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Database: UniProt
Entry: O96013
LinkDB: O96013
Original site: O96013 
ID   PAK4_HUMAN              Reviewed;         591 AA.
AC   O96013; B4DGG6; Q8N4E1; Q8NCH5; Q8NDE3; Q9BU33; Q9ULS8;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   26-FEB-2020, entry version 210.
DE   RecName: Full=Serine/threonine-protein kinase PAK 4;
DE            EC=2.7.11.1;
DE   AltName: Full=p21-activated kinase 4;
DE            Short=PAK-4;
GN   Name=PAK4; Synonyms=KIAA1142;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Lymphoma;
RX   PubMed=9822598; DOI=10.1093/emboj/17.22.6527;
RA   Abo A., Qu J., Cammarano M.S., Dan C., Fritsch A., Baud V., Belisle B.,
RA   Minden A.;
RT   "PAK4, a novel effector for Cdc42Hs, is implicated in the reorganization of
RT   the actin cytoskeleton and in the formation of filopodia.";
RL   EMBO J. 17:6527-6540(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Neuroblastoma;
RA   Melnick M.B.;
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RX   PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA   Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT   "Characterization of cDNA clones selected by the GeneMark analysis from
RT   size-fractionated cDNA libraries from human brain.";
RL   DNA Res. 6:329-336(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 264-591 (ISOFORM 1).
RC   TISSUE=Brain, and Teratocarcinoma;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC   TISSUE=Eye, Pancreas, and Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   FUNCTION IN PHOSPHORYLATION OF BAD.
RX   PubMed=11278822; DOI=10.1074/jbc.m011046200;
RA   Gnesutta N., Qu J., Minden A.;
RT   "The serine/threonine kinase PAK4 prevents caspase activation and protects
RT   cells from apoptosis.";
RL   J. Biol. Chem. 276:14414-14419(2001).
RN   [9]
RP   FUNCTION, AND MUTAGENESIS OF SER-445 AND SER-474.
RX   PubMed=11313478; DOI=10.1128/mcb.21.10.3523-3533.2001;
RA   Qu J., Cammarano M.S., Shi Q., Ha K.C., de Lanerolle P., Minden A.;
RT   "Activated PAK4 regulates cell adhesion and anchorage-independent growth.";
RL   Mol. Cell. Biol. 21:3523-3533(2001).
RN   [10]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12356872; DOI=10.1083/jcb.200207008;
RA   Zhang H., Li Z., Viklund E.K., Stromblad S.;
RT   "P21-activated kinase 4 interacts with integrin alpha v beta 5 and
RT   regulates alpha v beta 5-mediated cell migration.";
RL   J. Cell Biol. 158:1287-1297(2002).
RN   [11]
RP   FUNCTION.
RX   PubMed=14560027; DOI=10.1128/mcb.23.21.7838-7848.2003;
RA   Gnesutta N., Minden A.;
RT   "Death receptor-induced activation of initiator caspase 8 is antagonized by
RT   serine/threonine kinase PAK4.";
RL   Mol. Cell. Biol. 23:7838-7848(2003).
RN   [12]
RP   FUNCTION.
RX   PubMed=15660133; DOI=10.1038/sj.emboj.7600543;
RA   Soosairajah J., Maiti S., Wiggan O., Sarmiere P., Moussi N., Sarcevic B.,
RA   Sampath R., Bamburg J.R., Bernard O.;
RT   "Interplay between components of a novel LIM kinase-slingshot phosphatase
RT   complex regulates cofilin.";
RL   EMBO J. 24:473-486(2005).
RN   [13]
RP   INTERACTION WITH ARHGEF2.
