Tag |
Content |
dbPAF ID |
dbPAF-0052732 |
Uniprot Accession |
G5EGQ3; MAX2_CAEEL; G5EGS0; H2KMK1; Q9XWL8; |
Genbank Protein ID |
NP_001076635.1; NP_001076636.1; NP_001122655.1; NP_001254363.1; |
Genbank Nucleotide ID |
NM_001083166.2; NM_001083167.1; NM_001129183.2; NM_001267434.1; |
Protein Name |
Serine/threonine-protein kinase max-2 |
Protein Synonyms/Alias |
Motor axon guidance protein 2;p21-activated kinase; |
Gene Name |
max-2 |
Gene Synonyms/Alias |
Y38F1A.10; |
Organism |
Caenorhabditis elegans |
NCBI Taxa ID |
6239 |
Functional Description (View all) |
Serine/threonine-protein kinase, which phosphorylates mlk-1. Involved in the stress response to heavy metals by activating the mlk-1/mek-1/kgb-1 pathway (PubMed:20008556). In ventral cord commissural motoneurons, required for dorsal axon guidance downstream of unc-6/netrin repulsion receptor unc-5 and probably of Rho GTPases ced-10 and mig-2. Plays a redundant role with mig-10 in orientating axonal growth of HSN neurons (PubMed:18499456). Plays a redundant role with pak-1 in P neuroblast migration and in distal tip cell (DTC)-mediated guidance of gonad elongation probably downstream of Rho GTPases (PubMed:17050621, PubMed:19023419, PubMed:23390595). In association with pak-2, plays a role in embryogenesis. In association with pak-1, may be involved in spermatogenesis (PubMed:23390595).Functional Description
Serine/threonine-protein kinase, which phosphorylates mlk-1. Involved in the stress response to heavy metals by activating the mlk-1/mek-1/kgb-1 pathway (PubMed:20008556). In ventral cord commissural motoneurons, required for dorsal axon guidance downstream of unc-6/netrin repulsion receptor unc-5 and probably of Rho GTPases ced-10 and mig-2. Plays a redundant role with mig-10 in orientating axonal growth of HSN neurons (PubMed:18499456). Plays a redundant role with pak-1 in P neuroblast migration and in distal tip cell (DTC)-mediated guidance of gonad elongation probably downstream of Rho GTPases (PubMed:17050621, PubMed:19023419, PubMed:23390595). In association with pak-2, plays a role in embryogenesis. In association with pak-1, may be involved in spermatogenesis (PubMed:23390595).
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Phosphorylation Sites
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dbPAF PTMs: 3 Position | Peptides | Source | References ( PMIDs ) |
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145 | CSNGSATSPSTSVSA | PhosphoPep 2.0 | 19060867 | 187 | SERNNVPSPAPVPYS | PhosphoPep 2.0 | 19060867 | 196 | APVPYSESAPQLKTF | PhosphoPep 2.0 | 19060867 |
