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Q13627

- DYR1A_HUMAN

UniProt

Q13627 - DYR1A_HUMAN

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Protein

Dual specificity tyrosine-phosphorylation-regulated kinase 1A

Gene

DYRK1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

May play a role in a signaling pathway regulating nuclear functions of cell proliferation. Modulates alternative splicing by phosphorylating the splice factor SRSF6 (By similarity). Phosphorylates serine, threonine and tyrosine residues in its sequence and in exogenous substrates such as CRY2, FOXO1, SRSF6 and SIRT1. Exhibits a sugstrate preference for proline at position P+1 and arginine at position P-3.By similarity4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.4 Publications

Enzyme regulationi

Inhibited by RANBP9. Inhibited by harmine, leucettamine B and leucettine L41.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei188 – 1881ATPCurated
Active sitei287 – 2871Proton acceptor1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi165 – 1739ATPCurated
Nucleotide bindingi238 – 2414ATPCurated

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. non-membrane spanning protein tyrosine kinase activity Source: MGI
  3. protein kinase activity Source: ProtInc
  4. protein self-association Source: UniProtKB
  5. protein serine/threonine/tyrosine kinase activity Source: UniProtKB-EC
  6. protein serine/threonine kinase activity Source: UniProtKB
  7. protein tyrosine kinase activity Source: UniProtKB
  8. tau protein binding Source: BHF-UCL

GO - Biological processi

  1. circadian rhythm Source: UniProtKB
  2. mitotic cell cycle Source: Reactome
  3. negative regulation of DNA damage response, signal transduction by p53 class mediator Source: BHF-UCL
  4. nervous system development Source: ProtInc
  5. peptidyl-serine phosphorylation Source: Ensembl
  6. peptidyl-threonine phosphorylation Source: BHF-UCL
  7. peptidyl-tyrosine phosphorylation Source: UniProtKB
  8. positive regulation of protein deacetylation Source: BHF-UCL
  9. protein autophosphorylation Source: UniProtKB
  10. 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

BRENDAi2.7.12.1. 2681.
ReactomeiREACT_111214. G0 and Early G1.
SignaLinkiQ13627.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity tyrosine-phosphorylation-regulated kinase 1A (EC:2.7.12.1)
Alternative name(s):
Dual specificity YAK1-related kinase
HP86
Protein kinase minibrain homolog
Short name:
MNBH
Short name:
hMNB
Gene namesi
Name:DYRK1A
Synonyms:DYRK, MNB, MNBH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 21

Organism-specific databases

HGNCiHGNC:3091. DYRK1A.

Subcellular locationi

GO - Cellular componenti

  1. nuclear speck Source: UniProtKB
  2. nucleoplasm Source: Reactome
  3. nucleus Source: UniProtKB
  4. ribonucleoprotein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Mental retardation, autosomal dominant 7 (MRD7) [MIM:614104]: A disease characterized by primary microcephaly, severe mental retardation without speech, anxious autistic behavior, and dysmorphic features, including bitemporal narrowing, deep-set eyes, large simple ears, and a pointed nasal tip. Mental retardation is characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi188 – 1881K → R: Abolishes kinase activity. 1 Publication
Mutagenesisi321 – 3211Y → F: Mildly reduces kinase activity. Does not abolish autophosphorylation on tyrosine residues. 1 Publication

