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O75914 (PAK3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length559 AA.
Sequence statusComplete.
Protein existenceEvidence 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. May also be involved in early neuronal development. Ref.12

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

Neddylated.

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 adaptive 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.14 Ref.15

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 componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Mental retardation
   DomainSH3-binding
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
Ubl conjugation
   Technical termAllosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK cascade

Inferred from direct assay Ref.12. Source: GOC

activation of MAPK activity

Inferred from direct assay Ref.12. Source: GOC

axonogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite development

Inferred from sequence or structural similarity. Source: UniProtKB

dendritic spine morphogenesis

Traceable author statement Ref.13. Source: UniProtKB

regulation of actin filament polymerization

Inferred from direct assay Ref.12. Source: UniProtKB

signal transduction by phosphorylation

Inferred from Biological aspect of Ancestor. Source: GOC

synapse organization

Traceable author statement Ref.13. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase kinase activity

Inferred from direct assay Ref.12. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 11157984PubMed 11862216. Source: IntAct

receptor signaling protein serine/threonine kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 559559Serine/threonine-protein kinase PAK 3
PRO_0000086469

Regions

Domain70 – 8314CRIB
Domain283 – 534252Protein kinase
Nucleotide binding289 – 2979ATP By similarity
Region65 – 15086Autoregulatory region By similarity
Region65 – 12359GTPase-binding By similarity
Region84 – 282199Linker
Compositional bias187 – 20115Poly-Glu

Sites

Active site4021Proton acceptor By similarity
Binding site3121ATP By similarity

Amino acid modifications

Modified residue501Phosphoserine; by autocatalysis By similarity
Modified residue1541Phosphoserine; by autocatalysis By similarity
Modified residue4361Phosphothreonine; by autocatalysis By similarity

Natural variations

Alternative sequence92 – 10716TPDLY…GKLPE → TNSPFQTSRPVTVASSQSEG KM in isoform 4.
VSP_041840
Alternative sequence921T → TNSPFQTSRPVTVASSQSEG KM in isoform 3.
VSP_041839
Alternative sequence93 – 10715Missing in isoform 2.
VSP_010242
Natural variant671R → C in MRX30. Ref.14
VAR_023825
Natural variant3801A → E in MRX30. Ref.15
VAR_023826
Natural variant4401T → S in a colorectal adenocarcinoma sample; somatic mutation. Ref.16
VAR_046764

Experimental info

Sequence conflict321S → F in AAF67008. Ref.2
Sequence conflict361P → S in AAF67008. Ref.2
Sequence conflict731P → S in AAF67008. Ref.2
Sequence conflict106 – 1072PE → SL in AAF67008. Ref.2
Sequence conflict1231T → P in AAF67008. Ref.2
Sequence conflict127 – 1304QKKN → PEEE in AAF67008. Ref.2
Sequence conflict134 – 1374VLDV → CSRC in AAF67008. Ref.2
Sequence conflict146 – 1483TVN → PVT in AAF67008. Ref.2
Sequence conflict1751T → P in AAF67008. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (PAK3b) [UniParc].

Last modified May 10, 2004. Version 2.
Checksum: BC39AEC6F0A5478B

FASTA55962,310
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 230AF6952CB049E2
Show »

FASTA54460,693
Isoform 3 (PAK3cb) [UniParc].

Checksum: 9646E127F2F007A2
Show »

FASTA58064,530
Isoform 4 (PAK3c) [UniParc].

Checksum: 6A0C2190BBBBDC1F
Show »

FASTA56562,913

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]"Development and validation of a method for profiling post-translational modification activities using protein microarrays."
Del Rincon S.V., Rogers J., Widschwendter M., Sun D., Sieburg H.B., Spruck C.
PLoS ONE 5:E11332-E11332(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NEDDYLATION.
[12]"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.
[13]"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.
[14]"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.
[15]"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.
[16]"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. expand/collapse author list , 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.

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.
CCDSCCDS14554.1. [O75914-2]
CCDS48151.1. [O75914-3]
CCDS48152.1. [O75914-4]
CCDS48153.1. [O75914-1]
RefSeqNP_001121638.1. NM_001128166.1. [O75914-2]
NP_001121639.1. NM_001128167.1. [O75914-2]
NP_001121640.1. NM_001128168.1. [O75914-3]
NP_001121644.1. NM_001128172.1. [O75914-4]
NP_001121645.1. NM_001128173.1. [O75914-1]
NP_002569.1. NM_002578.3. [O75914-2]
XP_006724719.1. XM_006724656.1. [O75914-1]
UniGeneHs.593599.
Hs.656789.

3D structure databases

ProteinModelPortalO75914.
SMRO75914. Positions 65-156, 181-553.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111099. 7 interactions.
IntActO75914. 3 interactions.
MINTMINT-3001915.

Chemistry

BindingDBO75914.
ChEMBLCHEMBL2999.
GuidetoPHARMACOLOGY2135.

PTM databases

PhosphoSiteO75914.

Proteomic databases

PaxDbO75914.
PRIDEO75914.

Protocols and materials databases

DNASU5063.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262836; ENSP00000262836; ENSG00000077264. [O75914-1]
ENST00000360648; ENSP00000353864; ENSG00000077264. [O75914-3]
ENST00000372007; ENSP00000361077; ENSG00000077264. [O75914-2]
ENST00000372010; ENSP00000361080; ENSG00000077264. [O75914-1]
ENST00000417227; ENSP00000389172; ENSG00000077264. [O75914-4]
ENST00000425146; ENSP00000401982; ENSG00000077264. [O75914-2]
ENST00000446737; ENSP00000410853; ENSG00000077264. [O75914-2]
ENST00000518291; ENSP00000428921; ENSG00000077264. [O75914-3]
ENST00000519681; ENSP00000429113; ENSG00000077264. [O75914-4]
GeneID5063.
KEGGhsa:5063.
UCSCuc004eoz.2. human. [O75914-2]
uc004epa.2. human. [O75914-1]
uc010npv.1. human. [O75914-3]
uc010npw.1. human. [O75914-4]

Organism-specific databases

CTD5063.
GeneCardsGC0XP110226.
HGNCHGNC:8592. PAK3.
HPAHPA044791.
MIM300142. gene.
300558. phenotype.
neXtProtNX_O75914.
Orphanet777. X-linked non-syndromic intellectual disability.
PharmGKBPA32919.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000234202.
HOVERGENHBG108518.
KOK05733.
OMASANENDM.
OrthoDBEOG7CK36J.
PhylomeDBO75914.
TreeFamTF105351.

Enzyme and pathway databases

BRENDA2.7.11.1. 2681.
ReactomeREACT_111045. Developmental Biology.
SignaLinkO75914.

Gene expression databases

ArrayExpressO75914.
BgeeO75914.
GenevestigatorO75914.

Family and domain databases

Gene3D3.90.810.10. 1 hit.
InterProIPR000095. CRIB_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00786. PBD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00285. PBD. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50108. CRIB. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPAK3.
GenomeRNAi5063.
NextBio19502.
PROO75914.
SOURCESearch...

Entry information

Entry namePAK3_HUMAN
AccessionPrimary (citable) accession number: O75914
Secondary accession number(s): A8K389 expand/collapse secondary AC list , 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: July 9, 2014
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM