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Q9P286

- PAK7_HUMAN

UniProt

Q9P286 - PAK7_HUMAN

Protein

Serine/threonine-protein kinase PAK 7

Gene

PAK7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates the proto-oncogene RAF1 and stimulates its kinase activity. Promotes cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Phosphorylates CTNND1, probably to regulate cytoskeletal organization and cell morphology. Keeps microtubules stable through MARK2 inhibition and destabilizes the F-actin network leading to the disappearance of stress fibers and focal adhesions.5 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei478 – 4781ATPPROSITE-ProRule annotation
    Active sitei568 – 5681Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi455 – 4639ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein serine/threonine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. apoptotic process Source: UniProtKB
    2. cell growth Source: UniProtKB
    3. cell migration Source: UniProtKB
    4. cell proliferation Source: UniProtKB
    5. cytoskeleton organization Source: UniProtKB
    6. negative regulation of extrinsic apoptotic signaling pathway Source: Ensembl
    7. signal transduction Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 2681.
    ReactomeiREACT_19226. Activation of Rac.
    SignaLinkiQ9P286.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase PAK 7 (EC:2.7.11.1)
    Alternative name(s):
    p21-activated kinase 5
    Short name:
    PAK-5
    p21-activated kinase 7
    Short name:
    PAK-7
    Gene namesi
    Name:PAK7
    Synonyms:KIAA1264, PAK5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:15916. PAK7.

    Subcellular locationi

    Mitochondrion. Cytoplasm. Nucleus
    Note: Shuttles between the nucleus and the mitochondria, and mitochondrial localization is essential for the role in cell survival.

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi19 – 224HRVH → LRVL: Complete loss of CDC42 binding and CDC42-mediated autophosphorylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA32922.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 719719Serine/threonine-protein kinase PAK 7PRO_0000086477Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei104 – 1041PhosphoserineBy similarity
    Modified residuei107 – 1071PhosphothreonineBy similarity

    Post-translational modificationi

    Autophosphorylated when activated by CDC42/p21.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9P286.
    PRIDEiQ9P286.

    PTM databases

    PhosphoSiteiQ9P286.

    Expressioni

    Tissue specificityi

    Predominantly expressed in brain.

    Gene expression databases

    ArrayExpressiQ9P286.
    BgeeiQ9P286.
    CleanExiHS_PAK7.
    GenevestigatoriQ9P286.

    Organism-specific databases

    HPAiHPA020444.

    Interactioni

    Subunit structurei

    Interacts tightly with GTP-bound but not GDP-bound CDC42/p21 and RAC1. Interacts with MARK2, leading to inhibit MARK2 independently of kinase activity. Interacts with RHOD and RHOH.2 Publications

    Protein-protein interaction databases

    BioGridi121402. 13 interactions.
    IntActiQ9P286. 3 interactions.
    MINTiMINT-1443173.
    STRINGi9606.ENSP00000322957.

    Structurei

    Secondary structure

    1
    719
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi429 – 4379
    Helixi445 – 4473
    Beta strandi449 – 4579
    Beta strandi459 – 46810
    Turni469 – 4713
    Beta strandi474 – 4818
    Helixi482 – 4843
    Helixi488 – 50013
    Beta strandi509 – 5157
    Beta strandi518 – 5247
    Helixi531 – 5355
    Helixi542 – 56120
    Helixi571 – 5733
    Beta strandi574 – 5763
    Beta strandi582 – 5843
    Beta strandi595 – 5973
    Helixi607 – 6093
    Helixi612 – 6154
    Helixi623 – 63816
    Turni642 – 6454
    Helixi648 – 65710
    Helixi666 – 6683
    Helixi671 – 68010
    Helixi685 – 6873
    Helixi691 – 6955
    Helixi698 – 7025
    Helixi706 – 7083
    Helixi710 – 7123

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2F57X-ray1.80A/B425-719[»]
    ProteinModelPortaliQ9P286.
    SMRiQ9P286. Positions 10-42, 422-718.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9P286.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 2414CRIBPROSITE-ProRule annotationAdd
    BLAST
    Domaini449 – 700252Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni25 – 448424LinkerAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi4 – 85Poly-Lys
    Compositional biasi223 – 2264Poly-Ser
    Compositional biasi367 – 3704Poly-Ser

