Reviewed, UniProtKB/Swiss-Prot Q13627 (DYR1A_HUMAN)

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

Name:	DYRK1A
Synonyms:	DYRK, MNB, MNBH

Organism

Homo sapiens (Human) [Complete proteome]

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.
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. Ref.3
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Inhibited by RANBP9. Ref.7
Subunit structure	Interacts RAD54L2/ARIP4 By similarity. Interacts with RANBP9. Interacts with WDR68. Ref.7 Ref.8
Subcellular location	Nucleus speckle.
Tissue specificity	Ubiquitous. Highest levels in skeletal muscle, testis, fetal lung and fetal kidney. Ref.3 Ref.1 Ref.2 Ref.5
Developmental stage	Expressed in the developing central nervous system. Overexpressed 1.5-fold in fetal Down syndrome brain. Ref.3
Post-translational modification	Autophosphorylated on tyrosine residues. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16
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
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	nervous system development Ref.3 Traceable author statement. Source: ProtInc peptidyl-tyrosine phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB protein amino acid autophosphorylation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	nuclear speck Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Inferred from direct assay. Source: MGI protein self-association Inferred from sequence or structural similarity. Source: UniProtKB protein serine/threonine kinase activity Ref.3 Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
YWHAB	P31946	3	EBI-1053621,EBI-359815

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: 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

Feature identifier

Molecule processing

Chain

1 – 763

763

Dual specificity tyrosine-phosphorylation-regulated kinase 1A

PRO_0000085931

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 Ref.9 Ref.10 Ref.16

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 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16

Modified residue

324

1

Phosphoserine Ref.16

Modified residue

748

1

Phosphoserine Ref.13

Modified residue

758

1

Phosphoserine Ref.13

Natural variations

Alternative sequence

70 – 78

9

Missing in isoform 1.

VSP_004917

Alternative sequence

516 – 540

25

GGSSG…RHSGG → VEQHWMPGAFRMTVSFTLEV HDVPV in isoform 3.

VSP_004920

Alternative sequence

516 – 529

14

GGSSG…GRARS → GASAISCSSWLVRH in isoform 2.

VSP_004918

Alternative sequence

530 – 763

234

Missing in isoform 2.

VSP_004919

Alternative sequence

541 – 763

223

Missing in isoform 3.

VSP_004921

Alternative sequence

559 – 584

26

RQQFP…ETHPV → SSHVVHLLVSPAILRWSSTG CQVPLE in isoform 4.

VSP_004922

Alternative sequence

585 – 763

179

Missing in isoform 4.

VSP_004923

Natural variant

415

1

Y → F

VAR_009395

Natural variant

679

1

A → P: dbSNP rs55720916. Ref.1 Ref.17

VAR_040453

Natural variant

681

1

Q → H

VAR_009396

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

Secondary structure

1

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763

Helix Strand Turn

Details...

