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Protein

Dual specificity tyrosine-phosphorylation-regulated kinase 1B

Gene

DYRK1B

Organism
Homo sapiens (Human)
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 activities. 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).4 Publications

Catalytic activityi

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

Enzyme regulationi

Inhibited by RANBP9.

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

  1. ATP binding Source: UniProtKB-KW
  2. protein kinase activity Source: UniProtKB
  3. protein serine/threonine/tyrosine kinase activity Source: UniProtKB-EC
  4. protein serine/threonine kinase activity Source: UniProtKB-KW
  5. protein tyrosine kinase activity Source: UniProtKB-KW
  6. transcription coactivator activity Source: UniProtKB

GO - Biological processi

  1. adipose tissue development Source: UniProtKB
  2. myoblast fusion Source: Ensembl
  3. positive regulation of transcription, DNA-templated Source: UniProtKB
  4. protein phosphorylation Source: UniProtKB
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

BioCyciMetaCyc:HS02690-MONOMER.
BRENDAi2.7.12.1. 2681.
SignaLinkiQ9Y463.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity tyrosine-phosphorylation-regulated kinase 1B (EC:2.7.12.1)
Alternative name(s):
Minibrain-related kinase
Mirk protein kinase
Gene namesi
Name:DYRK1B
Synonyms:MIRK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:3092. DYRK1B.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Abdominal obesity-metabolic syndrome 31 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of abdominal obesity-metabolic syndrome, a disorder characterized by abdominal obesity, high triglycerides, low levels of high density lipoprotein cholesterol, high blood pressure, and elevated fasting glucose levels. AOMS3 is characterized by early-onset coronary artery disease, central obesity, hypertension, and diabetes.

See also OMIM:615812
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti90 – 901H → P in AOMS3; expression of glucose-6-phosphatase is significantly higher than wild-type. 1 Publication
VAR_071773
Natural varianti102 – 1021R → C in AOMS3; accumulation of intracellular lipid is significantly greater than with wild-type protein; cells expressing the variant are able to transform into mature adipocytes without requiring adipogenic medium; expression levels of CEBPA, PPARG forms 1 and 2 and PPARGC1A are higher and those of GLI1 and CDKN1B are lower in cells transfected with the mutant protein compared to wild-type; WNT1 signaling activity is lower in mutant cells compared to wild-type. 1 Publication
VAR_071774

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi140 – 1401K → R: Abolishes kinase activity. 1 Publication
Mutagenesisi271 – 2711Y → F: Abolishes kinase activity; when associated with F-273. 1 Publication
Mutagenesisi273 – 2731Y → F: Abolishes kinase activity; when associated with F-271. 1 Publication

Keywords - Diseasei

Diabetes mellitus, Obesity

Organism-specific databases

MIMi615812. phenotype.
PharmGKBiPA27549.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 629629Dual specificity tyrosine-phosphorylation-regulated kinase 1BPRO_0000085934Add
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 autocatalysis1 Publication
Modified residuei273 – 2731Phosphotyrosine; by autocatalysis1 Publication
Modified residuei401 – 4011PhosphotyrosineBy similarity
Modified residuei624 – 6241PhosphoserineBy similarity

Post-translational modificationi

Autophosphorylated on tyrosine residues. Phosphorylated by MAP kinase. Tyrosine phosphorylation may be required for dimerization.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y463.
PaxDbiQ9Y463.
PRIDEiQ9Y463.

PTM databases

PhosphoSiteiQ9Y463.

Expressioni

Tissue specificityi

Highest expression in skeletal muscle, testis, heart and brain with little expression in colon or lung. Expressed in a variety of tumor cell lines.1 Publication

Gene expression databases

BgeeiQ9Y463.
CleanExiHS_DYRK1B.
ExpressionAtlasiQ9Y463. baseline.
GenevestigatoriQ9Y463.

Organism-specific databases

HPAiHPA028786.

Interactioni

Subunit structurei

Dimer. Interacts with DCOHM, MAP2K3/MKK3, RANBP9 and TCF1/HNF1A. Part of a complex consisting of RANBP9, RAN, DYRK1B and COPS5. Interacts with DCAF7.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DCAF7P619622EBI-634187,EBI-359808
HNF1AP208234EBI-634187,EBI-636034
LZTS2Q9BRK43EBI-634187,EBI-741037
MAP2K3P467342EBI-634187,EBI-602462
PCBD2Q9H0N52EBI-634187,EBI-634289
RANBP9Q96S594EBI-634187,EBI-636085
RB1P064003EBI-634187,EBI-491274
RBL1P287493EBI-634187,EBI-971402
TROAPQ128153EBI-634187,EBI-2349743

Protein-protein interaction databases

BioGridi114596. 57 interactions.
IntActiQ9Y463. 54 interactions.
MINTiMINT-2790122.
STRINGi9606.ENSP00000312789.

