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Q9P286

- PAK7_HUMAN

UniProt

Q9P286 - PAK7_HUMAN

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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

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. learning Source: Ensembl
  7. locomotory behavior Source: Ensembl
  8. memory Source: Ensembl
  9. negative regulation of extrinsic apoptotic signaling pathway Source: Ensembl
  10. signal transduction Source: UniProtKB
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.

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
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 – 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

BgeeiQ9P286.
CleanExiHS_PAK7.
ExpressionAtlasiQ9P286. baseline and differential.
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. 14 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 – 4379Combined sources
Helixi445 – 4473Combined sources
Beta strandi449 – 4579Combined sources
Beta strandi459 – 46810Combined sources
Turni469 – 4713Combined sources
Beta strandi474 – 4818Combined sources
Helixi482 – 4843Combined sources
Helixi488 – 50013Combined sources
Beta strandi509 – 5157Combined sources
Beta strandi518 – 5247Combined sources
Helixi531 – 5355Combined sources
Helixi542 – 56120Combined sources
Helixi571 – 5733Combined sources
Beta strandi574 – 5763Combined sources
Beta strandi582 – 5843Combined sources
Beta strandi595 – 5973Combined sources
Helixi607 – 6093Combined sources
Helixi612 – 6154Combined sources
Helixi623 – 63816Combined sources
Turni642 – 6454Combined sources
Helixi648 – 65710Combined sources
Helixi666 – 6683Combined sources
Helixi671 – 68010Combined sources
Helixi685 – 6873Combined sources
Helixi691 – 6955Combined sources
Helixi698 – 7025Combined sources
Helixi706 – 7083Combined sources
Helixi710 – 7123Combined sources

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, 401-718.
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.
GeneTreeiENSGT00760000119176.
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.
[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

        10         20         30         40         50
MFGKKKKKIE ISGPSNFEHR VHTGFDPQEQ KFTGLPQQWH SLLADTANRP
60 70 80 90 100
KPMVDPSCIT PIQLAPMKTI VRGNKPCKET SINGLLEDFD NISVTRSNSL
110 120 130 140 150
RKESPPTPDQ GASSHGPGHA EENGFITFSQ YSSESDTTAD YTTEKYREKS
160 170 180 190 200
LYGDDLDPYY RGSHAAKQNG HVMKMKHGEA YYSEVKPLKS DFARFSADYH
210 220 230 240 250
SHLDSLSKPS EYSDLKWEYQ RASSSSPLDY SFQFTPSRTA GTSGCSKESL
260 270 280 290 300
AYSESEWGPS LDDYDRRPKS SYLNQTSPQP TMRQRSRSGS GLQEPMMPFG
310 320 330 340 350
ASAFKTHPQG HSYNSYTYPR LSEPTMCIPK VDYDRAQMVL SPPLSGSDTY
360 370 380 390 400
PRGPAKLPQS QSKSGYSSSS HQYPSGYHKA TLYHHPSLQS SSQYISTASY
410 420 430 440 450
LSSLSLSSST YPPPSWGSSS DQQPSRVSHE QFRAALQLVV SPGDPREYLA
460 470 480 490 500
NFIKIGEGST GIVCIATEKH TGKQVAVKKM DLRKQQRREL LFNEVVIMRD
510 520 530 540 550
YHHDNVVDMY SSYLVGDELW VVMEFLEGGA LTDIVTHTRM NEEQIATVCL
560 570 580 590 600
SVLRALSYLH NQGVIHRDIK SDSILLTSDG RIKLSDFGFC AQVSKEVPKR
610 620 630 640 650
KSLVGTPYWM APEVISRLPY GTEVDIWSLG IMVIEMIDGE PPYFNEPPLQ
660 670 680 690 700
AMRRIRDSLP PRVKDLHKVS SVLRGFLDLM LVREPSQRAT AQELLGHPFL
710
KLAGPPSCIV PLMRQYRHH
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, 401-718.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121402. 14 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.
GeneTreei ENSGT00760000119176.
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

Bgeei Q9P286.
CleanExi HS_PAK7.
ExpressionAtlasi Q9P286. baseline and differential.
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.
[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: October 29, 2014
This is version 147 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