Reviewed,
UniProtKB/Swiss-Prot Q13627 (DYR1A_HUMAN)
Last modified
September 2, 2008.
Version 90.
History...
Clusters with 100%,
90%,
50% identity |
Documents (7) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Dual specificity tyrosine-phosphorylation-regulated kinase 1A EC=2.7.12.1 Alternative name(s): Protein kinase minibrain homolog Short name=MNBH Short name=hMNB HP86 Dual specificity YAK1-related kinase | ||||
| Gene names |
| ||||
| 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 | 763 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | May play a role in a signaling pathway regulating nuclear functions of cell proliferation. Phosphorylates serine, threonine and tyrosine residues in its sequence and in exogenous substrates. |
| Catalytic activity | ATP + a protein = ADP + a phosphoprotein. |
| Enzyme regulation | Inhibited by RANBP9. |
| Subunit structure | Interacts RAD54L2/ARIP4 By similarity. Interacts with RANBP9. |
| Subcellular location | |
| Tissue specificity | Ubiquitous. Highest levels in skeletal muscle, testis, fetal lung and fetal kidney. |
| Developmental stage | Expressed in the developing central nervous system. |
| Post-translational modification | Autophosphorylated on tyrosine residues. |
| Involvement in disease | Overexpressed 1.5-fold in fetal Down syndrome brain. |
| 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 Polymorphism |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Serine/threonine-protein kinase Transferase Tyrosine-protein kinase |
| PTM | Phosphoprotein |
Gene Ontology (GO) | |
| Biological process | nervous system development Ref.3 Traceable author statement. Source: ProtInc peptidyl-tyrosine phosphorylationInferred from sequence or structural similarity. Source: UniProtKB protein amino acid autophosphorylationInferred from sequence or structural similarity. Source: UniProtKB |
| Cellular component | nuclear speck Inferred from sequence or structural similarity. Source: UniProtKB |
| Molecular function | protein self-association Inferred from sequence or structural similarity. Source: UniProtKB protein serine/threonine kinase activity Ref.3Inferred from sequence or structural similarity. Source: UniProtKB protein tyrosine kinase activityInferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Alternative products
| This entry describes 5 isoforms produced by alternative splicing. [Align] [Select] Notes: Additional isoforms seem to exist. | |||||
| Isoform Long (identifier: Q13627-1) 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 1 (identifier: Q13627-2) The sequence of this isoform differs from the canonical sequence as follows: 70-78: Missing. | |||||
| Isoform 2 (identifier: Q13627-3) The sequence of this isoform differs from the canonical sequence as follows: 516-529: GGSSGTSNSGRARS → GASAISCSSWLVRH 530-763: Missing. | |||||
| Isoform 3 (identifier: Q13627-4) The sequence of this isoform differs from the canonical sequence as follows: 516-540: GGSSGTSNSGRARSDPTHQHRHSGG → VEQHWMPGAFRMTVSFTLEVHDVPV 541-763: Missing. | |||||
| Isoform 4 (identifier: Q13627-5) The sequence of this isoform differs from the canonical sequence as follows: 559-584: RQQFPAPLGWSGTEAPTQVTVETHPV → SSHVVHLLVSPAILRWSSTGCQVPLE 585-763: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | ||||
Molecule processing | ||||||||
|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 763 | 763 | Dual specificity tyrosine-phosphorylation-regulated kinase 1A | |||||
Regions | ||||||||
| Domain | 159 – 479 | 321 | Protein kinase | |||||
| Nucleotide binding | 165 – 173 | 9 | ATP By similarity | |||||
| Motif | 117 – 134 | 18 | Bipartite nuclear localization signal Potential | |||||
| Compositional bias | 509 – 515 | 7 | Poly-Ser | |||||
| Compositional bias | 599 – 602 | 4 | Poly-His | |||||
| Compositional bias | 607 – 619 | 13 | Poly-His | |||||
| Compositional bias | 656 – 672 | 17 | Ser/Thr-rich | |||||
| Compositional bias | 664 – 671 | 8 | Poly-Ser | |||||
Sites | ||||||||
| Active site | 287 | 1 | Proton acceptor By similarity | |||||
| Binding site | 188 | 1 | ATP By similarity | |||||
Amino acid modifications | ||||||||
| Modified residue | 145 | 1 | Phosphotyrosine | |||||
| Modified residue | 219 | 1 | Phosphotyrosine; by autocatalysis By similarity | |||||
| Modified residue | 319 | 1 | Phosphotyrosine; by autocatalysis By similarity | |||||
| Modified residue | 321 | 1 | Phosphotyrosine; by autocatalysis | |||||
Natural variations | ||||||||
| Alternative sequence | 70 – 78 | 9 | Missing in isoform 1. | |||||
| Alternative sequence | 516 – 540 | 25 | GGSSG…RHSGG → VEQHWMPGAFRMTVSFTLEV HDVPV in isoform 3. | |||||
| Alternative sequence | 516 – 529 | 14 | GGSSG…GRARS → GASAISCSSWLVRH in isoform 2. | |||||
| Alternative sequence | 530 – 763 | 234 | Missing in isoform 2. | |||||
| Alternative sequence | 541 – 763 | 223 | Missing in isoform 3. | |||||