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Sequence (Fasta) | MSTSKSSKVR IRNFIGRIFS PSDKDKDRDD EMKPSSSAMD ISQPYNTVHR VHVGYDGQKF 60 SGLPQPWMDI LLRDISLADQ KKDPNAVVTA LKFYAQSMKE NEKTKFMTTN SVFTNSDDDD 120 VDVQLTGQVT EHLRNLQCSN GSATSPSTSV SASSSSARPL TNGNNHLSTA SSTDTSLSLS 180 ERNNVPSPAP VPYSESAPQL KTFTGETPKL HPRSPFPPQP PVLPQRSKTA SAVATTTTNP 240 TTSNGAPPPV PGSKGPPVPP KPSHLKIASS TVSSGCSSPQ QYSSARSVGN SLSNGSVVST 300 TSSDGDVQLS NKENSNDKSV GDKNGNTTTN KTTVEPPPPE EPPVRVRASH REKLSDSEVL 360 NQLREIVNPS NPLGKYEMKK QIGVGASGTV FVANVAGSTD VVAVKRMAFK TQPKKEMLLT 420 EIKVMKQYRH PNLVNYIESY LVDADDLWVV MDYLEGGNLT DVVVKTELDE GQIAAVLQEC 480 LKALHFLHRH SIVHRDIKSD NVLLGMNGEV KLTDMGFCAQ IQPGSKRDTV VGTPYWMSPE 540 ILNKKQYNYK VDIWSLGIMA LEMIDGEPPY LRETPLKAIY LIAQNGKPEI KQRDRLSSEF 600 NNFLDKCLVV DPDQRADTTE LLAHPFLKKA KPLSSLIPYI RAVREK
647Fasta Sequence
>G5EGQ3|max-2|Caenorhabditis elegans MSTSKSSKVRIRNFIGRIFSPSDKDKDRDDEMKPSSSAMDISQPYNTVHRVHVGYDGQKFSGLPQPWMDILLRDISLADQKKDPNAVVTALKFYAQSMKENEKTKFMTTNSVFTNSDDDDVDVQLTGQVTEHLRNLQCSNGSATSPSTSVSASSSSARPLTNGNNHLSTASSTDTSLSLSERNNVPSPAPVPYSESAPQLKTFTGETPKLHPRSPFPPQPPVLPQRSKTASAVATTTTNPTTSNGAPPPVPGSKGPPVPPKPSHLKIASSTVSSGCSSPQQYSSARSVGNSLSNGSVVSTTSSDGDVQLSNKENSNDKSVGDKNGNTTTNKTTVEPPPPEEPPVRVRASHREKLSDSEVLNQLREIVNPSNPLGKYEMKKQIGVGASGTVFVANVAGSTDVVAVKRMAFKTQPKKEMLLTEIKVMKQYRHPNLVNYIESYLVDADDLWVVMDYLEGGNLTDVVVKTELDEGQIAAVLQECLKALHFLHRHSIVHRDIKSDNVLLGMNGEVKLTDMGFCAQIQPGSKRDTVVGTPYWMSPEILNKKQYNYKVDIWSLGIMALEMIDGEPPYLRETPLKAIYLIAQNGKPEIKQRDRLSSEFNNFLDKCLVVDPDQRADTTELLAHPFLKKAKPLSSLIPYIRAVREK
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Keyword |
KW-0025--Alternative splicing KW-0067--ATP-binding KW-0966--Cell projection KW-0181--Complete proteome KW-0963--Cytoplasm KW-0221--Differentiation KW-0334--Gonadal differentiation KW-0418--Kinase KW-0460--Magnesium KW-0479--Metal-binding KW-0524--Neurogenesis KW-0547--Nucleotide-binding KW-1185--Reference proteome KW-0723--Serine/threonine-protein kinase KW-0346--Stress response KW-0808--Transferase
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Interpro |
IPR000095--CRIB_dom IPR011009--Kinase-like_dom IPR000719--Prot_kinase_dom IPR017441--Protein_kinase_ATP_BS IPR002290--Ser/Thr_dual-sp_kinase IPR008271--Ser/Thr_kinase_AS
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PROSITE |
PS50108--CRIB PS00107--PROTEIN_KINASE_ATP PS50011--PROTEIN_KINASE_DOM PS00108--PROTEIN_KINASE_ST
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Pfam |
PF00786--PBD PF00069--Pkinase
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Gene Ontology |
GO:0005737--C:cytoplasm GO:0030425--C:dendrite GO:0043204--C:perikaryon GO:0005524--F:ATP binding GO:0046872--F:metal ion binding GO:0031435--F:mitogen-activated protein kinase kinase kinase binding GO:0004674--F:protein serine/threonine kinase activity GO:0048365--F:Rac GTPase binding GO:0030036--P:actin cytoskeleton organization GO:0007257--P:activation of JUN kinase activity GO:0030154--P:cell differentiation GO:0035262--P:gonad morphogenesis GO:0007506--P:gonadal mesoderm development GO:0040039--P:inductive cell migration GO:0007254--P:JNK cascade GO:0007399--P:nervous system development GO:0006468--P:protein phosphorylation GO:0042981--P:regulation of apoptotic process GO:0007346--P:regulation of mitotic cell cycle GO:0046688--P:response to copper ion GO:0007266--P:Rho protein signal transduction
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