| Tag | Content |
|---|
| CPLM ID | CPLM-013612 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Serine/threonine-protein kinase TNNI3K |
Protein Synonyms/Alias | Cardiac ankyrin repeat kinase; TNNI3-interacting kinase |
Gene Name | Tnni3k |
Gene Synonyms/Alias | Cark |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 38 | LEDDLQIKENEFQEL | ubiquitination | [1] | | 622 | LDEDNMTKQPGNLRW | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | May play a role in cardiac physiology (By similarity). |
Sequence Annotation | REPEAT 66 96 ANK 1.
REPEAT 100 129 ANK 2.
REPEAT 133 162 ANK 3.
REPEAT 166 195 ANK 4.
REPEAT 199 229 ANK 5.
REPEAT 233 262 ANK 6.
REPEAT 268 297 ANK 7.
REPEAT 303 334 ANK 8.
REPEAT 338 367 ANK 9.
REPEAT 380 409 ANK 10.
DOMAIN 462 722 Protein kinase.
NP_BIND 468 476 ATP (By similarity).
ACT_SITE 587 587 Proton acceptor (By similarity).
BINDING 489 489 ATP (By similarity).
LIPID 2 2 N-myristoyl glycine (Potential). |
Keyword | Alternative splicing; ANK repeat; ATP-binding; Coiled coil; Complete proteome; Cytoplasm; Kinase; Lipoprotein; Magnesium; Metal-binding; Myristate; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 834 AA |
Protein Sequence | MGNYKSRPTQ TCSDEWKKKV SESYAIIIER LEDDLQIKEN EFQELRHIFG SDEAFSEVSL 60
NYRTERGLSL LHLCCACGGN KSHIRALMLK GLRPSRLTRN GFPALHLAVY KDSLELITSL 120
LHSGADVQQA GYGGLTALHI AAIAGHPEAV EVLLQHGANV NVQDAVFFTP LHIAAYYGHE 180
QVTSVLLKFG ADVNVSGEVG DRPLHLASAK GFFNIVKLLV EGNKADVNAQ DNEDHVPLHF 240
CSRFGHHNIV SYLLQSDLEV QPHVINIYGD TPLHLACYNG NFEVAKEIVH VTGTESLTKE 300
NIFSETAFHS ACTYGKNIDL VKFLLDQNAV NINHRGRDGH TGLHSACYHG HIRLVQFLLD 360
NGADMNLVAC DPSRSSGEKD EQTCLMWAYE KGHDAIVTLL KHYKRPQDEL PCNEYSQPGG 420
DGSYVSVPSP LGKIKSMTKE KADVLLLRAE LPSRFHLQLS EIEFHEIIGS GSFGKVYKGR 480
CRNKIVAIKR YRANTYCSKS DVDMFCREVS ILCQLNHPCV VQFVGACLDD PSQFAIVTQY 540
ISGGSLFSLL HEQKRILDLQ SKLIIAVDVA KGMEYLHSLT QPIIHRDLNS HNILLYEDGH 600
AVVADFGESR FLQSLDEDNM TKQPGNLRWM APEVFTQCTR YTIKADVFSY ALCLWELLTG 660
EIPFAHLKPA AAAADMAYHH IRPPIGYSIP KPISSLLMRG WNACPEGRPE FSEVVRKLEE 720
CLCNVELMSP ASSNSSGSLS PSSSSDCLLS RGGPGRSHVA ALRSRFELEY ALNARSYTGW 780
PQSVGTHTNP GLSLEEMNRG AQYSAVDKYG YVSDPMSPMH LHSRRNSGSF EDGN 834 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |