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Q9NQU5

- PAK6_HUMAN

UniProt

Q9NQU5 - PAK6_HUMAN

Protein

Serine/threonine-protein kinase PAK 6

Gene

PAK6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (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 the regulation of gene transcription. The kinase activity is induced by various effectors including AR or MAP2K6/MAPKK6. Phosphorylates the DNA-binding domain of androgen receptor/AR and thereby inhibits AR-mediated transcription. Inhibits also ESR1-mediated transcription. May play a role in cytoskeleton regulation by interacting with IQGAP1. May protect cells from apoptosis through phosphorylation of BAD.2 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei436 – 4361ATPPROSITE-ProRule annotation
    Active sitei526 – 5261Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi413 – 4219ATPPROSITE-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. cytoskeleton organization Source: UniProtKB
    3. regulation of transcription, DNA-templated Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_19226. Activation of Rac.
    SignaLinkiB3KYB0.
    Q9NQU5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase PAK 6 (EC:2.7.11.1)
    Alternative name(s):
    PAK-5
    p21-activated kinase 6
    Short name:
    PAK-6
    Gene namesi
    Name:PAK6
    Synonyms:PAK5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:16061. PAK6.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Cotranslocates into nucleus with AR in response to androgen induction.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi165 – 1651S → A: Almost complete loss of PAK6 activation by MAP2K6/MAPKK6; when associated with F-566. 1 Publication
    Mutagenesisi560 – 5601S → A: Complete loss of PAK6 activation by MAP2K6/MAPKK6; when associated with A-165. 1 Publication
    Mutagenesisi566 – 5661Y → F: Complete loss of PAK6 activation by MAP2K6/MAPKK6; when associated with A-165. 1 Publication

    Organism-specific databases

    PharmGKBiPA32921.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 681681Serine/threonine-protein kinase PAK 6PRO_0000086476Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei560 – 5601Phosphoserine; by autocatalysisBy similarity

    Post-translational modificationi

    Autophosphorylated. Phosphorylated by MAP2K6//MAPKK6, leading to PAK6 activation.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9NQU5.
    PaxDbiQ9NQU5.
    PRIDEiQ9NQU5.

    PTM databases

    PhosphoSiteiQ9NQU5.

    Expressioni

    Tissue specificityi

    Selectively expressed in brain and testis, with lower levels in multiple tissues including prostate and breast.2 Publications

    Gene expression databases

    BgeeiQ9NQU5.
    CleanExiHS_PAK6.
    GenevestigatoriQ9NQU5.

    Organism-specific databases

    HPAiHPA031124.

    Interactioni

    Subunit structurei

    Interacts tightly with GTP-bound but not GDP-bound CDC42/p21 and RAC1 By similarity. Interacts with the androgen receptor AR and the estrogen receptor ESR1. Interacts with IQGAP1 and PPM1B.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LRRK2Q5S0072EBI-1053685,EBI-5323863

    Protein-protein interaction databases

    BioGridi121251. 16 interactions.
    IntActiQ9NQU5. 11 interactions.
    MINTiMINT-8247581.
    STRINGi9606.ENSP00000260404.

    Structurei

    Secondary structure

    1
    681
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi387 – 3959
    Helixi404 – 4063
    Beta strandi407 – 41610
    Beta strandi419 – 4268
    Turni427 – 4293
    Beta strandi432 – 4398
    Turni440 – 4423
    Helixi446 – 4483
    Helixi449 – 45810
    Beta strandi467 – 4737
    Beta strandi476 – 4816
    Helixi489 – 4935
    Helixi500 – 51920
    Helixi529 – 5313
    Beta strandi532 – 5343
    Beta strandi540 – 5423
    Helixi545 – 5473
    Beta strandi553 – 5553
    Helixi565 – 5673
    Helixi570 – 5734
    Helixi581 – 59616
    Turni600 – 6034
    Helixi606 – 61510
    Helixi624 – 6263
    Helixi629 – 63810
    Turni643 – 6453
    Helixi649 – 6535
    Helixi656 – 6605
    Helixi664 – 6707

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2C30X-ray1.60A383-681[»]
    2ODBX-ray2.40B11-45[»]
    4KS7X-ray1.40A385-674[»]
    4KS8X-ray1.95A385-674[»]
    ProteinModelPortaliQ9NQU5.
    SMRiQ9NQU5. Positions 11-45, 385-674.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NQU5.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini12 – 2514CRIBPROSITE-ProRule annotationAdd
    BLAST
    Domaini407 – 658252Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni26 – 406381LinkerAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000234205.
    HOVERGENiHBG108518.
    InParanoidiQ9NQU5.
    KOiK05735.
    OMAiNRRGMKA.
    OrthoDBiEOG73804D.
    PhylomeDBiQ9NQU5.
    TreeFamiTF105352.

    Family and domain databases

    Gene3Di3.90.810.10. 1 hit.
    InterProiIPR000095. CRIB_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    [Graphical view]
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NQU5-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MFRKKKKKRP EISAPQNFQH RVHTSFDPKE GKFVGLPPQW QNILDTLRRP    50
    KPVVDPSRIT RVQLQPMKTV VRGSAMPVDG YISGLLNDIQ KLSVISSNTL 100
    RGRSPTSRRR AQSLGLLGDE HWATDPDMYL QSPQSERTDP HGLYLSCNGG 150
    TPAGHKQMPW PEPQSPRVLP NGLAAKAQSL GPAEFQGASQ RCLQLGACLQ 200
    SSPPGASPPT GTNRHGMKAA KHGSEEARPQ SCLVGSATGR PGGEGSPSPK 250
    TRESSLKRRL FRSMFLSTAA TAPPSSSKPG PPPQSKPNSS FRPPQKDNPP 300
    SLVAKAQSLP SDQPVGTFSP LTTSDTSSPQ KSLRTAPATG QLPGRSSPAG 350
    SPRTWHAQIS TSNLYLPQDP TVAKGALAGE DTGVVTHEQF KAALRMVVDQ 400
    GDPRLLLDSY VKIGEGSTGI VCLAREKHSG RQVAVKMMDL RKQQRRELLF 450
    NEVVIMRDYQ HFNVVEMYKS YLVGEELWVL MEFLQGGALT DIVSQVRLNE 500
    EQIATVCEAV LQALAYLHAQ GVIHRDIKSD SILLTLDGRV KLSDFGFCAQ 550
    ISKDVPKRKS LVGTPYWMAP EVISRSLYAT EVDIWSLGIM VIEMVDGEPP 600
    YFSDSPVQAM KRLRDSPPPK LKNSHKVSPV LRDFLERMLV RDPQERATAQ 650
    ELLDHPFLLQ TGLPECLVPL IQLYRKQTST C 681
    Length:681
    Mass (Da):74,869
    Last modified:October 1, 2000 - v1
    Checksum:iF20A4FA257649BB9
    GO
    Isoform 2 (identifier: Q9NQU5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         583-627: Missing.

    Show »
    Length:636
    Mass (Da):69,777
    Checksum:i3CA588AAB5B8E522
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti60 – 601T → A in BAG54772. (PubMed:14702039)Curated
    Sequence conflicti381 – 3811D → G in BAG54772. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti3 – 31R → H in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035631
    Natural varianti76 – 761M → V.1 Publication
    Corresponds to variant rs2412504 [ dbSNP | Ensembl ].
    VAR_019993
    Natural varianti103 – 1031R → C.
    Corresponds to variant rs36081263 [ dbSNP | Ensembl ].
    VAR_051655
    Natural varianti151 – 1511T → I.
    Corresponds to variant rs35593179 [ dbSNP | Ensembl ].
    VAR_051656
    Natural varianti184 – 1841E → K.1 Publication
    Corresponds to variant rs56349744 [ dbSNP | Ensembl ].
    VAR_040972
    Natural varianti205 – 2051G → E.1 Publication
    Corresponds to variant rs55920845 [ dbSNP | Ensembl ].
    VAR_040973
    Natural varianti208 – 2081P → T.1 Publication
    Corresponds to variant rs35501648 [ dbSNP | Ensembl ].
    VAR_040974
    Natural varianti210 – 2101T → M.1 Publication
    Corresponds to variant rs34869667 [ dbSNP | Ensembl ].
    VAR_040975
    Natural varianti215 – 2151H → R.1 Publication
    Corresponds to variant rs3743135 [ dbSNP | Ensembl ].
    VAR_019994
    Natural varianti337 – 3371P → L.1 Publication
    Corresponds to variant rs3743137 [ dbSNP | Ensembl ].
    VAR_019995
    Natural varianti376 – 3761A → V.1 Publication
    Corresponds to variant rs55806501 [ dbSNP | Ensembl ].
    VAR_040976
    Natural varianti475 – 4751E → K.
    Corresponds to variant rs34445577 [ dbSNP | Ensembl ].
    VAR_051657
    Natural varianti514 – 5141L → R in a lung small cell carcinoma sample; somatic mutation. 1 Publication
    VAR_040977