RX   PubMed=15827085; DOI=10.1242/jcs.02313;
RA   Callow M.G., Zozulya S., Gishizky M.L., Jallal B., Smeal T.;
RT   "PAK4 mediates morphological changes through the regulation of GEF-H1.";
RL   J. Cell Sci. 118:1861-1872(2005).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-104; SER-148;
RP   SER-167; SER-181; SER-258; SER-267; SER-291 AND SER-474, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-474, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-104; SER-148;
RP   SER-167; SER-181; THR-187; SER-195; SER-258; SER-291 AND SER-474, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-474, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [19]
RP   FUNCTION IN PHOSPHORYLATION OF ITGB5.
RX   PubMed=20507994; DOI=10.1074/jbc.m110.123497;
RA   Li Z., Zhang H., Lundin L., Thullberg M., Liu Y., Wang Y.,
RA   Claesson-Welsh L., Stromblad S.;
RT   "p21-activated kinase 4 phosphorylation of integrin beta5 Ser-759 and Ser-
RT   762 regulates cell migration.";
RL   J. Biol. Chem. 285:23699-23710(2010).
RN   [20]
RP   FUNCTION IN PHOSPHORYLATION OF RAN.
RX   PubMed=20805321; DOI=10.1083/jcb.200912056;
RA   Bompard G., Rabeharivelo G., Frank M., Cau J., Delsert C., Morin N.;
RT   "Subgroup II PAK-mediated phosphorylation regulates Ran activity during
RT   mitosis.";
RL   J. Cell Biol. 190:807-822(2010).
RN   [21]
RP   FUNCTION.
RX   PubMed=20631255; DOI=10.1091/mbc.e10-05-0429;
RA   Wallace S.W., Durgan J., Jin D., Hall A.;
RT   "Cdc42 regulates apical junction formation in human bronchial epithelial
RT   cells through PAK4 and Par6B.";
RL   Mol. Biol. Cell 21:2996-3006(2010).
RN   [22]
RP   REVIEW.
RX   PubMed=11950587; DOI=10.1016/s1357-2725(01)00158-3;
RA   Jaffer Z.M., Chernoff J.;
RT   "p21-activated kinases: three more join the Pak.";
RL   Int. J. Biochem. Cell Biol. 34:713-717(2002).
RN   [23]
RP   REVIEW ON FUNCTION.
RX   PubMed=20070256; DOI=10.1042/bj20091173;
RA   Wells C.M., Jones G.E.;
RT   "The emerging importance of group II PAKs.";
RL   Biochem. J. 425:465-473(2010).
RN   [24]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [25]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [26]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-474, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [27]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-181; THR-207 AND
RP   SER-474, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [28]
RP   INTERACTION WITH SH3RF2, UBIQUITINATION, AND PROTEASOMAL DEGRADATION.
RX   PubMed=24130170; DOI=10.1093/carcin/bgt338;
RA   Kim T.W., Kang Y.K., Park Z.Y., Kim Y.H., Hong S.W., Oh S.J., Sohn H.A.,
RA   Yang S.J., Jang Y.J., Lee D.C., Kim S.Y., Yoo H.S., Kim E., Yeom Y.I.,
RA   Park K.C.;
RT   "SH3RF2 functions as an oncogene by mediating PAK4 protein stability.";
RL   Carcinogenesis 35:624-634(2014).
RN   [29]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [30]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT LYS-78, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Colon carcinoma;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [31]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 300-591, AND PHOSPHORYLATION AT
RP   SER-474.
RA   Eswaran J., Debreczeni J.E., Bunkoczi G., Filippakopoulos P., Das S.,
RA   Fedorov O., Sundstrom M., Arrowsmith C., Edwards A., von Delft F.,
RA   Knapp S.;
RT   "Crystal structure of the human p21-activated kinase 4.";
RL   Submitted (JUL-2005) to the PDB data bank.
RN   [32]
RP   X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 286-591 IN COMPLEX WITH INKA1,
RP   FUNCTION, INTERACTION WITH INKA1, AND ACTIVITY REGULATION.
