O75914 (PAK3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase PAK 3
EC=2.7.11.1

Alternative name(s):
Beta-PAK
Oligophrenin-3
p21-activated kinase 3
Short name=PAK-3

Gene names

Name:	PAK3
Synonyms:	OPHN3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	559 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.11
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium By similarity.
Enzyme regulation	Activated by binding small G proteins. Binding of GTP-bound CDC42 or RAC1 to the autoregulatory region releases monomers from the autoinhibited dimer, enables phosphorylation of Thr-436 and allows the kinase domain to adopt an active structure By similarity.
Subunit structure	Interacts tightly with GTP-bound but not GDP-bound CDC42/p21 and RAC1. Shows highly specific binding to the SH3 domains of phospholipase C-gamma and of adapter protein NCK. Interacts with the C-terminal of APP By similarity. Interacts with ARHGEF6 and ARHGEF7. Ref.9
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Restricted to the nervous system. Highly expressed in postmitotic neurons of the developing and postnatal cerebral cortex and hippocampus. Ref.10
Post-translational modification	Autophosphorylated when activated by CDC42/p21. Ref.8
Involvement in disease	Mental retardation, X-linked 30 (MRX30) [MIM:300558]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.13 Ref.14
Sequence similarities	Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily. Contains 1 CRIB domain. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Mental retardation
Domain	SH3-binding
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	axonogenesis Inferred from sequence or structural similarity. Source: UniProtKB dendritic spine morphogenesis Traceable author statement Ref.12. Source: UniProtKB regulation of actin filament polymerization Inferred from direct assay Ref.11. Source: UniProtKB synapse organization Traceable author statement Ref.12. Source: UniProtKB
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase kinase activity Inferred from direct assay Ref.11. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC42	P60953-2	2	EBI-3389553,EBI-287394
RAC1	P63000	2	EBI-3389553,EBI-413628

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O75914-1)

Also known as: PAK3b;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O75914-2)

The sequence of this isoform differs from the canonical sequence as follows:
     93-107: Missing.

Isoform 3 (identifier: O75914-3)

Also known as: PAK3cb;

The sequence of this isoform differs from the canonical sequence as follows:
     92-92: T → TNSPFQTSRPVTVASSQSEGKM

Isoform 4 (identifier: O75914-4)

Also known as: PAK3c;

The sequence of this isoform differs from the canonical sequence as follows:
     92-107: TPDLYGSQMCPGKLPE → TNSPFQTSRPVTVASSQSEGKM