Structurei

3D structure databases

ProteinModelPortaliQ9Y463.
SMRiQ9Y463. Positions 100-432.
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 RANBP9Add
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

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119032.
HOGENOMiHOG000220863.
HOVERGENiHBG051425.
InParanoidiQ9Y463.
KOiK08825.
OMAiEPGHAPC.
OrthoDBiEOG77127N.
PhylomeDBiQ9Y463.
TreeFamiTF314624.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
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: Q9Y463-1) [UniParc]FASTAAdd to basket

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 TSAPLRKLSV
60 70 80 90 100
DLIKTYKHIN EVYYAKKKRR AQQAPPQDSS NKKEKKVLNH 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 QMNRIVEVLG IPPAAMLDQA 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 GGSSGSSSDN RTYRYSNRYC GGPGPPITDC
510 520 530 540 550
EMNSPQVPPS QPLRPWAGGD VPHKTHQAPA SASSLPGTGA QLPPQPRYLG
560 570 580 590 600
RPPSPTSPPP PELMDVSLVG GPADCSPPHP APAPQHPAAS ALRTRMTGGR
610 620
PPLPPPDDPA TLGPHLGLRG VPQSTAASS
Length:629
Mass (Da):69,198
Last modified:November 1, 1999 - v1
Checksum:iD7C354AC55943A8B
GO
Isoform 2 (identifier: Q9Y463-2) [UniParc]FASTAAdd to basket

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

Show »
Length:589
Mass (Da):64,934
Checksum:iE98BF9B257237A9D
GO
Isoform 3 (identifier: Q9Y463-3) [UniParc]FASTAAdd to basket

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

Show »
Length:601
Mass (Da):66,336
Checksum:i8601907D9652274B
GO

Sequence cautioni

The sequence AAC28914.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti28 – 281L → P.1 Publication
Corresponds to variant rs34587974 [ dbSNP | Ensembl ].
VAR_040454
Natural varianti90 – 901H → P in AOMS3; expression of glucose-6-phosphatase is significantly higher than wild-type. 1 Publication
VAR_071773
Natural varianti102 – 1021R → C in AOMS3; accumulation of intracellular lipid is significantly greater than with wild-type protein; cells expressing the variant are able to transform into mature adipocytes without requiring adipogenic medium; expression levels of CEBPA, PPARG forms 1 and 2 and PPARGC1A are higher and those of GLI1 and CDKN1B are lower in cells transfected with the mutant protein compared to wild-type; WNT1 signaling activity is lower in mutant cells compared to wild-type. 1 Publication
VAR_071774
Natural varianti102 – 1021R → H.1 Publication
Corresponds to variant rs55687541 [ dbSNP | Ensembl ].
VAR_040455
Natural varianti234 – 2341S → G.1 Publication
Corresponds to variant rs35858874 [ dbSNP | Ensembl ].
VAR_040456
Natural varianti275 – 2751Q → R in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_040457

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei366 – 40540Missing in isoform 2. 1 PublicationVSP_004925Add
BLAST
Alternative sequencei378 – 40528Missing in isoform 3. 1 PublicationVSP_004926Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS12543.1. [Q9Y463-1]
CCDS12544.1. [Q9Y463-3]
CCDS46075.1. [Q9Y463-2]
PIRiJG0195.
RefSeqiNP_004705.1. NM_004714.2. [Q9Y463-1]
NP_006474.1. NM_006483.2. [Q9Y463-2]
NP_006475.1. NM_006484.2. [Q9Y463-3]
XP_005259455.1. XM_005259398.2. [Q9Y463-1]
UniGeneiHs.130988.

