PKN1_MOUSE
ID PKN1_MOUSE Reviewed; 946 AA.
AC P70268; Q3UEA6; Q7TST2; Q8BTL8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 3.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Serine/threonine-protein kinase N1;
DE EC=2.7.11.13 {ECO:0000250|UniProtKB:Q16512};
DE AltName: Full=Protein kinase C-like 1;
DE AltName: Full=Protein kinase C-like PKN;
DE AltName: Full=Protein-kinase C-related kinase 1;
DE AltName: Full=Serine-threonine protein kinase N;
GN Name=Pkn1; Synonyms=Pkn, Prk1, Prkcl1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Olfactory epithelium;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 664-946.
RC STRAIN=129;
RX PubMed=8858105; DOI=10.1006/bbrc.1996.1469;
RA Batshake B., Sundelin S.;
RT "The mouse genes for the EP1 prostanoid receptor and the PKN protein kinase
RT overlap.";
RL Biochem. Biophys. Res. Commun. 227:70-76(1996).
RN [4]
RP ACTIVITY REGULATION, AND INTERACTION WITH RHOA.
RX PubMed=8571127; DOI=10.1126/science.271.5249.648;
RA Amano M., Mukai H., Ono Y., Chihara K., Matsui T., Hamajima Y., Okawa K.,
RA Iwamatsu A., Kaibuchi K.;
RT "Identification of a putative target for Rho as the serine-threonine kinase
RT protein kinase N.";
RL Science 271:648-650(1996).
RN [5]
RP INTERACTION WITH ZFAND6.
RC TISSUE=Liver, Mammary gland, and Uterus;
RX PubMed=11054541; DOI=10.1016/s0378-1119(00)00365-6;
RA Duan W., Sun B., Li T.W., Tan B.J., Lee M.K., Teo T.S.;
RT "Cloning and characterization of AWP1, a novel protein that associates with
RT serine/threonine kinase PRK1 in vivo.";
RL Gene 256:113-121(2000).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-920, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-536; SER-540; THR-918 AND
RP SER-920, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: PKC-related serine/threonine-protein kinase involved in
CC various processes such as regulation of the intermediate filaments of
CC the actin cytoskeleton, cell migration, tumor cell invasion and
CC transcription regulation. Part of a signaling cascade that begins with
CC the activation of the adrenergic receptor ADRA1B and leads to the
CC activation of MAPK14. Regulates the cytoskeletal network by
CC phosphorylating proteins such as VIM and neurofilament proteins NEFH,
CC NEFL and NEFM, leading to inhibit their polymerization. Phosphorylates
CC 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau, lowering its ability to
CC bind to microtubules, resulting in disruption of tubulin assembly. Acts
CC as a key coactivator of androgen receptor (ANDR)-dependent
CC transcription, by being recruited to ANDR target genes and specifically
CC mediating phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a
CC specific tag for epigenetic transcriptional activation that promotes
CC demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C.
CC Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their import
CC in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser-159', 'Ser-
CC 163' and 'Ser-170' of MARCKS, and GFAP. Able to phosphorylate RPS6 in
CC vitro. {ECO:0000250|UniProtKB:Q16512}.
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=2.7.11.13;
CC Evidence={ECO:0000250|UniProtKB:Q16512};
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=2.7.11.13; Evidence={ECO:0000250|UniProtKB:Q16512};
CC -!- ACTIVITY REGULATION: Kinase activity is activated upon binding to Rho
CC proteins (RHOA, RHOB and RAC1). Activated by lipids, particularly
CC cardiolipin and to a lesser extent by other acidic phospholipids.
CC Activated by caspase-3 (CASP3) cleavage during apoptosis. Two specific
CC sites, Thr-778 (activation loop of the kinase domain) and Ser-920 (turn
CC motif), need to be phosphorylated for its full activation.
CC {ECO:0000269|PubMed:8571127}.
CC -!- SUBUNIT: Interacts with ZFAND6 (PubMed:11054541). Interacts with ANDR.
CC Interacts with PRKCB. Interacts (via REM 1 and REM 2 repeats) with RAC1
CC (By similarity). Interacts (via REM 1 repeat) with RHOA
CC (PubMed:8571127). Interacts with RHOB. Interacts (via C-terminus) with
CC PDPK1. Interacts with CCNT2; enhances MYOD1-dependent transcription.