    Domaini

    An autoinhibitory domain is present in the N-terminal region of the protein.1 Publication

    Sequence similaritiesi

    Contains 1 CRIB domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000234205.
    HOVERGENiHBG108518.
    InParanoidiQ9P286.
    KOiK05736.
    OMAiSHAAKQN.
    OrthoDBiEOG73804D.
    PhylomeDBiQ9P286.
    TreeFamiTF105352.

    Family and domain databases

    Gene3Di3.90.810.10. 1 hit.
    InterProiIPR000095. CRIB_dom.
    IPR011009. Kinase-like_dom.
    IPR028754. PAK7.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    [Graphical view]
    PANTHERiPTHR24361:SF183. PTHR24361:SF183. 1 hit.
    PfamiPF00786. PBD. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00285. PBD. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS50108. CRIB. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9P286-1 [UniParc]FASTAAdd to Basket

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    MFGKKKKKIE ISGPSNFEHR VHTGFDPQEQ KFTGLPQQWH SLLADTANRP    50
    KPMVDPSCIT PIQLAPMKTI VRGNKPCKET SINGLLEDFD NISVTRSNSL 100
    RKESPPTPDQ GASSHGPGHA EENGFITFSQ YSSESDTTAD YTTEKYREKS 150
    LYGDDLDPYY RGSHAAKQNG HVMKMKHGEA YYSEVKPLKS DFARFSADYH 200
    SHLDSLSKPS EYSDLKWEYQ RASSSSPLDY SFQFTPSRTA GTSGCSKESL 250
    AYSESEWGPS LDDYDRRPKS SYLNQTSPQP TMRQRSRSGS GLQEPMMPFG 300
    ASAFKTHPQG HSYNSYTYPR LSEPTMCIPK VDYDRAQMVL SPPLSGSDTY 350
    PRGPAKLPQS QSKSGYSSSS HQYPSGYHKA TLYHHPSLQS SSQYISTASY 400
    LSSLSLSSST YPPPSWGSSS DQQPSRVSHE QFRAALQLVV SPGDPREYLA 450
    NFIKIGEGST GIVCIATEKH TGKQVAVKKM DLRKQQRREL LFNEVVIMRD 500
    YHHDNVVDMY SSYLVGDELW VVMEFLEGGA LTDIVTHTRM NEEQIATVCL 550
    SVLRALSYLH NQGVIHRDIK SDSILLTSDG RIKLSDFGFC AQVSKEVPKR 600
    KSLVGTPYWM APEVISRLPY GTEVDIWSLG IMVIEMIDGE PPYFNEPPLQ 650
    AMRRIRDSLP PRVKDLHKVS SVLRGFLDLM LVREPSQRAT AQELLGHPFL 700
    KLAGPPSCIV PLMRQYRHH 719
    Length:719
    Mass (Da):80,745
    Last modified:October 1, 2000 - v1
    Checksum:i07A12B1EEC4E2A02
    GO

    Sequence cautioni

    The sequence BAA86578.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti118 – 1181G → D.1 Publication
    Corresponds to variant rs55923311 [ dbSNP | Ensembl ].
    VAR_040978
    Natural varianti187 – 1871P → A.1 Publication
    Corresponds to variant rs34280805 [ dbSNP | Ensembl ].
    VAR_040979
    Natural varianti312 – 3121S → P in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_040980
    Natural varianti335 – 3351R → P.1 Publication
    Corresponds to variant rs11700112 [ dbSNP | Ensembl ].
    VAR_040981
    Natural varianti511 – 5111S → N.2 Publications
    Corresponds to variant rs2297345 [ dbSNP | Ensembl ].
    VAR_021865
    Natural varianti538 – 5381T → N in a lung adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_040982
    Natural varianti555 – 5551A → S.1 Publication
    Corresponds to variant rs34102290 [ dbSNP | Ensembl ].
    VAR_040983
    Natural varianti604 – 6041V → I in a metastatic melanoma sample; somatic mutation. 1 Publication
    VAR_040984
    Natural varianti704 – 7041G → S in a metastatic melanoma sample; somatic mutation. 1 Publication
    VAR_040985

