KSRB_CAEEL
ID KSRB_CAEEL Reviewed; 550 AA.
AC G5EDA5; B3KYC3; G5EEY7;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Kinase suppressor of Ras B {ECO:0000305};
GN Name=ksr-2 {ECO:0000312|WormBase:F58D5.4a};
GN ORFNames=F58D5.4 {ECO:0000312|WormBase:F58D5.4a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:AAL79358.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=11882296; DOI=10.1016/s0960-9822(02)00690-5;
RA Ohmachi M., Rocheleau C.E., Church D., Lambie E., Schedl T., Sundaram M.V.;
RT "C. elegans ksr-1 and ksr-2 have both unique and redundant functions and
RT are required for MPK-1 ERK phosphorylation.";
RL Curr. Biol. 12:427-433(2002).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH NDK-1.
RX PubMed=23900546; DOI=10.1242/dev.094011;
RA Masoudi N., Fancsalszky L., Pourkarimi E., Vellai T., Alexa A., Remenyi A.,
RA Gartner A., Mehta A., Takacs-Vellai K.;
RT "The NM23-H1/H2 homolog NDK-1 is required for full activation of Ras
RT signaling in C. elegans.";
RL Development 140:3486-3495(2013).
RN [4]
RP FUNCTION.
RX PubMed=26510792; DOI=10.1534/genetics.115.177295;
RA Yin Y., Donlevy S., Smolikove S.;
RT "Coordination of Recombination with Meiotic Progression in the
RT Caenorhabditis elegans Germline by KIN-18, a TAO Kinase That Regulates the
RT Timing of MPK-1 Signaling.";
RL Genetics 202:45-59(2016).
CC -!- FUNCTION: Probable inactive protein kinase which positively regulates
CC Ras-mediated signaling probably acting at the level of let-60/ras
CC or/and lin-45/raf (PubMed:23900546, PubMed:11882296). In the germline,
CC regulates meiotic progression during oogenesis and mpk-1 (isoform b)
CC phosphorylation (PubMed:11882296, PubMed:26510792). Plays a role in
CC meiotic recombination events (PubMed:26510792). Functions redundantly
CC with ksr-1 in the Ras-mediated regulation of larval survival, the
CC development of excretory canal, in determining vulval precursor cell
CC fate during vulval induction and in mpk-1 phosphorylation in somatic
CC cells (PubMed:11882296). {ECO:0000269|PubMed:11882296,
CC ECO:0000269|PubMed:23900546, ECO:0000269|PubMed:26510792}.
CC -!- SUBUNIT: Interacts with ndk-1. {ECO:0000269|PubMed:23900546}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000312|WormBase:F58D5.4a};
CC IsoId=G5EDA5-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F58D5.4b};
CC IsoId=G5EDA5-2; Sequence=VSP_057950, VSP_057951;
CC Name=c {ECO:0000312|WormBase:F58D5.4c};
CC IsoId=G5EDA5-3; Sequence=VSP_057949;
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes sterility
CC characterized by a lack of oocytes. In a ksr-1 n2526 mutant background,
CC causes larval lethality. {ECO:0000269|PubMed:11882296}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY077614; AAL79358.1; -; mRNA.
DR EMBL; AY077615; AAL79359.1; -; mRNA.
DR EMBL; BX284601; CAB70239.2; -; Genomic_DNA.
DR EMBL; BX284601; CAB70240.2; -; Genomic_DNA.
DR EMBL; BX284601; CAQ76483.1; -; Genomic_DNA.
DR RefSeq; NP_001021518.1; NM_001026347.2. [G5EDA5-1]
DR RefSeq; NP_001021519.1; NM_001026348.2. [G5EDA5-2]
DR RefSeq; NP_001129779.1; NM_001136307.2. [G5EDA5-3]
DR AlphaFoldDB; G5EDA5; -.
DR SMR; G5EDA5; -.
DR STRING; 6239.F58D5.4a; -.
DR PaxDb; G5EDA5; -.
DR EnsemblMetazoa; F58D5.4a.1; F58D5.4a.1; WBGene00002240. [G5EDA5-1]
DR EnsemblMetazoa; F58D5.4b.1; F58D5.4b.1; WBGene00002240. [G5EDA5-2]
DR EnsemblMetazoa; F58D5.4c.1; F58D5.4c.1; WBGene00002240. [G5EDA5-3]
DR GeneID; 173085; -.
DR KEGG; cel:CELE_F58D5.4; -.
DR CTD; 173085; -.
DR WormBase; F58D5.4a; CE31017; WBGene00002240; ksr-2. [G5EDA5-1]
DR WormBase; F58D5.4b; CE31018; WBGene00002240; ksr-2. [G5EDA5-2]
DR WormBase; F58D5.4c; CE42786; WBGene00002240; ksr-2. [G5EDA5-3]
DR eggNOG; KOG0193; Eukaryota.
DR InParanoid; G5EDA5; -.
DR OMA; AHENPLF; -.
DR OrthoDB; 281487at2759; -.
DR PhylomeDB; G5EDA5; -.
DR Reactome; R-CEL-5674135; MAP2K and MAPK activation.
DR SignaLink; G5EDA5; -.
DR PRO; PR:G5EDA5; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00002240; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IGI:WormBase.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IGI:WormBase.
DR GO; GO:0045138; P:nematode male tail tip morphogenesis; IGI:WormBase.
DR GO; GO:0040026; P:positive regulation of vulval development; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IGI:WormBase.
DR GO; GO:0007265; P:Ras protein signal transduction; IGI:WormBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0040025; P:vulval development; IGI:WormBase.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Meiosis; Metal-binding; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..550
FT /note="Kinase suppressor of Ras B"
FT /evidence="ECO:0000305"
FT /id="PRO_0000434555"
FT DOMAIN 248..528
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ZN_FING 90..145
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 21..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..92
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_057949"
FT VAR_SEQ 9..12
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057950"
FT VAR_SEQ 163..198
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057951"
SQ SEQUENCE 550 AA; 62796 MW; 56DC2F02D2360720 CRC64;
MSDEKKKKRG FFRYSVLTTS SFSSWRRSST SGSISQSSRT TSKTTTSSSV TSSNPINAPP
PTATSSSSVL PSTSSEPPPP ASAPPRISIY HKMVPSKSKF RQCDVCEHIF IFDFVRKQHL
DDVYACNVCG IRVHKGCLDR VKNDCKITTQ YMGGILENAV IQSNKKQWEK PTTASISKSL
TTSPTCSTST TMSPAGVEKN VHKTRKLISM TTSTLDDVTT FNSEINEEMD EETVLMTWED
VTIKLTDVDV MTKIGDGRFG SVYFGGYHGN AAVRFVNMNY LSQEDRRADV FATEIVSAYK
NSRHDHIALF YGYVSDPVTN TYAIVTNFYQ HNTLYHRIHE QLSEDFDQSW TFQISLQICQ
AMSYLHKKKI LHRDLRTKNI LLDNPNRVVV TDFALMKLER LENPRRNCTL LIPNHWIDYL
SPEIAGNLMI DWRGDVLFQH ELPFSQESDV YSFGTIFFEL LLRRMPTGCD SWDQKLYAKM
CGQKAALQRL DAQLQKIDGK LHELLLECWS SQPEKRPSFQ QIVKRITVQM PRKESNKQKR
RSTAHENPLF
