Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-559292-00319
Entry Name
UniProt Accession
Theoretical PI
9.1
Molecular Weight
62079.17
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Casein kinase I homolog 2
Protein Synonyms/Alias
2.7.11.1;
Gene Name
YCK2
Gene Synonyms/Alias
CKI1; YNL154C; N1755;
Created Date
01-NOV-1991
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
545
Canonical
GFFSKLGCC******
[1][2]
S-Palmitoylation
546
Canonical
FFSKLGCC*******
[1][2]
S-Palmitoylation
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
NCBI Taxa ID
559292
Reference
[1] Roth AF, Feng Y, Chen L, Davis NG. The yeast DHHC cysteine-rich domain proteinAkr1p is a palmitoyl transferase. J Cell Biol. 2002 Oct 14;159(1):23-8. Epub 2002Oct 7.[PMID:12370247]
[2] Babu P, Deschenes RJ, Robinson LC. Akr1p-dependent palmitoylation of Yck2pyeast casein kinase 1 is necessary and sufficient for plasma membrane targeting. J Biol Chem. 2004 Jun 25;279(26):27138-47. Epub 2004 Apr 22.[PMID:15105419]
Functional Description
Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates.
Sequence Annotation
Domain: 76 360 Protein kinase.
Nucleotide-binding: 82 90 ATP.
Active site: 195 195 Proton acceptor.
Binding site: 105 105 ATP.
Modified residue: 2 2 N-acetylserine.
Modified residue: 455 455 Phosphoserine.
Protein Length
546 AA.
Protein Sequence
(Canonical)
MSQVQSPLTA TNSGLAVNNN TMNSQMPNRS NVRLVNGTLP PSLHVSSNLN HNTGNSSASY  60
SGSQSRDDST IVGLHYKIGK KIGEGSFGVL FEGTNMINGL PVAIKFEPRK TEAPQLKDEY  120
RTYKILAGTP GIPQEYYFGQ EGLHNILVID LLGPSLEDLF DWCGRRFSVK TVVQVAVQMI  180
TLIEDLHAHD LIYRDIKPDN FLIGRPGQPD ANKVHLIDFG MAKQYRDPKT KQHIPYREKK  240
SLSGTARYMS INTHLGREQS RRDDMEAMGH VFFYFLRGQL PWQGLKAPNN KQKYEKIGEK  300
KRLTNVYDLA QGLPIQFGRY LEIVRNLSFE ETPDYEGYRM LLLSVLDDLG ETADGQYDWM  360
KLNGGRGWDL SINKKPNLHG YGHPNPPNEK SKRHRSKNHQ YSSPDHHHHY NQQQQQQQAQ  420
AQAQAQAQAK VQQQQLQQAQ AQQQANRYQL QPDDSHYDEE REASKLDPTS YEAYQQQTQQ  480
KYAQQQQKQM QQKSKQFANT GANGQTNKYP YNAQPTANDE QNAKNAAQDR NSNKSSKGFF  540
SKLGCC                                                             546
FASTA
(Canonical)
>LipidDB-559292-00319|P23292
MSQVQSPLTATNSGLAVNNNTMNSQMPNRSNVRLVNGTLPPSLHVSSNLNHNTGNSSASY
SGSQSRDDSTIVGLHYKIGKKIGEGSFGVLFEGTNMINGLPVAIKFEPRKTEAPQLKDEY
RTYKILAGTPGIPQEYYFGQEGLHNILVIDLLGPSLEDLFDWCGRRFSVKTVVQVAVQMI
TLIEDLHAHDLIYRDIKPDNFLIGRPGQPDANKVHLIDFGMAKQYRDPKTKQHIPYREKK
SLSGTARYMSINTHLGREQSRRDDMEAMGHVFFYFLRGQLPWQGLKAPNNKQKYEKIGEK
KRLTNVYDLAQGLPIQFGRYLEIVRNLSFEETPDYEGYRMLLLSVLDDLGETADGQYDWM
KLNGGRGWDLSINKKPNLHGYGHPNPPNEKSKRHRSKNHQYSSPDHHHHYNQQQQQQQAQ
AQAQAQAQAKVQQQQLQQAQAQQQANRYQLQPDDSHYDEEREASKLDPTSYEAYQQQTQQ
KYAQQQQKQMQQKSKQFANTGANGQTNKYPYNAQPTANDEQNAKNAAQDRNSNKSSKGFF
SKLGCC
Gene Ontology
GO:0005935; C:cellular bud neck; IDA:SGD
GO:0005937; C:mating projection; IDA:SGD
GO:0005886; C:plasma membrane; IDA:SGD
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD
GO:0000902; P:cell morphogenesis; IGI:SGD
GO:0006897; P:endocytosis; IGI:SGD
GO:0006468; P:protein phosphorylation; IMP:SGD
GO:0009749; P:response to glucose; IMP:SGD
Interpro
InterPro; IPR011009; Kinase-like_dom
InterPro; IPR000719; Prot_kinase_dom
InterPro; IPR017441; Protein_kinase_ATP_BS
InterPro; IPR008271; Ser/Thr_kinase_AS
Pfam
Pfam; PF00069; Pkinase;
SMART
PROSITE
PROSITE; PS00107; PROTEIN_KINASE_ATP;
PROSITE; PS50011; PROTEIN_KINASE_DOM;
PROSITE; PS00108; PROTEIN_KINASE_ST;
PRINTS