| Tag | Content |
|---|
| CPLM ID | CPLM-023417 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Serine/threonine-protein kinase PITSLRE |
Protein Synonyms/Alias | Cell division cycle 2-like |
Gene Name | Pitslre |
Gene Synonyms/Alias | CG4268 |
Created Date | July 27, 2013 |
Organism | Drosophila melanogaster (Fruit fly) |
NCBI Taxa ID | 7227 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 363 | SKPDNYEKEIKLKKR | acetylation | [1] |
|
Reference | [1] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation. Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C. Sci Signal. 2011 Jul 26;4(183):ra48. [ PMID: 21791702] |
Functional Description | Acts as a negative regulator of the normal cell cycle progression. May function in regulating proliferation by the phosphorylation and subsequent plasma membrane targeting of galactosyltransferase (By similarity). |
Sequence Annotation | DOMAIN 558 851 Protein kinase.
NP_BIND 564 572 ATP (By similarity).
MOTIF 51 56 Nuclear localization signal (Potential).
ACT_SITE 685 685 Proton acceptor (By similarity).
BINDING 587 587 ATP (By similarity).
MOD_RES 439 439 Phosphoserine.
MOD_RES 442 442 Phosphoserine.
MOD_RES 447 447 Phosphotyrosine.
MOD_RES 449 449 Phosphoserine.
MOD_RES 881 881 Phosphoserine.
MOD_RES 886 886 Phosphoserine. |
Keyword | ATP-binding; Cell cycle; Complete proteome; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 952 AA |
Protein Sequence | MVNSSGSEDG QLRSPNDVHY HSRGEEDEHE GDADALYIQP PQASRESGSG PRREKKKHSR 60
ERRRHKERDD VGGAALALER DHRYDYRSRE EHYHHHQRER SSNAAAAYAK HHLGHAYHYP 120
QPPQQQQQPL PPAPSYAAHH YHHHQHLSGA RAAPREYHSY PSGYHSGSRH GDYPMEEPTR 180
RSSKYAESKD AESLEQDLRS RLLKKRHNYV KDYETEENYE HRVERSDRRE GGRKERERTV 240
RSTHKQNRHD RVIELLDSPE QEHHHQHQHK SHRSKWREEV EVIRRKVPED LELLARREKL 300
LAAERESRQR KQTAREELEA RRELLRERNE HSDALSPTTV AASVTAGLNI HVKRKSKPDN 360
YEKEIKLKKR REDDIEVIRD DDDEESEESD SNEEVPEQDS EGSATESGSE DSYASKKKSK 420
IKSKSQLEDD DEDLPLPDSP LSVGELYKSP KQRQRSRSVS SKSSSQSSRS SRSRSRSRSQ 480
SSLEDEVDRQ DVGADASPSS STRSEERGMT QEQPEEKPEE KLKEKQKSLE EQIPCDDKGI 540
PLPNYYPGVQ GCRSVEEFQC LNRIEEGTYG VVYRAKDKRT NEIVALKRLK MEKEKEGFPI 600
TSLREINTLL KGQHPNIVTV REIVVGSNMD KIFIVMDYVE HDLKSLMETM KNRKQSFFPG 660
EVKCLTQQLL RAVAHLHDNW ILHRDLKTSN LLLSHKGILK VGDFGLAREY GSPIKKYTSL 720
VVTLWYRAPE LLLCSPVYST PIDVWSVGCI FAEFLQMLPL FPGKSEIDEL NRIFKELGTP 780
NEKIWPGYTE LPAVKNMLSQ NSQFTEYPVS QLRKHFQEKT SEMGLSLLQG LLTYDPKQRL 840
SADAALKHGF FKELPLPIDP SMFPTWPAKS ELGARKAQAS SPKPPSGGSQ FKQLGRDEPI 900
IVGPGNKLSS GIITGNKKSH GAGGSSASTG FVLNAGITQR QLAMGPGFSL KF 952 |
Gene Ontology | GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:EC. GO:0004674; F:protein serine/threonine kinase activity; ISS:FlyBase. GO:0007155; P:cell adhesion; IMP:FlyBase. GO:0008360; P:regulation of cell shape; IMP:FlyBase. |
Interpro | |
Pfam | |
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PROSITE | |
PRINTS | |