Identification |
BMDB Protein ID
| BMDBP01142 |
Secondary Accession Numbers
| None |
Name
| Serine/threonine-protein kinase PAK 1 |
Synonyms
|
Not Available
|
Gene Name
| PAK1 |
Protein Type
| Enzyme |
Biological Properties |
General Function
| Involved in ATP binding |
Specific Function
| Protein kinase involved in intracellular signaling pathways downstream of integrins and receptor-type kinases that plays an important role in cytoskeleton dynamics, in cell adhesion, migration, proliferation, apoptosis, mitosis, and in vesicle-mediated transport processes. Can directly phosphorylate BAD and protects cells against apoptosis. Activated by interaction with CDC42 and RAC1. Functions as GTPase effector that links the Rho-related GTPases CDC42 and RAC1 to the JNK MAP kinase pathway. Phosphorylates and activates MAP2K1, and thereby mediates activation of downstream MAP kinases. Involved in the reorganization of the actin cytoskeleton, actin stress fibers and of focal adhesion complexes. Phosphorylates the tubulin chaperone TBCB and thereby plays a role in the regulation of microtubule biogenesis and organization of the tubulin cytoskeleton. Plays a role in the regulation of insulin secretion in response to elevated glucose levels. Part of a ternary complex that contains PAK1, DVL1 and MUSK that is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ). Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2. Phosphorylates MYL9/MLC2. Phosphorylates RAF1 at 'Ser-338' and 'Ser-339' resulting in: activation of RAF1, stimulation of RAF1 translocation to mitochondria, phosphorylation of BAD by RAF1, and RAF1 binding to BCL2. Phosphorylates SNAI1 at 'Ser-246' promoting its transcriptional repressor activity by increasing its accumulation in the nucleus. In podocytes, promotes NR3C2 nuclear localization. Required for atypical chemokine receptor ACKR2-induced phosphorylation of LIMK1 and cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3, maybe through CFL1 phosphorylation and inactivation. Plays a role in RUFY3-mediated facilitating gastric cancer cells migration and invasion. In response to DNA damage, phosphorylates MORC2 which activates its ATPase activity and facilitates chromatin remodeling (By similarity). |
Pathways
|
- FAS signaling pathway ( CD95 )
- Intracellular Signalling Through Adenosine Receptor A2a and Adenosine
- Intracellular Signalling Through Adenosine Receptor A2b and Adenosine
- NF-kB Signaling Pathway
- Rac 1 cell motility signaling pathway
- Rac 1 Cell Motility Signaling Pathway
|
Reactions
|
Mitogen-activated protein kinase kinase kinase 1 → Mitogen-activated protein kinase kinase kinase 1 + Hydrogen phosphate |
details
|
Dual specificity mitogen-activated protein kinase kinase 6 → Dual specificity mitogen-activated protein kinase kinase 6 + Hydrogen phosphate |
details
|
|
GO Classification
|
Not Available
|
Cellular Location
|
Not Available
|
Gene Properties |
Chromosome Location
| 29 |
Locus
| Not Available |
SNPs
| PAK1 |
Gene Sequence
|
>1635 bp
ATGTCAAATAACGGCCTAGACATTCAAGACAAACCTCCAGCCCCTCCGATGAGAAATACC
AGCACTATGATTGGAGCTGGCAGCAAAGACGCTGGAACCCTAAACCACGGTTCCAAACCT
CTGCCACCAAACCCAGAGGAAAAGAAAAAAAAGGACCGATTTTACCGAGCCATCTTACCT
GGAGATAAAACAAATAAAAAGAAGGAGAAGGAACGGCCAGAGATTTCTCTTCCTTCAGAT
TTTGAGCACACGATTCATGTTGGTTTTGATGCTGTCACAGGCGAGTTTACAGGGATGCCA
GAGCAATGGGCCCGCTTGCTTCAGACATCAAATATCACTAAGTCGGAGCAGAAGAAAAAC
CCGCAGGCTGTTCTGGATGTGTTGGAATTTTATAACTCAAAGAAGACCTCCAACAGCCAG
AAGTATATGAGCTTTACAGATAAATCAGCTGAGGATTATAATTCTTCTAACACTTTGAAT
GTGAAGGCGGTGTCTGAGACCCCTGCAGTGCCACCAGTTTCAGAAGATGAAGATGATGAT
GATGATGGCACCCCACCCCCAGTGATTGCTCCACGCCCAGAGCACACAAAATCTGTATAC
ACACGGTCTGTGATTGAACCACTTCCTATTACTCCAACTCGGGATGTGGCTACATCTCCC
ATTTCACCTACTGAGAATAATACCACTCCACCTGATGCTCTGACTCGGAATACTGAGAAG
CAGAAGAAGAAGCCTAAGATGTCTGATGAGGAGATCTTGGAGAAATTACGCAGCATAGTG
AGTGTGGGTGATCCTAAGAAGAAATACACACGGTTTGAGAAGATTGGACAAGGTGCTTCG
GGCACTGTGTACACTGCAATGGATGTAGCCACAGGACAGGAGGTGGCCATTAAGCAGATG
AACCTTCAGCAGCAGCCGAAGAAAGAGCTGATTATTAATGAGATCCTGGTCATGAGGGAA
AACAAGAACCCAAATATTGTGAACTACTTGGACAGTTACCTTGTGGGAGATGAGCTATGG
GTTGTCATGGAATATTTGGCTGGAGGTTCTTTGACAGACGTGGTAACAGAAACTTGCATG
GACGAAGGTCAGATTGCAGCTGTGTGCCGTGAGTGCCTGCAAGCTTTGGAGTTTCTGCAT
TCGAACCAAGTTATTCATAGAGACATCAAGAGTGACAACATCCTGTTGGGAATGGATGGC
TCTGTCAAGTTAACTGATTTTGGATTTTGTGCTCAGATCACCCCAGAGCAGAGCAAACGG
AGCACCATGGTGGGAACACCGTACTGGATGGCACCAGAGGTTGTAACCCGGAAAGCCTAT
GGGCCTAAGGTTGACATTTGGTCCTTGGGCATCATGGCCATTGAAATGATTGAAGGGGAG
CCCCCATACCTCAACGAAAACCCTCTGAGAGCCTTGTACCTCATTGCCACCAATGGGACC
CCAGAGCTTCAGAACCCAGAGAAGCTGTCAGCTATCTTCCGAGACTTTCTGAACCGCTGT
CTTGAGATGGATGTGGAGAAGAGAGGTTCGGCTAAAGAACTGCTGCAGCATCAATTTCTG
AAGATTGCCAAGCCTCTCTCCAGCCTCACTCCACTGATTGCTGCTGCAAAGGAAGCAACC
AAGAACAATCACTAA
|
Protein Properties |
Number of Residues
| 544 |
Molecular Weight
| 60546.0 |
Theoretical pI
| 5.61 |
Pfam Domain Function
|
Not Available |
Signals
|
|
Transmembrane Regions
|
Not Available
|
Protein Sequence
|
>Serine/threonine-protein kinase PAK 1
MSNNGLDIQDKPPAPPMRNTSTMIGAGSKDAGTLNHGSKPLPPNPEEKKKKDRFYRAILP
GDKTNKKKEKERPEISLPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKSEQKKN
PQAVLDVLEFYNSKKTSNSQKYMSFTDKSAEDYNSSNTLNVKAVSETPAVPPVSEDEDDD
DDGTPPPVIAPRPEHTKSVYTRSVIEPLPITPTRDVATSPISPTENNTTPPDALTRNTEK
QKKKPKMSDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQM
NLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCM
DEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKR
STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGT
PELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAAKEAT
KNNH
|
External Links |
GenBank ID Protein
| AAI23417.1 |
UniProtKB/Swiss-Prot ID
| Q08E52 |
UniProtKB/Swiss-Prot Entry Name
| PAK1_BOVIN |
PDB IDs
|
|
GenBank Gene ID
| BC123416 |
GeneCard ID
| PAK1 |
GenAtlas ID
| Not Available |
HGNC ID
| Not Available |
References |
General References
| Not Available |