Q7YQL3

SS
Gene name
PAK3
Protein name
Serine/threonine-protein kinase PAK 3
Names
Beta-PAK, p21-activated kinase 3, PAK-3
Species
Pongo pygmaeus (Bornean orangutan)
KEGG Pathway
EC number
2.7.11.1: Protein-serine/threonine kinases
Protein Class

Descriptions

The p21-activated kinases (PAKs) controls cytoskeletal actin assembly and activate MAP-kinase pathways. In a study with PAK1, the kinase domain in the C terminus of PAK1 is inhibited by the IS domain via the C lobe, in which the kinase inhibitory segment hinders a part of the kinase domain and stabilizes a disabled catalytic site.

Autoinhibitory domains (AIDs)

65-161 (IS domain) SS

Target domain

283-534 (Protein kinase domain)

Relief mechanism

Partner binding

Assay

Accessory elements

419-442 (Activation loop from InterPro)

Target domain

283-534 (Protein kinase domain)

Relief mechanism

Assay

References

Autoinhibited structure

Activated structure

1 structures for Q7YQL3

Entry ID Method Resolution Chain Position Source
AF-Q7YQL3-F1 Predicted AlphaFoldDB

No variants for Q7YQL3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q7YQL3

No associated diseases with Q7YQL3

4 regional properties for Q7YQL3

Type Name Position InterPro Accession
domain CRIB domain 69 - 141 IPR000095
domain Protein kinase domain 283 - 534 IPR000719
active_site Serine/threonine-protein kinase, active site 398 - 410 IPR008271
binding_site Protein kinase, ATP binding site 289 - 312 IPR017441

Functions

Description
EC Number 2.7.11.1 Protein-serine/threonine kinases
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

6 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
MAP kinase kinase activity Catalysis of the concomitant phosphorylation of threonine (T) and tyrosine (Y) residues in a Thr-Glu-Tyr (TEY) thiolester sequence in a MAP kinase (MAPK) substrate.
metal ion binding Binding to a metal ion.
protein serine kinase activity Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate.
protein serine/threonine kinase activity Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate.
SH3 domain binding Binding to a SH3 domain (Src homology 3) of a protein, small protein modules containing approximately 50 amino acid residues found in a great variety of intracellular or membrane-associated proteins.

4 GO annotations of biological process

Name Definition
axonogenesis De novo generation of a long process of a neuron, including the terminal branched region. Refers to the morphogenesis or creation of shape or form of the developing axon, which carries efferent (outgoing) action potentials from the cell body towards target cells.
dendrite development The process whose specific outcome is the progression of the dendrite over time, from its formation to the mature structure.
dendritic spine morphogenesis The process in which the anatomical structures of a dendritic spine are generated and organized. A dendritic spine is a protrusion from a dendrite and a specialized subcellular compartment involved in synaptic transmission.
regulation of actin filament polymerization Any process that modulates the frequency, rate or extent of the assembly of actin filaments by the addition of actin monomers to a filament.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSDGLDNEEK PPAPPLRMNS NNRDSSALNH SSKPLPMAPE EKNKKARLRS IFPGGGDKTN
70 80 90 100 110 120
KKKEKERPEI SLPSDFEHTI HVGFDAVTGE FTPDLYGSQM CPGKLPEGIP EQWARLLQTS
130 140 150 160 170 180
NITKLEQKKN PQAVLDVLKF YDSKETVNNQ KYMSFTSGDK SAHGYIAAHP SSTKTASEPP
190 200 210 220 230 240
LAPPVSEEED EEEEEEEDEN EPPPVIAPRP EHTKSIYTRS VVESIASPAV PNKEVTPPSA
250 260 270 280 290 300
ENANSSTLYR NTDRQRKKSK MTDEEILEKL RSIVSVGDPK KKYTRFEKIG QGASGTVYTA
310 320 330 340 350 360
LDIATGQEVA IKQMNLQQQP KKELIINEIL VMRENKNPNI VNYLDSYLVG DELWVVMEYL
370 380 390 400 410 420
AGGSLTDVVT ETCMDEGQIA AVCRECLQAL DFLHSNQVIH RDIKSDNILL GMDGSVKLTD
430 440 450 460 470 480
FGFCAQITPE QSKRSTMVGT PYWMAPEVVT RKAYGPKVDI WSLGIMAIEM VEGEPPYLNE
490 500 510 520 530 540
NPLRALYLIA TNGTPELQNP ERLSAVFRDF LNRCLEMDVD RRGSAKELLQ HPFLKLAKPL
550
SSLTPLIIAA KEAIKNSSR