| Tag | Content |
|---|
| EKPD ID | EKS-SAC-00065 |
| Classification | | Group/Family | Score | E-Value | Start | End | Domain Length |
|---|
| CMGC/CDK | 388.9 | 4.1E-117 | 7 | 297 | 291 |
|
| Status | Reviewed |
| Ensembl Protein | YPL031C |
| UniProt Accession | P17157; D6W3Y2; Q03089; Q06888; |
| Protein Name | Cyclin-dependent protein kinase PHO85 |
| Protein Synonyms/Alias | Negative regulator of the PHO system; Serine/threonine-protein kinase PHO85; |
| Gene Name | PHO85 |
| Gene Synonyms/Alias | PHO85; SSG3; YPL031C; P7102.18A; |
| Ensembl Information | |
| Organism | Saccharomyces cerevisiae |
| Functional Description | Cyclin-dependent protein kinase (CDK) catalytic subunitthat regulates multiple cell cycle and metabolic processes in response to nutrient availability. Associates with different cyclins, that control kinase activity, substrate-specificity and subcellular location of the kinase. Favorable growth conditions always result in activated cyclin-CDK complexes. Regulates metabolic processes when associated with PHO80 cyclin family members (PH080, PCL6, PCL7, PCL8 and PCL10), and cell cycle and morphogenesis processes when associated with PCL1,2 cyclin family members (PCL1, PCL2, CLG1, PCL5 and PCL9). When associated with PHO80, negatively regulates the expression of phosphate- starvation-responsive genes under phosphate-rich conditions. The PHO80-PHO85 cyclin-CDK holoenzyme phosphorylates and inactivates the transcription factor PHO4 by promoting its export to the cytoplasm. PHO80-PHO85 phosphorylates and inactivates protein kinase RIM15 by retaining it in the cytoplasm, antagonizing RIM15- induced entry into stationary phase. PHO80-PHO85 also phosphorylates and inactivates the calcineurin-responsive transcription factor CRZ1, linking cyclin-CDK activity to calcium signaling. Together with the cyclins PCL6/PCL7 and PCL8/PCL10, negatively controls glycogen accumulation. When associated with cyclins PCL6 and PCL7, controls glycogen phosphorylase and glycogen synthase activities. PCL6-PHO85 and PCL7-PHO85 phosphorylate and inactivate the phosphatase PP1-2 inhibitor GLC8, causing activation of PP1-2, which then dephosphorylates and activates glycogen phosphorylase. When associated with cyclins PCL8 and PCL10, has glycogen synthase kinase activity. PCL10-PHO85 phosphorylates and negatively regulates glycogen synthase GSY2. Association with PCL1 and PCL2 is required for cell cycle progression at start in the absence of the CDC28-dependent G1 cyclins CLN1 and CLN2. PCL1-PHO85 is involved in phosphorylation of the CDK inhibitor (CKI) SIC1, which is required for its ubiquitination and degradation, releasing repression of b-type cyclins and promoting exit from mitosis. When associated with cyclins PCL1 and PCL2, positively controls degradation of sphingoid long chain base kinase LCB4 via phosphorylation of LCB4, which is required for its ubiquitination and degradation. PCL1- PHO85 also phosphorylates HMS1, NCP1 and NPA3, which may all have a role in mitotic exit. PCL2-PHO85 also phosphorylates RVS167, linking cyclin-CDK activity with organization of the actin cytoskeleton. When associated with PCL5, positively controls degradation of transcription factor GCN4 via phosphorylation of GCN4, which is required for its degradation by the E3 ubiquitin ligase complex SCF(Cdc4). When associated with PCL9, may have a role in bud site selection in G1 phase. PHO85 also phosphorylates the transcription factor SWI5. |
| Protein Length | 305 |
Protein Sequence
(FASTA) | | MSSSSQFKQL EKLGNGTYAT VYKGLNKTTG VYVALKEVKL DSEEGTPSTA IREISLMKEL 60 | | KHENIVRLYD VIHTENKLTL VFEFMDNDLK KYMDSRTVGN TPRGLELNLV KYFQWQLLQG 120 | | LAFCHENKIL HRDLKPQNLL INKRGQLKLG DFGLARAFGI PVNTFSSEVV TLWYRAPDVL 180 | | MGSRTYSTSI DIWSCGCILA EMITGKPLFP GTNDEEQLKL IFDIMGTPNE SLWPSVTKLP 240 | | KYNPNIQQRP PRDLRQVLQP HTKEPLDGNL MDFLHGLLQL NPDMRLSAKQ ALHHPWFAEY 300 | | YHHAS 305 |
|
Nucleotide Sequence
(FASTA) | | ATGTCTTCTT CTTCACAATT TAAGCAGTTA GAAAAGCTTG GCAATGGTAC GTATGCCACA 60 | | GTGTACAAGG GACTGAACAA AACCACAGGG GTATATGTTG CCCTGAAAGA GGTAAAACTG 120 | | GATTCAGAGG AAGGTACACC CTCTACGGCC ATCCGTGAGA TCTCCCTAAT GAAAGAATTG 180 | | AAACATGAGA ACATTGTTAG ACTTTATGAC GTTATTCACA CAGAGAACAA GTTGACTTTG 240 | | GTTTTTGAAT TCATGGACAA CGATTTAAAG AAATACATGG ATTCCCGCAC CGTGGGCAAC 300 | | ACACCAAGAG GGCTAGAACT AAACTTGGTT AAATACTTCC AGTGGCAACT ACTGCAAGGG 360 | | CTGGCCTTTT GCCATGAAAA CAAGATTCTC CACCGTGATT TAAAACCTCA AAACCTATTA 420 | | ATCAACAAGA GAGGCCAGTT GAAATTGGGT GATTTCGGTC TGGCCCGTGC TTTCGGTATT 480 | | CCGGTCAACA CATTTTCAAG CGAAGTCGTA ACGTTGTGGT ACCGTGCTCC TGATGTGCTA 540 | | ATGGGTTCTA GGACGTACTC CACATCCATT GATATATGGT CGTGTGGGTG CATTCTTGCG 600 | | GAAATGATAA CGGGTAAGCC TTTGTTTCCT GGCACCAACG ACGAAGAACA ACTGAAATTG 660 | | ATCTTCGACA TCATGGGCAC TCCTAATGAG TCCCTATGGC CCAGTGTAAC AAAGTTACCC 720 | | AAATACAACC CAAATATCCA GCAACGACCA CCAAGAGACC TACGTCAAGT ATTGCAACCA 780 | | CACACCAAAG AACCGCTAGA CGGGAATCTC ATGGATTTCT TACACGGACT CTTGCAACTT 840 | | AATCCGGATA TGAGGCTGAG CGCCAAGCAG GCTCTGCATC ACCCTTGGTT TGCAGAGTAC 900 | | TACCACCACG CTTCATAA 918 |
|
| Domain Profile | S: 1 yeklekigeGtygkvykakdketgevvAlKkirlekekegvpitalrEisllkelkhkni 60 | +++lek+g+Gty++vyk+ +k+tg vAlK+++l++e eg p+ta+rEisl+kelkh+ni | Q: 7 FKQLEKLGNGTYATVYKGLNKTTGVYVALKEVKLDSE-EGTPSTAIREISLMKELKHENI 65 | 789*********************************9.9********************* |
| S: 61 vkLlevvakdkkklyLvfefleqdLkkllkkkkkk....klsleevkslllqlleglayl 116 | v+L++v++ +++kl+Lvfef+++dLkk++++ + +l+l+ vk + +qll+gla++ | Q: 66 VRLYDVIH-TENKLTLVFEFMDNDLKKYMDSRTVGntprGLELNLVKYFQWQLLQGLAFC 124 | ********.99*******************9988777889******************** |
| S: 117 HsnkilHRDlKpqNlLiskegklklaDfGlarafssplktytkevvTlwYraPelLlgak 176 | H+nkilHRDlKpqNlLi+k+g+lkl+DfGlaraf+ p++t+++evvTlwYraP++L+g++ | Q: 125 HENKILHRDLKPQNLLINKRGQLKLGDFGLARAFGIPVNTFSSEVVTLWYRAPDVLMGSR 184 | ************************************************************ |
| S: 177 eYstavDiWsvgcilaelltrkplfqgkseidqlerifkllgtpsekvwpevsklpeykk 236 | +Yst++DiWs+gcilae++t kplf+g+++ +ql+ if+++gtp+e+ wp+v+klp+y+ | Q: 185 TYSTSIDIWSCGCILAEMITGKPLFPGTNDEEQLKLIFDIMGTPNESLWPSVTKLPKYNP 244 | ************************************************************ |
| S: 237 sfpkkkkkklkekvkklke.....kaldllekllaldpkkRisakealqhkyf 284 | +++++++++l+++++ ++ + +d+l+ ll+l+p+ R+sak+al+h++f | Q: 245 NIQQRPPRDLRQVLQPHTKepldgNLMDFLHGLLQLNPDMRLSAKQALHHPWF 297 | *************9554432232267**************************9 |
|
Domain Sequence
(FASTA) | | FKQLEKLGNG TYATVYKGLN KTTGVYVALK EVKLDSEEGT PSTAIREISL MKELKHENIV 60 | | RLYDVIHTEN KLTLVFEFMD NDLKKYMDSR TVGNTPRGLE LNLVKYFQWQ LLQGLAFCHE 120 | | NKILHRDLKP QNLLINKRGQ LKLGDFGLAR AFGIPVNTFS SEVVTLWYRA PDVLMGSRTY 180 | | STSIDIWSCG CILAEMITGK PLFPGTNDEE QLKLIFDIMG TPNESLWPSV TKLPKYNPNI 240 | | QQRPPRDLRQ VLQPHTKEPL DGNLMDFLHG LLQLNPDMRL SAKQALHHPW F 291 |
|
| Keyword | 3D-structure; ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; Transferase. |
| Sequence Source | Ensembl |
| Orthology | |
| Gene Ontology | | GO:0000307 | ; C:cyclin-dependent protein kinase holoenzyme complex | | GO:0005737 | ; C:cytoplasm | | GO:0005634 | ; C:nucleus | | GO:0005524 | ; F:ATP binding | | GO:0004693 | ; F:cyclin-dependent protein kinase activity | | GO:0031505 | ; P:fungal-type cell wall organization | | GO:0050849 | ; P:negative regulation of calcium-mediated signaling | | GO:0045719 | ; P:negative regulation of glycogen biosynthetic process | | GO:0016242 | ; P:negative regulation of macroautophagy | | GO:0045936 | ; P:negative regulation of phosphate metabolic process | | GO:0043433 | ; P:negative regulation of sequence-specific DNA binding transcription factor activity | | GO:0000122 | ; P:negative regulation of transcription from RNA polymerase II promoter | | GO:0016239 | ; P:positive regulation of macroautophagy | | GO:0032878 | ; P:regulation of establishment or maintenance of cell polarity | | GO:0032880 | ; P:regulation of protein localization | | GO:0031647 | ; P:regulation of protein stability | | GO:0000083 | ; P:regulation of transcription involved in G1/S phase of mitotic cell cycle | | GO:0006974 | ; P:response to DNA damage stimulus |
|
| KEGG | |
| InterPros | |
| Pfam | |
| SMARTs | |
| Prosites | |
| Prints | |
| Created Date | 20-Feb-2013 |