Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O96013 (PAK4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase PAK 4

EC=2.7.11.1
Alternative name(s):
p21-activated kinase 4
Short name=PAK-4
Gene names
Name:PAK4
Synonyms:KIAA1142
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length591 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, growth, 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 and inactivates the protein phosphatase SSH1, leading to increased inhibitory phosphorylation of the actin binding/depolymerizing factor cofilin. Decreased cofilin activity may lead to stabilization of actin filaments. Phosphorylates LIMK1, a kinase that also inhibits the activity of cofilin. Phosphorylates integrin beta5/ITGB5 and thus regulates cell motility. Phosphorylates ARHGEF2 and activates the downstream target RHOA that plays a role in the regulation of assembly of focal adhesions and actin stress fibers. Stimulates cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Alternatively, inhibits apoptosis by preventing caspase-8 binding to death domain receptors in a kinase independent manner. Plays a role in cell-cycle progression by controlling levels of the cell-cycle regulatory protein CDKN1A and by phosphorylating RAN. Ref.8 Ref.9 Ref.11 Ref.12 Ref.19 Ref.20 Ref.21

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Interacts with FGFR2 and GRB2 By similarity. Interacts tightly with GTP-bound but not GDP-bound CDC42/p21 and weakly with RAC1. Ref.13

Subcellular location

Cytoplasm. Note: Seems to shuttle between cytoplasmic compartments depending on the activating effector. For example, can be found on the cell periphery after activation of growth-factor or integrin-mediated signaling pathways. Ref.10

Tissue specificity

Highest expression in prostate, testis and colon.

Post-translational modification

Autophosphorylated on serine residues when activated by CDC42/p21. Ref.27

Phosphorylated on tyrosine residues upon stimulation of FGFR2 By similarity. Ref.27

Sequence similarities

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

Contains 1 CRIB domain.

Contains 1 protein kinase domain.

Sequence caution

The sequence BAA86456.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAC11166.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processApoptosis
Cell cycle
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Traceable author statement Ref.23. Source: UniProtKB

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell growth

Traceable author statement Ref.23. Source: UniProtKB

cell migration

Traceable author statement Ref.23. Source: UniProtKB

cell proliferation

Traceable author statement Ref.23. Source: UniProtKB

cellular component movement

Traceable author statement Ref.1. Source: ProtInc

cytoskeleton organization

Traceable author statement Ref.23. Source: UniProtKB

signal transduction

Traceable author statement Ref.23. Source: UniProtKB

signal transduction by phosphorylation

Inferred from Biological aspect of Ancestor. Source: GOC

   Cellular_componentGolgi apparatus

Traceable author statement Ref.1. Source: ProtInc

cytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 20936779PubMed 22653441. Source: IntAct

protein kinase activity

Non-traceable author statement Ref.1. Source: ProtInc

receptor signaling protein serine/threonine kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CDC42P609532EBI-713738,EBI-81752

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O96013-1)

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.
Isoform 2 (identifier: O96013-2)

The sequence of this isoform differs from the canonical sequence as follows:
     120-120: E → K
     121-285: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: O96013-3)

The sequence of this isoform differs from the canonical sequence as follows:
     69-221: Missing.
Isoform 4 (identifier: O96013-4)

The sequence of this isoform differs from the canonical sequence as follows:
     132-221: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 591591Serine/threonine-protein kinase PAK 4
PRO_0000086474

Regions

Domain11 – 2414CRIB
Domain321 – 572252Protein kinase
Nucleotide binding327 – 3359ATP By similarity
Region25 – 320296Linker
Region298 – 32326GEF-interaction domain (GID)
Compositional bias105 – 1084Poly-Pro
Compositional bias242 – 2476Poly-Ser

Sites

Active site4401Proton acceptor By similarity
Binding site3501ATP By similarity

Amino acid modifications

Modified residue411Phosphoserine Ref.15 Ref.17
Modified residue1041Phosphoserine Ref.15 Ref.17
Modified residue1481Phosphoserine Ref.15 Ref.17
Modified residue1671Phosphoserine Ref.15 Ref.17
Modified residue1811Phosphoserine Ref.15 Ref.16 Ref.17 Ref.18 Ref.26
Modified residue1871Phosphothreonine Ref.17
Modified residue1951Phosphoserine Ref.17
Modified residue2581Phosphoserine Ref.15 Ref.17
Modified residue2671Phosphoserine Ref.15
Modified residue2911Phosphoserine Ref.15 Ref.17
Modified residue4741Phosphoserine; by autocatalysis Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.24 Ref.26 Ref.27

Natural variations

Alternative sequence69 – 221153Missing in isoform 3.
VSP_017572
Alternative sequence1201E → K in isoform 2.
VSP_004892
Alternative sequence121 – 285165Missing in isoform 2.
VSP_004893
Alternative sequence132 – 22190Missing in isoform 4.
VSP_017573
Natural variant1351R → Q. Ref.28
Corresponds to variant rs56099436 [ dbSNP | Ensembl ].
VAR_040970
Natural variant1391A → T. Ref.28
Corresponds to variant rs35655056 [ dbSNP | Ensembl ].
VAR_040971

Experimental info

Mutagenesis4451S → N: Approximately 30-fold increased autophosphorylation (constitutively active mutant). Ref.9
Mutagenesis4741S → E: Approximately 3-fold increased autophosphorylation. Ref.9

Secondary structure

........................................................................ 591
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 04C2A5C0B06427D5

FASTA59164,072
        10         20         30         40         50         60 
MFGKRKKRVE ISAPSNFEHR VHTGFDQHEQ KFTGLPRQWQ SLIEESARRP KPLVDPACIT 

        70         80         90        100        110        120 
SIQPGAPKTI VRGSKGAKDG ALTLLLDEFE NMSVTRSNSL RRDSPPPPAR ARQENGMPEE 

       130        140        150        160        170        180 
PATTARGGPG KAGSRGRFAG HSEAGGGSGD RRRAGPEKRP KSSREGSGGP QESSRDKRPL 

       190        200        210        220        230        240 
SGPDVGTPQP AGLASGAKLA AGRPFNTYPR ADTDHPSRGA QGEPHDVAPN GPSAGGLAIP 

       250        260        270        280        290        300 
QSSSSSSRPP TRARGAPSPG VLGPHASEPQ LAPPACTPAA PAVPGPPGPR SPQREPQRVS 

       310        320        330        340        350        360 
HEQFRAALQL VVDPGDPRSY LDNFIKIGEG STGIVCIATV RSSGKLVAVK KMDLRKQQRR 

       370        380        390        400        410        420 
ELLFNEVVIM RDYQHENVVE MYNSYLVGDE LWVVMEFLEG GALTDIVTHT RMNEEQIAAV 

       430        440        450        460        470        480 
CLAVLQALSV LHAQGVIHRD IKSDSILLTH DGRVKLSDFG FCAQVSKEVP RRKSLVGTPY 

       490        500        510        520        530        540 
WMAPELISRL PYGPEVDIWS LGIMVIEMVD GEPPYFNEPP LKAMKMIRDN LPPRLKNLHK 

       550        560        570        580        590 
VSPSLKGFLD RLLVRDPAQR ATAAELLKHP FLAKAGPPAS IVPLMRQNRT R 

« Hide

Isoform 2 [UniParc].

Checksum: 505879690593E93A
Show »

FASTA42647,924
Isoform 3 [UniParc].

Checksum: 4A596EBBCECE9883
Show »

FASTA43848,268
Isoform 4 [UniParc].

Checksum: 6EE6240ECE65E79D
Show »

FASTA50154,940

References

« Hide 'large scale' references
[1]"PAK4, a novel effector for Cdc42Hs, is implicated in the reorganization of the actin cytoskeleton and in the formation of filopodia."
Abo A., Qu J., Cammarano M.S., Dan C., Fritsch A., Baud V., Belisle B., Minden A.
EMBO J. 17:6527-6540(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Lymphoma.
[2]Melnick M.B.
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Neuroblastoma.
[3]"Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain.
[4]"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. expand/collapse author list , 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] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 264-591 (ISOFORM 1).
Tissue: Brain and Teratocarcinoma.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] (ISOFORMS 1; 2 AND 4).
Tissue: Eye, Pancreas and Placenta.
[8]"The serine/threonine kinase PAK4 prevents caspase activation and protects cells from apoptosis."
Gnesutta N., Qu J., Minden A.
J. Biol. Chem. 276:14414-14419(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF BAD.
[9]"Activated PAK4 regulates cell adhesion and anchorage-independent growth."
Qu J., Cammarano M.S., Shi Q., Ha K.C., de Lanerolle P., Minden A.
Mol. Cell. Biol. 21:3523-3533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF SER-445 AND SER-474.
[10]"P21-activated kinase 4 interacts with integrin alpha v beta 5 and regulates alpha v beta 5-mediated cell migration."
Zhang H., Li Z., Viklund E.K., Stromblad S.
J. Cell Biol. 158:1287-1297(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[11]"Death receptor-induced activation of initiator caspase 8 is antagonized by serine/threonine kinase PAK4."
Gnesutta N., Minden A.
Mol. Cell. Biol. 23:7838-7848(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Interplay between components of a novel LIM kinase-slingshot phosphatase complex regulates cofilin."
Soosairajah J., Maiti S., Wiggan O., Sarmiere P., Moussi N., Sarcevic B., Sampath R., Bamburg J.R., Bernard O.
EMBO J. 24:473-486(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"PAK4 mediates morphological changes through the regulation of GEF-H1."
Callow M.G., Zozulya S., Gishizky M.L., Jallal B., Smeal T.
J. Cell Sci. 118:1861-1872(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARHGEF2.
[14]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-104; SER-148; SER-167; SER-181; SER-258; SER-267; SER-291 AND SER-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-104; SER-148; SER-167; SER-181; THR-187; SER-195; SER-258; SER-291 AND SER-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"p21-activated kinase 4 phosphorylation of integrin beta5 Ser-759 and Ser-762 regulates cell migration."
Li Z., Zhang H., Lundin L., Thullberg M., Liu Y., Wang Y., Claesson-Welsh L., Stromblad S.
J. Biol. Chem. 285:23699-23710(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF ITGB5.
[20]"Subgroup II PAK-mediated phosphorylation regulates Ran activity during mitosis."
Bompard G., Rabeharivelo G., Frank M., Cau J., Delsert C., Morin N.
J. Cell Biol. 190:807-822(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF RAN.
[21]"Cdc42 regulates apical junction formation in human bronchial epithelial cells through PAK4 and Par6B."
Wallace S.W., Durgan J., Jin D., Hall A.
Mol. Biol. Cell 21:2996-3006(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[22]"p21-activated kinases: three more join the Pak."
Jaffer Z.M., Chernoff J.
Int. J. Biochem. Cell Biol. 34:713-717(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[23]"The emerging importance of group II PAKs."
Wells C.M., Jones G.E.
Biochem. J. 425:465-473(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[24]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"Crystal structure of the human p21-activated kinase 4."
Eswaran J., Debreczeni J.E., Bunkoczi G., Filippakopoulos P., Das S., Fedorov O., Sundstrom M., Arrowsmith C., Edwards A., von Delft F., Knapp S.
Submitted (JUL-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 300-591, PHOSPHORYLATION AT SER-474.
[28]"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. expand/collapse author list , 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] GLN-135 AND THR-139.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ011855 mRNA. Translation: CAA09820.1.
AF005046 mRNA. Translation: AAD01210.1.
AB032968 mRNA. Translation: BAA86456.1. Different initiation.
AK074728 mRNA. Translation: BAC11166.1. Different initiation.
AK294586 mRNA. Translation: BAG57777.1.
AL834236 mRNA. Translation: CAD38914.2.
CH471126 Genomic DNA. Translation: EAW56861.1.
BC002921 mRNA. Translation: AAH02921.1.
BC011368 mRNA. Translation: AAH11368.1.
BC025282 mRNA. Translation: AAH25282.1.
BC034511 mRNA. Translation: AAH34511.1.
CCDSCCDS12528.1. [O96013-1]
CCDS33019.1. [O96013-3]
RefSeqNP_001014831.1. NM_001014831.2. [O96013-1]
NP_001014832.1. NM_001014832.1. [O96013-1]
NP_001014834.1. NM_001014834.2. [O96013-3]
NP_001014835.1. NM_001014835.1. [O96013-3]
NP_005875.1. NM_005884.3. [O96013-1]
XP_006723034.1. XM_006722971.1. [O96013-1]
XP_006723035.1. XM_006722972.1. [O96013-3]
UniGeneHs.20447.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BVAX-ray2.30A/B300-591[»]
2CDZX-ray2.30A291-591[»]
2J0IX-ray1.60A291-591[»]
2OV2X-ray2.10I/J/K/L/M/N/O/P10-44[»]
2Q0NX-ray1.75A291-591[»]
2X4ZX-ray2.10A297-591[»]
4APPX-ray2.20A300-591[»]
4FIEX-ray3.11A/B5-591[»]
4FIFX-ray2.60A/B286-591[»]
C/D49-56[»]
4FIGX-ray3.01A/B286-591[»]
4FIHX-ray1.97A286-591[»]
4FIIX-ray2.00A286-591[»]
B49-56[»]
4FIJX-ray2.30A286-591[»]
4JDHX-ray2.00A286-591[»]
4JDIX-ray1.85A286-591[»]
4JDJX-ray2.30A286-591[»]
4JDKX-ray2.40A286-591[»]
4L67X-ray2.80A300-591[»]
B36-60[»]
4NJDX-ray2.50A300-591[»]
4O0VX-ray2.80A300-591[»]
4O0XX-ray2.48A300-591[»]
4O0YX-ray2.20A300-591[»]
ProteinModelPortalO96013.
SMRO96013. Positions 10-44, 300-589.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115586. 23 interactions.
DIPDIP-39742N.
IntActO96013. 14 interactions.
MINTMINT-1387795.
STRING9606.ENSP00000351049.

