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UniProtKB - Q13153 (PAK1_HUMAN)

Protein

Serine/threonine-protein kinase PAK 1

Gene

PAK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Protein kinase involved in intracellular signaling pathways downstream of integrins and receptor-type kinases that plays an important role in cytoskeleton dynamics, in cell adhesion, migration, proliferation, apoptosis, mitosis, and in vesicle-mediated transport processes. Can directly phosphorylate BAD and protects cells against apoptosis. Activated by interaction with CDC42 and RAC1. Functions as GTPase effector that links the Rho-related GTPases CDC42 and RAC1 to the JNK MAP kinase pathway. Phosphorylates and activates MAP2K1, and thereby mediates activation of downstream MAP kinases. Involved in the reorganization of the actin cytoskeleton, actin stress fibers and of focal adhesion complexes. Phosphorylates the tubulin chaperone TBCB and thereby plays a role in the regulation of microtubule biogenesis and organization of the tubulin cytoskeleton. Plays a role in the regulation of insulin secretion in response to elevated glucose levels. Part of a ternary complex that contains PAK1, DVL1 and MUSK that is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ). Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2. Phosphorylates MYL9/MLC2. Phosphorylates RAF1 at 'Ser-338' and 'Ser-339' resulting in: activation of RAF1, stimulation of RAF1 translocation to mitochondria, phosphorylation of BAD by RAF1, and RAF1 binding to BCL2. Phosphorylates SNAI1 at 'Ser-246' promoting its transcriptional repressor activity by increasing its accumulation in the nucleus. In podocytes, promotes NR3C2 nuclear localization. Required for atypical chemokine receptor ACKR2-induced phosphorylation of LIMK1 and cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3, maybe through CFL1 phosphorylation and inactivation. Plays a role in RUFY3-mediated facilitating gastric cancer cells migration and invasion (PubMed:25766321).18 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.3 Publications

Cofactori

Mg2+

Activity regulationi

Phosphorylation of Thr-84 by OXSR1 inhibits activation (By similarity). Activated by binding small G proteins. Binding of GTP-bound CDC42 or RAC1 to the autoregulatory region releases monomers from the autoinhibited dimer, and enables activation by phosphorylation of Thr-423.By similarity4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei299ATP1
Active sitei389Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi276 – 284ATP9
Nucleotide bindingi345 – 347ATP3

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • collagen binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • protein kinase activity Source: UniProtKB
  • protein kinase binding Source: Ensembl
  • protein serine/threonine kinase activity Source: UniProtKB
  • Rac GTPase binding Source: GO_Central
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionAllosteric enzyme, Kinase, Serine/threonine-protein kinase, Transferase
Biological processApoptosis, Exocytosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1 2681
ReactomeiR-HSA-202433 Generation of second messenger molecules
R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation
R-HSA-2871796 FCERI mediated MAPK activation
R-HSA-376172 DSCAM interactions
R-HSA-389359 CD28 dependent Vav1 pathway
R-HSA-3928662 EPHB-mediated forward signaling
R-HSA-3928664 Ephrin signaling
R-HSA-399954 Sema3A PAK dependent Axon repulsion
R-HSA-428540 Activation of RAC1
R-HSA-445144 Signal transduction by L1
R-HSA-445355 Smooth Muscle Contraction
R-HSA-5218920 VEGFR2 mediated vascular permeability
R-HSA-5621575 CD209 (DC-SIGN) signaling
R-HSA-5625740 RHO GTPases activate PKNs
R-HSA-5627117 RHO GTPases Activate ROCKs
R-HSA-5627123 RHO GTPases activate PAKs
R-HSA-5687128 MAPK6/MAPK4 signaling
SignaLinkiQ13153
SIGNORiQ13153

Protein family/group databases

MoonDBiQ13153 Predicted

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase PAK 11 Publication (EC:2.7.11.13 Publications)
Alternative name(s):
Alpha-PAK1 Publication
p21-activated kinase 11 Publication
Short name:
PAK-1
p65-PAKBy similarity
Gene namesi
Name:PAK1Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000149269.9
HGNCiHGNC:8590 PAK1
MIMi602590 gene
neXtProtiNX_Q13153