Turn

156 – 158

3

Beta strand

159 – 164

6

Beta strand

173 – 178

6

Turn

179 – 182

4

Beta strand

183 – 189

7

Helix

194 – 212

19

Helix

216 – 220

5

Beta strand

224 – 230

7

Beta strand

233 – 239

7

Helix

245 – 251

7

Turn

252 – 254

3

Helix

259 – 276

18

Turn

279 – 281

3

Helix

290 – 292

3

Beta strand

293 – 297

5

Beta strand

303 – 305

3

Helix

325 – 327

3

Helix

330 – 333

4

Helix

341 – 346

6

Helix

350 – 355

6

Helix

366 – 376

11

Helix

382 – 385

4

Helix

391 – 394

4

Beta strand

395 – 397

3

Beta strand

403 – 405

3

Helix

423 – 426

4

Helix

446 – 459

14

Turn

464 – 466

3

Helix

470 – 473

4

Helix

477 – 479

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified July 15, 1998. Version 2. Checksum: 7C3A52A3CBB04FB5	FASTA	763	85,584
	10 20 30 40 50 60 MHTGGETSAC KPSSVRLAPS FSFHAAGLQM AGQMPHSHQY SDRRQPNISD QQVSALSYSD 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 GTWNLKKTKD 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 HFTAAVQAMD 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 YMTEGHLTMR QGADREESPM TGVCVQQSPV ASS
	Isoform 1. Checksum: 59518E25F1D4FF96	FASTA	754	84,556
	10 20 30 40 50 60 MHTGGETSAC KPSSVRLAPS FSFHAAGLQM AGQMPHSHQY SDRRQPNISD QQVSALSYSD 70 80 90 100 110 120 QIQQPLTNQR RMPQTFRDPA TAPLRKLSVD LIKTYKHINE VYYAKKKRRH QQGQGDDSSH 130 140 150 160 170 180 KKERKVYNDG YDDDNYDYIV KNGEKWMDRY EIDSLIGKGS FGQVVKAYDR VEQEWVAIKI 190 200 210 220 230 240 IKNKKAFLNQ AQIEVRLLEL MNKHDTEMKY YIVHLKRHFM FRNHLCLVFE MLSYNLYDLL 250 260 270 280 290 300 RNTNFRGVSL NLTRKFAQQM CTALLFLATP ELSIIHCDLK PENILLCNPK RSAIKIVDFG 310 320 330 340 350 360 SSCQLGQRIY QYIQSRFYRS PEVLLGMPYD LAIDMWSLGC ILVEMHTGEP LFSGANEVDQ 370 380 390 400 410 420 MNKIVEVLGI PPAHILDQAP KARKFFEKLP DGTWNLKKTK DGKREYKPPG TRKLHNILGV 430 440 450 460 470 480 ETGGPGGRRA GESGHTVADY LKFKDLILRM LDYDPKTRIQ PYYALQHSFF KKTADEGTNT 490 500 510 520 530 540 SNSVSTSPAM EQSQSSGTTS STSSSSGGSS GTSNSGRARS DPTHQHRHSG GHFTAAVQAM 550 560 570 580 590 600 DCETHSPQVR QQFPAPLGWS GTEAPTQVTV ETHPVQETTF HVAPQQNALH HHHGNSSHHH 610 620 630 640 650 660 HHHHHHHHHH GQQALGNRTR PRVYNSPTNS SSTQDSMEVG HSHHSMTSLS SSTTSSSTSS 670 680 690 700 710 720 SSTGNQGNQA YQNRPVAANT LDFGQNGAMD VNLTVYSNPR QETGIAGHPT YQFSANTGPA 730 740 750 HYMTEGHLTM RQGADREESP MTGVCVQQSP VASS
	Isoform 2. Checksum: F639B3152ACC7750	FASTA	529	60,330
	10 20 30 40 50 60 MHTGGETSAC KPSSVRLAPS FSFHAAGLQM AGQMPHSHQY SDRRQPNISD QQVSALSYSD 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 GTWNLKKTKD GKREYKPPGT 430 440 450 460 470 480 RKLHNILGVE TGGPGGRRAG ESGHTVADYL KFKDLILRML DYDPKTRIQP YYALQHSFFK 490 500 510 520 KTADEGTNTS NSVSTSPAME QSQSSGTTSS TSSSSGASAI SCSSWLVRH
	Isoform 3. Checksum: E02CE08DF1AE0AED	FASTA	540	61,770
	10 20 30 40 50 60 MHTGGETSAC KPSSVRLAPS FSFHAAGLQM AGQMPHSHQY SDRRQPNISD QQVSALSYSD 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 GTWNLKKTKD GKREYKPPGT 430 440 450 460 470 480 RKLHNILGVE TGGPGGRRAG ESGHTVADYL KFKDLILRML DYDPKTRIQP YYALQHSFFK 490 500 510 520 530 540 KTADEGTNTS NSVSTSPAME QSQSSGTTSS TSSSSVEQHW MPGAFRMTVS FTLEVHDVPV
	Isoform 4. Checksum: BA2480B34BAB2878	FASTA	584	66,099
	10 20 30 40 50 60 MHTGGETSAC KPSSVRLAPS FSFHAAGLQM AGQMPHSHQY SDRRQPNISD QQVSALSYSD 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 GTWNLKKTKD 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 HFTAAVQAMD CETHSPQVSS HVVHLLVSPA ILRWSSTGCQ VPLE

References

	« Hide 'large scale' referencesShow '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]	"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: 14593110] [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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-145 AND TYR-321, MASS SPECTROMETRY.
[10]	"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. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-145, MASS SPECTROMETRY.
[11]	"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.
[12]	"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.
[13]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-321; SER-748 AND SER-758, MASS SPECTROMETRY.
[14]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-321, MASS SPECTROMETRY.
[15]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-321, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[16]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-145; TYR-321 AND SER-324, MASS SPECTROMETRY. Tissue: T-cell.
[17]	"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: 17344846] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] PRO-679.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00014344.
IPI00219250.
IPI00219251.
IPI00219252.
IPI00941492.

PIR

JC4898.

RefSeq

NP_001387.2.
NP_567824.1.
NP_569120.1.
NP_569121.1.
NP_569122.1.

UniGene

Hs.368240

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ModBase

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Protein-protein interaction databases

IntAct

Q13627. 6 interactions.

STRING

Q13627.

PTM databases

PhosphoSite

Q13627.

Proteomic databases

PRIDE

Q13627.

Genome annotation databases

Ensembl

ENST00000398960; ENSP00000381932; ENSG00000157540; Homo sapiens. [Genome view]

GeneID

1859.

KEGG

hsa:1859.

UCSC

uc002ywi.1. human.
uc002ywj.1. human.
uc002ywk.1. human.
uc002ywl.1. human.

Organism-specific databases

CTD

1859.

GeneCards

GC21P037661.

H-InvDB

HIX0040839.

HGNC

HGNC:3091. DYRK1A.

HPA

HPA015323.
HPA015810.

MIM

600855. gene.

PharmGKB

PA27545.

GenAtlas

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Phylogenomic databases

eggNOG

prNOG04928.

HOGENOM

HBG755340.

HOVERGEN

Q13627.

InParanoid

Q13627.

OMA

HRHSGGH.

Enzyme and pathway databases

BRENDA

2.7.12.1. 247.

Gene expression databases

ArrayExpress

Q13627.

Bgee

Q13627.

CleanEx

HS_DYRK1A.

Genevestigator

Q13627.

GermOnline

ENSG00000157540. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR002290. Ser/Thr_prot_kinase_dom.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

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Other Resources

NextBio

7615.

SOURCE

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Entry information

Entry name

DYR1A_HUMAN

Accession

Primary (citable) accession number: Q13627
Secondary accession number(s): O60769 , Q92582, Q92810, Q9UNM5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 15, 1998
Last modified:	January 19, 2010
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.