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB040812 mRNA. Translation: BAA94194.1.
    AB033090 mRNA. Translation: BAA86578.1. Different initiation.
    AK291401 mRNA. Translation: BAF84090.1.
    AL031652, AL135935, AL353612 Genomic DNA. Translation: CAI42211.1.
    AL135935, AL031652, AL353612 Genomic DNA. Translation: CAH71126.1.
    AL353612, AL031652, AL135935 Genomic DNA. Translation: CAI23529.1.
    CH471133 Genomic DNA. Translation: EAX10358.1.
    CH471133 Genomic DNA. Translation: EAX10359.1.
    CH471133 Genomic DNA. Translation: EAX10360.1.
    CCDSiCCDS13107.1.
    RefSeqiNP_065074.1. NM_020341.3.
    NP_817127.1. NM_177990.2.
    XP_005260823.1. XM_005260766.2.
    XP_006723660.1. XM_006723597.1.
    UniGeneiHs.32539.

    Genome annotation databases

    EnsembliENST00000353224; ENSP00000322957; ENSG00000101349.
    ENST00000378423; ENSP00000367679; ENSG00000101349.
    ENST00000378429; ENSP00000367686; ENSG00000101349.
    GeneIDi57144.
    KEGGihsa:57144.
    UCSCiuc002wnj.2. human.

    Polymorphism databases

    DMDMi12585290.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB040812 mRNA. Translation: BAA94194.1 .
    AB033090 mRNA. Translation: BAA86578.1 . Different initiation.
    AK291401 mRNA. Translation: BAF84090.1 .
    AL031652 , AL135935 , AL353612 Genomic DNA. Translation: CAI42211.1 .
    AL135935 , AL031652 , AL353612 Genomic DNA. Translation: CAH71126.1 .
    AL353612 , AL031652 , AL135935 Genomic DNA. Translation: CAI23529.1 .
    CH471133 Genomic DNA. Translation: EAX10358.1 .
    CH471133 Genomic DNA. Translation: EAX10359.1 .
    CH471133 Genomic DNA. Translation: EAX10360.1 .
    CCDSi CCDS13107.1.
    RefSeqi NP_065074.1. NM_020341.3.
    NP_817127.1. NM_177990.2.
    XP_005260823.1. XM_005260766.2.
    XP_006723660.1. XM_006723597.1.
    UniGenei Hs.32539.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2F57 X-ray 1.80 A/B 425-719 [» ]
    ProteinModelPortali Q9P286.
    SMRi Q9P286. Positions 10-42, 422-718.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121402. 13 interactions.
    IntActi Q9P286. 3 interactions.
    MINTi MINT-1443173.
    STRINGi 9606.ENSP00000322957.

    Chemistry

    BindingDBi Q9P286.
    ChEMBLi CHEMBL4524.
    GuidetoPHARMACOLOGYi 2138.

    PTM databases

    PhosphoSitei Q9P286.

    Polymorphism databases

    DMDMi 12585290.

    Proteomic databases

    PaxDbi Q9P286.
    PRIDEi Q9P286.

    Protocols and materials databases

    DNASUi 57144.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000353224 ; ENSP00000322957 ; ENSG00000101349 .
    ENST00000378423 ; ENSP00000367679 ; ENSG00000101349 .
    ENST00000378429 ; ENSP00000367686 ; ENSG00000101349 .
    GeneIDi 57144.
    KEGGi hsa:57144.
    UCSCi uc002wnj.2. human.

    Organism-specific databases

    CTDi 57144.
    GeneCardsi GC20M009518.
    HGNCi HGNC:15916. PAK7.
    HPAi HPA020444.
    MIMi 608038. gene.
    neXtProti NX_Q9P286.
    PharmGKBi PA32922.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000234205.
    HOVERGENi HBG108518.
    InParanoidi Q9P286.
    KOi K05736.
    OMAi SHAAKQN.
    OrthoDBi EOG73804D.
    PhylomeDBi Q9P286.
    TreeFami TF105352.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 2681.
    Reactomei REACT_19226. Activation of Rac.
    SignaLinki Q9P286.