Chemistry

BindingDBO96013.
ChEMBLCHEMBL4482.
GuidetoPHARMACOLOGY2136.

PTM databases

PhosphoSiteO96013.

Proteomic databases

MaxQBO96013.
PaxDbO96013.
PRIDEO96013.

Protocols and materials databases

DNASU10298.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000321944; ENSP00000326864; ENSG00000130669. [O96013-4]
ENST00000358301; ENSP00000351049; ENSG00000130669. [O96013-1]
ENST00000360442; ENSP00000353625; ENSG00000130669. [O96013-1]
ENST00000435673; ENSP00000392753; ENSG00000130669. [O96013-1]
ENST00000593690; ENSP00000469413; ENSG00000130669. [O96013-1]
ENST00000599386; ENSP00000471157; ENSG00000130669. [O96013-3]
ENST00000599470; ENSP00000470284; ENSG00000130669. [O96013-3]
GeneID10298.
KEGGhsa:10298.
UCSCuc002okj.1. human. [O96013-1]
uc002okm.1. human. [O96013-3]
uc002okp.1. human. [O96013-4]

Organism-specific databases

CTD10298.
GeneCardsGC19P039616.
HGNCHGNC:16059. PAK4.
HPACAB025747.
MIM605451. gene.
neXtProtNX_O96013.
PharmGKBPA32920.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG108518.
InParanoidO96013.
KOK05734.
OMAIDPACIT.
OrthoDBEOG73804D.
PhylomeDBO96013.
TreeFamTF105352.

Enzyme and pathway databases

BRENDA2.7.11.1. 2681.
ReactomeREACT_111045. Developmental Biology.
SignaLinkO96013.

Gene expression databases

ArrayExpressO96013.
BgeeO96013.
CleanExHS_PAK4.
GenevestigatorO96013.

Family and domain databases

Gene3D3.90.810.10. 1 hit.
InterProIPR000095. CRIB_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
[Graphical view]
PfamPF00786. PBD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00285. PBD. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50108. CRIB. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPAK4. human.
EvolutionaryTraceO96013.
GeneWikiPAK4.
GenomeRNAi10298.
NextBio39028.
PROO96013.
SOURCESearch...

Entry information

Entry namePAK4_HUMAN
AccessionPrimary (citable) accession number: O96013
Secondary accession number(s): B4DGG6 expand/collapse secondary AC list , Q8N4E1, Q8NCH5, Q8NDE3, Q9BU33, Q9ULS8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM