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Protein

Serine/threonine-protein kinase PAK 5

Gene

PAK5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei478ATPPROSITE-ProRule annotation1
Active sitei568Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi455 – 463ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

  • apoptotic process Source: UniProtKB
  • cell growth Source: UniProtKB
  • cell migration Source: UniProtKB
  • cell proliferation Source: UniProtKB
  • cytoskeleton organization Source: UniProtKB
  • learning Source: Ensembl
  • locomotory behavior Source: Ensembl
  • memory Source: Ensembl
  • negative regulation of extrinsic apoptotic signaling pathway Source: Ensembl
  • 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

BioCyciZFISH:HS02251-MONOMER.
BRENDAi2.7.11.1. 2681.
2.7.12.2. 2681.
ReactomeiR-HSA-428540. Activation of Rac.
SignaLinkiQ9P286.
SIGNORiQ9P286.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase PAK 5Curated (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:PAK5Imported
Synonyms:KIAA1264, PAK7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:15916. PAK5.

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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi19 – 22HRVH → LRVL: Complete loss of CDC42 binding and CDC42-mediated autophosphorylation. 1 Publication4

Organism-specific databases

DisGeNETi57144.
OpenTargetsiENSG00000101349.
PharmGKBiPA32922.

Chemistry databases

ChEMBLiCHEMBL4524.
GuidetoPHARMACOLOGYi2138.

Polymorphism and mutation databases

BioMutaiPAK7.
DMDMi12585290.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000864771 – 719Serine/threonine-protein kinase PAK 5Add BLAST719

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei104PhosphoserineBy similarity1
Modified residuei107PhosphothreonineBy similarity1

Post-translational modificationi

Autophosphorylated when activated by CDC42/p21.

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9P286.
MaxQBiQ9P286.
PaxDbiQ9P286.
PeptideAtlasiQ9P286.
PRIDEiQ9P286.

PTM databases

iPTMnetiQ9P286.
PhosphoSitePlusiQ9P286.

Expressioni

Tissue specificityi

Predominantly expressed in brain.

Gene expression databases

BgeeiENSG00000101349.
CleanExiHS_PAK7.
GenevisibleiQ9P286. HS.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC42P609533EBI-1051061,EBI-81752

Protein-protein interaction databases

BioGridi121402. 68 interactors.
IntActiQ9P286. 14 interactors.
MINTiMINT-1443173.
STRINGi9606.ENSP00000322957.

Chemistry databases

BindingDBiQ9P286.

Structurei

Secondary structure

1719
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi429 – 437Combined sources9
Helixi445 – 447Combined sources3
Beta strandi449 – 457Combined sources9
Beta strandi459 – 468Combined sources10
Turni469 – 471Combined sources3
Beta strandi474 – 481Combined sources8
Helixi482 – 484Combined sources3
Helixi488 – 500Combined sources13
Beta strandi509 – 515Combined sources7
Beta strandi518 – 524Combined sources7
Helixi531 – 535Combined sources5
Helixi542 – 561Combined sources20
Helixi571 – 573Combined sources3
Beta strandi574 – 576Combined sources3
Beta strandi582 – 584Combined sources3
Beta strandi595 – 597Combined sources3
Helixi607 – 609Combined sources3
Helixi612 – 615Combined sources4
Helixi623 – 638Combined sources16
Turni642 – 645Combined sources4
Helixi648 – 657Combined sources10
Helixi666 – 668Combined sources3
Helixi671 – 680Combined sources10
Helixi685 – 687Combined sources3
Helixi691 – 695Combined sources5
Helixi698 – 702Combined sources5
Helixi706 – 708Combined sources3
Helixi710 – 712Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2F57X-ray1.80A/B425-719[»]
ProteinModelPortaliQ9P286.
SMRiQ9P286.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9P286.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 24CRIBPROSITE-ProRule annotationAdd BLAST14
Domaini449 – 700Protein kinasePROSITE-ProRule annotationAdd BLAST252

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni25 – 448LinkerAdd BLAST424

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi4 – 8Poly-Lys5
Compositional biasi223 – 226Poly-Ser4
Compositional biasi367 – 370Poly-Ser4

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

eggNOGiKOG0578. Eukaryota.
ENOG410XP4K. LUCA.
GeneTreeiENSGT00860000133680.
HOGENOMiHOG000234205.
HOVERGENiHBG108518.
InParanoidiQ9P286.
KOiK05736.
OMAiNQTSPQP.
OrthoDBiEOG091G0OT5.
PhylomeDBiQ9P286.
TreeFamiTF105352.