CC Component of a signaling complex containing at least AKAP13, PKN1,
CC MAPK14, ZAK and MAP2K3. Within this complex, AKAP13 interacts directly
CC with PKN1, which in turn recruits MAPK14, MAP2K3 and ZAK (By
CC similarity). {ECO:0000250|UniProtKB:Q16512,
CC ECO:0000269|PubMed:11054541, ECO:0000269|PubMed:8571127}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16512}. Nucleus
CC {ECO:0000250|UniProtKB:Q16512}. Endosome
CC {ECO:0000250|UniProtKB:Q16512}. Cell membrane
CC {ECO:0000250|UniProtKB:Q63433}; Peripheral membrane protein
CC {ECO:0000250}. Cleavage furrow {ECO:0000250|UniProtKB:Q16512}. Midbody
CC {ECO:0000250|UniProtKB:Q16512}. Note=Associates with chromatin in a
CC ligand-dependent manner. Localization to endosomes is mediated via its
CC interaction with RHOB. Association to the cell membrane is dependent on
CC Ser-377 phosphorylation. Accumulates during telophase at the cleavage
CC furrow and finally concentrates around the midbody in cytokinesis.
CC {ECO:0000250|UniProtKB:Q16512, ECO:0000250|UniProtKB:Q63433}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P70268-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P70268-2; Sequence=VSP_039223;
CC -!- DOMAIN: The C1 domain does not bind the diacylglycerol (DAG).
CC {ECO:0000250}.
CC -!- PTM: Autophosphorylated; preferably on serine. {ECO:0000250}.
CC -!- PTM: Activated by limited proteolysis with trypsin. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000305}.
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DR EMBL; AK089431; BAC40880.2; -; mRNA.
DR EMBL; AK149649; BAE29005.1; -; mRNA.
DR EMBL; BC052923; AAH52923.1; -; mRNA.
DR EMBL; Y07611; CAA68883.1; -; Genomic_DNA.
DR CCDS; CCDS22459.1; -. [P70268-1]
DR CCDS; CCDS57627.1; -. [P70268-2]
DR PIR; PC4220; PC4220.
DR RefSeq; NP_001186522.1; NM_001199593.1. [P70268-2]
DR RefSeq; NP_796236.2; NM_177262.4. [P70268-1]
DR AlphaFoldDB; P70268; -.
DR SMR; P70268; -.
DR BioGRID; 236296; 6.
DR IntAct; P70268; 3.
DR STRING; 10090.ENSMUSP00000005616; -.
DR iPTMnet; P70268; -.
DR PhosphoSitePlus; P70268; -.
DR EPD; P70268; -.
DR jPOST; P70268; -.
DR MaxQB; P70268; -.
DR PaxDb; P70268; -.
DR PeptideAtlas; P70268; -.
DR PRIDE; P70268; -.
DR ProteomicsDB; 289751; -. [P70268-1]
DR ProteomicsDB; 289752; -. [P70268-2]
DR Antibodypedia; 1296; 252 antibodies from 34 providers.
DR DNASU; 320795; -.
DR Ensembl; ENSMUST00000005616; ENSMUSP00000005616; ENSMUSG00000057672. [P70268-1]
DR Ensembl; ENSMUST00000144258; ENSMUSP00000116235; ENSMUSG00000057672. [P70268-2]
DR GeneID; 320795; -.
DR KEGG; mmu:320795; -.
DR UCSC; uc009mkw.2; mouse. [P70268-2]
DR UCSC; uc009mkx.2; mouse. [P70268-1]
DR CTD; 5585; -.
DR MGI; MGI:108022; Pkn1.
DR VEuPathDB; HostDB:ENSMUSG00000057672; -.
DR eggNOG; KOG0694; Eukaryota.
DR GeneTree; ENSGT00940000154990; -.
DR HOGENOM; CLU_000288_132_1_1; -.
DR InParanoid; P70268; -.
DR OMA; CTELRIE; -.
DR OrthoDB; 520651at2759; -.
DR PhylomeDB; P70268; -.
DR TreeFam; TF102005; -.
DR Reactome; R-MMU-5625740; RHO GTPases activate PKNs.
DR Reactome; R-MMU-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 320795; 8 hits in 75 CRISPR screens.
DR ChiTaRS; Pkn1; mouse.
DR PRO; PR:P70268; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P70268; protein.
DR Bgee; ENSMUSG00000057672; Expressed in granulocyte and 227 other tissues.
DR ExpressionAtlas; P70268; baseline and differential.
DR Genevisible; P70268; MM.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004698; F:calcium-dependent protein kinase C activity; IEA:UniProtKB-EC.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; ISS:UniProtKB.
DR GO; GO:0035402; F:histone kinase activity (H3-T11 specific); ISS:UniProtKB.
DR GO; GO:0050681; F:nuclear androgen receptor binding; ISS:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IMP:MGI.
DR GO; GO:0004697; F:protein kinase C activity; ISO:MGI.
DR GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0001783; P:B cell apoptotic process; IMP:MGI.