RX   PubMed=26607847; DOI=10.1038/ncomms9681;
RA   Baskaran Y., Ang K.C., Anekal P.V., Chan W.L., Grimes J.M., Manser E.,
RA   Robinson R.C.;
RT   "An in cellulo-derived structure of PAK4 in complex with its inhibitor
RT   Inka1.";
RL   Nat. Commun. 6:8681-8681(2015).
RN   [33]
RP   VARIANTS [LARGE SCALE ANALYSIS] GLN-135 AND THR-139.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA   Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA   Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA   Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA   Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA   Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA   Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA   Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA   Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA   Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA   Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA   Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
CC   -!- FUNCTION: Serine/threonine protein kinase that plays a role in a
CC       variety of different signaling pathways including cytoskeleton
CC       regulation, cell migration, growth, proliferation or cell survival.
CC       Activation by various effectors including growth factor receptors or
CC       active CDC42 and RAC1 results in a conformational change and a
CC       subsequent autophosphorylation on several serine and/or threonine
CC       residues. Phosphorylates and inactivates the protein phosphatase SSH1,
CC       leading to increased inhibitory phosphorylation of the actin
CC       binding/depolymerizing factor cofilin. Decreased cofilin activity may
CC       lead to stabilization of actin filaments. Phosphorylates LIMK1, a
CC       kinase that also inhibits the activity of cofilin. Phosphorylates
CC       integrin beta5/ITGB5 and thus regulates cell motility. Phosphorylates
CC       ARHGEF2 and activates the downstream target RHOA that plays a role in
CC       the regulation of assembly of focal adhesions and actin stress fibers.
CC       Stimulates cell survival by phosphorylating the BCL2 antagonist of cell
CC       death BAD. Alternatively, inhibits apoptosis by preventing caspase-8
CC       binding to death domain receptors in a kinase independent manner. Plays
CC       a role in cell-cycle progression by controlling levels of the cell-
CC       cycle regulatory protein CDKN1A and by phosphorylating RAN.
CC       {ECO:0000269|PubMed:11278822, ECO:0000269|PubMed:11313478,
CC       ECO:0000269|PubMed:14560027, ECO:0000269|PubMed:15660133,
CC       ECO:0000269|PubMed:20507994, ECO:0000269|PubMed:20631255,
CC       ECO:0000269|PubMed:20805321, ECO:0000269|PubMed:26607847}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- ACTIVITY REGULATION: Inhibited by INKA1; which inhibits the
CC       serine/threonine-protein kinase activity by binding PAK4 in a
CC       substrate-like manner (PubMed:26607847). {ECO:0000269|PubMed:26607847}.
CC   -!- SUBUNIT: Interacts with FGFR2 and GRB2 (By similarity). Interacts
CC       tightly with GTP-bound but not GDP-bound CDC42/p21 and weakly with RAC1
CC       (PubMed:15827085). Interacts with INKA1 (PubMed:26607847). Interacts
CC       with SH3RF2 (PubMed:24130170). {ECO:0000250|UniProtKB:Q8BTW9,
CC       ECO:0000269|PubMed:15827085, ECO:0000269|PubMed:24130170,
CC       ECO:0000269|PubMed:26607847}.
CC   -!- INTERACTION:
CC       P60953:CDC42; NbExp=2; IntAct=EBI-713738, EBI-81752;
CC       P54274:TERF1; NbExp=2; IntAct=EBI-713738, EBI-710997;
CC       P63104:YWHAZ; NbExp=2; IntAct=EBI-713738, EBI-347088;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12356872}.
CC       Note=Seems to shuttle between cytoplasmic compartments depending on the
CC       activating effector. For example, can be found on the cell periphery
CC       after activation of growth-factor or integrin-mediated signaling
CC       pathways. {ECO:0000269|PubMed:12356872}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=O96013-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O96013-2; Sequence=VSP_004892, VSP_004893;
CC       Name=3;
CC         IsoId=O96013-3; Sequence=VSP_017572;
CC       Name=4;
CC         IsoId=O96013-4; Sequence=VSP_017573;
CC   -!- TISSUE SPECIFICITY: Highest expression in prostate, testis and colon.
