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Dual specificity protein kinase CLK2 (EC 2.7.12.1) (CDC-like kinase 2)

 CLK2_HUMAN              Reviewed;         499 AA.
P49760; B1AVS9; B5MBX6; Q96CQ0;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
22-NOV-2017, entry version 178.
RecName: Full=Dual specificity protein kinase CLK2;
EC=2.7.12.1;
AltName: Full=CDC-like kinase 2;
Name=CLK2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
PubMed=7990150; DOI=10.1006/jmbi.1994.1763;
Hanes J.J., der Kammer H., Klaudiny J.J., Scheit K.H.;
"Characterization by cDNA cloning of two new human protein kinases.
Evidence by sequence comparison of a new family of mammalian protein
kinases.";
J. Mol. Biol. 244:665-672(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=9331372;
Winfield S.L., Tayebi N., Martin B.M., Ginns E.I., Sidransky E.;
"Identification of three additional genes contiguous to the
glucocerebrosidase locus on chromosome 1q21: implications for Gaucher
disease.";
Genome Res. 7:1020-1026(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Lung, and Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[5]
FUNCTION.
PubMed=8910305; DOI=10.1074/jbc.271.44.27299;
Lee K., Du C., Horn M., Rabinow L.;
"Activity and autophosphorylation of LAMMER protein kinases.";
J. Biol. Chem. 271:27299-27303(1996).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=9637771; DOI=10.1006/excr.1998.4083;
Duncan P.I., Stojdl D.F., Marius R.M., Scheit K.H., Bell J.C.;
"The Clk2 and Clk3 dual-specificity protein kinases regulate the
intranuclear distribution of SR proteins and influence pre-mRNA
splicing.";
Exp. Cell Res. 241:300-308(1998).
[7]
FUNCTION.
PubMed=10480872; DOI=10.1074/jbc.274.38.26697;
Moeslein F.M., Myers M.P., Landreth G.E.;
"The CLK family kinases, CLK1 and CLK2, phosphorylate and activate the
tyrosine phosphatase, PTP-1B.";
J. Biol. Chem. 274:26697-26704(1999).
[8]
INTERACTION WITH UBL5.
PubMed=12705895; DOI=10.1016/S0006-291X(03)00549-7;
Kantham L., Kerr-Bayles L., Godde N., Quick M., Webb R.,
Sunderland T., Bond J., Walder K., Augert G., Collier G.;
"Beacon interacts with cdc2/cdc28-like kinases.";
Biochem. Biophys. Res. Commun. 304:125-129(2003).
[9]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
FUNCTION, ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
PubMed=19168442; DOI=10.1161/CIRCRESAHA.108.183905;
Eisenreich A., Bogdanov V.Y., Zakrzewicz A., Pries A., Antoniak S.,
Poller W., Schultheiss H.P., Rauch U.;
"Cdc2-like kinases and DNA topoisomerase I regulate alternative
splicing of tissue factor in human endothelial cells.";
Circ. Res. 104:589-599(2009).
[13]
INTERACTION WITH RBMX.
PubMed=19282290; DOI=10.1074/jbc.M901026200;
Heinrich B., Zhang Z., Raitskin O., Hiller M., Benderska N.,
Hartmann A.M., Bracco L., Elliott D., Ben-Ari S., Soreq H.,
Sperling J., Sperling R., Stamm S.;
"Heterogeneous nuclear ribonucleoprotein G regulates splice site
selection by binding to CC(A/C)-rich regions in pre-mRNA.";
J. Biol. Chem. 284:14303-14315(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142 AND TYR-153, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[15]
PHOSPHORYLATION AT SER-34 AND THR-127, AND INTERACTION WITH AKT1.
PubMed=20682768; DOI=10.1074/jbc.M110.122044;
Nam S.Y., Seo H.H., Park H.S., An S., Kim J.Y., Yang K.H., Kim C.S.,
Jeong M., Jin Y.W.;
"Phosphorylation of CLK2 at serine 34 and threonine 127 by AKT
controls cell survival after ionizing radiation.";
J. Biol. Chem. 285:31157-31163(2010).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98 AND SER-142, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) OF 135-496.
Structural genomics consortium (SGC);
"Structure of human cdc2-like kinase 2 (clk2).";
Submitted (AUG-2010) to the PDB data bank.
-!- FUNCTION: Dual specificity kinase acting on both serine/threonine
and tyrosine-containing substrates. Phosphorylates serine- and
arginine-rich (SR) proteins of the spliceosomal complex. May be a
constituent of a network of regulatory mechanisms that enable SR
proteins to control RNA splicing and can cause redistribution of
SR proteins from speckles to a diffuse nucleoplasmic distribution.