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei583 – 62745Missing in isoform 2. 1 PublicationVSP_056733Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF276893 mRNA. Translation: AAF82800.1.
    AJ236915 mRNA. Translation: CAC18720.1.
    AK131522 mRNA. Translation: BAG54772.1.
    AK290227 mRNA. Translation: BAF82916.1.
    AK315813 mRNA. Translation: BAF98704.1.
    AK315817 mRNA. Translation: BAF98708.1.
    AC020658 Genomic DNA. No translation available.
    AC025429 Genomic DNA. No translation available.
    CH471125 Genomic DNA. Translation: EAW92395.1.
    CH471125 Genomic DNA. Translation: EAW92401.1.
    BC035596 mRNA. Translation: AAH35596.1.
    CCDSiCCDS10054.1.
    RefSeqiNP_001122100.1. NM_001128628.2.
    NP_001122101.1. NM_001128629.2.
    NP_001263646.1. NM_001276717.1.
    NP_001263647.1. NM_001276718.1.
    NP_064553.1. NM_020168.5.
    UniGeneiHs.513645.
    Hs.732375.
    Hs.745440.

    Genome annotation databases

    EnsembliENST00000260404; ENSP00000260404; ENSG00000137843.
    ENST00000455577; ENSP00000409465; ENSG00000137843.
    ENST00000542403; ENSP00000439597; ENSG00000137843.
    ENST00000560346; ENSP00000453858; ENSG00000137843.
    GeneIDi56924.
    KEGGihsa:56924.
    UCSCiuc001zky.4. human.
    uc001zlb.3. human.

    Polymorphism databases

    DMDMi23396789.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF276893 mRNA. Translation: AAF82800.1 .
    AJ236915 mRNA. Translation: CAC18720.1 .
    AK131522 mRNA. Translation: BAG54772.1 .
    AK290227 mRNA. Translation: BAF82916.1 .
    AK315813 mRNA. Translation: BAF98704.1 .
    AK315817 mRNA. Translation: BAF98708.1 .
    AC020658 Genomic DNA. No translation available.
    AC025429 Genomic DNA. No translation available.
    CH471125 Genomic DNA. Translation: EAW92395.1 .
    CH471125 Genomic DNA. Translation: EAW92401.1 .
    BC035596 mRNA. Translation: AAH35596.1 .
    CCDSi CCDS10054.1.
    RefSeqi NP_001122100.1. NM_001128628.2.
    NP_001122101.1. NM_001128629.2.
    NP_001263646.1. NM_001276717.1.
    NP_001263647.1. NM_001276718.1.
    NP_064553.1. NM_020168.5.
    UniGenei Hs.513645.
    Hs.732375.
    Hs.745440.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2C30 X-ray 1.60 A 383-681 [» ]
    2ODB X-ray 2.40 B 11-45 [» ]
    4KS7 X-ray 1.40 A 385-674 [» ]
    4KS8 X-ray 1.95 A 385-674 [» ]
    ProteinModelPortali Q9NQU5.
    SMRi Q9NQU5. Positions 11-45, 385-674.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121251. 16 interactions.
    IntActi Q9NQU5. 11 interactions.
    MINTi MINT-8247581.
    STRINGi 9606.ENSP00000260404.

    Chemistry

    BindingDBi Q9NQU5.
    ChEMBLi CHEMBL4311.
    GuidetoPHARMACOLOGYi 2137.

    PTM databases

    PhosphoSitei Q9NQU5.

    Polymorphism databases

    DMDMi 23396789.

    Proteomic databases

    MaxQBi Q9NQU5.
    PaxDbi Q9NQU5.
    PRIDEi Q9NQU5.

    Protocols and materials databases

    DNASUi 56924.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000260404 ; ENSP00000260404 ; ENSG00000137843 .
    ENST00000455577 ; ENSP00000409465 ; ENSG00000137843 .
    ENST00000542403 ; ENSP00000439597 ; ENSG00000137843 .
    ENST00000560346 ; ENSP00000453858 ; ENSG00000137843 .
    GeneIDi 56924.
    KEGGi hsa:56924.
    UCSCi uc001zky.4. human.
    uc001zlb.3. human.

