiQ9Z188.
TreeFamiTF314624.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Z188-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAVPPGHGPF SGFPGPQEHT QVLPDVRLLP RRLPLAFRDA ASAPLRKLSV
60 70 80 90 100
DLIKTYKHIN EVYYAKKKRR AQQAPPQDSS TKKEKKVLNH GYDDDNHDYI
110 120 130 140 150
VRSGERWLER YEIDSLIGKG SFGQVVKAYD HQTQELVAIK IIKNKKAFLN
160 170 180 190 200
QAQIELRLLE LMNQHDTEMK YYIVHLKRHF MFRNHLCLVF ELLSYNLYDL
210 220 230 240 250
LRNTHFRGVS LNLTRKLAQQ LCTALLFLAT PELSIIHCDL KPENILLCNP
260 270 280 290 300
KRSAIKIVDF GSSCQLGQRI YQYIQSRFYR SPEVLLGTPY DLAIDMWSLG
310 320 330 340 350
CILVEMHTGE PLFSGSNEVD QMSRIVEVLG IPPAPMLEQA PKARKYFERL
360 370 380 390 400
PGGGWTLRRT KELRKDYQGP GTRRLQEVLG VQTGGPGGRR AGEPGHSPAD
410 420 430 440 450
YLRFQDLVLR MLEYEPAARI SPLGALQHGF FRRTADEATN TGPAGSSAST
460 470 480 490 500
SPAPLDTCPS SSTASSISSS GGSSGSSNDN RAYRYSNRYC GGPGPPITDC
510 520 530 540 550
EMNSPQVLPS QPLRPWAGGD VPHKTHQAPI SASTLPGTGA QLPPLPRCLG
560 570 580 590 600
RPPSPTSPPP PELMDVSLVG SPPDCSPPPP APAPQHPAAS ALRTRMTGGR
610 620
PPLPPPDDPA TLGPRLGLHG VPQSTAASS
Length:629
Mass (Da):69,178
Last modified:February 6, 2007 - v3
Checksum:i54FCE6DBD3918D1C
GO
Isoform 2 (identifier: Q9Z188-2) [UniParc]FASTAAdd to basket

Also known as: p65

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

Note: Inactive.
Show »
Length:589
Mass (Da):64,914
Checksum:i48B4242AD6E8401E
GO
Isoform 3 (identifier: Q9Z188-3) [UniParc]FASTAAdd to basket

Also known as: p75

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

Show »
Length:689
Mass (Da):75,095
Checksum:i8A1437EF65C65B50
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti459 – 4591P → H in BAE28495 (PubMed:16141072).Curated
Sequence conflicti531 – 5311S → P in BAE28495 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MLAARPPHWGPHRAPAPRGP SAIPDPGLSGGGSRGAGCEK APPGRAPAPGLTPLRPSEPT M in isoform 3. 1 PublicationVSP_022954
Alternative sequencei366 – 40540Missing in isoform 2. 2 PublicationsVSP_022955Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS21037.1. [Q9Z188-1]
CCDS57532.1. [Q9Z188-2]
PIRiJG0196.
RefSeqiNP_001033046.1. NM_001037957.3. [Q9Z188-1]
NP_001258299.1. NM_001271370.1. [Q9Z188-3]
NP_034222.1. NM_010092.2. [Q9Z188-2]
UniGeneiMm.57249.

Genome annotation databases

EnsembliENSMUST00000085901; ENSMUSP00000083064; ENSMUSG00000002409. [Q9Z188-1]
ENSMUST00000172467; ENSMUSP00000133431; ENSMUSG00000002409. [Q9Z188-3]
ENSMUST00000172761; ENSMUSP00000133719; ENSMUSG00000002409. [Q9Z188-2]
GeneIDi13549.
KEGGimmu:13549.
UCSCiuc009fxz.2. mouse. [Q9Z188-2]
uc009fya.2. mouse. [Q9Z188-1]
uc009fyb.2. mouse. [Q9Z188-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS21037.1. [Q9Z188-1]
CCDS57532.1. [Q9Z188-2]
PIRiJG0196.
RefSeqiNP_001033046.1. NM_001037957.3. [Q9Z188-1]
NP_001258299.1. NM_001271370.1. [Q9Z188-3]
NP_034222.1. NM_010092.2. [Q9Z188-2]
UniGeneiMm.57249.

3D structure databases

ProteinModelPortaliQ9Z188.
SMRiQ9Z188. Positions 100-459.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000083064.

PTM databases

iPTMnetiQ9Z188.
PhosphoSiteiQ9Z188.

Proteomic databases

EPDiQ9Z188.
MaxQBiQ9Z188.
PaxDbiQ9Z188.
PRIDEiQ9Z188.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000085901; ENSMUSP00000083064; ENSMUSG00000002409. [Q9Z188-1]
ENSMUST00000172467; ENSMUSP00000133431; ENSMUSG00000002409. [Q9Z188-3]
ENSMUST00000172761; ENSMUSP00000133719; ENSMUSG00000002409. [Q9Z188-2]
GeneIDi13549.
KEGGimmu:13549.
UCSCiuc009fxz.2. mouse. [Q9Z188-2]
uc009fya.2. mouse. [Q9Z188-1]
uc009fyb.2. mouse. [Q9Z188-3]

Organism-specific databases

CTDi9149.
MGIiMGI:1330302. Dyrk1b.

Phylogenomic databases

eggNOGiKOG0667. Eukaryota.
ENOG410XPET. LUCA.
GeneTreeiENSGT00760000119032.
HOGENOMiHOG000220863.
HOVERGENiHBG051425.
InParanoidiQ9Z188.
KOiK08825.
OMAiRAYRYSN.
OrthoDBiEOG77127N.
PhylomeDBiQ9Z188.
TreeFamiTF314624.

Enzyme and pathway databases

BRENDAi2.7.12.1. 3474.

Miscellaneous databases

NextBioi284162.
PROiQ9Z188.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z188.
GenevisibleiQ9Z188. MM.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-533 (ISOFORM 2).
    Strain: C57BL/6J.

Entry informationi

Entry nameiDYR1B_MOUSE
AccessioniPrimary (citable) accession number: Q9Z188
Secondary accession number(s): Q3UFR5, Q70UR5, Q9EPM2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: February 6, 2007
Last modified: May 11, 2016
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.