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi83H → L: Abolishes interaction with CDC42, leading to strongly decreased activity; when associated with L-86. 2 Publications1
Mutagenesisi86H → L: Abolishes interaction with CDC42, leading to strongly decreased activity; when associated with L-83. 2 Publications1
Mutagenesisi107L → F: Abolishes autoinhibition, leading to constitutive kinase activity. 1 Publication1
Mutagenesisi299K → R: Strongly decreases activity. Abolishes kinase activity; when associated with N-389. 1 Publication1
Mutagenesisi389D → N: Abolishes kinase activity; when associated with R-299. 1 Publication1
Mutagenesisi393D → A: Abolishes autophosphorylation at Thr-423. 1
Mutagenesisi423T → A: Decreases CDC42-stimulated activity and autophosphorylation. 1 Publication1
Mutagenesisi423T → E: Constitutive kinase activity. 1 Publication1

Organism-specific databases

DisGeNETi5058
OpenTargetsiENSG00000149269
PharmGKBiPA32917

Chemistry databases

ChEMBLiCHEMBL4600
GuidetoPHARMACOLOGYi2133

Polymorphism and mutation databases

BioMutaiPAK1
DMDMi90111767

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000864602 – 545Serine/threonine-protein kinase PAK 1Add BLAST544

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei21Phosphoserine; by PKB and autocatalysis2 Publications1
Modified residuei57Phosphoserine; by autocatalysis1 Publication1
Modified residuei84Phosphothreonine; by OXSR1By similarity1
Modified residuei115PhosphoserineCombined sources1
Modified residuei131Phosphotyrosine1 Publication1
Modified residuei142Phosphotyrosine1 Publication1
Modified residuei144PhosphoserineCombined sources1
Modified residuei149PhosphoserineCombined sources1
Modified residuei153Phosphotyrosine; by JAK22 Publications1
Modified residuei174PhosphoserineCombined sources1 Publication1
Modified residuei185Phosphothreonine1 Publication1
Modified residuei199Phosphoserine; by autocatalysisBy similarity1
Modified residuei201Phosphotyrosine; by JAK21 Publication1
Modified residuei204PhosphoserineCombined sources1
Modified residuei212PhosphothreonineCombined sources1 Publication1
Modified residuei219PhosphothreonineCombined sources1
Modified residuei220PhosphoserineCombined sources1
Modified residuei223PhosphoserineCombined sources1
Modified residuei225PhosphothreonineBy similarity1
Modified residuei229PhosphothreonineBy similarity1
Modified residuei230PhosphothreonineCombined sources1
Modified residuei285Phosphotyrosine; by JAK22 Publications1
Modified residuei423Phosphothreonine; by autocatalysis, BRSK2 and PDPK14 Publications1

Post-translational modificationi

Autophosphorylated in trans, meaning that in a dimer, one kinase molecule phosphorylates the other one. Activated by autophosphorylation at Thr-423 in response to a conformation change, triggered by interaction with GTP-bound CDC42 or RAC1. Activated by phosphorylation at Thr-423 by BRSK2 and by PDPK1. Phosphorylated by JAK2 in response to PRL; this increases PAK1 kinase activity. Phosphorylated at Ser-21 by PKB/AKT; this reduces interaction with NCK1 and association with focal adhesion sites.8 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ13153
MaxQBiQ13153
PaxDbiQ13153
PeptideAtlasiQ13153
PRIDEiQ13153
ProteomicsDBi59193
59194 [Q13153-2]

PTM databases

iPTMnetiQ13153
PhosphoSitePlusiQ13153

Expressioni

Tissue specificityi

Overexpressed in gastric cancer cells and tissues (at protein level) (PubMed:25766321).1 Publication

Gene expression databases

BgeeiENSG00000149269 Expressed in 203 organ(s), highest expression level in middle temporal gyrus
CleanExiHS_PAK1
ExpressionAtlasiQ13153 baseline and differential
GenevisibleiQ13153 HS