Keywords - Diseasei

Mental retardation

Organism-specific databases

MIMi614104. phenotype.
Orphaneti178469. Autosomal dominant non-syndromic intellectual disability.
PharmGKBiPA27545.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 763763Dual specificity tyrosine-phosphorylation-regulated kinase 1APRO_0000085931Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei111 – 1111Phosphotyrosine; by autocatalysis1 Publication
Modified residuei140 – 1401Phosphotyrosine; by autocatalysis1 Publication
Modified residuei145 – 1451Phosphotyrosine1 Publication
Modified residuei159 – 1591Phosphotyrosine; by autocatalysis1 Publication
Modified residuei177 – 1771Phosphotyrosine; by autocatalysis1 Publication
Modified residuei219 – 2191Phosphotyrosine; by autocatalysisBy similarity
Modified residuei310 – 3101Phosphoserine; by autocatalysis1 Publication
Modified residuei319 – 3191Phosphotyrosine; by autocatalysis1 Publication
Modified residuei321 – 3211Phosphotyrosine; by autocatalysis1 Publication
Modified residuei402 – 4021Phosphothreonine; by autocatalysis1 Publication
Modified residuei449 – 4491Phosphotyrosine; by autocatalysis1 Publication
Modified residuei748 – 7481Phosphoserine1 Publication
Modified residuei758 – 7581Phosphoserine1 Publication

Post-translational modificationi

Autophosphorylated on numerous tyrosine residues. Can also autophosphorylate on serine and threonine residues (in vitro).3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ13627.
PaxDbiQ13627.
PRIDEiQ13627.

PTM databases

PhosphoSiteiQ13627.

Expressioni

Tissue specificityi

Ubiquitous. Highest levels in skeletal muscle, testis, fetal lung and fetal kidney.4 Publications

Developmental stagei

Expressed in the developing central nervous system. Overexpressed 1.5-fold in fetal Down syndrome brain.1 Publication

Gene expression databases

BgeeiQ13627.
CleanExiHS_DYRK1A.
ExpressionAtlasiQ13627. baseline and differential.
GenevestigatoriQ13627.

Organism-specific databases

HPAiHPA015323.
HPA015810.

Interactioni

Subunit structurei

Interacts RAD54L2/ARIP4. Interacts with CRY2 (By similarity). Interacts with RANBP9. Interacts with WDR68. Interacts with SRSF6.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DCAF7P619623EBI-1053596,EBI-359808
LZTS2Q9BRK43EBI-1053596,EBI-741037
RB1P064003EBI-1053596,EBI-491274
RBL1P287493EBI-1053596,EBI-971402
TROAPQ128153EBI-1053596,EBI-2349743
YWHABP319463EBI-1053621,EBI-359815

Protein-protein interaction databases

BioGridi108192. 59 interactions.
DIPiDIP-39750N.
IntActiQ13627. 32 interactions.
MINTiMINT-1205413.
STRINGi9606.ENSP00000381932.

Structurei

Secondary structure

1
763
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi137 – 1393Combined sources
Turni156 – 1583Combined sources
Beta strandi159 – 16810Combined sources
Beta strandi171 – 1788Combined sources
Turni179 – 1824Combined sources
Beta strandi183 – 1908Combined sources
Helixi194 – 21118Combined sources
Helixi216 – 2205Combined sources
Beta strandi224 – 2307Combined sources
Beta strandi233 – 2397Combined sources
Helixi245 – 2517Combined sources
Turni252 – 2543Combined sources
Helixi259 – 27618Combined sources
Turni279 – 2813Combined sources
Helixi290 – 2923Combined sources
Beta strandi293 – 2975Combined sources
Beta strandi303 – 3053Combined sources
Helixi308 – 3103Combined sources
Beta strandi312 – 3165Combined sources
Helixi325 – 3273Combined sources
Helixi330 – 3334Combined sources
Helixi341 – 35616Combined sources
Helixi366 – 37712Combined sources
Helixi382 – 3854Combined sources
Helixi391 – 3944Combined sources
Beta strandi395 – 3973Combined sources
Beta strandi403 – 4053Combined sources
Helixi423 – 4264Combined sources
Turni427 – 4326Combined sources
Helixi434 – 4363Combined sources
Turni437 – 4404Combined sources
Helixi446 – 45914Combined sources
Turni464 – 4663Combined sources
Helixi470 – 4745Combined sources
Helixi477 – 4793Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VX3X-ray2.40A/B/C/D127-485[»]
2WO6X-ray2.50A/B127-485[»]
3ANQX-ray2.60A/B/C/D126-490[»]
3ANRX-ray2.60A/B/C/D126-490[»]
4AZEX-ray3.15A/B/C128-485[»]
4MQ1X-ray2.35A/B/C/D127-485[»]
4MQ2X-ray2.80A/B/C/D127-485[»]
ProteinModelPortaliQ13627.
SMRiQ13627. Positions 148-480.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13627.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini159 – 479321Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi117 – 13418Bipartite nuclear localization signalSequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi509 – 5157Poly-Ser
Compositional biasi599 – 6024Poly-His
Compositional biasi607 – 61913Poly-HisAdd
BLAST
Compositional biasi656 – 67217Ser/Thr-richAdd
BLAST
Compositional biasi664 – 6718Poly-Ser

Domaini

The polyhistidine repeats act as targeting signals to nuclear speckles.1 Publication

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119032.
HOGENOMiHOG000220863.
HOVERGENiHBG051425.
InParanoidiQ13627.
KOiK08825.
OMAiLTNQRRM.
OrthoDBiEOG77127N.
PhylomeDBiQ13627.
TreeFamiTF314624.

Family and domain databases

InterProiIPR028318. DYRK1A.
IPR011009. 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]
PANTHERiPTHR24058:SF28. PTHR24058:SF28. 1 hit.
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform Long (identifier: Q13627-1) [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
MHTGGETSAC KPSSVRLAPS FSFHAAGLQM AGQMPHSHQY SDRRQPNISD
60 70 80 90 100
QQVSALSYSD QIQQPLTNQV MPDIVMLQRR MPQTFRDPAT APLRKLSVDL
110 120 130 140 150
IKTYKHINEV YYAKKKRRHQ QGQGDDSSHK KERKVYNDGY DDDNYDYIVK
160 170 180 190 200
NGEKWMDRYE IDSLIGKGSF GQVVKAYDRV EQEWVAIKII KNKKAFLNQA
210 220 230 240 250
QIEVRLLELM NKHDTEMKYY IVHLKRHFMF RNHLCLVFEM LSYNLYDLLR
260 270 280 290 300
NTNFRGVSLN LTRKFAQQMC TALLFLATPE LSIIHCDLKP ENILLCNPKR
310 320 330 340 350
SAIKIVDFGS SCQLGQRIYQ YIQSRFYRSP EVLLGMPYDL AIDMWSLGCI
360 370 380 390 400
LVEMHTGEPL FSGANEVDQM NKIVEVLGIP PAHILDQAPK ARKFFEKLPD
410 420 430 440 450
GTWNLKKTKD GKREYKPPGT RKLHNILGVE TGGPGGRRAG ESGHTVADYL
460 470 480 490 500
KFKDLILRML DYDPKTRIQP YYALQHSFFK KTADEGTNTS NSVSTSPAME
510 520 530 540 550
QSQSSGTTSS TSSSSGGSSG TSNSGRARSD PTHQHRHSGG HFTAAVQAMD
560 570 580 590 600
CETHSPQVRQ QFPAPLGWSG TEAPTQVTVE THPVQETTFH VAPQQNALHH
610 620 630 640 650
HHGNSSHHHH HHHHHHHHHG QQALGNRTRP RVYNSPTNSS STQDSMEVGH
660 670 680 690 700
SHHSMTSLSS STTSSSTSSS STGNQGNQAY QNRPVAANTL DFGQNGAMDV
710 720 730 740 750
NLTVYSNPRQ ETGIAGHPTY QFSANTGPAH YMTEGHLTMR QGADREESPM
760
TGVCVQQSPV ASS
Length:763
Mass (Da):85,584
Last modified:July 15, 1998 - v2
Checksum:i7C3A52A3CBB04FB5
GO
Isoform 1 (identifier: Q13627-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     70-78: Missing.

Show »
Length:754
Mass (Da):84,556
Checksum:i59518E25F1D4FF96
GO
Isoform 2 (identifier: Q13627-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     516-529: GGSSGTSNSGRARS → GASAISCSSWLVRH
     530-763: Missing.

Show »
Length:529
Mass (Da):60,330
Checksum:iF639B3152ACC7750
GO
Isoform 3 (identifier: Q13627-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     516-540: GGSSGTSNSGRARSDPTHQHRHSGG → VEQHWMPGAFRMTVSFTLEVHDVPV
     541-763: Missing.

Show »
Length:540
Mass (Da):61,770
Checksum:iE02CE08DF1AE0AED
GO
Isoform 4 (identifier: Q13627-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     559-584: RQQFPAPLGWSGTEAPTQVTVETHPV → SSHVVHLLVSPAILRWSSTGCQVPLE
     585-763: Missing.

Show »
Length:584
Mass (Da):66,099
Checksum:iBA2480B34BAB2878
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321G → A in AAC50939. (PubMed:8975710)Curated
Sequence conflicti47 – 471N → S in AAC50939. (PubMed:8975710)Curated
Sequence conflicti57 – 571S → P in AAC50939. (PubMed:8975710)Curated
Sequence conflicti123 – 1231Q → R in AAC50939. (PubMed:8975710)Curated
Sequence conflicti266 – 2661A → V in CAA05059. (PubMed:9503011)Curated
Sequence conflicti357 – 3571G → R in CAA05059. (PubMed:9503011)Curated
Sequence conflicti397 – 3971K → N in AAC50939. (PubMed:8975710)Curated
Sequence conflicti592 – 5921A → G in AAC50939. (PubMed:8975710)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti415 – 4151Y → F.1 Publication
VAR_009395
Natural varianti679 – 6791A → P.2 Publications
Corresponds to variant rs55720916 [ dbSNP | Ensembl ].
VAR_040453
Natural varianti681 – 6811Q → H.1 Publication
VAR_009396

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei70 – 789Missing in isoform 1. 2 PublicationsVSP_004917
Alternative sequencei516 – 54025GGSSG…RHSGG → VEQHWMPGAFRMTVSFTLEV HDVPV in isoform 3. CuratedVSP_004920Add
BLAST
Alternative sequencei516 – 52914GGSSG…GRARS → GASAISCSSWLVRH in isoform 2. CuratedVSP_004918Add
BLAST
Alternative sequencei530 – 763234Missing in isoform 2. CuratedVSP_004919Add
BLAST
Alternative sequencei541 – 763223Missing in isoform 3. CuratedVSP_004921Add
BLAST
Alternative sequencei559 – 58426RQQFP…ETHPV → SSHVVHLLVSPAILRWSSTG CQVPLE in isoform 4. 1 PublicationVSP_004922Add
BLAST
Alternative sequencei585 – 763179Missing in isoform 4. 1 PublicationVSP_004923Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13653.1. [Q13627-2]
CCDS13654.1. [Q13627-3]
CCDS42925.1. [Q13627-1]
CCDS42926.1. [Q13627-5]
PIRiJC4898.
RefSeqiNP_001387.2. NM_001396.3. [Q13627-1]
NP_567824.1. NM_101395.2. [Q13627-5]
NP_569120.1. NM_130436.2. [Q13627-2]
NP_569122.1. NM_130438.2. [Q13627-3]
XP_006724039.1. XM_006723976.1. [Q13627-1]
XP_006724040.1. XM_006723977.1. [Q13627-1]
XP_006724041.1. XM_006723978.1. [Q13627-1]
XP_006724042.1. XM_006723979.1. [Q13627-2]
UniGeneiHs.368240.

Genome annotation databases

EnsembliENST00000338785; ENSP00000342690; ENSG00000157540. [Q13627-5]
ENST00000339659; ENSP00000340373; ENSG00000157540. [Q13627-2]
ENST00000398956; ENSP00000381929; ENSG00000157540. [Q13627-3]
ENST00000398960; ENSP00000381932; ENSG00000157540. [Q13627-1]
GeneIDi1859.
KEGGihsa:1859.
UCSCiuc002ywi.3. human. [Q13627-5]
uc002ywj.3. human. [Q13627-2]
uc002ywk.3. human. [Q13627-1]
uc002ywm.3. human. [Q13627-3]

Polymorphism databases

DMDMi3219996.

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
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 .
CCDSi CCDS13653.1. [Q13627-2 ]
CCDS13654.1. [Q13627-3 ]
CCDS42925.1. [Q13627-1 ]
CCDS42926.1. [Q13627-5 ]
PIRi JC4898.
RefSeqi NP_001387.2. NM_001396.3. [Q13627-1 ]
NP_567824.1. NM_101395.2. [Q13627-5 ]
NP_569120.1. NM_130436.2. [Q13627-2 ]
NP_569122.1. NM_130438.2. [Q13627-3 ]
XP_006724039.1. XM_006723976.1. [Q13627-1 ]
XP_006724040.1. XM_006723977.1. [Q13627-1 ]
XP_006724041.1. XM_006723978.1. [Q13627-1 ]
XP_006724042.1. XM_006723979.1. [Q13627-2 ]
UniGenei Hs.368240.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2VX3 X-ray 2.40 A/B/C/D 127-485 [» ]
2WO6 X-ray 2.50 A/B 127-485 [» ]
3ANQ X-ray 2.60 A/B/C/D 126-490 [» ]
3ANR X-ray 2.60 A/B/C/D 126-490 [» ]
4AZE X-ray 3.15 A/B/C 128-485 [» ]
4MQ1 X-ray 2.35 A/B/C/D 127-485 [» ]
4MQ2 X-ray 2.80 A/B/C/D 127-485 [» ]
ProteinModelPortali Q13627.
SMRi Q13627. Positions 148-480.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108192. 59 interactions.
DIPi DIP-39750N.
IntActi Q13627. 32 interactions.
MINTi MINT-1205413.
STRINGi 9606.ENSP00000381932.

Chemistry

BindingDBi Q13627.
ChEMBLi CHEMBL2292.
GuidetoPHARMACOLOGYi 2009.

PTM databases

PhosphoSitei Q13627.

Polymorphism databases

DMDMi 3219996.

Proteomic databases

MaxQBi Q13627.
PaxDbi Q13627.
PRIDEi Q13627.

Protocols and materials databases

DNASUi 1859.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000338785 ; ENSP00000342690 ; ENSG00000157540 . [Q13627-5 ]
ENST00000339659 ; ENSP00000340373 ; ENSG00000157540 . [Q13627-2 ]
ENST00000398956 ; ENSP00000381929 ; ENSG00000157540 . [Q13627-3 ]
ENST00000398960 ; ENSP00000381932 ; ENSG00000157540 . [Q13627-1 ]
GeneIDi 1859.
KEGGi hsa:1859.
UCSCi uc002ywi.3. human. [Q13627-5 ]
uc002ywj.3. human. [Q13627-2 ]
uc002ywk.3. human. [Q13627-1 ]
uc002ywm.3. human. [Q13627-3 ]

Organism-specific databases

CTDi 1859.
GeneCardsi GC21P038739.
HGNCi HGNC:3091. DYRK1A.
HPAi HPA015323.
HPA015810.
MIMi 600855. gene.
614104. phenotype.
neXtProti NX_Q13627.
Orphaneti 178469. Autosomal dominant non-syndromic intellectual disability.
PharmGKBi PA27545.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119032.
HOGENOMi HOG000220863.
HOVERGENi HBG051425.
InParanoidi Q13627.
KOi K08825.
OMAi LTNQRRM.
OrthoDBi EOG77127N.
PhylomeDBi Q13627.
TreeFami TF314624.

Enzyme and pathway databases

BRENDAi 2.7.12.1. 2681.
Reactomei REACT_111214. G0 and Early G1.
SignaLinki Q13627.

Miscellaneous databases

ChiTaRSi DYRK1A. human.
EvolutionaryTracei Q13627.
GeneWikii DYRK1A.
GenomeRNAii 1859.
NextBioi 7615.
PROi Q13627.
SOURCEi Search...

Gene expression databases

Bgeei Q13627.
CleanExi HS_DYRK1A.
ExpressionAtlasi Q13627. baseline and differential.
Genevestigatori Q13627.

Family and domain databases

InterProi IPR028318. DYRK1A.
IPR011009. 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 ]
PANTHERi PTHR24058:SF28. PTHR24058:SF28. 1 hit.
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 2 hits.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY, POSSIBLE INVOLVEMENT IN DOWN SYNDROME, VARIANTS PHE-415 AND HIS-681, ALTERNATIVE SPLICING.
  6. 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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RANBP9, ENZYME REGULATION.
  8. "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 WDR68.
  9. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-748 AND SER-758, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Genome-wide analysis of histidine repeats reveals their role in the localization of human proteins to the nuclear speckles compartment."
    Salichs E., Ledda A., Mularoni L., Alba M.M., de la Luna S.
    PLoS Genet. 5:E1000397-E1000397(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: POLY-HISTIDINE REPEATS.
  12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. Cited for: INVOLVEMENT IN MRD7.
  14. "Splice variants of the dual specificity tyrosine phosphorylation-regulated kinase 4 (DYRK4) differ in their subcellular localization and catalytic activity."
    Papadopoulos C., Arato K., Lilienthal E., Zerweck J., Schutkowski M., Chatain N., Muller-Newen G., Becker W., de la Luna S.
    J. Biol. Chem. 286:5494-5505(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBSTRATE SPECIFICITY.
  15. "Dual-specificity tyrosine phosphorylation-regulated kinase 1A (Dyrk1A) modulates serine/arginine-rich protein 55 (SRp55)-promoted Tau exon 10 inclusion."
    Yin X., Jin N., Gu J., Shi J., Zhou J., Gong C.X., Iqbal K., Grundke-Iqbal I., Liu F.
    J. Biol. Chem. 287:30497-30506(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRSF6.
  16. "Development of a novel selective inhibitor of the Down syndrome-related kinase Dyrk1A."
    Ogawa Y., Nonaka Y., Goto T., Ohnishi E., Hiramatsu T., Kii I., Yoshida M., Ikura T., Onogi H., Shibuya H., Hosoya T., Ito N., Hagiwara M.
    Nat. Commun. 1:86-86(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 126-490 IN COMPLEXES WITH THE SYNTHETIC INHIBITORS HARMINE AND INDY, CATALYTIC ACTIVITY, FUNCTION.
  17. "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: X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 128-485, CATALYTIC ACTIVITY, ENZYME REGULATION.
  18. Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 127-485 IN COMPLEX WITH SYNTHETIC INHIBITOR, CATALYTIC ACTIVITY.
  19. "Structures of Down syndrome kinases, DYRKs, reveal mechanisms of kinase activation and substrate recognition."
    Soundararajan M., Roos A.K., Savitsky P., Filippakopoulos P., Kettenbach A.N., Olsen J.V., Gerber S.A., Eswaran J., Knapp S., Elkins J.M.
    Structure 21:986-996(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 127-485 IN COMPLEXES WITH PEPTIDE SUBSTRATE AND INHIBITOR DJM2005, CATALYTIC ACTIVITY, FUNCTION, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-188 AND TYR-321, PHOSPHORYLATION AT TYR-111; TYR-140; TYR-159; TYR-177; SER-310; TYR-319; TYR-321; THR-402 AND TYR-449, ACTIVE SITE, IDENTIFICATION BY MASS SPECTROMETRY.
  20. "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: VARIANT [LARGE SCALE ANALYSIS] PRO-679.

Entry informationi

Entry nameiDYR1A_HUMAN
AccessioniPrimary (citable) accession number: Q13627
Secondary accession number(s): O60769
, Q92582, Q92810, Q9UNM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1998
Last modified: November 26, 2014
This is version 158 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 21
    Human chromosome 21: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3