    Miscellaneous databases

    EvolutionaryTracei Q9P286.
    GeneWikii PAK7.
    GenomeRNAii 57144.
    NextBioi 63091.
    PROi Q9P286.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9P286.
    Bgeei Q9P286.
    CleanExi HS_PAK7.
    Genevestigatori Q9P286.

    Family and domain databases

    Gene3Di 3.90.810.10. 1 hit.
    InterProi IPR000095. CRIB_dom.
    IPR011009. Kinase-like_dom.
    IPR028754. PAK7.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    [Graphical view ]
    PANTHERi PTHR24361:SF183. PTHR24361:SF183. 1 hit.
    Pfami PF00786. PBD. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00285. PBD. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS50108. CRIB. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of PAK5, a novel member of mammalian p21-activated kinase-II subfamily that is predominantly expressed in brain."
      Pandey A., Dan I., Kristiansen T.Z., Watanabe N.M., Voldby J., Kajikawa E., Khosravi-Far R., Blagoev B., Mann M.
      Oncogene 21:3939-3948(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
      DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    3. "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], VARIANT ASN-511.
      Tissue: Brain.
    4. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "Identification of an autoinhibitory domain of p21-activated protein kinase 5."
      Ching Y.P., Leong V.Y., Wong C.M., Kung H.F.
      J. Biol. Chem. 278:33621-33624(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN, MUTAGENESIS OF 19-HIS--HIS-22.
    7. "p21-Activated kinase 5 (Pak5) localizes to mitochondria and inhibits apoptosis by phosphorylating BAD."
      Cotteret S., Jaffer Z.M., Beeser A., Chernoff J.
      Mol. Cell. Biol. 23:5526-5539(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    8. "PAK5 kinase is an inhibitor of MARK/Par-1, which leads to stable microtubules and dynamic actin."
      Matenia D., Griesshaber B., Li X.Y., Thiessen A., Johne C., Jiao J., Mandelkow E., Mandelkow E.M.
      Mol. Biol. Cell 16:4410-4422(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MARK2.
    9. "Multiple Rho proteins regulate the subcellular targeting of PAK5."
      Wu X., Frost J.A.
      Biochem. Biophys. Res. Commun. 351:328-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RHOD AND RHOH.
    10. "Nucleocytoplasmic shuttling of Pak5 regulates its antiapoptotic properties."
      Cotteret S., Chernoff J.
      Mol. Cell. Biol. 26:3215-3230(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    11. "p21 activated kinase 5 activates Raf-1 and targets it to mitochondria."
      Wu X., Carr H.S., Dan I., Ruvolo P.P., Frost J.A.
      J. Cell. Biochem. 105:167-175(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF RAF1.
    12. "p120-catenin is a binding partner and substrate for Group B Pak kinases."
      Wong L.E., Reynolds A.B., Dissanayaka N.T., Minden A.
      J. Cell. Biochem. 110:1244-1254(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CTNND1.
    13. "Crystal Structures of the p21-activated kinases PAK4, PAK5, and PAK6 reveal catalytic domain plasticity of active group II PAKs."
      Eswaran J., Lee W.H., Debreczeni J.E., Filippakopoulos P., Turnbull A., Fedorov O., Deacon S.W., Peterson J.R., Knapp S.
      Structure 15:201-213(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 425-719.
    14. "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: VARIANTS [LARGE SCALE ANALYSIS] ASP-118; ALA-187; PRO-312; PRO-335; ASN-511; ASN-538; SER-555; ILE-604 AND SER-704.

    Entry informationi

    Entry nameiPAK7_HUMAN
    AccessioniPrimary (citable) accession number: Q9P286
    Secondary accession number(s): A8K5T6
    , D3DW14, Q5W115, Q9BX09, Q9ULF6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 146 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3