Organism-specific databases

HPAiCAB005312
HPA003565

Interactioni

Subunit structurei

Homodimer in its autoinhibited state. Active as monomer. Component of cytoplasmic complexes, which also contains PXN, ARHGEF6 and GIT1. Interacts with NISCH (By similarity). Interacts with DVL1; mediates the formation of a DVL1, MUSK and PAK1 ternary complex involved in AChR clustering (By similarity). Binds to the caspase-cleaved p110 isoform of CDC2L1 and CDC2L2, p110C, but not the full-length proteins (PubMed:12624090). Interacts with ARHGEF7 (PubMed:16101281). Interacts tightly with GTP-bound but not GDP-bound CDC42/P21 and RAC1 (By similarity). Probably found in a ternary complex composed of DSCAM, PAK1 and RAC1. Interacts with DSCAM (via cytoplasmic domain); the interaction is direct and enhanced in presence of RAC1 (PubMed:15169762). Interacts with SCRIB (PubMed:18716323). Interacts with PDPK1 (PubMed:10995762). Interacts (via kinase domain) with RAF1 (PubMed:11733498). Interacts with NCK1 and NCK2 (PubMed:10026169). Interacts with TBCB (PubMed:15831477). Interacts with CRIPAK (PubMed:16278681). Interacts with BRSK2 (By similarity). Interacts with SNAI1 (PubMed:15833848). Interacts with CIB1 isoform 2 (PubMed:23503467). Interacts with CIB1 (via N-terminal region); the interaction is direct, promotes PAK1 activity and occurs in a calcium-dependent manner. Interacts with INPP5K (PubMed:26940976).By similarity19 Publications

Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi111095, 89 interactors
CORUMiQ13153
DIPiDIP-31016N
ELMiQ13153
IntActiQ13153, 65 interactors
MINTiQ13153
STRINGi9606.ENSP00000278568

Chemistry databases

BindingDBiQ13153

Structurei

Secondary structure

1545
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ13153
SMRiQ13153
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13153

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini75 – 88CRIBPROSITE-ProRule annotationAdd BLAST14
Domaini270 – 521Protein kinasePROSITE-ProRule annotationAdd BLAST252

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni70 – 140Autoregulatory regionAdd BLAST71
Regioni75 – 105GTPase-bindingAdd BLAST31
Regioni132 – 270Interaction with CRIPAK1 PublicationAdd BLAST139

Sequence similaritiesi

Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.Curated

Phylogenomic databases

eggNOGiKOG0578 Eukaryota
ENOG410XP4K LUCA
GeneTreeiENSGT00930000150829
HOGENOMiHOG000234202
HOVERGENiHBG108518
InParanoidiQ13153
KOiK04409
OMAiTKMVGVV
OrthoDBiEOG091G04H8
PhylomeDBiQ13153
TreeFamiTF105351

Family and domain databases

CDDicd01093 CRIB_PAK_like, 1 hit
Gene3Di3.90.810.10, 1 hit
InterProiView protein in InterPro
IPR000095 CRIB_dom
IPR036936 CRIB_dom_sf
IPR011009 Kinase-like_dom_sf
IPR033923 PAK_BD
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00786 PBD, 1 hit
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00285 PBD, 1 hit
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50108 CRIB, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 10 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q13153-1) [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
MSNNGLDIQD KPPAPPMRNT STMIGAGSKD AGTLNHGSKP LPPNPEEKKK 
        60         70         80         90        100
KDRFYRSILP GDKTNKKKEK ERPEISLPSD FEHTIHVGFD AVTGEFTGMP 
       110        120        130        140        150
EQWARLLQTS NITKSEQKKN PQAVLDVLEF YNSKKTSNSQ KYMSFTDKSA 
       160        170        180        190        200
EDYNSSNALN VKAVSETPAV PPVSEDEDDD DDDATPPPVI APRPEHTKSV 
       210        220        230        240        250
YTRSVIEPLP VTPTRDVATS PISPTENNTT PPDALTRNTE KQKKKPKMSD 
       260        270        280        290        300
EEILEKLRSI VSVGDPKKKY TRFEKIGQGA SGTVYTAMDV ATGQEVAIKQ 
       310        320        330        340        350
MNLQQQPKKE LIINEILVMR ENKNPNIVNY LDSYLVGDEL WVVMEYLAGG 
       360        370        380        390        400
SLTDVVTETC MDEGQIAAVC RECLQALEFL HSNQVIHRDI KSDNILLGMD 
       410        420        430        440        450
GSVKLTDFGF CAQITPEQSK RSTMVGTPYW MAPEVVTRKA YGPKVDIWSL 
       460        470        480        490        500
GIMAIEMIEG EPPYLNENPL RALYLIATNG TPELQNPEKL SAIFRDFLNR 
       510        520        530        540 
CLEMDVEKRG SAKELLQHQF LKIAKPLSSL TPLIAAAKEA TKNNH
Length:545
Mass (Da):60,647
Last modified:March 7, 2006 - v2
Checksum:i1A95CD5F2195CD7B
GO
Isoform 2 (identifier: Q13153-2) [UniParc]FASTAAdd to basket
Also known as: PAK1B

The sequence of this isoform differs from the canonical sequence as follows:
     518-545: HQFLKIAKPLSSLTPLIAAAKEATKNNH → VRKLRFQVFSNFSMIAASIPEDCQAPLQPHSTDCCS

Show »
Length:553
Mass (Da):61,632
Checksum:i6A3BB134DD2A82A8
GO

Computationally mapped potential isoform sequencesi

There are 10 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B3KNX7B3KNX7_HUMAN
Non-specific serine/threonine prote...
PAK1
522Annotation score:
E9PM17E9PM17_HUMAN
Serine/threonine-protein kinase PAK...
PAK1
455Annotation score:
H0YCG5H0YCG5_HUMAN
Serine/threonine-protein kinase PAK...
PAK1
244Annotation score:
E9PKH9E9PKH9_HUMAN
Serine/threonine-protein kinase PAK...
PAK1
106Annotation score:
E9PQW5E9PQW5_HUMAN
Serine/threonine-protein kinase PAK...
PAK1
99Annotation score:
E9PMP2E9PMP2_HUMAN
Serine/threonine-protein kinase PAK...
PAK1
89Annotation score:
H0YCM0H0YCM0_HUMAN
Serine/threonine-protein kinase PAK...
PAK1
167Annotation score:
E9PRP6E9PRP6_HUMAN
Serine/threonine-protein kinase PAK...
PAK1
63Annotation score:
E9PJF8E9PJF8_HUMAN
Serine/threonine-protein kinase PAK...
PAK1
26Annotation score:
H0YF55H0YF55_HUMAN
Serine/threonine-protein kinase PAK...
PAK1
18Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti26A → V in AAA65441 (PubMed:9395435).Curated1
Sequence conflicti26A → V in AAC24716 (Ref. 3) Curated1
Sequence conflicti237R → L in AAC50590 (PubMed:8805275).Curated1
Sequence conflicti379F → S in AAC50590 (PubMed:8805275).Curated1
Sequence conflicti503E → D in AAA65441 (PubMed:9395435).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_051654515L → V. Corresponds to variant dbSNP:rs35345144Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_017507518 – 545HQFLK…TKNNH → VRKLRFQVFSNFSMIAASIP EDCQAPLQPHSTDCCS in isoform 2. 1 PublicationAdd BLAST28