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 559	559	Serine/threonine-protein kinase PAK 3		PRO_0000086469
Regions
	Domain	70 – 83	14	CRIB
	Domain	283 – 534	252	Protein kinase
	Nucleotide binding	289 – 297	9	ATP By similarity
	Region	65 – 150	86	Autoregulatory region By similarity
	Region	65 – 123	59	GTPase-binding By similarity
	Region	84 – 282	199	Linker
	Compositional bias	187 – 201	15	Poly-Glu
Sites
	Active site	402	1	Proton acceptor By similarity
	Binding site	312	1	ATP By similarity
Amino acid modifications
	Modified residue	50	1	Phosphoserine; by autocatalysis By similarity
	Modified residue	154	1	Phosphoserine; by autocatalysis By similarity
	Modified residue	436	1	Phosphothreonine; by autocatalysis By similarity
Natural variations
	Alternative sequence	92 – 107	16	TPDLY…GKLPE → TNSPFQTSRPVTVASSQSEG KM in isoform 4.		VSP_041840
	Alternative sequence	92	1	T → TNSPFQTSRPVTVASSQSEG KM in isoform 3.		VSP_041839
	Alternative sequence	93 – 107	15	Missing in isoform 2.		VSP_010242
	Natural variant	67	1	R → C in MRX30. Ref.13		VAR_023825
	Natural variant	380	1	A → E in MRX30. Ref.14		VAR_023826
	Natural variant	440	1	T → S in a colorectal adenocarcinoma sample; somatic mutation. Ref.15		VAR_046764
Experimental info
	Sequence conflict	32	1	S → F in AAF67008. Ref.2
	Sequence conflict	36	1	P → S in AAF67008. Ref.2
	Sequence conflict	73	1	P → S in AAF67008. Ref.2
	Sequence conflict	106 – 107	2	PE → SL in AAF67008. Ref.2
	Sequence conflict	123	1	T → P in AAF67008. Ref.2
	Sequence conflict	127 – 130	4	QKKN → PEEE in AAF67008. Ref.2
	Sequence conflict	134 – 137	4	VLDV → CSRC in AAF67008. Ref.2
	Sequence conflict	146 – 148	3	TVN → PVT in AAF67008. Ref.2
	Sequence conflict	175	1	T → P in AAF67008. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (PAK3b) [UniParc]. Last modified May 10, 2004. Version 2. Checksum: BC39AEC6F0A5478B	FASTA	559	62,310
	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
	Isoform 2 [UniParc]. Checksum: 230AF6952CB049E2	FASTA	544	60,693
	10 20 30 40 50 60 MSDGLDNEEK PPAPPLRMNS NNRDSSALNH SSKPLPMAPE EKNKKARLRS IFPGGGDKTN 70 80 90 100 110 120 KKKEKERPEI SLPSDFEHTI HVGFDAVTGE FTGIPEQWAR LLQTSNITKL EQKKNPQAVL 130 140 150 160 170 180 DVLKFYDSKE TVNNQKYMSF TSGDKSAHGY IAAHPSSTKT ASEPPLAPPV SEEEDEEEEE 190 200 210 220 230 240 EEDENEPPPV IAPRPEHTKS IYTRSVVESI ASPAVPNKEV TPPSAENANS STLYRNTDRQ 250 260 270 280 290 300 RKKSKMTDEE ILEKLRSIVS VGDPKKKYTR FEKIGQGASG TVYTALDIAT GQEVAIKQMN 310 320 330 340 350 360 LQQQPKKELI INEILVMREN KNPNIVNYLD SYLVGDELWV VMEYLAGGSL TDVVTETCMD 370 380 390 400 410 420 EGQIAAVCRE CLQALDFLHS NQVIHRDIKS DNILLGMDGS VKLTDFGFCA QITPEQSKRS 430 440 450 460 470 480 TMVGTPYWMA PEVVTRKAYG PKVDIWSLGI MAIEMVEGEP PYLNENPLRA LYLIATNGTP 490 500 510 520 530 540 ELQNPERLSA VFRDFLNRCL EMDVDRRGSA KELLQHPFLK LAKPLSSLTP LIIAAKEAIK NSSR
	Isoform 3 (PAK3cb) [UniParc]. Checksum: 9646E127F2F007A2	FASTA	580	64,530
	10 20 30 40 50 60 MSDGLDNEEK PPAPPLRMNS NNRDSSALNH SSKPLPMAPE EKNKKARLRS IFPGGGDKTN 70 80 90 100 110 120 KKKEKERPEI SLPSDFEHTI HVGFDAVTGE FTNSPFQTSR PVTVASSQSE GKMPDLYGSQ 130 140 150 160 170 180 MCPGKLPEGI PEQWARLLQT SNITKLEQKK NPQAVLDVLK FYDSKETVNN QKYMSFTSGD 190 200 210 220 230 240 KSAHGYIAAH PSSTKTASEP PLAPPVSEEE DEEEEEEEDE NEPPPVIAPR PEHTKSIYTR 250 260 270 280 290 300 SVVESIASPA VPNKEVTPPS AENANSSTLY RNTDRQRKKS KMTDEEILEK LRSIVSVGDP 310 320 330 340 350 360 KKKYTRFEKI GQGASGTVYT ALDIATGQEV AIKQMNLQQQ PKKELIINEI LVMRENKNPN 370 380 390 400 410 420 IVNYLDSYLV GDELWVVMEY LAGGSLTDVV TETCMDEGQI AAVCRECLQA LDFLHSNQVI 430 440 450 460 470 480 HRDIKSDNIL LGMDGSVKLT DFGFCAQITP EQSKRSTMVG TPYWMAPEVV TRKAYGPKVD 490 500 510 520 530 540 IWSLGIMAIE MVEGEPPYLN ENPLRALYLI ATNGTPELQN PERLSAVFRD FLNRCLEMDV 550 560 570 580 DRRGSAKELL QHPFLKLAKP LSSLTPLIIA AKEAIKNSSR
	Isoform 4 (PAK3c) [UniParc]. Checksum: 6A0C2190BBBBDC1F	FASTA	565	62,913
	10 20 30 40 50 60 MSDGLDNEEK PPAPPLRMNS NNRDSSALNH SSKPLPMAPE EKNKKARLRS IFPGGGDKTN 70 80 90 100 110 120 KKKEKERPEI SLPSDFEHTI HVGFDAVTGE FTNSPFQTSR PVTVASSQSE GKMGIPEQWA 130 140 150 160 170 180 RLLQTSNITK LEQKKNPQAV LDVLKFYDSK ETVNNQKYMS FTSGDKSAHG YIAAHPSSTK 190 200 210 220 230 240 TASEPPLAPP VSEEEDEEEE EEEDENEPPP VIAPRPEHTK SIYTRSVVES IASPAVPNKE 250 260 270 280 290 300 VTPPSAENAN SSTLYRNTDR QRKKSKMTDE EILEKLRSIV SVGDPKKKYT RFEKIGQGAS 310 320 330 340 350 360 GTVYTALDIA TGQEVAIKQM NLQQQPKKEL IINEILVMRE NKNPNIVNYL DSYLVGDELW 370 380 390 400 410 420 VVMEYLAGGS LTDVVTETCM DEGQIAAVCR ECLQALDFLH SNQVIHRDIK SDNILLGMDG 430 440 450 460 470 480 SVKLTDFGFC AQITPEQSKR STMVGTPYWM APEVVTRKAY GPKVDIWSLG IMAIEMVEGE 490 500 510 520 530 540 PPYLNENPLR ALYLIATNGT PELQNPERLS AVFRDFLNRC LEMDVDRRGS AKELLQHPFL 550 560 KLAKPLSSLT PLIIAAKEAI KNSSR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"PAK3 mutation in nonsyndromic X-linked mental retardation." Allen K.M., Gleeson J.G., Bagrodia S., Partington M.W., Macmillan J.C., Cerione R.A., Mulley J.C., Walsh C.A. Nat. Genet. 20:25-30(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INVOLVEMENT IN MRX30.
[2]	"A novel gene expressed in the human adrenal gland." Jiang C., Gu J., Fu S., Ren S., Gu Y., Huang Q., Dong H., Yu Y., Fu G., Wang Y., Chen Z., Han Z. Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Adrenal gland.
[3]	"Gene diversity patterns at 10 X-chromosomal loci in humans and chimpanzees." Kitano T., Schwarz C., Nickel B., Paeaebo S. Mol. Biol. Evol. 20:1281-1289(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	"The four mammalian splice variants encoded by the p21-activated kinase 3 gene have different biological properties." Kreis P., Rousseau V., Thevenot E., Combeau G., Barnier J.V. J. Neurochem. 106:1184-1197(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4). Tissue: Brain.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[6]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity." Chong C., Tan L., Lim L., Manser E. J. Biol. Chem. 276:17347-17353(2001) [PubMed] [Europe PMC] [Abstract] Cited for: AUTOPHOSPHORYLATION.
[9]	"Regulation of the Cool/Pix proteins: key binding partners of the Cdc42/Rac targets, the p21-activated kinases." Feng Q., Albeck J.G., Cerione R.A., Yang W. J. Biol. Chem. 277:5644-5650(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ARHGEF6 AND ARHGEF7.