| Alternative sequence | 559 – 584 | 26 | RQQFP…ETHPV → SSHVVHLLVSPAILRWSSTG CQVPLE in isoform 4. | |||||
| Alternative sequence | 585 – 763 | 179 | Missing in isoform 4. | |||||
| Natural variant | 415 | 1 | Y → F | |||||
| Natural variant | 679 | 1 | A → P | |||||
| Natural variant | 681 | 1 | Q → H | |||||
Experimental info | ||||||||
| Sequence conflict | 32 | 1 | G → A in AAC50939. Ref.1 | |||||
| Sequence conflict | 47 | 1 | N → S in AAC50939. Ref.1 | |||||
| Sequence conflict | 57 | 1 | S → P in AAC50939. Ref.1 | |||||
| Sequence conflict | 123 | 1 | Q → R in AAC50939. Ref.1 | |||||
| Sequence conflict | 266 | 1 | A → V in CAA05059. Ref.6 | |||||
| Sequence conflict | 357 | 1 | G → R in CAA05059. Ref.6 | |||||
| Sequence conflict | 397 | 1 | K → N in AAC50939. Ref.1 | |||||
| Sequence conflict | 592 | 1 | A → G in AAC50939. Ref.1 | |||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Isolation of human and murine homologues of the Drosophila minibrain gene: human homologue maps to 21q22.2 in the Down syndrome 'critical region'." Song W.J., Sternberg L.R., Kasten-Sportes C., van Keuren M.L., Chung S.H., Slack A.C., Miller D.E., Glover T.W., Chiang P.W., Lou L., Kurnit D.W. Genomics 38:331-339(1996) [PubMed: 8975710] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANT PRO-679, TISSUE SPECIFICITY. Tissue: Fetal brain. |
| [2] | "A human homologue of Drosophila minibrain (MNB) is expressed in the neuronal regions affected in Down syndrome and maps to the critical region." Guimera J., Casas C., Pucharcos C., Solans A., Domenech A., Planas A.M., Ashley J., Lovett M., Estivill X., Pritchard M.A. Hum. Mol. Genet. 5:1305-1310(1996) [PubMed: 8872470] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), TISSUE SPECIFICITY, POSSIBLE INVOLVEMENT IN DOWN SYNDROME. |
| [3] | "Cloning of a human homolog of the Drosophila minibrain/rat Dyrk gene from 'the Down syndrome critical region' of chromosome 21." Shindoh N., Kudoh J., Maeda H., Yamaki A., Minoshima S., Shimizu Y., Shimizu N. Biochem. Biophys. Res. Commun. 225:92-99(1996) [PubMed: 8769099] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Tissue: Fetal brain. |
| [4] | "Gene identification in 1.6-Mb region of the Down syndrome region on chromosome 21." Ohira M., Seki N., Nagase T., Suzuki E., Nomura N., Ohara O., Hattori M., Sakaki Y., Eki T., Murakami Y., Saito T., Ichikawa H., Ohki M. Genome Res. 7:47-58(1997) [PubMed: 9037601] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Promyelocytic leukemia. |
| [5] | "Human minibrain homologue (MNBH/DYRK1): characterization, alternative splicing, differential tissue expression, and overexpression in Down syndrome." Guimera J., Casas C., Estivill X., Pritchard M.A. Genomics 57:407-418(1999) [PubMed: 10329007] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY, POSSIBLE INVOLVEMENT IN DOWN SYNDROME, VARIANTS PHE-415 AND HIS-681, ALTERNATIVE SPLICING. |
| [6] | "Transcriptional map of the 2.5-Mb CBR-ERG region of chromosome 21 involved in Down syndrome." Dahmane N., Ait Ghezala G., Gosset P., Chamoun Z., Dufresne-Zacharia M.-C., Lopes C., Rabatel N., Gassanova-Maugenre S., Chettouh Z., Abramowski V., Fayet E., Yaspo M.-L., Korn B., Blouin J.-L., Lehrach H., Poustka A., Antonarakis S.E., Sinet P.-M., Creau N., Delabar J.-M. Genomics 48:12-23(1998) [PubMed: 9503011] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 234-380. Tissue: Fetal brain. |
| [7] | "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: INTERACTION WITH RANBP9, ENZYME REGULATION. |
| [8] | "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-145 AND TYR-321, MASS SPECTROMETRY. |
| [9] | "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. Comb M.J.Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-145, MASS SPECTROMETRY. |
| [10] | "Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry." Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H. Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-321, MASS SPECTROMETRY. |
| [11] | "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-321, MASS SPECTROMETRY. Tissue: Platelet. |
| [12] | "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. Stratton M.R.Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] PRO-679. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| U58496 mRNA. Translation: AAC50939.1. U52373 mRNA. Translation: AAB18639.1. D85759 mRNA. Translation: BAA12866.1. D86550 mRNA. Translation: BAA13110.1. AF108830 mRNA. Translation: AAD31169.1. AJ001870 mRNA. Translation: CAA05059.1. | |
| PIR | JC4898. |
| RefSeq | NP_001387.2. NP_567824.1. NP_569120.1. NP_569121.1. NP_569122.1. |
| UniGene | Hs.705437 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1I09 based on UniProtKB P49841. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q13627. |
PTM databases | |
| PhosphoSite | Q13627. |
Genome annotation databases | |
| Ensembl | ENSG00000157540. Homo sapiens. [Contig view] |

Clusters with