CC   -!- PTM: Autophosphorylated on serine residues when activated by CDC42/p21
CC       (Ref.31). Phosphorylated on tyrosine residues upon stimulation of FGFR2
CC       (By similarity). {ECO:0000250|UniProtKB:Q8BTW9, ECO:0000269|Ref.31}.
CC   -!- PTM: Polyubiquitinated, leading to its proteasomal degradation.
CC       {ECO:0000269|PubMed:24130170}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA86456.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC11166.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AJ011855; CAA09820.1; -; mRNA.
DR   EMBL; AF005046; AAD01210.1; -; mRNA.
DR   EMBL; AB032968; BAA86456.1; ALT_INIT; mRNA.
DR   EMBL; AK074728; BAC11166.1; ALT_INIT; mRNA.
DR   EMBL; AK294586; BAG57777.1; -; mRNA.
DR   EMBL; AL834236; CAD38914.2; -; mRNA.
DR   EMBL; CH471126; EAW56861.1; -; Genomic_DNA.
DR   EMBL; BC002921; AAH02921.1; -; mRNA.
DR   EMBL; BC011368; AAH11368.1; -; mRNA.
DR   EMBL; BC025282; AAH25282.1; -; mRNA.
DR   EMBL; BC034511; AAH34511.1; -; mRNA.
DR   CCDS; CCDS12528.1; -. [O96013-1]
DR   CCDS; CCDS33019.1; -. [O96013-3]
DR   RefSeq; NP_001014831.1; NM_001014831.2. [O96013-1]
DR   RefSeq; NP_001014832.1; NM_001014832.1. [O96013-1]
DR   RefSeq; NP_001014834.1; NM_001014834.2. [O96013-3]
DR   RefSeq; NP_001014835.1; NM_001014835.1. [O96013-3]
DR   RefSeq; NP_005875.1; NM_005884.3. [O96013-1]
DR   RefSeq; XP_011524618.1; XM_011526316.1. [O96013-1]
DR   RefSeq; XP_011524619.1; XM_011526317.2. [O96013-1]
DR   RefSeq; XP_011524620.1; XM_011526318.2. [O96013-1]
DR   RefSeq; XP_011524621.1; XM_011526319.2. [O96013-1]
DR   RefSeq; XP_011524622.1; XM_011526320.1. [O96013-3]
DR   PDB; 2BVA; X-ray; 2.30 A; A/B=300-591.
DR   PDB; 2CDZ; X-ray; 2.30 A; A=291-591.
DR   PDB; 2J0I; X-ray; 1.60 A; A=291-591.
DR   PDB; 2OV2; X-ray; 2.10 A; I/J/K/L/M/N/O/P=10-44.
DR   PDB; 2Q0N; X-ray; 1.75 A; A=291-591.
DR   PDB; 2X4Z; X-ray; 2.10 A; A=297-591.
DR   PDB; 4APP; X-ray; 2.20 A; A=300-591.
DR   PDB; 4FIE; X-ray; 3.11 A; A/B=5-591.
DR   PDB; 4FIF; X-ray; 2.60 A; A/B=286-591, C/D=49-56.
DR   PDB; 4FIG; X-ray; 3.01 A; A/B=286-591.
DR   PDB; 4FIH; X-ray; 1.97 A; A=286-591.
DR   PDB; 4FII; X-ray; 2.00 A; A=286-591, B=49-56.
DR   PDB; 4FIJ; X-ray; 2.30 A; A=286-591.
DR   PDB; 4JDH; X-ray; 2.00 A; A=286-591.
DR   PDB; 4JDI; X-ray; 1.85 A; A=286-591.
DR   PDB; 4JDJ; X-ray; 2.30 A; A=286-591.
DR   PDB; 4JDK; X-ray; 2.40 A; A=286-591.
DR   PDB; 4L67; X-ray; 2.80 A; A=300-591, B=36-60.
