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Kinase suppressor of Ras B

 KSRB_CAEEL              Reviewed;         550 AA.
G5EDA5; B3KYC3; G5EEY7;
14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
14-DEC-2011, sequence version 1.
20-JUN-2018, entry version 62.
RecName: Full=Kinase suppressor of Ras B {ECO:0000305};
Name=ksr-2 {ECO:0000312|WormBase:F58D5.4a};
ORFNames=F58D5.4 {ECO:0000312|WormBase:F58D5.4a};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
[1] {ECO:0000312|EMBL:AAL79358.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, AND
DISRUPTION PHENOTYPE.
PubMed=11882296; DOI=10.1016/S0960-9822(02)00690-5;
Ohmachi M., Rocheleau C.E., Church D., Lambie E., Schedl T.,
Sundaram M.V.;
"C. elegans ksr-1 and ksr-2 have both unique and redundant functions
and are required for MPK-1 ERK phosphorylation.";
Curr. Biol. 12:427-433(2002).
[2] {ECO:0000312|Proteomes:UP000001940}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3] {ECO:0000305}
FUNCTION, AND INTERACTION WITH NDK-1.
PubMed=23900546; DOI=10.1242/dev.094011;
Masoudi N., Fancsalszky L., Pourkarimi E., Vellai T., Alexa A.,
Remenyi A., Gartner A., Mehta A., Takacs-Vellai K.;
"The NM23-H1/H2 homolog NDK-1 is required for full activation of Ras
signaling in C. elegans.";
Development 140:3486-3495(2013).
-!- FUNCTION: Probable inactive protein kinase which positively
regulates Ras-mediated signaling probably acting at the level of
let-60/ras or/and lin-45/raf. In the germline, regulates meiotic
progression during oogenesis and mpk-1 (isoform b)
phosphorylation. Functions redundantly with ksr-1 in the Ras-
mediated regulation of larval survival, the development of
excretory canal, in determining vulval precursor cell fate during
vulval induction and in mpk-1 phosphorylation in somatic cells.
{ECO:0000269|PubMed:11882296, ECO:0000269|PubMed:23900546}.
-!- SUBUNIT: Interacts with ndk-1. {ECO:0000269|PubMed:23900546}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=a {ECO:0000312|WormBase:F58D5.4a};
IsoId=G5EDA5-1; Sequence=Displayed;
Name=b {ECO:0000312|WormBase:F58D5.4b};
IsoId=G5EDA5-2; Sequence=VSP_057950, VSP_057951;
Name=c {ECO:0000312|WormBase:F58D5.4c};
IsoId=G5EDA5-3; Sequence=VSP_057949;
Note=No experimental confirmation available. {ECO:0000305};
-!- DOMAIN: The protein kinase domain is predicted to be catalytically
inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes sterility
characterized by a lack of oocytes. In a ksr-1 n2526 mutant
background, causes larval lethality.
{ECO:0000269|PubMed:11882296}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. {ECO:0000305}.
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EMBL; AY077614; AAL79358.1; -; mRNA.
EMBL; AY077615; AAL79359.1; -; mRNA.
EMBL; BX284601; CAB70239.2; -; Genomic_DNA.
EMBL; BX284601; CAB70240.2; -; Genomic_DNA.
EMBL; BX284601; CAQ76483.1; -; Genomic_DNA.
RefSeq; NP_001021518.1; NM_001026347.2. [G5EDA5-1]
RefSeq; NP_001021519.1; NM_001026348.2. [G5EDA5-2]
RefSeq; NP_001129779.1; NM_001136307.2. [G5EDA5-3]
UniGene; Cel.181; -.
ProteinModelPortal; G5EDA5; -.
STRING; 6239.F58D5.4a; -.
PaxDb; G5EDA5; -.
EnsemblMetazoa; F58D5.4a; F58D5.4a; WBGene00002240. [G5EDA5-1]
GeneID; 173085; -.
KEGG; cel:CELE_F58D5.4; -.
CTD; 173085; -.
WormBase; F58D5.4a; CE31017; WBGene00002240; ksr-2. [G5EDA5-1]
WormBase; F58D5.4b; CE31018; WBGene00002240; ksr-2. [G5EDA5-2]
WormBase; F58D5.4c; CE42786; WBGene00002240; ksr-2. [G5EDA5-3]
eggNOG; KOG0193; Eukaryota.
eggNOG; ENOG410Y4UP; LUCA.
GeneTree; ENSGT00900000140880; -.
HOGENOM; HOG000020703; -.
OMA; QICQAMS; -.
OrthoDB; EOG091G02ZN; -.
PhylomeDB; G5EDA5; -.
PRO; PR:G5EDA5; -.
Proteomes; UP000001940; Chromosome I.
Bgee; WBGene00002240; -.
GO; GO:0005622; C:intracellular; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; IGI:WormBase.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
GO; GO:0051321; P:meiotic cell cycle; IMP:WormBase.
GO; GO:0002119; P:nematode larval development; IGI:WormBase.
GO; GO:0045138; P:nematode male tail tip morphogenesis; IGI:WormBase.
GO; GO:0040026; P:positive regulation of vulval development; IMP:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IGI:WormBase.
GO; GO:0007265; P:Ras protein signal transduction; IGI:WormBase.
GO; GO:0040025; P:vulval development; IGI:WormBase.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
Pfam; PF07714; Pkinase_Tyr; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Meiosis; Metal-binding;
Reference proteome; Zinc; Zinc-finger.
CHAIN 1 550 Kinase suppressor of Ras B.
{ECO:0000305}.
/FTId=PRO_0000434555.
DOMAIN 248 528 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ZN_FING 90 145 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
COMPBIAS 77 80 Poly-Pro. {ECO:0000255}.
VAR_SEQ 1 92 Missing (in isoform c). {ECO:0000305}.
/FTId=VSP_057949.
VAR_SEQ 9 12 Missing (in isoform b). {ECO:0000305}.
/FTId=VSP_057950.
VAR_SEQ 163 198 Missing (in isoform b). {ECO:0000305}.
/FTId=VSP_057951.
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


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