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UniProtKB/Swiss-Prot entry O96013


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PAK4_HUMAN
Primary accession number O96013
Secondary accession numbers Q8N4E1 Q8NCH5 Q8NDE3 Q9BU33 Q9ULS8
Integrated into Swiss-Prot on January 24, 2001
Sequence was last modified on May 1, 1999 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 91)
Name and origin of the protein
Protein name Serine/threonine-protein kinase PAK 4
Synonyms EC 2.7.11.1
p21-activated kinase 4
PAK-4
Gene name
Name: PAK4
Synonyms: KIAA1142
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Lymphoma;
DOI=10.1093/emboj/17.22.6527; PubMed=9822598 [NCBI, ExPASy, EBI, Israel, Japan]
Abo A., Qu J., Cammarano M.S., Dan C., Fritsch A., Baud V., Belisle B., Minden A.;
"PAK4, a novel effector for Cdc42Hs, is implicated in the reorganization of the actin cytoskeleton and in the formation of filopodia.";
EMBO J. 17:6527-6540(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Neuroblastoma;
Melnick M.B.;
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain;
DOI=10.1093/dnares/6.5.329; PubMed=10574461 [NCBI, ExPASy, EBI, Israel, Japan]
Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
"Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain.";
DNA Res. 6:329-336(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain;
The German cDNA consortium;
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
TISSUE=Eye, Pancreas, and Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 264-591 (ISOFORM 1).
TISSUE=Teratocarcinoma;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
FUNCTION.
DOI=10.1038/sj.emboj.7600543; PubMed=15660133 [NCBI, ExPASy, EBI, Israel, Japan]
Soosairajah J., Maiti S., Wiggan O., Sarmiere P., Moussi N., Sarcevic B., Sampath R., Bamburg J.R., Bernard O.;
"Interplay between components of a novel LIM kinase-slingshot phosphatase complex regulates cofilin.";
EMBO J. 24:473-486(2005).
[8]
INTERACTION WITH ARHGEF2.
DOI=10.1242/jcs.02313; PubMed=15827085 [NCBI, ExPASy, EBI, Israel, Japan]
Callow M.G., Zozulya S., Gishizky M.L., Jallal B., Smeal T.;
"PAK4 mediates morphological changes through the regulation of GEF-H1.";
J. Cell Sci. 118:1861-1872(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-104; SER-148; SER-167; SER-181; THR-207; SER-267; SER-291 AND SER-474, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.T600062-MCP200; PubMed=17192257 [NCBI, ExPASy, EBI, Israel, Japan]
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.;
"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry.";
Mol. Cell. Proteomics 6:537-547(2007).
[11]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 300-591, AND PHOSPHORYLATION AT SER-474.
Eswaran J., Debreczeni J.E., Bunkoczi G., Filippakopoulos P., Das S., Fedorov O., Sundstrom M., Arrowsmith C., Edwards A., von Delft F., Knapp S.;
"Crystal structure of the human p21-activated kinase 4.";
Submitted (JUL-2005) to the PDB data bank.
[12]
VARIANTS [LARGE SCALE ANALYSIS] GLN-135 AND THR-139.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AJ011855; CAA09820.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF005046; AAD01210.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB032968; BAA86456.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL834236; CAD38914.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002921; AAH02921.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011368; AAH11368.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC025282; AAH25282.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC034511; AAH34511.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK074728; BAC11166.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001014831.1; -.
NP_001014832.1; -.
NP_001014834.1; -.
NP_001014835.1; -.
NP_005875.1; -.
UniGene Hs.20447
3D structure databases
PDB
2BVA; X-ray; 2.30 A; A/B=300-591.[ExPASy / RCSB / EBI]
2CDZ; X-ray; 2.30 A; A=291-591.[ExPASy / RCSB / EBI]
2J0I; X-ray; 1.60 A; A=291-591.[ExPASy / RCSB / EBI]
2OV2; X-ray; 2.10 A; I/J/K/L/M/N/O/P=10-44.[ExPASy / RCSB / EBI]
2Q0N; X-ray; 1.75 A; A=291-591.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2BVA; -.
2CDZ; -.
2J0I; -.
2OV2; -.
2Q0N; -.
ModBase O96013.
Protein-protein interaction databases
IntAct O96013; -.
PTM databases
PhosphoSite O96013; -.
Organism-specific databases
H-InvDB HIX0015110; -.
HGNC HGNC:16059; PAK4.
GenAtlas PAK4.
MIM 605451; gene. [NCBI / EBI]
PharmGKB PA32920; -.
GeneCards O96013.
HUGE KIAA1142.
Gene expression databases
ArrayExpress O96013; -.
CleanEx HS_PAK4; -.
GermOnline ENSG00000130669; Homo sapiens.
Ontologies
GO
GO:0005794; Cellular component: Golgi apparatus (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004672; Molecular function: protein kinase activity (non-traceable author statement from ProtInc).
GO:0006928; Biological process: cell motion (traceable author statement from ProtInc).
GO:0007165; Biological process: signal transduction (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000095; PAK_box_Rho_bd.
IPR015750; Pak_like.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.
PANTHER PTHR22986:SF84; Pak_like; 1.
Pfam PF00786; PBD; 1.
PF00069; Pkinase; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00285; PBD; 1.
SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS50108; CRIB; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).
BLOCKS O96013.
ProtoNet O96013.
Genome annotation databases
Ensembl ENSG00000130669; Homo sapiens. [Contig view]
GeneID 10298; -.
KEGG hsa:10298; -.
Phylogenomic databases
HOGENOM O96013; -.
HOVERGEN O96013; -.
Other
NextBio 39028; -.
SOURCE PAK4; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; Polymorphism; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   591  591     Serine/threonine-protein kinase PAK 4. PRO_0000086474
DOMAIN   11    24  14     CRIB. 
DOMAIN   321   572  252     Protein kinase. 
NP_BIND   327   335  9     ATP (By similarity). 
REGION   25   320  296     Linker. 
REGION   298   323  26     GEF-interaction domain (GID). 
ACT_SITE   440   440        Proton acceptor (By similarity). 
BINDING   350   350        ATP (By similarity). 
MOD_RES   99    99        Phosphoserine. 
MOD_RES   104   104        Phosphoserine. 
MOD_RES   148   148        Phosphoserine. 
MOD_RES   167   167        Phosphoserine. 
MOD_RES   181   181        Phosphoserine. 
MOD_RES   207   207        Phosphothreonine. 
MOD_RES   267   267        Phosphoserine. 
MOD_RES   291   291        Phosphoserine. 
MOD_RES   474   474        Phosphoserine; by autocatalysis. 
VAR_SEQ   69   221        Missing (in isoform 3). VSP_017572
VAR_SEQ   120   120        E -> K (in isoform 2). VSP_004892
VAR_SEQ   121   285        Missing (in isoform 2). VSP_004893
VAR_SEQ   132   221        Missing (in isoform 4). VSP_017573
VARIANT   135   135  1     R -> Q. VAR_040970 
VARIANT   139   139  1     A -> T. VAR_040971 
STRAND   15    26  12      
TURN   27    30  4      
STRAND   31    34  4      
HELIX   37    39  3      
TURN   40    42  3      
HELIX   306   309  4      
TURN   318   320  3      
HELIX   364   371  8      
STRAND   381   389  9      
STRAND   391   395  5      
HELIX   404   407  4      
HELIX   414   433  20      
HELIX   443   445  3      
STRAND   446   448  3      
STRAND   454   456  3      
HELIX   479   481  3      
HELIX   484   487  4      
HELIX   495   509  15      
TURN   514   517  4      
HELIX   520   528  9      
HELIX   543   552  10      
HELIX   557   559  3      
HELIX   563   566  4      
HELIX   570   574  5      
HELIX   578   585  8      
Sequence information
Length: 591 AA [This is the length of the unprocessed precursor] Molecular weight: 64072 Da [This is the MW of the unprocessed precursor] CRC64: 04C2A5C0B06427D5 [This is a checksum on the sequence]
        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 

O96013 in FASTA format

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