DR   PDB; 4NJD; X-ray; 2.50 A; A=300-591.
DR   PDB; 4O0V; X-ray; 2.80 A; A=300-591.
DR   PDB; 4O0X; X-ray; 2.48 A; A=300-591.
DR   PDB; 4O0Y; X-ray; 2.20 A; A=300-591.
DR   PDB; 4XBR; X-ray; 2.94 A; A=278-591.
DR   PDB; 4XBU; X-ray; 2.06 A; A=286-591.
DR   PDB; 5BMS; X-ray; 2.90 A; A=300-591.
DR   PDB; 5I0B; X-ray; 3.09 A; A=300-591.
DR   PDB; 5UPK; X-ray; 2.40 A; A=1-45, B=286-591.
DR   PDB; 5UPL; X-ray; 3.00 A; A=2-591.
DR   PDB; 5VED; X-ray; 2.30 A; A=286-591.
DR   PDB; 5VEE; X-ray; 2.50 A; A=286-591.
DR   PDB; 5VEF; X-ray; 1.75 A; A=286-591.
DR   PDB; 5XVA; X-ray; 1.85 A; A=300-591.
DR   PDB; 5XVF; X-ray; 2.65 A; A=300-588.
DR   PDB; 5XVG; X-ray; 2.10 A; A=300-591.
DR   PDB; 5ZJW; X-ray; 1.80 A; A=300-591.
DR   PDBsum; 2BVA; -.
DR   PDBsum; 2CDZ; -.
DR   PDBsum; 2J0I; -.
DR   PDBsum; 2OV2; -.
DR   PDBsum; 2Q0N; -.
DR   PDBsum; 2X4Z; -.
DR   PDBsum; 4APP; -.
DR   PDBsum; 4FIE; -.
DR   PDBsum; 4FIF; -.
DR   PDBsum; 4FIG; -.
DR   PDBsum; 4FIH; -.
DR   PDBsum; 4FII; -.
DR   PDBsum; 4FIJ; -.
DR   PDBsum; 4JDH; -.
DR   PDBsum; 4JDI; -.
DR   PDBsum; 4JDJ; -.
DR   PDBsum; 4JDK; -.
DR   PDBsum; 4L67; -.
DR   PDBsum; 4NJD; -.
DR   PDBsum; 4O0V; -.
DR   PDBsum; 4O0X; -.
DR   PDBsum; 4O0Y; -.
DR   PDBsum; 4XBR; -.
DR   PDBsum; 4XBU; -.
DR   PDBsum; 5BMS; -.
DR   PDBsum; 5I0B; -.
DR   PDBsum; 5UPK; -.
DR   PDBsum; 5UPL; -.
DR   PDBsum; 5VED; -.
DR   PDBsum; 5VEE; -.
DR   PDBsum; 5VEF; -.
DR   PDBsum; 5XVA; -.
DR   PDBsum; 5XVF; -.
DR   PDBsum; 5XVG; -.
DR   PDBsum; 5ZJW; -.
DR   SMR; O96013; -.
DR   BioGrid; 115586; 72.
DR   DIP; DIP-39742N; -.
DR   IntAct; O96013; 37.
DR   MINT; O96013; -.
DR   STRING; 9606.ENSP00000469413; -.
DR   BindingDB; O96013; -.
DR   ChEMBL; CHEMBL4482; -.
DR   DrugBank; DB12010; Fostamatinib.
DR   DrugCentral; O96013; -.
DR   GuidetoPHARMACOLOGY; 2136; -.
DR   iPTMnet; O96013; -.
DR   PhosphoSitePlus; O96013; -.
DR   BioMuta; PAK4; -.
DR   EPD; O96013; -.
DR   jPOST; O96013; -.
DR   MassIVE; O96013; -.
DR   MaxQB; O96013; -.
DR   PaxDb; O96013; -.
DR   PeptideAtlas; O96013; -.