[10]	"DNA synthesis and neuronal apoptosis caused by familial Alzheimer disease mutants of the amyloid precursor protein are mediated by the p21 activated kinase PAK3." McPhie D.L., Coopersmith R., Hines-Peralta A., Chen Y., Ivins K.J., Manly S.P., Kozlowski M.R., Neve K.A., Neve R.L. J. Neurosci. 23:6914-6927(2003) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[11]	"Activation loop phosphorylation of ERK3/ERK4 by group I p21-activated kinases (PAKs) defines a novel PAK-ERK3/4-MAPK-activated protein kinase 5 signaling pathway." Deleris P., Trost M., Topisirovic I., Tanguay P.L., Borden K.L., Thibault P., Meloche S. J. Biol. Chem. 286:6470-6478(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF MAPK4 AND MAPK6.
[12]	"PAK signalling in neuronal physiology." Kreis P., Barnier J.V. Cell. Signal. 21:384-393(2009) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[13]	"Missense mutation in PAK3, R67C, causes X-linked nonspecific mental retardation." Bienvenu T., des Portes V., McDonell N., Carrie A., Zemni R., Couvert P., Ropers H.-H., Moraine C., van Bokhoven H., Fryns J.-P., Allen K., Walsh C.A., Boue J., Kahn A., Chelly J., Beldjord C. Am. J. Med. Genet. 93:294-298(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MRX30 CYS-67.
[14]	"X-linked mild non-syndromic mental retardation with neuropsychiatric problems and the missense mutation A365E in PAK3." Gedeon A.K., Nelson J., Gecz J., Mulley J.C. Am. J. Med. Genet. A 120:509-517(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MRX30 GLU-380.
[15]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-440.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF068864 mRNA. Translation: AAC36097.1. AF155651 mRNA. Translation: AAF67008.1. AB102659 mRNA. Translation: BAC81128.1. AB102251 Genomic DNA. Translation: BAC80750.1. AB102252 Genomic DNA. Translation: BAC80751.1. AB102253 Genomic DNA. Translation: BAC80752.1. AB102254 Genomic DNA. Translation: BAC80753.1. AB102255 Genomic DNA. Translation: BAC80754.1. AB102256 Genomic DNA. Translation: BAC80755.1. AB102257 Genomic DNA. Translation: BAC80756.1. AB102258 Genomic DNA. Translation: BAC80757.1. AB102259 Genomic DNA. Translation: BAC80758.1. AB102260 Genomic DNA. Translation: BAC80759.1. AB102261 Genomic DNA. Translation: BAC80760.1. AB102262 Genomic DNA. Translation: BAC80761.1. AB102263 Genomic DNA. Translation: BAC80762.1. AB102264 Genomic DNA. Translation: BAC80763.1. AB102265 Genomic DNA. Translation: BAC80764.1. AB102266 Genomic DNA. Translation: BAC80765.1. AB102267 Genomic DNA. Translation: BAC80766.1. AB102268 Genomic DNA. Translation: BAC80767.1. AB102269 Genomic DNA. Translation: BAC80768.1. AB102270 Genomic DNA. Translation: BAC80769.1. AB102281 Genomic DNA. Translation: BAC80780.1. AB102282 Genomic DNA. Translation: BAC80781.1. AB102283 Genomic DNA. Translation: BAC80782.1. AB102284 Genomic DNA. Translation: BAC80783.1. AB102285 Genomic DNA. Translation: BAC80784.1. AB102286 Genomic DNA. Translation: BAC80785.1. AB102287 Genomic DNA. Translation: BAC80786.1. AB102288 Genomic DNA. Translation: BAC80787.1. AB102289 Genomic DNA. Translation: BAC80788.1. AB102290 Genomic DNA. Translation: BAC80789.1. AB102291 Genomic DNA. Translation: BAC80790.1. AB102292 Genomic DNA. Translation: BAC80791.1. AB102293 Genomic DNA. Translation: BAC80792.1. AB102294 Genomic DNA. Translation: BAC80793.1. AB102295 Genomic DNA. Translation: BAC80794.1. AB102296 Genomic DNA. Translation: BAC80795.1. AB102297 Genomic DNA. Translation: BAC80796.1. AB102298 Genomic DNA. Translation: BAC80797.1. AB102299 Genomic DNA. Translation: BAC80798.1. AB102300 Genomic DNA. Translation: BAC80799.1. AM943850 mRNA. Translation: CAQ16016.1. AM943851 mRNA. Translation: CAQ16017.1. AM943852 mRNA. Translation: CAQ16018.1. AK290504 mRNA. Translation: BAF83193.1. AL356578 Genomic DNA. No translation available. AL357774, AL031117, AL117326 Genomic DNA. Translation: CAI40843.1. AL357774, AL031117, AL117326 Genomic DNA. Translation: CAI40844.1. AL031117, AL117326, AL357774 Genomic DNA. Translation: CAI43157.1. AL031117, AL117326, AL357774 Genomic DNA. Translation: CAI43158.1. AL117326, AL031117, AL357774 Genomic DNA. Translation: CAI43167.1. AL117326, AL031117, AL357774 Genomic DNA. Translation: CAI43168.1. CH471120 Genomic DNA. Translation: EAX02654.1.
IPI	IPI00027382. IPI00410084.
RefSeq	NP_001121638.1. NM_001128166.1. NP_001121639.1. NM_001128167.1. NP_001121640.1. NM_001128168.1. NP_001121644.1. NM_001128172.1. NP_001121645.1. NM_001128173.1. NP_002569.1. NM_002578.3.
UniGene	Hs.656789.
3D structure databases
ProteinModelPortal	O75914.
ModBase	Search...
Protein-protein interaction databases
IntAct	O75914. 2 interactions.
PTM databases
PhosphoSite	O75914.
Proteomic databases
PaxDb	O75914.
PRIDE	O75914.
Protocols and materials databases
DNASU	5063.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000262836; ENSP00000262836; ENSG00000077264. ENST00000360648; ENSP00000353864; ENSG00000077264. ENST00000372007; ENSP00000361077; ENSG00000077264. ENST00000372010; ENSP00000361080; ENSG00000077264. ENST00000417227; ENSP00000389172; ENSG00000077264. ENST00000425146; ENSP00000401982; ENSG00000077264. ENST00000446737; ENSP00000410853; ENSG00000077264. ENST00000518291; ENSP00000428921; ENSG00000077264. ENST00000519681; ENSP00000429113; ENSG00000077264.
GeneID	5063.
KEGG	hsa:5063.
UCSC	uc004eoz.2. human. uc004epa.2. human.
Organism-specific databases
CTD	5063.
GeneCards	GC0XP110226.
HGNC	HGNC:8592. PAK3.
HPA	HPA044791.
MIM	300142. gene. 300558. phenotype.
neXtProt	NX_O75914.
Orphanet	777. X-linked nonsyndromic intellectual deficit.
PharmGKB	PA32919.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000234202.
HOVERGEN	HBG108518.
KO	K05733.
OMA	SEPPIAP.
OrthoDB	EOG45DWP5.
PhylomeDB	O75914.
Enzyme and pathway databases
BRENDA	2.7.11.1. 2681.
Pathway_Interaction_DB	p38alphabetapathway. Regulation of p38-alpha and p38-beta.
Reactome	REACT_111045. Developmental Biology.
Gene expression databases
ArrayExpress	O75914.
Bgee	O75914.
Genevestigator	O75914.
GermOnline	ENSG00000077264. Homo sapiens.
Family and domain databases
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. [Graphical view]
Pfam	PF00786. PBD. 1 hit. PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00285. PBD. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS50108. CRIB. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	O75914.
ChEMBL	CHEMBL2999.
GenomeRNAi	5063.
NextBio	19502.
SOURCE	Search...

Entry information

Entry name

PAK3_HUMAN

Accession

Primary (citable) accession number: O75914
Secondary accession number(s): A8K389 , B1GX77, B1GX78, B1GX79, Q5JWX1, Q5JWX2, Q7Z2D6, Q7Z2E4, Q7Z3Z8, Q8WWK5, Q8WX23, Q9P0J8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	May 10, 2004
Last modified:	May 1, 2013
This is version 137 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.