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51120 mRNA Translation: AAC50590.1
U24152 mRNA Translation: AAA65441.1
AF071884 mRNA Translation: AAC24716.1
AP000486 Genomic DNA No translation available.
AP003680 Genomic DNA No translation available.
BC109299 mRNA Translation: AAI09300.1
CCDSiCCDS44687.1 [Q13153-2]
CCDS8250.1 [Q13153-1]
PIRiG01773
RefSeqiNP_001122092.1, NM_001128620.1 [Q13153-2]
NP_002567.3, NM_002576.4 [Q13153-1]
XP_011543382.1, XM_011545080.2 [Q13153-2]
XP_011543383.1, XM_011545081.2 [Q13153-2]
XP_011543384.1, XM_011545082.2 [Q13153-2]
XP_011543385.1, XM_011545083.2 [Q13153-2]
XP_011543386.1, XM_011545084.2 [Q13153-2]
XP_016873335.1, XM_017017846.1 [Q13153-1]
XP_016873336.1, XM_017017847.1 [Q13153-1]
XP_016873337.1, XM_017017848.1 [Q13153-1]
XP_016873338.1, XM_017017849.1 [Q13153-1]
XP_016873339.1, XM_017017850.1 [Q13153-1]
UniGeneiHs.435714

Genome annotation databases

EnsembliENST00000278568; ENSP00000278568; ENSG00000149269 [Q13153-2]
ENST00000356341; ENSP00000348696; ENSG00000149269 [Q13153-1]
GeneIDi5058
KEGGihsa:5058
UCSCiuc001oyg.5 human [Q13153-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51120 mRNA Translation: AAC50590.1
U24152 mRNA Translation: AAA65441.1
AF071884 mRNA Translation: AAC24716.1
AP000486 Genomic DNA No translation available.
AP003680 Genomic DNA No translation available.
BC109299 mRNA Translation: AAI09300.1
CCDSiCCDS44687.1 [Q13153-2]
CCDS8250.1 [Q13153-1]
PIRiG01773
RefSeqiNP_001122092.1, NM_001128620.1 [Q13153-2]
NP_002567.3, NM_002576.4 [Q13153-1]
XP_011543382.1, XM_011545080.2 [Q13153-2]
XP_011543383.1, XM_011545081.2 [Q13153-2]
XP_011543384.1, XM_011545082.2 [Q13153-2]
XP_011543385.1, XM_011545083.2 [Q13153-2]
XP_011543386.1, XM_011545084.2 [Q13153-2]
XP_016873335.1, XM_017017846.1 [Q13153-1]
XP_016873336.1, XM_017017847.1 [Q13153-1]
XP_016873337.1, XM_017017848.1 [Q13153-1]
XP_016873338.1, XM_017017849.1 [Q13153-1]
XP_016873339.1, XM_017017850.1 [Q13153-1]
UniGeneiHs.435714

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F3MX-ray2.30A/B70-149[»]
C/D249-545[»]
1YHVX-ray1.80A249-545[»]
1YHWX-ray1.80A249-545[»]
1ZSGNMR-B183-204[»]
2HY8X-ray2.001249-545[»]
2QMEX-ray1.75I74-109[»]
3DVPX-ray2.50C/D212-221[»]
3FXZX-ray1.64A249-545[»]
3FY0X-ray2.35A249-545[»]
3Q4ZX-ray1.89A/B248-545[»]
3Q52X-ray1.80A248-545[»]
3Q53X-ray2.09A248-545[»]
4DAWX-ray2.00A249-545[»]
4EQCX-ray2.01A249-545[»]
4O0RX-ray2.40A/B249-545[»]
4O0TX-ray2.60A/B249-545[»]
4P90X-ray2.49A/B249-545[»]
4ZJIX-ray1.99A/B/C/D249-545[»]
4ZJJX-ray2.20A/B/C/D249-545[»]
4ZLOX-ray2.50A/B249-545[»]
4ZY4X-ray2.60A/B249-545[»]
4ZY5X-ray2.35A/B249-545[»]
4ZY6X-ray2.15A/B249-545[»]
5DEWX-ray1.90A/B249-545[»]
5DEYX-ray2.10A/B249-545[»]
5DFPX-ray2.20A249-545[»]
5IMEX-ray2.22A/B249-545[»]
5KBQX-ray2.58A/B254-542[»]
5KBRX-ray2.36A/B254-542[»]
6B16X-ray2.29A/B249-545[»]
ProteinModelPortaliQ13153
SMRiQ13153
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111095, 89 interactors
CORUMiQ13153
DIPiDIP-31016N
ELMiQ13153
IntActiQ13153, 65 interactors
MINTiQ13153
STRINGi9606.ENSP00000278568