DR   PRIDE; O96013; -.
DR   ProteomicsDB; 51192; -. [O96013-1]
DR   ProteomicsDB; 51193; -. [O96013-2]
DR   ProteomicsDB; 51194; -. [O96013-3]
DR   ProteomicsDB; 51195; -. [O96013-4]
DR   DNASU; 10298; -.
DR   Ensembl; ENST00000321944; ENSP00000326864; ENSG00000130669. [O96013-4]
DR   Ensembl; ENST00000358301; ENSP00000351049; ENSG00000130669. [O96013-1]
DR   Ensembl; ENST00000360442; ENSP00000353625; ENSG00000130669. [O96013-1]
DR   Ensembl; ENST00000593690; ENSP00000469413; ENSG00000130669. [O96013-1]
DR   Ensembl; ENST00000599386; ENSP00000471157; ENSG00000130669. [O96013-3]
DR   Ensembl; ENST00000599470; ENSP00000470284; ENSG00000130669. [O96013-3]
DR   GeneID; 10298; -.
DR   KEGG; hsa:10298; -.
DR   UCSC; uc002okj.2; human. [O96013-1]
DR   CTD; 10298; -.
DR   DisGeNET; 10298; -.
DR   GeneCards; PAK4; -.
DR   HGNC; HGNC:16059; PAK4.
DR   HPA; CAB025747; -.
DR   HPA; CAB044670; -.
DR   HPA; HPA070175; -.
DR   HPA; HPA072220; -.
DR   MIM; 605451; gene.
DR   neXtProt; NX_O96013; -.
DR   OpenTargets; ENSG00000130669; -.
DR   PharmGKB; PA32920; -.
DR   eggNOG; KOG0578; Eukaryota.
DR   eggNOG; ENOG410XP4K; LUCA.
DR   GeneTree; ENSGT00940000159792; -.
DR   HOGENOM; CLU_000288_26_6_1; -.
DR   InParanoid; O96013; -.
DR   KO; K05734; -.
DR   OMA; RDYRHEN; -.
DR   OrthoDB; 757766at2759; -.
DR   PhylomeDB; O96013; -.
DR   TreeFam; TF105352; -.
DR   BRENDA; 2.7.11.1; 2681.
DR   Reactome; R-HSA-428540; Activation of RAC1.
DR   SignaLink; O96013; -.
DR   SIGNOR; O96013; -.
DR   ChiTaRS; PAK4; human.
DR   EvolutionaryTrace; O96013; -.
DR   GeneWiki; PAK4; -.
DR   GenomeRNAi; 10298; -.
DR   Pharos; O96013; Tchem.
DR   PRO; PR:O96013; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; O96013; protein.
DR   Bgee; ENSG00000130669; Expressed in type B pancreatic cell and 232 other tissues.
DR   ExpressionAtlas; O96013; baseline and differential.
DR   Genevisible; O96013; HS.
DR   GO; GO:0005912; C:adherens junction; HDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; HDA:BHF-UCL.
DR   GO; GO:0004672; F:protein kinase activity; NAS:ProtInc.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR   GO; GO:0032147; P:activation of protein kinase activity; IBA:GO_Central.
DR   GO; GO:0006915; P:apoptotic process; TAS:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0016477; P:cell migration; TAS:UniProtKB.
DR   GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
DR   GO; GO:0007010; P:cytoskeleton organization; TAS:UniProtKB.
DR   GO; GO:0060996; P:dendritic spine development; IEA:Ensembl.
DR   GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IMP:BHF-UCL.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
DR   GO; GO:0001558; P:regulation of cell growth; TAS:UniProtKB.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
DR   GO; GO:0023014; P:signal transduction by protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0031098; P:stress-activated protein kinase signaling cascade; IBA:GO_Central.
DR   CDD; cd01093; CRIB_PAK_like; 1.
DR   DisProt; DP01184; -.
DR   Gene3D; 3.90.810.10; -; 1.
DR   InterPro; IPR000095; CRIB_dom.
DR   InterPro; IPR036936; CRIB_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR033923; PAK_BD.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   Pfam; PF00786; PBD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00285; PBD; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50108; CRIB; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Apoptosis; ATP-binding; Cell cycle;
KW   Cytoplasm; Kinase; Methylation; Nucleotide-binding; Phosphoprotein;
KW   Polymorphism; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase; Ubl conjugation.
FT   CHAIN           1..591
FT                   /note="Serine/threonine-protein kinase PAK 4"
FT                   /id="PRO_0000086474"
FT   DOMAIN          11..24
FT                   /note="CRIB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT   DOMAIN          321..572
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   NP_BIND         327..335
FT                   /note="ATP"
FT                   /evidence="ECO:0000244|PDB:4XBR, ECO:0000244|PDB:4XBU,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000269|PubMed:26607847"
FT   NP_BIND         396..398
FT                   /note="ATP"
FT                   /evidence="ECO:0000244|PDB:4XBR, ECO:0000244|PDB:4XBU,
FT                   ECO:0000269|PubMed:26607847"
FT   NP_BIND         458..460
FT                   /note="ATP"
FT                   /evidence="ECO:0000244|PDB:4XBR, ECO:0000244|PDB:4XBU,
FT                   ECO:0000269|PubMed:26607847"
FT   REGION          25..320
FT                   /note="Linker"
FT   REGION          298..323
FT                   /note="GEF-interaction domain (GID)"
FT   COMPBIAS        105..108
FT                   /note="Poly-Pro"
FT   COMPBIAS        242..247
FT                   /note="Poly-Ser"
FT   ACT_SITE        440
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         350
FT                   /note="ATP"
FT                   /evidence="ECO:0000244|PDB:4XBR, ECO:0000244|PDB:4XBU,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000269|PubMed:26607847"
FT   MOD_RES         41
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18691976,
FT                   ECO:0000244|PubMed:19369195, ECO:0000244|PubMed:23186163"
FT   MOD_RES         78
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000244|PubMed:24129315"
FT   MOD_RES         104
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18691976,
FT                   ECO:0000244|PubMed:19369195"
FT   MOD_RES         148
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18691976,
FT                   ECO:0000244|PubMed:19369195"
FT   MOD_RES         167
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18691976,
FT                   ECO:0000244|PubMed:19369195"
FT   MOD_RES         181
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:18691976, ECO:0000244|PubMed:19369195,
FT                   ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:21406692,
FT                   ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569"
FT   MOD_RES         187
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:19369195"
FT   MOD_RES         195
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:19369195"
FT   MOD_RES         207
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         258
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18691976,
FT                   ECO:0000244|PubMed:19369195"
FT   MOD_RES         267
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18691976"
FT   MOD_RES         291
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18691976,
FT                   ECO:0000244|PubMed:19369195"
FT   MOD_RES         474
FT                   /note="Phosphoserine; by autocatalysis"
FT                   /evidence="ECO:0000244|PubMed:17081983,
FT                   ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:18691976,
FT                   ECO:0000244|PubMed:19369195, ECO:0000244|PubMed:19690332,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692,
FT                   ECO:0000244|PubMed:23186163, ECO:0000269|Ref.31"
FT   VAR_SEQ         69..221
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:10574461,
FT                   ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:17974005"
FT                   /id="VSP_017572"
FT   VAR_SEQ         120
FT                   /note="E -> K (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_004892"
FT   VAR_SEQ         121..285
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_004893"
FT   VAR_SEQ         132..221
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_017573"
FT   VARIANT         135
FT                   /note="R -> Q (in dbSNP:rs56099436)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_040970"
FT   VARIANT         139
FT                   /note="A -> T (in dbSNP:rs35655056)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_040971"
FT   MUTAGEN         445
FT                   /note="S->N: Approximately 30-fold increased
FT                   autophosphorylation (constitutively active mutant)."
FT                   /evidence="ECO:0000269|PubMed:11313478"
FT   MUTAGEN         474
FT                   /note="S->E: Approximately 3-fold increased
FT                   autophosphorylation."
FT                   /evidence="ECO:0000269|PubMed:11313478"
FT   STRAND          15..26
FT                   /evidence="ECO:0000244|PDB:2OV2"
FT   TURN            27..30
FT                   /evidence="ECO:0000244|PDB:2OV2"
FT   STRAND          31..34
FT                   /evidence="ECO:0000244|PDB:2OV2"
FT   HELIX           37..39
FT                   /evidence="ECO:0000244|PDB:2OV2"
FT   TURN            40..42
FT                   /evidence="ECO:0000244|PDB:2OV2"
FT   TURN            46..48
FT                   /evidence="ECO:0000244|PDB:4L67"
FT   HELIX           301..311
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   STRAND          312..315
FT                   /evidence="ECO:0000244|PDB:4O0Y"
FT   HELIX           317..319
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   STRAND          321..329
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   STRAND          331..333
FT                   /evidence="ECO:0000244|PDB:4L67"
FT   STRAND          334..340
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   TURN            341..343
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   STRAND          346..353
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   HELIX           354..356
FT                   /evidence="ECO:0000244|PDB:2Q0N"
FT   HELIX           360..362
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   HELIX           363..369
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   TURN            370..372
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   STRAND          381..387
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   STRAND          390..395
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   HELIX           403..409
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   HELIX           414..433
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   HELIX           443..445
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   STRAND          446..448
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   STRAND          454..456
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   HELIX           459..461
FT                   /evidence="ECO:0000244|PDB:4FII"
FT   STRAND          467..469
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   STRAND          475..477
FT                   /evidence="ECO:0000244|PDB:2Q0N"
FT   HELIX           479..481
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   HELIX           484..487
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   HELIX           495..510
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   TURN            514..517
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   HELIX           520..529
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   HELIX           538..540
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   HELIX           543..552
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   TURN            557..559
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   HELIX           563..566
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   HELIX           570..574
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   HELIX           578..581
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   HELIX           582..584
FT                   /evidence="ECO:0000244|PDB:2J0I"
FT   TURN            586..588
FT                   /evidence="ECO:0000244|PDB:2J0I"
SQ   SEQUENCE   591 AA;  64072 MW;  04C2A5C0B06427D5 CRC64;
     MFGKRKKRVE ISAPSNFEHR VHTGFDQHEQ KFTGLPRQWQ SLIEESARRP KPLVDPACIT
     SIQPGAPKTI VRGSKGAKDG ALTLLLDEFE NMSVTRSNSL RRDSPPPPAR ARQENGMPEE
     PATTARGGPG KAGSRGRFAG HSEAGGGSGD RRRAGPEKRP KSSREGSGGP QESSRDKRPL
     SGPDVGTPQP AGLASGAKLA AGRPFNTYPR ADTDHPSRGA QGEPHDVAPN GPSAGGLAIP
     QSSSSSSRPP TRARGAPSPG VLGPHASEPQ LAPPACTPAA PAVPGPPGPR SPQREPQRVS
     HEQFRAALQL VVDPGDPRSY LDNFIKIGEG STGIVCIATV RSSGKLVAVK KMDLRKQQRR
     ELLFNEVVIM RDYQHENVVE MYNSYLVGDE LWVVMEFLEG GALTDIVTHT RMNEEQIAAV
     CLAVLQALSV LHAQGVIHRD IKSDSILLTH DGRVKLSDFG FCAQVSKEVP RRKSLVGTPY
     WMAPELISRL PYGPEVDIWS LGIMVIEMVD GEPPYFNEPP LKAMKMIRDN LPPRLKNLHK
     VSPSLKGFLD RLLVRDPAQR ATAAELLKHP FLAKAGPPAS IVPLMRQNRT R
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