Acts as a suppressor of hepatic gluconeogenesis and glucose output
by repressing PPARGC1A transcriptional activity on gluconeogenic
genes via its phosphorylation. Phosphorylates PPP2R5B thereby
stimulating the assembly of PP2A phosphatase with the PPP2R5B-AKT1
complex leading to dephosphorylation of AKT1. Phosphorylates:
PTPN1, SRSF1 and SRSF3. Regulates the alternative splicing of
tissue factor (F3) pre-mRNA in endothelial cells.
{ECO:0000269|PubMed:10480872, ECO:0000269|PubMed:19168442,
ECO:0000269|PubMed:8910305, ECO:0000269|PubMed:9637771}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: 5,6-dichloro-1-b-D-ribofuranosylbenzimidazole
(DRB) inhibits autophosphorylation. TG003 inhibits its kinase
activity and affects the regulation of alternative splicing
mediated by phosphorylation of SR proteins (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Interacts with RBMX. Interacts with AKT1 and UBL5.
{ECO:0000269|PubMed:12705895, ECO:0000269|PubMed:19282290,
ECO:0000269|PubMed:20682768}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-750020, EBI-750020;
Q8WUQ7:CACTIN; NbExp=4; IntAct=EBI-750020, EBI-348479;
P49759-3:CLK1; NbExp=6; IntAct=EBI-750020, EBI-11981867;
P49761:CLK3; NbExp=12; IntAct=EBI-750020, EBI-745579;
Q8N684:CPSF7; NbExp=3; IntAct=EBI-750020, EBI-746909;
P42892:ECE1; NbExp=5; IntAct=EBI-750020, EBI-2859983;
Q53SE7:FLJ13057; NbExp=3; IntAct=EBI-750020, EBI-10172181;
O95198:KLHL2; NbExp=5; IntAct=EBI-750020, EBI-746999;
Q8TBB1:LNX1; NbExp=7; IntAct=EBI-750020, EBI-739832;
Q9P127:LUZP4; NbExp=5; IntAct=EBI-750020, EBI-10198848;
Q9BYD3:MRPL4; NbExp=3; IntAct=EBI-750020, EBI-721368;
Q8NAV1:PRPF38A; NbExp=3; IntAct=EBI-750020, EBI-715374;
Q14498:RBM39; NbExp=8; IntAct=EBI-750020, EBI-395290;
D3DU92:RNPS1; NbExp=5; IntAct=EBI-750020, EBI-10176640;
Q15287:RNPS1; NbExp=4; IntAct=EBI-750020, EBI-395959;
Q9BUV0:RSRP1; NbExp=5; IntAct=EBI-750020, EBI-745604;
O00560:SDCBP; NbExp=3; IntAct=EBI-750020, EBI-727004;
Q8TAD8:SNIP1; NbExp=8; IntAct=EBI-750020, EBI-749336;
P08621:SNRNP70; NbExp=4; IntAct=EBI-750020, EBI-1049228;
P78362:SRPK2; NbExp=3; IntAct=EBI-750020, EBI-593303;
Q8IYB3:SRRM1; NbExp=3; IntAct=EBI-750020, EBI-1055880;
P14373:TRIM27; NbExp=3; IntAct=EBI-750020, EBI-719493;
Q01081-2:U2AF1; NbExp=3; IntAct=EBI-750020, EBI-10176676;
Q7KZS0:UBE2I; NbExp=3; IntAct=EBI-750020, EBI-10180829;
Q96MU7:YTHDC1; NbExp=5; IntAct=EBI-750020, EBI-2849854;
O14978:ZNF263; NbExp=3; IntAct=EBI-750020, EBI-744493;
Q53GI3:ZNF394; NbExp=3; IntAct=EBI-750020, EBI-10211248;
Q8TD17:ZNF398; NbExp=5; IntAct=EBI-750020, EBI-8643207;
Q8WTR7:ZNF473; NbExp=3; IntAct=EBI-750020, EBI-751409;
Q96NG5:ZNF558; NbExp=4; IntAct=EBI-750020, EBI-373363;
Q96EG3:ZNF837; NbExp=4; IntAct=EBI-750020, EBI-11962574;
Q15696:ZRSR2; NbExp=5; IntAct=EBI-750020, EBI-6657923;
-!- SUBCELLULAR LOCATION: Isoform 1: Nucleus. Nucleus speckle.
Note=Inhibition of phosphorylation at Ser-142 results in
accumulation in the nuclear speckle. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 2: Nucleus speckle. Note=Co-
localizes with serine- and arginine-rich (SR) proteins in the
nuclear speckles.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Long;
IsoId=P49760-1; Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=P49760-2; Sequence=VSP_004856, VSP_004857;
Note=Lacks the kinase domain. May be produced at very low levels
due to a premature stop codon in the mRNA, leading to
nonsense-mediated mRNA decay.;
Name=3;
IsoId=P49760-3; Sequence=VSP_038744;
-!- TISSUE SPECIFICITY: Endothelial cells.
