| Tag | Content |
|---|
| CPLM ID | CPLM-010845 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Serine/threonine-protein kinase BCK1/SLK1/SSP31 |
Protein Synonyms/Alias | |
Gene Name | BCK1 |
Gene Synonyms/Alias | LAS3; SLK1; SSP31; YJL095W; J0906 |
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 |
|---|
| 522 | PDCINPDKTVPVPVN | 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 | Serine/threonine protein kinase involved in a signal transduction pathway that play a role in yeast cell morphogenesis and cell growth. This pathway seems to start by SMP3; then involve the kinase PKC1 that may act on this kinase. BCK1 probably phosphorylates MKK1 and MKK2 which themselves phosphorylate the MPK1 kinase. |
Sequence Annotation | DOMAIN 1175 1440 Protein kinase.
NP_BIND 1181 1189 ATP (By similarity).
ACT_SITE 1303 1303 Proton acceptor (By similarity).
BINDING 1204 1204 ATP (By similarity).
MOD_RES 407 407 Phosphothreonine.
MOD_RES 411 411 Phosphoserine.
MOD_RES 491 491 Phosphoserine.
MOD_RES 747 747 Phosphoserine.
MOD_RES 816 816 Phosphoserine.
MOD_RES 1058 1058 Phosphoserine.
MOD_RES 1061 1061 Phosphoserine.
MOD_RES 1134 1134 Phosphoserine; by PKC (Potential). |
Keyword | ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1478 AA |
Protein Sequence | MPFLRKIAGT AHTHSRSDSN SSVKFGHQPT SSVASTKSSS KSPRATSRKS IYDDIRSQFP 60
NLTPNSTSSQ FYESTPVIEQ SFNWTTDDHI SAGTLENPTS FTNSSYKNDN GPSSLSDSRK 120
SSGGNSVNSL SFDKLILSWD PTDPDEWTMH RVTSWFKFHD FPESWILFFK KHQLFGHRFI 180
KLLAYDNFAV YEKYLPQTKT ASYTRFQQLL KKTMTKNVTN SHIRQKSASK LKSSRSSSES 240
IKSKLKNSKS QEDISNSRST SESALSPTKS GPSKTDEKNF LHSTSTHQKT KSASSLYRRS 300
FISLRGSSSS NASSAKSPSN IKLSIPARPH SIIESNSTLT KSASPPASPS YPSIFRRHHK 360
SSSSESSLLN SLFGSGIGEE APTKPNPQGH SLSSENLAKG KSKHYETNVS SPLKQSSLPT 420
SDDKGNLWNK FKRKSQIGVP SPNTVAYVTS QETPSLKSNS STATLTVQTA DVNIPSPSSS 480
PPPIPKTANR SLEVISTEDT PKISSTTASF KETYPDCINP DKTVPVPVNN QKYSVKNFLL 540
DQKFYPLKKT GLNDSENKYI LVTKDNVSFV PLNLKSVAKL SSFKESALTK LGINHKNVTF 600
HMTDFDCDIG AAIPDDTLEF LKKSLFLNTS GKIYIKDQMK LQQKPKPAPL TSENNVPLKS 660
VKSKSSMRSG TSSLIASTDD VSIVTSSSDI TSFDEHASGS GRRYPQTPSY YYDRVSNTNP 720
TEELNYWNIK EVLSHEENAP KMVFKTSPKL ELNLPDKGSK LNIPTPITEN ESKSSFQVLR 780
KDEGTEIDFN HRRESPYTKP ELAPKREAPK PPANTSPQRT LSTSKQNKPI RLVRASTKIS 840
RSKRSKPLPP QLLSSPIEAS SSSPDSLTSS YTPASTHVLI PQPYKGANDV MRRLKTDQDS 900
TSTSPSLKMK QKVNRSNSTV STSNSIFYSP SPLLKRGNSK RVVSSTSAAD IFEENDITFA 960
DAPPMFDSDD SDDDSSSSDD IIWSKKKTAP ETNNENKKDE KSDNSSTHSD EIFYDSQTQD 1020
KMERKMTFRP SPEVVYQNLE KFFPRANLDK PITEGIASPT SPKSLDSLLS PKNVASSRTE 1080
PSTPSRPVPP DSSYEFIQDG LNGKNKPLNQ AKTPKRTKTI RTIAHEASLA RKNSVKLKRQ 1140
NTKMWGTRMV EVTENHMVSI NKAKNSKGEY KEFAWMKGEM IGKGSFGAVY LCLNVTTGEM 1200
MAVKQVEVPK YSSQNEAILS TVEALRSEVS TLKDLDHLNI VQYLGFENKN NIYSLFLEYV 1260
AGGSVGSLIR MYGRFDEPLI KHLTTQVLKG LAYLHSKGIL HRDMKADNLL LDQDGICKIS 1320
DFGISRKSKD IYSNSDMTMR GTVFWMAPEM VDTKQGYSAK VDIWSLGCIV LEMFAGKRPW 1380
SNLEVVAAMF KIGKSKSAPP IPEDTLPLIS QIGRNFLDAC FEINPEKRPT ANELLSHPFS 1440
EVNETFNFKS TRLAKFIKSN DKLNSSKLRI TSQENKTE 1478 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:SGD. GO:0043332; C:mating projection tip; IDA:SGD. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0004709; F:MAP kinase kinase kinase activity; IGI:SGD. GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW. GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:SGD. GO:0030010; P:establishment of cell polarity; IMP:SGD. GO:0030242; P:peroxisome degradation; IMP:SGD. GO:0060237; P:regulation of fungal-type cell wall organization; IMP:SGD. GO:0001101; P:response to acid; IMP:SGD. GO:0007584; P:response to nutrient; IMP:SGD. |
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