UniProt Accession

 PAK3_HUMAN; O75914; A8K389; B1GX77; B1GX78; B1GX79; Q5JWX1; Q5JWX2; Q7Z2D6; Q7Z2E4; Q7Z3Z8; Q8WWK5; Q8WX23; Q9P0J8 

Genbank Protein ID

 AF068864; AF155651; AB102659; AB102251; AB102252; AB102253; AB102254; AB102255; AB102256; AB102257; AB102258; AB102259; AB102260; AB102261; AB102262; AB102263; AB102264; AB102265; AB102266; AB102267; AB102268; AB102269; AB102270; AB102281; AB102282; AB102283; AB102284; AB102285; AB102286; AB102287; AB102288; AB102289; AB102290; AB102291; AB102292; AB102293; AB102294; AB102295; AB102296; AB102297; AB102298; AB102299; AB102300; AM943850; AM943851; AM943852; AK290504; AL356578; AL357774; AL031117; AL117326; AL357774; AL031117; AL117326; AL031117; AL117326; AL357774; AL031117; AL117326; AL357774; AL117326; AL031117; AL357774; AL117326; AL031117; AL357774; CH471120 

Genbank Nucleotide ID

 AAC36097.1; AAF67008.1; BAC81128.1; BAC80750.1; BAC80751.1; BAC80752.1; BAC80753.1; BAC80754.1; BAC80755.1; BAC80756.1; BAC80757.1; BAC80758.1; BAC80759.1; BAC80760.1; BAC80761.1; BAC80762.1; BAC80763.1; BAC80764.1; BAC80765.1; BAC80766.1; BAC80767.1; BAC80768.1; BAC80769.1; BAC80780.1; BAC80781.1; BAC80782.1; BAC80783.1; BAC80784.1; BAC80785.1; BAC80786.1; BAC80787.1; BAC80788.1; BAC80789.1; BAC80790.1; BAC80791.1; BAC80792.1; BAC80793.1; BAC80794.1; BAC80795.1; BAC80796.1; BAC80797.1; BAC80798.1; BAC80799.1; CAQ16016.1; CAQ16017.1; CAQ16018.1; BAF83193.1; CAI40843.1; CAI40843.1; CAI40843.1; CAI40844.1; CAI40844.1; CAI40844.1; CAI43157.1; CAI43157.1; CAI43157.1; CAI43158.1; CAI43158.1; CAI43158.1; CAI43167.1; CAI43167.1; CAI43167.1; CAI43168.1; CAI43168.1; CAI43168.1; EAX02654.1 

Protein Name

 Serine/threonine-protein kinase PAK 3 

Protein Synonyms/Alias

 Beta-PAK; Oligophrenin-3; p21-activated kinase 3; PAK-3 

Gene Name

 PAK3 

Gene Synonyms/Alias

 OPHN3 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
433	QITPEQSKRSTMVGT	ubiquitination	[1]
526	VDRRGSAKELLQHPF	ubiquitination	[1, 2, 3]
535	LLQHPFLKLAKPLSS	acetylation	[4]
535	LLQHPFLKLAKPLSS	ubiquitination	[5]

Reference

 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473] 

Functional Description

 Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, or cell cycle regulation. Plays a role in dendrite spine morphogenesis as well as synapse formation and plasticity. Acts as downstream effector of the small GTPases CDC42 and RAC1. Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration. Additionally, phosphorylates TNNI3/troponin I to modulate calcium sensitivity and relaxation kinetics of thin myofilaments. 

Sequence Annotation

 DOMAIN 70 83 CRIB.
 DOMAIN 283 534 Protein kinase.
 NP_BIND 289 297 ATP (By similarity).
 REGION 65 150 Autoregulatory region (By similarity).
 REGION 65 123 GTPase-binding (By similarity).
 REGION 84 282 Linker.
 ACT_SITE 402 402 Proton acceptor (By similarity).
 BINDING 312 312 ATP (By similarity).
 MOD_RES 50 50 Phosphoserine; by autocatalysis (By
 MOD_RES 154 154 Phosphoserine; by autocatalysis (By
 MOD_RES 436 436 Phosphothreonine; by autocatalysis (By  

Keyword

 Allosteric enzyme; Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; Developmental protein; Disease mutation; Kinase; Magnesium; Mental retardation; Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; SH3-binding; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 559 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004708; F:MAP kinase kinase activity; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
 GO:0007409; P:axonogenesis; ISS:UniProtKB.
 GO:0060997; P:dendritic spine morphogenesis; TAS:UniProtKB.
 GO:0030833; P:regulation of actin filament polymerization; IDA:UniProtKB.
 GO:0050808; P:synapse organization; TAS:UniProtKB. 

Interpro

 IPR011009; Kinase-like_dom.
 IPR000095; PAK_box_Rho-bd.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 IPR002290; Ser/Thr_dual-sp_kinase_dom.
 IPR008271; Ser/Thr_kinase_AS. 

Pfam

 PF00786; PBD
 PF00069; Pkinase 

SMART

 SM00285; PBD
 SM00220; S_TKc 

PROSITE

 PS50108; CRIB
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST 

PRINTS