| Tag | Content |
|---|
| CPLM ID | CPLM-005316 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Protein kinase C-like 1 |
Protein Synonyms/Alias | PKC 1 |
Gene Name | PKC1 |
Gene Synonyms/Alias | HPO2; STT1; YBL105C; YBL0807 |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 39 | SNVMVIQKCNTNIRE | ubiquitination | [1] | | 64 | SLKKLRLKTAQQSQG | ubiquitination | [1] | | 106 | FSRLDLVKYDCPSLA | ubiquitination | [1] | | 142 | EANTKLTKLYQIDGD | ubiquitination | [1] | | 164 | EGGAMESKYRIQMLN | ubiquitination | [1] | | 464 | VVTKCIAKTSTDTDP | ubiquitination | [1] |
|
Reference | [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J. Nat Methods. 2013 Jul;10(7):676-82. [ PMID: 23749301] |
Functional Description | Required for cell growth and for the G2->M transition of the cell division cycle. Mediates a protein kinase cascade; it activates BCK1 which itself activates MKK1/MKK2. |
Sequence Annotation | REPEAT 5 77 REM 1.
REPEAT 118 193 REM 2.
DOMAIN 196 288 C2.
DOMAIN 824 1083 Protein kinase.
DOMAIN 1084 1151 AGC-kinase C-terminal.
ZN_FING 414 461 Phorbol-ester/DAG-type 1.
ZN_FING 481 531 Phorbol-ester/DAG-type 2.
NP_BIND 830 838 ATP (By similarity).
ACT_SITE 949 949 Proton acceptor (By similarity).
BINDING 853 853 ATP (By similarity).
MOD_RES 226 226 Phosphoserine.
MOD_RES 761 761 Phosphoserine. |
Keyword | ATP-binding; Calcium; Cell cycle; Complete proteome; Kinase; Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1151 AA |
Protein Sequence | MSFSQLEQNI KKKIAVEENI IRGASALKKK TSNVMVIQKC NTNIREARQN LEYLEDSLKK 60
LRLKTAQQSQ GENGSEDNER CNSKEYGFLS TKSPNEHIFS RLDLVKYDCP SLAQRIQYML 120
QQLEFKLQVE KQYQEANTKL TKLYQIDGDQ RSSSAAEGGA MESKYRIQML NKALKKYQAI 180
NVDFDQFKHQ PNDIMDNQQP KFRRKQLTGV LTIGITAARD VDHIQSPMFA RKPESYVTIK 240
IDDTIKARTK PSRNDRWSED FQIPVEKGNE IEITVYDKVN DSLIPVAIMW LLLSDIAEEI 300
RKKKAGQTNE QQGWVNASNI NGGSSLASEE GSTLTSTYSN SAIQSTSAKN VQGENTSTSQ 360
ISTNSWFVLE PSGQILLTLG FHKSSQIERK QLMGGLHRHG AIINRKEEIF EQHGHHFVQK 420
SFYNIMCCAY CGDFLRYTGF QCQDCKFLCH KKCYTNVVTK CIAKTSTDTD PDEAKLNHRI 480
PHRFLPTSNR GTKWCCHCGY ILPWGRHKVR KCSECGIMCH AQCAHLVPDF CGMSMEMANK 540
ILKTIQDTKR NQEKKKRTVP SAQLGSSIGT ANGSDLSPSK LAERANAPLP PQPRKHDKTP 600
SPQKVGRDSP TKQHDPIIDK RISLQTHGRE KLNKFIDENE AYLNFTEGAQ QTAEFSSPEK 660
TLDPTSNRRS LGLTDLSIEH SQTWESKDDL MRDELELWKA QREEMELEIK QDSGEIQEDL 720
EVDHIDLETK QKLDWENKND FREADLTIDS THTNPFRDMN SETFQIEQDH ASKEVLQETV 780
SLAPTSTHAS RTTDQQSPQK SQTSTSAKHK KRAAKRRKVS LDNFVLLKVL GKGNFGKVIL 840
SKSKNTDRLC AIKVLKKDNI IQNHDIESAR AEKKVFLLAT KTKHPFLTNL YCSFQTENRI 900
YFAMEFIGGG DLMWHVQNQR LSVRRAKFYA AEVLLALKYF HDNGVIYRDL KLENILLTPE 960
GHIKIADYGL CKDEMWYGNR TSTFCGTPEF MAPEILKEQE YTKAVDWWAF GVLLYQMLLC 1020
QSPFSGDDED EVFNAILTDE PLYPIDMAGE IVQIFQGLLT KDPEKRLGAG PRDADEVMEE 1080
PFFRNINFDD ILNLRVKPPY IPEIKSPEDT SYFEQEFTSA PPTLTPLPSV LTTSQQEEFR 1140
GFSFMPDDLD L 1151 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:SGD. GO:0005856; C:cytoskeleton; IDA:SGD. GO:0005634; C:nucleus; IDA:SGD. GO:0005886; C:plasma membrane; IDA:SGD. GO:0030427; C:site of polarized growth; IDA:SGD. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0004697; F:protein kinase C activity; IDA:SGD. GO:0007015; P:actin filament organization; IGI:SGD. GO:0007049; P:cell cycle; IEA:UniProtKB-KW. GO:0033962; P:cytoplasmic mRNA processing body assembly; IMP:SGD. GO:0007243; P:intracellular protein kinase cascade; IMP:SGD. GO:0030242; P:peroxisome degradation; IMP:SGD. GO:0060237; P:regulation of fungal-type cell wall organization; IMP:SGD. GO:0060211; P:regulation of nuclear-transcribed mRNA poly(A) tail shortening; IMP:SGD. |
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