Family and domain databases

CDDicd01093. CRIB_PAK_like. 1 hit.
Gene3Di3.90.810.10. 1 hit.
InterProiIPR000095. CRIB_dom.
IPR011009. Kinase-like_dom.
IPR028754. PAK7.
IPR033923. PAK_BD.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
[Graphical view]
PANTHERiPTHR24361:SF183. PTHR24361:SF183. 2 hits.
PfamiPF00786. PBD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00285. PBD. 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 differs from that shown. Reason: Erroneous initiation.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_040978118G → D.1 PublicationCorresponds to variant rs55923311dbSNPEnsembl.1
Natural variantiVAR_040979187P → A.1 PublicationCorresponds to variant rs34280805dbSNPEnsembl.1
Natural variantiVAR_040980312S → P in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_040981335R → P.1 PublicationCorresponds to variant rs11700112dbSNPEnsembl.1
Natural variantiVAR_021865511S → N.2 PublicationsCorresponds to variant rs2297345dbSNPEnsembl.1
Natural variantiVAR_040982538T → N in a lung adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_040983555A → S.1 PublicationCorresponds to variant rs34102290dbSNPEnsembl.1
Natural variantiVAR_040984604V → I in a metastatic melanoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_040985704G → S in a metastatic melanoma sample; somatic mutation. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_016883449.1. XM_017027960.1.
XP_016883450.1. XM_017027961.1.
XP_016883451.1. XM_017027962.1.
XP_016883452.1. XM_017027963.1.
XP_016883453.1. XM_017027964.1.
XP_016883454.1. XM_017027965.1.
UniGeneiHs.32539.

Genome annotation databases

EnsembliENST00000353224; ENSP00000322957; ENSG00000101349.
ENST00000378423; ENSP00000367679; ENSG00000101349.
ENST00000378429; ENSP00000367686; ENSG00000101349.
GeneIDi57144.
KEGGihsa:57144.
UCSCiuc002wnj.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_016883449.1. XM_017027960.1.
XP_016883450.1. XM_017027961.1.
XP_016883451.1. XM_017027962.1.
XP_016883452.1. XM_017027963.1.
XP_016883453.1. XM_017027964.1.
XP_016883454.1. XM_017027965.1.
UniGeneiHs.32539.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2F57X-ray1.80A/B425-719[»]
ProteinModelPortaliQ9P286.
SMRiQ9P286.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121402. 68 interactors.
IntActiQ9P286. 14 interactors.
MINTiMINT-1443173.
STRINGi9606.ENSP00000322957.

Chemistry databases

BindingDBiQ9P286.
ChEMBLiCHEMBL4524.
GuidetoPHARMACOLOGYi2138.

PTM databases

iPTMnetiQ9P286.
PhosphoSitePlusiQ9P286.

Polymorphism and mutation databases

BioMutaiPAK7.
DMDMi12585290.

Proteomic databases

EPDiQ9P286.
MaxQBiQ9P286.
PaxDbiQ9P286.
PeptideAtlasiQ9P286.
PRIDEiQ9P286.

Protocols and materials databases

DNASUi57144.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000353224; ENSP00000322957; ENSG00000101349.
ENST00000378423; ENSP00000367679; ENSG00000101349.
ENST00000378429; ENSP00000367686; ENSG00000101349.
GeneIDi57144.
KEGGihsa:57144.
UCSCiuc002wnj.3. human.

Organism-specific databases

CTDi57144.
DisGeNETi57144.
GeneCardsiPAK7.
HGNCiHGNC:15916. PAK5.
HPAiHPA020444.
MIMi608038. gene.
neXtProtiNX_Q9P286.
OpenTargetsiENSG00000101349.
PharmGKBiPA32922.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0578. Eukaryota.
ENOG410XP4K. LUCA.
GeneTreeiENSGT00860000133680.
HOGENOMiHOG000234205.
HOVERGENiHBG108518.
InParanoidiQ9P286.
KOiK05736.
OMAiNQTSPQP.
OrthoDBiEOG091G0OT5.
PhylomeDBiQ9P286.
TreeFamiTF105352.

Enzyme and pathway databases

BioCyciZFISH:HS02251-MONOMER.
BRENDAi2.7.11.1. 2681.
2.7.12.2. 2681.
ReactomeiR-HSA-428540. Activation of Rac.
SignaLinkiQ9P286.
SIGNORiQ9P286.

Miscellaneous databases

ChiTaRSiPAK7. human.
EvolutionaryTraceiQ9P286.
GeneWikiiPAK7.
GenomeRNAii57144.
PROiQ9P286.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000101349.
CleanExiHS_PAK7.
GenevisibleiQ9P286. HS.

Family and domain databases

CDDicd01093. CRIB_PAK_like. 1 hit.
Gene3Di3.90.810.10. 1 hit.
InterProiIPR000095. CRIB_dom.
IPR011009. Kinase-like_dom.
IPR028754. PAK7.
IPR033923. PAK_BD.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
[Graphical view]
PANTHERiPTHR24361:SF183. PTHR24361:SF183. 2 hits.
PfamiPF00786. PBD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00285. PBD. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiPAK5_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: November 30, 2016
This is version 170 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.