Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9NQU5

- PAK6_HUMAN

UniProt

Q9NQU5 - PAK6_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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
Complete GO annotation...

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-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

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.
ExpressionAtlasiQ9NQU5. baseline.
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. 17 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
Beta strandi16 – 2712Combined sources
Turni28 – 314Combined sources
Beta strandi32 – 354Combined sources
Helixi38 – 447Combined sources
Helixi387 – 3959Combined sources
Helixi404 – 4063Combined sources
Beta strandi407 – 41610Combined sources
Beta strandi419 – 4268Combined sources
Turni427 – 4293Combined sources
Beta strandi432 – 4398Combined sources
Turni440 – 4423Combined sources
Helixi446 – 4483Combined sources
Helixi449 – 45810Combined sources
Beta strandi467 – 4737Combined sources
Beta strandi476 – 4816Combined sources
Helixi489 – 4935Combined sources
Helixi500 – 51920Combined sources
Helixi529 – 5313Combined sources
Beta strandi532 – 5343Combined sources
Beta strandi540 – 5423Combined sources
Helixi545 – 5473Combined sources
Beta strandi553 – 5553Combined sources
Helixi565 – 5673Combined sources
Helixi570 – 5734Combined sources
Helixi581 – 59616Combined sources
Turni600 – 6034Combined sources
Helixi606 – 61510Combined sources
Helixi624 – 6263Combined sources
Helixi629 – 63810Combined sources
Turni643 – 6453Combined sources
Helixi649 – 6535Combined sources
Helixi656 – 6605Combined sources
Helixi664 – 6707Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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, 340-674.
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.
GeneTreeiENSGT00760000119176.
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.
[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

        10         20         30         40         50
MFRKKKKKRP EISAPQNFQH RVHTSFDPKE GKFVGLPPQW QNILDTLRRP
60 70 80 90 100
KPVVDPSRIT RVQLQPMKTV VRGSAMPVDG YISGLLNDIQ KLSVISSNTL
110 120 130 140 150
RGRSPTSRRR AQSLGLLGDE HWATDPDMYL QSPQSERTDP HGLYLSCNGG
160 170 180 190 200
TPAGHKQMPW PEPQSPRVLP NGLAAKAQSL GPAEFQGASQ RCLQLGACLQ
210 220 230 240 250
SSPPGASPPT GTNRHGMKAA KHGSEEARPQ SCLVGSATGR PGGEGSPSPK
260 270 280 290 300
TRESSLKRRL FRSMFLSTAA TAPPSSSKPG PPPQSKPNSS FRPPQKDNPP
310 320 330 340 350
SLVAKAQSLP SDQPVGTFSP LTTSDTSSPQ KSLRTAPATG QLPGRSSPAG
360 370 380 390 400
SPRTWHAQIS TSNLYLPQDP TVAKGALAGE DTGVVTHEQF KAALRMVVDQ
410 420 430 440 450
GDPRLLLDSY VKIGEGSTGI VCLAREKHSG RQVAVKMMDL RKQQRRELLF
460 470 480 490 500
NEVVIMRDYQ HFNVVEMYKS YLVGEELWVL MEFLQGGALT DIVSQVRLNE
510 520 530 540 550
EQIATVCEAV LQALAYLHAQ GVIHRDIKSD SILLTLDGRV KLSDFGFCAQ
560 570 580 590 600
ISKDVPKRKS LVGTPYWMAP EVISRSLYAT EVDIWSLGIM VIEMVDGEPP
610 620 630 640 650
YFSDSPVQAM KRLRDSPPPK LKNSHKVSPV LRDFLERMLV RDPQERATAQ
660 670 680
ELLDHPFLLQ TGLPECLVPL IQLYRKQTST C
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:
EMBLi
GenBanki
DDBJi
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. [Q9NQU5-1]
RefSeqiNP_001122100.1. NM_001128628.2. [Q9NQU5-1]
NP_001122101.1. NM_001128629.2. [Q9NQU5-1]
NP_001263646.1. NM_001276717.1. [Q9NQU5-1]
NP_001263647.1. NM_001276718.1. [Q9NQU5-2]
NP_064553.1. NM_020168.5. [Q9NQU5-1]
UniGeneiHs.513645.
Hs.732375.
Hs.745440.

Genome annotation databases

EnsembliENST00000260404; ENSP00000260404; ENSG00000137843. [Q9NQU5-1]
ENST00000441369; ENSP00000406873; ENSG00000259288. [Q9NQU5-1]
ENST00000453867; ENSP00000401153; ENSG00000259288. [Q9NQU5-1]
ENST00000455577; ENSP00000409465; ENSG00000137843. [Q9NQU5-2]
ENST00000542403; ENSP00000439597; ENSG00000137843. [Q9NQU5-1]
ENST00000560346; ENSP00000453858; ENSG00000137843. [Q9NQU5-1]
GeneIDi56924.
KEGGihsa:56924.
UCSCiuc001zlb.3. human. [Q9NQU5-1]

Polymorphism databases

DMDMi23396789.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [Q9NQU5-1 ]
RefSeqi NP_001122100.1. NM_001128628.2. [Q9NQU5-1 ]
NP_001122101.1. NM_001128629.2. [Q9NQU5-1 ]
NP_001263646.1. NM_001276717.1. [Q9NQU5-1 ]
NP_001263647.1. NM_001276718.1. [Q9NQU5-2 ]
NP_064553.1. NM_020168.5. [Q9NQU5-1 ]
UniGenei Hs.513645.
Hs.732375.
Hs.745440.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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, 340-674.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121251. 17 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 . [Q9NQU5-1 ]
ENST00000441369 ; ENSP00000406873 ; ENSG00000259288 . [Q9NQU5-1 ]
ENST00000453867 ; ENSP00000401153 ; ENSG00000259288 . [Q9NQU5-1 ]
ENST00000455577 ; ENSP00000409465 ; ENSG00000137843 . [Q9NQU5-2 ]
ENST00000542403 ; ENSP00000439597 ; ENSG00000137843 . [Q9NQU5-1 ]
ENST00000560346 ; ENSP00000453858 ; ENSG00000137843 . [Q9NQU5-1 ]
GeneIDi 56924.
KEGGi hsa:56924.
UCSCi uc001zlb.3. human. [Q9NQU5-1 ]

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.
GeneTreei ENSGT00760000119176.
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 35518220.
PROi Q9NQU5.
SOURCEi Search...

Gene expression databases

Bgeei Q9NQU5.
CleanExi HS_PAK6.
ExpressionAtlasi Q9NQU5. baseline.
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.
[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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 137 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

Dasty 3