DR GO; GO:0001782; P:B cell homeostasis; IMP:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0010631; P:epithelial cell migration; ISS:UniProtKB.
DR GO; GO:0035407; P:histone H3-T11 phosphorylation; ISO:MGI.
DR GO; GO:0006972; P:hyperosmotic response; IDA:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0030889; P:negative regulation of B cell proliferation; IMP:MGI.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0043687; P:post-translational protein modification; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:2000145; P:regulation of cell motility; ISS:UniProtKB.
DR GO; GO:0002634; P:regulation of germinal center formation; IMP:MGI.
DR GO; GO:0002637; P:regulation of immunoglobulin production; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0003014; P:renal system process; IMP:MGI.
DR GO; GO:0048536; P:spleen development; IMP:MGI.
DR CDD; cd08687; C2_PKN-like; 1.
DR CDD; cd11630; HR1_PKN1_2; 1.
DR CDD; cd11622; HR1_PKN_1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037784; C2_PKN.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR036274; HR1_rpt_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR037317; PKN1_HR1_2.
DR InterPro; IPR037313; PKN_HR1_1.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF02185; HR1; 3.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00742; Hr1; 3.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF46585; SSF46585; 3.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51860; REM_1; 3.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cell membrane;
KW Chromatin regulator; Coiled coil; Cytoplasm; Endosome; Kinase; Membrane;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transcription; Transcription regulation;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q16512"
FT CHAIN 2..946
FT /note="Serine/threonine-protein kinase N1"
FT /id="PRO_0000055720"
FT DOMAIN 25..100
FT /note="REM-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 114..193
FT /note="REM-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 202..283
FT /note="REM-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 310..473
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 619..878
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 879..946
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 345..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 744
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 625..633
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 648
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 108..109
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250"
FT SITE 457..458
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250"
FT SITE 561..562
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q16512"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16512"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63433"
FT MOD_RES 451
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q16512"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16512"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16512"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16512"
FT MOD_RES 778
FT /note="Phosphothreonine; by PDPK1"
FT /evidence="ECO:0000250|UniProtKB:Q16512"
FT MOD_RES 782
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16512"
FT MOD_RES 918
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 920
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..7
FT /note="MAGDAVQ -> MAADPPLDSELE (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039223"
SQ SEQUENCE 946 AA; 104411 MW; FCB4E61AD27C1271 CRC64;
MAGDAVQSEP RSWSLLEQLG LAGADLAAPG VQQQLELERE RLKREIRKEL KLKEGAENLR
RATTDLGRSL APVELLLRGS ARRLDLLHQQ LQELHAHVVL PDPAAGSDAT QSLAEGSPIC
SSTNLSRVAG LEKQLAIELK VKQGAENMIQ TYSNGSSKDR KLLLTAQQML QDSKTKIDII
RMQLRRALQA LQAGELESQA APDEAQGDPE LGAVELRIEE LRHHFRVEHA VAEGAKNVLR
LLSGAKAPDR KAVSEAQEKL TESNQKLGLL RESLERRLGE LPADHPKGRL LREELTAASS
SAFSAILPGP FPATHYSTLS KPAPLTGTLE VRVVGCKNLP ETIPWSPPPS VGASGTPESR
TPFLSRPARG LYSRSGSLSG RSSLRGEAEN ATEVSTVLKL DNTVVGQTAW KPCGPNAWDQ
SFTLELERAR ELELAVFWRD QRGLCALKFL KLEDFLDNER HEVQLDMEPQ GCLVAEVTFR
NPIIERIPRL QRQKKIFSKQ QGKAFQRARQ MNIDVATWVR LLRRLIPSAV ATGTFSPNAS
PGAEIRHTGD ISMEKLNLGA DSDSSSQKSP PGLPSTSCSL SSPTHESTTS PELPSETQET
PGPGLCSPLR KSPLTLEDFK FLAVLGRGHF GKVLLSEFRS SGELFAIKAL KKGDIVARDE
VESLMCEKRI LAAVTRAGHP FLVNLFGCFQ TPEHVCFVME YSAGGDLMLH IHSDVFSEPR
AVFYSACVVL GLQFLHEHKI VYRDLKLDNL LLDTEGYVKI ADFGLCKEGM GYGDRTSTFC
GTPEFLAPEV LTDTSYTRAV DWWGLGVLLY EMLVGESPFP GDDEEEVFDS IVNDEVRYPR
FLSAEAIGIM RRLLRRNPER RLGSTERDAE DVKKQPFFRS LGWDVLLARR LPPPFVPTLS
GRTDVSNFDE EFTGEAPTLS PPRDARPLTA AEQAAFRDFD FVAGGY