Chemistry databases

BindingDBiQ13153
ChEMBLiCHEMBL4600
GuidetoPHARMACOLOGYi2133

Protein family/group databases

MoonDBiQ13153 Predicted

PTM databases

iPTMnetiQ13153
PhosphoSitePlusiQ13153

Polymorphism and mutation databases

BioMutaiPAK1
DMDMi90111767

Proteomic databases

EPDiQ13153
MaxQBiQ13153
PaxDbiQ13153
PeptideAtlasiQ13153
PRIDEiQ13153
ProteomicsDBi59193
59194 [Q13153-2]

Protocols and materials databases

DNASUi5058
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000278568; ENSP00000278568; ENSG00000149269 [Q13153-2]
ENST00000356341; ENSP00000348696; ENSG00000149269 [Q13153-1]
GeneIDi5058
KEGGihsa:5058
UCSCiuc001oyg.5 human [Q13153-1]

Organism-specific databases

CTDi5058
DisGeNETi5058
EuPathDBiHostDB:ENSG00000149269.9
GeneCardsiPAK1
HGNCiHGNC:8590 PAK1
HPAiCAB005312
HPA003565
MIMi602590 gene
neXtProtiNX_Q13153
OpenTargetsiENSG00000149269
PharmGKBiPA32917
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0578 Eukaryota
ENOG410XP4K LUCA
GeneTreeiENSGT00930000150829
HOGENOMiHOG000234202
HOVERGENiHBG108518
InParanoidiQ13153
KOiK04409
OMAiTKMVGVV
OrthoDBiEOG091G04H8
PhylomeDBiQ13153
TreeFamiTF105351

Enzyme and pathway databases

BRENDAi2.7.11.1 2681
ReactomeiR-HSA-202433 Generation of second messenger molecules
R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation
R-HSA-2871796 FCERI mediated MAPK activation
R-HSA-376172 DSCAM interactions
R-HSA-389359 CD28 dependent Vav1 pathway
R-HSA-3928662 EPHB-mediated forward signaling
R-HSA-3928664 Ephrin signaling
R-HSA-399954 Sema3A PAK dependent Axon repulsion
R-HSA-428540 Activation of RAC1
R-HSA-445144 Signal transduction by L1
R-HSA-445355 Smooth Muscle Contraction
R-HSA-5218920 VEGFR2 mediated vascular permeability
R-HSA-5621575 CD209 (DC-SIGN) signaling
R-HSA-5625740 RHO GTPases activate PKNs
R-HSA-5627117 RHO GTPases Activate ROCKs
R-HSA-5627123 RHO GTPases activate PAKs
R-HSA-5687128 MAPK6/MAPK4 signaling
SignaLinkiQ13153
SIGNORiQ13153

Miscellaneous databases

ChiTaRSiPAK1 human
EvolutionaryTraceiQ13153
GeneWikiiPAK1
GenomeRNAii5058
PROiPR:Q13153
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000149269 Expressed in 203 organ(s), highest expression level in middle temporal gyrus
CleanExiHS_PAK1
ExpressionAtlasiQ13153 baseline and differential
GenevisibleiQ13153 HS

Family and domain databases

CDDicd01093 CRIB_PAK_like, 1 hit
Gene3Di3.90.810.10, 1 hit
InterProiView protein in InterPro
IPR000095 CRIB_dom
IPR036936 CRIB_dom_sf
IPR011009 Kinase-like_dom_sf
IPR033923 PAK_BD
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00786 PBD, 1 hit
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00285 PBD, 1 hit
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50108 CRIB, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPAK1_HUMAN
AccessioniPrimary (citable) accession number: Q13153
Secondary accession number(s): O75561
, Q13567, Q32M53, Q32M54, Q86W79
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 7, 2006
Last modified: November 7, 2018
This is version 209 of the entry and version 2 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  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 chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  7. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
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Main funding by: National Institutes of Health

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