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Reviewed, UniProtKB/Swiss-Prot O75914 (PAK3_HUMAN)

Last modified January 19, 2010. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Serine/threonine-protein kinase PAK 3
    EC=2.7.11.1
Alternative name(s):
    p21-activated kinase 3
      Short name=PAK-3
    Beta-PAK
    Oligophrenin-3
Gene names
Name: PAK3
Synonyms: OPHN3
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length559 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Key regulator of synapse formation and plasticity in the hippocampus By similarity.

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.

Tissue specificity

Highly expressed in postmitotic neurons of the developing and postnatal cerebral cortex and hippocampus.

Post-translational modification

Autophosphorylated when activated by CDC42/p21.

Involvement in disease

Defects in PAK3 are the cause of mental retardation X-linked type 30 (MRX30) [MIM:300558]; also called X-linked mental retardation type 47 (MRX47). Mental retardation is a mental disorder characterized by significantly sub-average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. Non-syndromic mental retardation patients do not manifest other clinical signs. Ref.1 Ref.9 Ref.10

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.

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Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75914-1)

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.

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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

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
Modified residue5351N6-acetyllysine Ref.8

Natural variations

Alternative sequence93 – 10715Missing in isoform 2.
VSP_010242
Natural variant671R → C in MRX30. Ref.9
VAR_023825
Natural variant3801A → E in MRX30. Ref.10
VAR_023826
Natural variant4401T → S in a colorectal adenocarcinoma sample; somatic mutation. Ref.11
VAR_046764

Experimental info

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

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Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [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.

Checksum: 230AF6952CB049E2
Show »

FASTA54460,693

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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: 9731525] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), DISEASE.
[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: 12777533] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[5]"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: 15772651] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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].
[7]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-535, MASS SPECTROMETRY.
[9]"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: 10946356] [Abstract]
Cited for: VARIANT MRX30 CYS-67.
[10]"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: 12884430] [Abstract]
Cited for: VARIANT MRX30 GLU-380.
[11]"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: 17344846] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-440.
+Additional computationally mapped references.

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Web resources

GeneReviews

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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.
AK290504 mRNA. Translation: BAF83193.1.
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.
IPIIPI00027382.
IPI00410084.
RefSeqNP_001121638.1.
NP_001121639.1.
NP_001121640.1.
NP_001121644.1.
NP_001121645.1.
NP_002569.1.
UniGeneHs.656789

3D structure databases

SMRO75914. Positions 73-156, 262-553.
ModBaseSearch...

Protein-protein interaction databases

STRINGO75914.

PTM databases

PhosphoSiteO75914.

Proteomic databases

PRIDEO75914.

Genome annotation databases

EnsemblENST00000262836; ENSP00000262836; ENSG00000077264; Homo sapiens. [Genome view]
ENST00000372010; ENSP00000361080; ENSG00000077264; Homo sapiens. [Genome view]
GeneID5063.
KEGGhsa:5063.
UCSCuc004eoz.2. human.
uc004epa.2. human.

Organism-specific databases

CTD5063.
GeneCardsGC0XP110226.
H-InvDBHIX0016993.
HGNCHGNC:8592. PAK3.
MIM300142. gene.
300558. phenotype.
Orphanet101685. Rare intellectual deficit without developmental anomaly.
PharmGKBPA32919.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG07467.
HOVERGENO75914.
OrthoDBEOG9N8TQ5.
PhylomeDBO75914.

Enzyme and pathway databases

BRENDA2.7.11.1. 247.
Pathway_Interaction_DBp38alphabetapathway. Regulation of p38-alpha and p38-beta.
ReactomeREACT_18266. Axon guidance.

Gene expression databases

ArrayExpressO75914.
BgeeO75914.
GenevestigatorO75914.
GermOnlineENSG00000077264. Homo sapiens.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000095. PAK_box_Rho_bd.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR015750. Ser/Thr_kinase_Pak-rel.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR002290. Ser/Thr_prot_kinase_dom.
[Graphical view]
PANTHERPTHR22986:SF84. Pak_like. 1 hit.
PfamPF00786. PBD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00285. PBD. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
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 Resources

NextBio19502.
SOURCESearch...

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Entry information

Entry namePAK3_HUMAN
AccessionPrimary (citable) accession number: O75914
Secondary accession number(s): A8K389 expand/collapse secondary AC list , 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: January 19, 2010
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents