CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004723
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein kinase YPK2/YKR2 
Protein Synonyms/Alias
  
Gene Name
 YPK2 
Gene Synonyms/Alias
 YKR2; YMR104C; YM9718.03C 
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
94GIGNDNSKASERKASubiquitination[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
 May act as a downstream kinase in the sphingolipid- mediated signaling pathway. Plays an essential role in the proliferation of yeast cells. Involved in a signaling pathway, required for optimal cell wall integrity, that acts in parallel with the PKC1-SLT2-dependent pathway. A substrate of TOR complex 2 (TORC2) and required for TORC2 to regulate spatial aspects of cell growth. Phosphorylation of residue Thr-501 is indispensable for function. 
Sequence Annotation
 DOMAIN 344 599 Protein kinase.
 DOMAIN 600 670 AGC-kinase C-terminal.
 NP_BIND 350 358 ATP (By similarity).
 ACT_SITE 467 467 Proton acceptor (By similarity).
 BINDING 373 373 ATP (By similarity).
 MOD_RES 63 63 Phosphothreonine.
 MOD_RES 72 72 Phosphoserine.
 MOD_RES 499 499 Phosphothreonine.
 MOD_RES 501 501 Phosphothreonine; by PKH2.
 MOD_RES 641 641 Phosphoserine; by TOR2.
 MOD_RES 650 650 Phosphoserine.
 MOD_RES 659 659 Phosphothreonine; by TOR2.
 MOD_RES 669 669 Phosphoserine.  
Keyword
 ATP-binding; Cell shape; Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 677 AA 
Protein Sequence
MHSWRISKFK LGRSKEDDGS SEDENEKSWG NGLFHFHHGE KHHDGSPKNH NHEHEHHIRK 60
INTNETLPSS LSSPKLRNDA SFKNPSGIGN DNSKASERKA SQSSTETQGP SSESGLMTVK 120
VYSGKDFTLP FPITSNSTIL QKLLSSGILT SSSNDASEVA AIMRQLPRYK RVDQDSAGEG 180
LIDRAFATKF IPSSILLPGS TNSSPLLYFT IEFDNSITTI SPDMGTMEQP VFNKISTFDV 240
TRKLRFLKID VFARIPSLLL PSKNWQQEIG EQDEVLKEIL KKINTNQDIH LDSFHLPLNL 300
KIDSAAQIRL YNHHWISLER GYGKLNITVD YKPSKNKPLS IDDFDLLKVI GKGSFGKVMQ 360
VRKKDTQKIY ALKALRKAYI VSKCEVTHTL AERTVLARVD CPFIVPLKFS FQSPEKLYLV 420
LAFINGGELF YHLQHEGRFS LARSRFYIAE LLCALDSLHK LDVIYRDLKP ENILLDYQGH 480
IALCDFGLCK LNMKDNDKTD TFCGTPEYLA PEILLGQGYT KTVDWWTLGI LLYEMMTGLP 540
PYYDENVPVM YKKILQQPLL FPDGFDPAAK DLLIGLLSRD PSRRLGVNGT DEIRNHPFFK 600
DISWKKLLLK GYIPPYKPIV KSEIDTANFD QEFTKEKPID SVVDEYLSAS IQKQFGGWTY 660
IGDEQLGDSP SQGRSIS 677 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004672; F:protein kinase activity; ISS:SGD.
 GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
 GO:0070941; P:eisosome assembly; IGI:SGD.
 GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. 
Interpro
 IPR000961; AGC-kinase_C.
 IPR011009; Kinase-like_dom.
 IPR017892; Pkinase_C.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 IPR002290; Ser/Thr_dual-sp_kinase_dom.
 IPR008271; Ser/Thr_kinase_AS. 
Pfam
 PF00069; Pkinase
 PF00433; Pkinase_C 
SMART
 SM00133; S_TK_X
 SM00220; S_TKc 
PROSITE
 PS51285; AGC_KINASE_CTER
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST 
PRINTS