| Tag | Content |
|---|
| CPLM ID | CPLM-000772 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Dual specificity tyrosine-phosphorylation-regulated kinase 3 |
Protein Synonyms/Alias | Regulatory erythroid kinase; REDK |
Gene Name | DYRK3 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 446 | AKYFINSKGIPRYCS | ubiquitination | [1] | | 554 | AFQGLGSKLPPVVGI | ubiquitination | [1] | | 564 | PVVGIANKLKANLMS | ubiquitination | [1] | | 566 | VGIANKLKANLMSET | ubiquitination | [1] |
|
Reference | [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA. Mol Cell Proteomics. 2013 Mar;12(3):825-31. [ PMID: 23266961] |
Functional Description | Negative regulator of EPO-dependent erythropoiesis, may place an upper limit on red cell production during stress erythropoiesis. Inhibits cell death due to cytokine withdrawal in hematopoietic progenitor cells. May act by regulating CREB/CRE signaling. |
Sequence Annotation | DOMAIN 209 522 Protein kinase.
NP_BIND 215 223 ATP (By similarity).
ACT_SITE 335 335 Proton acceptor (By similarity).
BINDING 238 238 ATP (By similarity).
MOD_RES 318 318 Phosphoserine (By similarity).
MOD_RES 369 369 Phosphotyrosine (By similarity). |
Keyword | Alternative splicing; ATP-binding; Complete proteome; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 588 AA |
Protein Sequence | MGGTARGPGR KDAGPPGAGL PPQQRRLGDG VYDTFMMIDE TKCPPCSNVL CNPSEPPPPR 60
RLNMTTEQFT GDHTQHFLDG GEMKVEQLFQ EFGNRKSNTI QSDGISDSEK CSPTVSQGKS 120
SDCLNTVKSN SSSKAPKVVP LTPEQALKQY KHHLTAYEKL EIINYPEIYF VGPNAKKRHG 180
VIGGPNNGGY DDADGAYIHV PRDHLAYRYE VLKIIGKGSF GQVARVYDHK LRQYVALKMV 240
RNEKRFHRQA AEEIRILEHL KKQDKTGSMN VIHMLESFTF RNHVCMAFEL LSIDLYELIK 300
KNKFQGFSVQ LVRKFAQSIL QSLDALHKNK IIHCDLKPEN ILLKHHGRSS TKVIDFGSSC 360
FEYQKLYTYI QSRFYRAPEI ILGSRYSTPI DIWSFGCILA ELLTGQPLFP GEDEGDQLAC 420
MMELLGMPPP KLLEQSKRAK YFINSKGIPR YCSVTTQADG RVVLVGGRSR RGKKRGPPGS 480
KDWGTALKGC DDYLFIEFLK RCLHWDPSAR LTPAQALRHP WISKSVPRPL TTIDKVSGKR 540
VVNPASAFQG LGSKLPPVVG IANKLKANLM SETNGSIPLC SVLPKLIS 588 |
Gene Ontology | GO:0005634; C:nucleus; IDA:UniProtKB. GO:0005524; F:ATP binding; IDA:UniProtKB. GO:0000287; F:magnesium ion binding; IDA:UniProtKB. GO:0004672; F:protein kinase activity; IDA:UniProtKB. GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:EC. GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW. GO:0030218; P:erythrocyte differentiation; IDA:UniProtKB. |
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