Q61214

PR
Gene name
Dyrk1a (Dyrk)
Protein name
Dual specificity tyrosine-phosphorylation-regulated kinase 1A
Names
Dual specificity YAK1-related kinase, MP86, Protein kinase minibrain homolog, MNBH
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:13548
EC number
2.7.11.23: Protein-serine/threonine kinases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

504-589 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

306-326 (Activation loop from InterPro)

Target domain

148-484 (Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1)

Relief mechanism

Assay

References

Autoinhibited structure

Activated structure

1 structures for Q61214

Entry ID Method Resolution Chain Position Source
AF-Q61214-F1 Predicted AlphaFoldDB

24 variants for Q61214

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389407193 24 H>L No EVA
rs3407463651 69 Q>QVISPSFLIIMKLPG*LEVAES No EVA
rs3406709277 89 A>T No EVA
rs3389418569 115 K>R No EVA
rs3389418506 144 N>D No EVA
rs3389387373 154 K>E No EVA
rs3389341229 180 V>M No EVA
rs3389396639 189 I>F No EVA
rs3389376811 233 H>L No EVA
rs3389428638 278 T>S No EVA
rs3389387390 381 P>S No EVA
rs3389437088 399 P>L No EVA
rs3406327292 407 K>* No EVA
rs3389376830 412 K>I No EVA
rs3389437103 416 K>N No EVA
rs3389396699 471 Y>C No EVA
rs3389434654 475 Q>* No EVA
rs3389428666 481 K>I No EVA
rs3389437126 483 A>D No EVA
rs3389430468 488 N>T No EVA
rs3407239126 553 T>S No EVA
rs3389443648 558 V>L No EVA
rs3407239098 662 T>S No EVA
rs3389437132 743 A>V No EVA

No associated diseases with Q61214

3 regional properties for Q61214

Type Name Position InterPro Accession
conserved_site 14-3-3 protein, conserved site 53 - 63 IPR023409-1
conserved_site 14-3-3 protein, conserved site 225 - 244 IPR023409-2
domain 14-3-3 domain 10 - 256 IPR023410

Functions

Description
EC Number 2.7.11.23 Protein-serine/threonine kinases
Subcellular Localization
  • Nucleus speckle
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

10 GO annotations of cellular component

Name Definition
actin filament A filamentous structure formed of a two-stranded helical polymer of the protein actin and associated proteins. Actin filaments are a major component of the contractile apparatus of skeletal muscle and the microfilaments of the cytoskeleton of eukaryotic cells. The filaments, comprising polymerized globular actin molecules, appear as flexible structures with a diameter of 5-9 nm. They are organized into a variety of linear bundles, two-dimensional networks, and three dimensional gels. In the cytoskeleton they are most highly concentrated in the cortex of the cell just beneath the plasma membrane.
axon The long process of a neuron that conducts nerve impulses, usually away from the cell body to the terminals and varicosities, which are sites of storage and release of neurotransmitter.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytoskeleton A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles.
dendrite A neuron projection that has a short, tapering, morphology. Dendrites receive and integrate signals from other neurons or from sensory stimuli, and conduct nerve impulses towards the axon or the cell body. In most neurons, the impulse is conveyed from dendrites to axon via the cell body, but in some types of unipolar neuron, the impulse does not travel via the cell body.
microtubule Any of the long, generally straight, hollow tubes of internal diameter 12-15 nm and external diameter 24 nm found in a wide variety of eukaryotic cells; each consists (usually) of 13 protofilaments of polymeric tubulin, staggered in such a manner that the tubulin monomers are arranged in a helical pattern on the microtubular surface, and with the alpha/beta axes of the tubulin subunits parallel to the long axis of the tubule; exist in equilibrium with pool of tubulin monomers and can be rapidly assembled or disassembled in response to physiological stimuli; concerned with force generation, e.g. in the spindle.
neurofilament A type of intermediate filament found in the core of neuronal axons. Neurofilaments are heteropolymers composed of three type IV polypeptides: NF-L, NF-M, and NF-H (for low, middle, and high molecular weight). Neurofilaments are responsible for the radial growth of an axon and determine axonal diameter.
nuclear speck A discrete extra-nucleolar subnuclear domain, 20-50 in number, in which splicing factors are seen to be localized by immunofluorescence microscopy.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
ribonucleoprotein complex A macromolecular complex that contains both RNA and protein molecules.

15 GO annotations of molecular function

Name Definition
actin binding Binding to monomeric or multimeric forms of actin, including actin filaments.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
cytoskeletal protein binding Binding to a protein component of a cytoskeleton (actin, microtubule, or intermediate filament cytoskeleton).
identical protein binding Binding to an identical protein or proteins.
non-membrane spanning protein tyrosine kinase activity Catalysis of the reaction: ATP + protein L-tyrosine = ADP + protein L-tyrosine phosphate by a non-membrane spanning protein.
protein kinase activity Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP.
protein self-association Binding to a domain within the same polypeptide.
protein serine kinase activity Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate.
protein serine/threonine kinase activity Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate.
protein serine/threonine/tyrosine kinase activity Catalysis of the reactions: ATP + a protein serine = ADP + protein serine phosphate; ATP + a protein threonine = ADP + protein threonine phosphate; and ATP + a protein tyrosine = ADP + protein tyrosine phosphate.
protein tyrosine kinase activity Catalysis of the reaction: ATP + a protein tyrosine = ADP + protein tyrosine phosphate.
RNA polymerase II CTD heptapeptide repeat kinase activity Catalysis of the reaction: ATP + RNA polymerase II large subunit CTD heptapeptide repeat (YSPTSPS) = ADP + H+ + phosphorylated RNA polymerase II.
tau protein binding Binding to tau protein. tau is a microtubule-associated protein, implicated in Alzheimer's disease, Down Syndrome and ALS.
transcription coactivator activity A transcription coregulator activity that activates or increases the transcription of specific gene sets via binding to a DNA-bound DNA-binding transcription factor, either on its own or as part of a complex. Coactivators often act by altering chromatin structure and modifications. For example, one class of transcription coactivators modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators. A fourth class of coactivator activity is the bridging of a DNA-binding transcription factor to the general (basal) transcription machinery. The Mediator complex, which bridges sequence-specific DNA binding transcription factors and RNA polymerase, is also a transcription coactivator.
tubulin binding Binding to monomeric or multimeric forms of tubulin, including microtubules.

15 GO annotations of biological process

Name Definition
amyloid-beta formation The generation of amyloid-beta by cleavage of the amyloid precursor protein (APP).
circadian rhythm Any biological process in an organism that recurs with a regularity of approximately 24 hours.
negative regulation of DNA damage response, signal transduction by p53 class mediator Any process that stops, prevents, or reduces the frequency, rate or extent of the cascade of processes induced by the cell cycle regulator phosphoprotein p53, or an equivalent protein, in response to the detection of DNA damage.
negative regulation of microtubule polymerization Any process that stops, prevents, or reduces the frequency, rate or extent of microtubule polymerization.
negative regulation of mRNA splicing, via spliceosome Any process that stops, prevents or reduces the rate or extent of mRNA splicing via a spliceosomal mechanism.
peptidyl-serine phosphorylation The phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine.
peptidyl-threonine phosphorylation The phosphorylation of peptidyl-threonine to form peptidyl-O-phospho-L-threonine.
peptidyl-tyrosine autophosphorylation The phosphorylation by a protein of one or more of its own tyrosine amino acid residues, or a tyrosine residue on an identical protein.
peptidyl-tyrosine phosphorylation The phosphorylation of peptidyl-tyrosine to form peptidyl-O4'-phospho-L-tyrosine.
positive regulation of DNA-templated transcription Any process that activates or increases the frequency, rate or extent of cellular DNA-templated transcription.
positive regulation of protein deacetylation Any process that increases the rate, frequency, or extent of protein deacetylation, the removal of an acetyl group from a protein amino acid. An acetyl group is CH3CO-, derived from acetic
positive regulation of RNA splicing Any process that activates or increases the frequency, rate or extent of RNA splicing.
protein autophosphorylation The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation).
protein phosphorylation The process of introducing a phosphate group on to a protein.
regulation of alternative mRNA splicing, via spliceosome Any process that modulates the frequency, rate or extent of alternative splicing of nuclear mRNAs.

10 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q8NE63 HIPK4 Homeodomain-interacting protein kinase 4 Homo sapiens (Human) PR
Q9H422 HIPK3 Homeodomain-interacting protein kinase 3 Homo sapiens (Human) SS
Q92630 DYRK2 Dual specificity tyrosine-phosphorylation-regulated kinase 2 Homo sapiens (Human) PR
Q9H2X6 HIPK2 Homeodomain-interacting protein kinase 2 Homo sapiens (Human) EV
Q9NR20 DYRK4 Dual specificity tyrosine-phosphorylation-regulated kinase 4 Homo sapiens (Human) PR
Q13627 DYRK1A Dual specificity tyrosine-phosphorylation-regulated kinase 1A Homo sapiens (Human) PR
Q3V016 Hipk4 Homeodomain-interacting protein kinase 4 Mus musculus (Mouse) PR
Q9QZR5 Hipk2 Homeodomain-interacting protein kinase 2 Mus musculus (Mouse) SS
Q8BI55 Dyrk4 Dual specificity tyrosine-phosphorylation-regulated kinase 4 Mus musculus (Mouse) PR
Q4V793 Hipk4 Homeodomain-interacting protein kinase 4 Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MHTGGETSAC KPSSVRLAPS FSFHAAGLQM AAQMPHSHQY SDRRQPSISD QQVSALPYSD
70 80 90 100 110 120
QIQQPLTNQV MPDIVMLQRR MPQTFRDPAT APLRKLSVDL IKTYKHINEV YYAKKKRRHQ
130 140 150 160 170 180
QGQGDDSSHK KERKVYNDGY DDDNYDYIVK NGEKWMDRYE IDSLIGKGSF GQVVKAYDRV
190 200 210 220 230 240
EQEWVAIKII KNKKAFLNQA QIEVRLLELM NKHDTEMKYY IVHLKRHFMF RNHLCLVFEM
250 260 270 280 290 300
LSYNLYDLLR NTNFRGVSLN LTRKFAQQMC TALLFLATPE LSIIHCDLKP ENILLCNPKR
310 320 330 340 350 360
SAIKIVDFGS SCQLGQRIYQ YIQSRFYRSP EVLLGMPYDL AIDMWSLGCI LVEMHTGEPL
370 380 390 400 410 420
FSGANEVDQM NKIVEVLGIP PAHILDQAPK ARKFFEKLPD GTWSLKKTKD GKREYKPPGT
430 440 450 460 470 480
RKLHNILGVE TGGPGGRRAG ESGHTVADYL KFKDLILRML DYDPKTRIQP YYALQHSFFK
490 500 510 520 530 540
KTADEGTNTS NSVSTSPAME QSQSSGTTSS TSSSSGGSSG TSNSGRARSD PTHQHRHSGG
550 560 570 580 590 600
HFAAAVQAMD CETHSPQVRQ QFPAPLGWSG TEAPTQVTVE THPVQETTFH VAPQQNALHH
610 620 630 640 650 660
HHGNSSHHHH HHHHHHHHHG QQALGNRTRP RVYNSPTNSS STQDSMEVGH SHHSMTSLSS
670 680 690 700 710 720
STTSSSTSSS STGNQGNQAY QNRPVAANTL DFGQNGAMDV NLTVYSNPRQ ETGIAGHPTY
730 740 750 760
QFSANTGPAH YMTEGHLAMR QGADREESPM TGVCVQQSPV ASS