{ECO:0000269|PubMed:19168442}.
-!- PTM: Autophosphorylates on all three types of residues.
Phosphorylation on Ser-34 and Thr-127 by AKT1 is induced by
ionizing radiation or insulin. Phosphorylation plays a critical
role in cell proliferation following low dose radiation and
prevents cell death following high dose radiation. Phosphorylation
at Thr-344 by PKB/AKT2 induces its kinase activity which is
required for its stability. The phosphorylation status at Ser-142
influences its subnuclear localization; inhibition of
phosphorylation at Ser-142 results in accumulation in the nuclear
speckle. {ECO:0000269|PubMed:20682768,
ECO:0000269|PubMed:9637771}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. Lammer subfamily. {ECO:0000305}.
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EMBL; L29218; AAA61482.1; -; mRNA.
EMBL; L29216; AAA61481.1; -; mRNA.
EMBL; AF023268; AAC51817.1; -; Genomic_DNA.
EMBL; AL713999; CAI95098.1; -; Genomic_DNA.
EMBL; BC014067; AAH14067.1; -; mRNA.
EMBL; BC053603; AAH53603.1; -; mRNA.
CCDS; CCDS1107.1; -. [P49760-3]
CCDS; CCDS72939.1; -. [P49760-1]
PIR; S53637; S53637.
PIR; S53638; S53638.
RefSeq; NP_001281267.1; NM_001294338.1. [P49760-1]
RefSeq; NP_001281268.1; NM_001294339.1.
RefSeq; NP_003984.2; NM_003993.3. [P49760-3]
UniGene; Hs.73986; -.
PDB; 3NR9; X-ray; 2.89 A; A/B/C=135-496.
PDBsum; 3NR9; -.
ProteinModelPortal; P49760; -.
SMR; P49760; -.
BioGrid; 107607; 108.
DIP; DIP-42277N; -.
IntAct; P49760; 79.
MINT; MINT-1683264; -.
STRING; 9606.ENSP00000354856; -.
BindingDB; P49760; -.
ChEMBL; CHEMBL4225; -.
GuidetoPHARMACOLOGY; 1991; -.
iPTMnet; P49760; -.
PhosphoSitePlus; P49760; -.
BioMuta; CLK2; -.
DMDM; 1705919; -.
MaxQB; P49760; -.
PaxDb; P49760; -.
PeptideAtlas; P49760; -.
PRIDE; P49760; -.
DNASU; 1196; -.
Ensembl; ENST00000361168; ENSP00000354856; ENSG00000176444. [P49760-3]
Ensembl; ENST00000368361; ENSP00000357345; ENSG00000176444. [P49760-1]
Ensembl; ENST00000572269; ENSP00000459461; ENSG00000261893. [P49760-3]
Ensembl; ENST00000574445; ENSP00000460443; ENSG00000261893. [P49760-1]
GeneID; 1196; -.
KEGG; hsa:1196; -.
UCSC; uc001fjw.4; human. [P49760-1]
CTD; 1196; -.
DisGeNET; 1196; -.
EuPathDB; HostDB:ENSG00000176444.18; -.
GeneCards; CLK2; -.
H-InvDB; HIX0001112; -.
HGNC; HGNC:2069; CLK2.
HPA; HPA055366; -.
HPA; HPA059507; -.
MIM; 602989; gene.
neXtProt; NX_P49760; -.
OpenTargets; ENSG00000176444; -.
PharmGKB; PA26595; -.
eggNOG; KOG0671; Eukaryota.
eggNOG; ENOG410XQF2; LUCA.
GeneTree; ENSGT00580000081366; -.
HOGENOM; HOG000203417; -.
HOVERGEN; HBG107720; -.
InParanoid; P49760; -.
KO; K08823; -.
OMA; LGMCVYD; -.
OrthoDB; EOG09370FW4; -.
PhylomeDB; P49760; -.
TreeFam; TF101041; -.
BRENDA; 2.7.12.1; 2681.
SignaLink; P49760; -.
SIGNOR; P49760; -.
ChiTaRS; CLK2; human.
EvolutionaryTrace; P49760; -.
GeneWiki; CLK2; -.
GenomeRNAi; 1196; -.
PRO; PR:P49760; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000176444; -.
CleanEx; HS_CLK2; -.
ExpressionAtlas; P49760; baseline and differential.
Genevisible; P49760; HS.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
GO; GO:0045721; P:negative regulation of gluconeogenesis; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0043484; P:regulation of RNA splicing; IDA:UniProtKB.
GO; GO:0010212; P:response to ionizing radiation; IMP:UniProtKB.
GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Complete proteome;
Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Transferase;
Tyrosine-protein kinase.
CHAIN 1 499 Dual specificity protein kinase CLK2.
/FTId=PRO_0000085868.
DOMAIN 163 479 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 169 177 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 290 290 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 193 193 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 34 34 Phosphoserine; by PKB/AKT1.
{ECO:0000269|PubMed:20682768}.
MOD_RES 98 98 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 99 99 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:O35491}.
MOD_RES 127 127 Phosphothreonine; by PKB/AKT1.
{ECO:0000269|PubMed:20682768}.
MOD_RES 142 142 Phosphoserine; by autocatalysis.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163}.
MOD_RES 153 153 Phosphotyrosine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 344 344 Phosphothreonine; by PKB/AKT2.
{ECO:0000250|UniProtKB:O35491}.
VAR_SEQ 134 139 QHSSRR -> MKSLAP (in isoform 2).
{ECO:0000303|PubMed:7990150}.
/FTId=VSP_004856.
VAR_SEQ 134 134 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_038744.
VAR_SEQ 140 499 Missing (in isoform 2).
{ECO:0000303|PubMed:7990150}.
/FTId=VSP_004857.
TURN 146 149 {ECO:0000244|PDB:3NR9}.
TURN 160 162 {ECO:0000244|PDB:3NR9}.
STRAND 163 172 {ECO:0000244|PDB:3NR9}.
STRAND 175 182 {ECO:0000244|PDB:3NR9}.
TURN 183 187 {ECO:0000244|PDB:3NR9}.
STRAND 189 195 {ECO:0000244|PDB:3NR9}.
HELIX 199 218 {ECO:0000244|PDB:3NR9}.
STRAND 229 235 {ECO:0000244|PDB:3NR9}.
STRAND 238 244 {ECO:0000244|PDB:3NR9}.
HELIX 250 256 {ECO:0000244|PDB:3NR9}.
TURN 257 259 {ECO:0000244|PDB:3NR9}.
HELIX 264 283 {ECO:0000244|PDB:3NR9}.
HELIX 293 295 {ECO:0000244|PDB:3NR9}.
STRAND 296 299 {ECO:0000244|PDB:3NR9}.
TURN 309 311 {ECO:0000244|PDB:3NR9}.
STRAND 317 319 {ECO:0000244|PDB:3NR9}.
STRAND 323 325 {ECO:0000244|PDB:3NR9}.
STRAND 332 336 {ECO:0000244|PDB:3NR9}.
HELIX 345 347 {ECO:0000244|PDB:3NR9}.
HELIX 350 353 {ECO:0000244|PDB:3NR9}.
HELIX 361 376 {ECO:0000244|PDB:3NR9}.
HELIX 386 397 {ECO:0000244|PDB:3NR9}.
HELIX 402 407 {ECO:0000244|PDB:3NR9}.
HELIX 411 413 {ECO:0000244|PDB:3NR9}.
HELIX 426 434 {ECO:0000244|PDB:3NR9}.
HELIX 438 441 {ECO:0000244|PDB:3NR9}.
HELIX 447 459 {ECO:0000244|PDB:3NR9}.
TURN 464 466 {ECO:0000244|PDB:3NR9}.
HELIX 470 475 {ECO:0000244|PDB:3NR9}.
HELIX 477 479 {ECO:0000244|PDB:3NR9}.
HELIX 480 483 {ECO:0000244|PDB:3NR9}.
SEQUENCE 499 AA; 60090 MW; E43BBF3BAD6EF991 CRC64;
MPHPRRYHSS ERGSRGSYRE HYRSRKHKRR RSRSWSSSSD RTRRRRREDS YHVRSRSSYD
DRSSDRRVYD RRYCGSYRRN DYSRDRGDAY YDTDYRHSYE YQRENSSYRS QRSSRRKHRR
RRRRSRTFSR SSSQHSSRRA KSVEDDAEGH LIYHVGDWLQ ERYEIVSTLG EGTFGRVVQC
VDHRRGGARV ALKIIKNVEK YKEAARLEIN VLEKINEKDP DNKNLCVQMF DWFDYHGHMC
ISFELLGLST FDFLKDNNYL PYPIHQVRHM AFQLCQAVKF LHDNKLTHTD LKPENILFVN
SDYELTYNLE KKRDERSVKS TAVRVVDFGS ATFDHEHHST IVSTRHYRAP EVILELGWSQ
PCDVWSIGCI IFEYYVGFTL FQTHDNREHL AMMERILGPI PSRMIRKTRK QKYFYRGRLD
WDENTSAGRY VRENCKPLRR YLTSEAEEHH QLFDLIESML EYEPAKRLTL GEALQHPFFA
RLRAEPPNKL WDSSRDISR


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