SubmitCancel

Skip Header

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

Q9P286

- PAK7_HUMAN

UniProt

Q9P286 - PAK7_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 7

Gene
PAK7, KIAA1264, PAK5
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 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 – 4781ATP By similarity
Active sitei568 – 5681Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi455 – 4639ATP By similarity

GO - Molecular functioni

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

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
  8. signal transduction by phosphorylation Source: GOC
Complete GO annotation...

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.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: RefGenome
  2. mitochondrion Source: UniProtKB-SubCell
  3. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

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 – 1041Phosphoserine By similarity
Modified residuei107 – 1071Phosphothreonine By 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. 2 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.

Miscellaneous databases

EvolutionaryTraceiQ9P286.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 2414CRIBAdd
BLAST
Domaini449 – 700252Protein kinaseAdd
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.

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

« Hide

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. 2 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 145 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

Similar proteinsi