    Organism-specific databases

    CTDi 56924.
    GeneCardsi GC15P040509.
    HGNCi HGNC:16061. PAK6.
    HPAi HPA031124.
    MIMi 608110. gene.
    neXtProti NX_Q9NQU5.
    PharmGKBi PA32921.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000234205.
    HOVERGENi HBG108518.
    InParanoidi Q9NQU5.
    KOi K05735.
    OMAi NRRGMKA.
    OrthoDBi EOG73804D.
    PhylomeDBi Q9NQU5.
    TreeFami TF105352.

    Enzyme and pathway databases

    Reactomei REACT_19226. Activation of Rac.
    SignaLinki B3KYB0.
    Q9NQU5.

    Miscellaneous databases

    EvolutionaryTracei Q9NQU5.
    GeneWikii PAK6.
    GenomeRNAii 56924.
    NextBioi 62436.
    PROi Q9NQU5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9NQU5.
    CleanExi HS_PAK6.
    Genevestigatori Q9NQU5.

    Family and domain databases

    Gene3Di 3.90.810.10. 1 hit.
    InterProi IPR000095. CRIB_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    [Graphical view ]
    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. "Androgen receptor specifically interacts with a novel p21-activated kinase, PAK6."
      Yang F., Li X., Sharma M., Zarnegar M., Lim B., Sun Z.
      J. Biol. Chem. 276:15345-15353(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH AR.
    2. "Pak5, a new member of the p21-activated kinase family, affects Cdc42 signalling to the actin cytoskeleton."
      Wagner T., Puls A., Frischauf A.M., Hall A.
      Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] (ISOFORMS 1 AND 2).
      Tissue: Amygdala, Brain and Thalamus.
    4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    7. "AR and ER interaction with a p21-activated kinase (PAK6)."
      Lee S.R., Ramos S.M., Ko A., Masiello D., Swanson K.D., Lu M.L., Balk S.P.
      Mol. Endocrinol. 16:85-99(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH AR AND ESR1.
    8. "Mechanism of p21-activated kinase 6-mediated inhibition of androgen receptor signaling."
      Schrantz N., da Silva Correia J., Fowler B., Ge Q., Sun Z., Bokoch G.M.
      J. Biol. Chem. 279:1922-1931(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF AR.
    9. "Activation of p21-activated kinase 6 by MAP kinase kinase 6 and p38 MAP kinase."
      Kaur R., Liu X., Gjoerup O., Zhang A., Yuan X., Balk S.P., Schneider M.C., Lu M.L.
      J. Biol. Chem. 280:3323-3330(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY MAP2K6, AUTOPHOSPHORYLATION, MUTAGENESIS OF SER-165; SER-560 AND TYR-566.
    10. "Increased PAK6 expression in prostate cancer and identification of PAK6 associated proteins."
      Kaur R., Yuan X., Lu M.L., Balk S.P.
      Prostate 68:1510-1516(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IQGAP1 AND PPM1B.
    11. "Inhibition of p21-activated kinase 6 (PAK6) increases radiosensitivity of prostate cancer cells."
      Zhang M., Siedow M., Saia G., Chakravarti A.
      Prostate 70:807-816(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Crystal structure of the human p21-activated kinase 6."
      Filippakopoulos P., Berridge G., Bray J., Burgess N., Colebrook S., Das S., Eswaran J., Gileadi O., Papagrigoriou E., Savitsky P., Smee C., Turnbull A., Sundstrom M., Arrowsmith C., Weigelt J., Edwards A., Von Delft F., Knapp S.
      Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 383-681, PHOSPHORYLATION AT SER-560.
    13. "The crystal structure of human CDC42 in complex with the CRIB domain of human p21-activated kinase 6 (PAK6)."
      Structural genomics consortium (SGC)
      Submitted (JAN-2007) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 11-45 IN COMPLEX WITH CDC42.
    14. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-3.
    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: VARIANTS [LARGE SCALE ANALYSIS] VAL-76; LYS-184; GLU-205; THR-208; MET-210; ARG-215; LEU-337; VAL-376 AND ARG-514.

    Entry informationi

    Entry nameiPAK6_HUMAN
    AccessioniPrimary (citable) accession number: Q9NQU5
    Secondary accession number(s): A8K2G2, B3KYB0, G5E9R2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2002
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 135 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 15
      Human chromosome 15: 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

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