Genome annotation databases

EnsembliENST00000323039; ENSP00000312789; ENSG00000105204. [Q9Y463-1]
ENST00000348817; ENSP00000221803; ENSG00000105204. [Q9Y463-3]
ENST00000430012; ENSP00000403182; ENSG00000105204. [Q9Y463-2]
ENST00000593685; ENSP00000469863; ENSG00000105204. [Q9Y463-1]
ENST00000597639; ENSP00000472941; ENSG00000105204. [Q9Y463-3]
GeneIDi9149.
KEGGihsa:9149.
UCSCiuc002omi.3. human. [Q9Y463-3]
uc002omj.3. human. [Q9Y463-1]
uc002omk.3. human. [Q9Y463-2]

Polymorphism databases

DMDMi9296963.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS12543.1. [Q9Y463-1]
CCDS12544.1. [Q9Y463-3]
CCDS46075.1. [Q9Y463-2]
PIRiJG0195.
RefSeqiNP_004705.1. NM_004714.2. [Q9Y463-1]
NP_006474.1. NM_006483.2. [Q9Y463-2]
NP_006475.1. NM_006484.2. [Q9Y463-3]
XP_005259455.1. XM_005259398.2. [Q9Y463-1]
UniGeneiHs.130988.

3D structure databases

ProteinModelPortaliQ9Y463.
SMRiQ9Y463. Positions 100-432.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114596. 57 interactions.
IntActiQ9Y463. 54 interactions.
MINTiMINT-2790122.
STRINGi9606.ENSP00000312789.

Chemistry

BindingDBiQ9Y463.
ChEMBLiCHEMBL5543.
GuidetoPHARMACOLOGYi2010.

PTM databases

PhosphoSiteiQ9Y463.

Polymorphism databases

DMDMi9296963.

Proteomic databases

MaxQBiQ9Y463.
PaxDbiQ9Y463.
PRIDEiQ9Y463.

Protocols and materials databases

DNASUi9149.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000323039; ENSP00000312789; ENSG00000105204. [Q9Y463-1]
ENST00000348817; ENSP00000221803; ENSG00000105204. [Q9Y463-3]
ENST00000430012; ENSP00000403182; ENSG00000105204. [Q9Y463-2]
ENST00000593685; ENSP00000469863; ENSG00000105204. [Q9Y463-1]
ENST00000597639; ENSP00000472941; ENSG00000105204. [Q9Y463-3]
GeneIDi9149.
KEGGihsa:9149.
UCSCiuc002omi.3. human. [Q9Y463-3]
uc002omj.3. human. [Q9Y463-1]
uc002omk.3. human. [Q9Y463-2]

Organism-specific databases

CTDi9149.
GeneCardsiGC19M040316.
HGNCiHGNC:3092. DYRK1B.
HPAiHPA028786.
MIMi604556. gene.
615812. phenotype.
neXtProtiNX_Q9Y463.
PharmGKBiPA27549.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119032.
HOGENOMiHOG000220863.
HOVERGENiHBG051425.
InParanoidiQ9Y463.
KOiK08825.
OMAiEPGHAPC.
OrthoDBiEOG77127N.
PhylomeDBiQ9Y463.
TreeFamiTF314624.

Enzyme and pathway databases

BioCyciMetaCyc:HS02690-MONOMER.
BRENDAi2.7.12.1. 2681.
SignaLinkiQ9Y463.

Miscellaneous databases

ChiTaRSiDYRK1B. human.
GeneWikiiDYRK1B.
GenomeRNAii9149.
NextBioi34319.
PROiQ9Y463.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y463.
CleanExiHS_DYRK1B.
ExpressionAtlasiQ9Y463. baseline.
GenevestigatoriQ9Y463.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
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 [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION AT TYR-271 AND TYR-273, 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DCAF7.
  8. "Selectivity, cocrystal structures, and neuroprotective properties of leucettines, a family of protein kinase inhibitors derived from the marine sponge alkaloid leucettamine B."
    Tahtouh T., Elkins J.M., Filippakopoulos P., Soundararajan M., Burgy G., Durieu E., Cochet C., Schmid R.S., Lo D.C., Delhommel F., Oberholzer A.E., Pearl L.H., Carreaux F., Bazureau J.P., Knapp S., Meijer L.
    J. Med. Chem. 55:9312-9330(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.
  9. Cited for: FUNCTION, VARIANTS AOMS3 PRO-90 AND CYS-102, CHARACTERIZATION OF VARIANTS AOMS3 PRO-90 AND CYS-102.
  10. "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] PRO-28; HIS-102; GLY-234 AND ARG-275.

Entry informationi

Entry nameiDYR1B_HUMAN
AccessioniPrimary (citable) accession number: Q9Y463
Secondary accession number(s): O75258, O75788, O75789
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: March 4, 2015
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.