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KN motif and ankyrin repeat domain-containing protein 1 (Ankyrin repeat domain-containing protein 15) (Kidney ankyrin repeat-containing protein)

 KANK1_HUMAN             Reviewed;        1352 AA.
Q14678; A2A2W8; D3DRH3; Q5W0W0; Q8IY65; Q8WX74;
29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
30-AUG-2005, sequence version 3.
25-OCT-2017, entry version 150.
RecName: Full=KN motif and ankyrin repeat domain-containing protein 1;
AltName: Full=Ankyrin repeat domain-containing protein 15;
AltName: Full=Kidney ankyrin repeat-containing protein;
Name=KANK1; Synonyms=ANKRD15, KANK, KIAA0172;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ALA-464.
TISSUE=Bone marrow;
PubMed=8724849; DOI=10.1093/dnares/3.1.17;
Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. V.
The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 3:17-24(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLN-432.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
LYS-206 AND GLN-432.
TISSUE=Testis;
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]
PUTATIVE FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12133830; DOI=10.1074/jbc.M204244200;
Sarkar S., Roy B.C., Hatano N., Aoyagi T., Gohji K., Kiyama R.;
"A novel ankyrin repeat-containing gene (Kank) located at 9p24 is a
growth suppressor of renal cell carcinoma.";
J. Biol. Chem. 277:36585-36591(2002).
[6]
ALTERNATIVE PROMOTER USAGE (ISOFORM 2), AND TISSUE SPECIFICITY.
PubMed=15823577; DOI=10.1016/j.bbrc.2005.03.106;
Wang Y., Onishi Y., Kakinuma N., Roy B.C., Aoyagi T., Kiyama R.;
"Alternative splicing of the human Kank gene produces two types of
Kank protein.";
Biochem. Biophys. Res. Commun. 330:1247-1253(2005).
[7]
INVOLVEMENT IN CPSQ2.
PubMed=16301218; DOI=10.1093/hmg/ddi415;
Lerer I., Sagi M., Meiner V., Cohen T., Zlotogora J., Abeliovich D.;
"Deletion of the ANKRD15 gene at 9p24.3 causes parent-of-origin-
dependent inheritance of familial cerebral palsy.";
Hum. Mol. Genet. 14:3911-3920(2005).
[8]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CTNNB1, AND
MUTAGENESIS OF LEU-43; ILE-52; 65-LYS--LYS-68; LEU-125; LEU-129;
ILE-134; LEU-613; LEU-616; LEU-620; LEU-622; 979-LYS--LYS-981 AND
991-LYS-LYS-992.
PubMed=16968744; DOI=10.1242/jcs.03169;
Wang Y., Kakinuma N., Zhu Y., Kiyama R.;
"Nucleo-cytoplasmic shuttling of human Kank protein accompanies
intracellular translocation of beta-catenin.";
J. Cell Sci. 119:4002-4010(2006).
[9]
FUNCTION, PHOSPHORYLATION AT SER-325, INTERACTION WITH YWHAB; YWHAG;
YWHAE; YWHAH; YWHAQ; YWHAZ AND SFN, AND MUTAGENESIS OF SER-325.
PubMed=18458160; DOI=10.1083/jcb.200707022;
Kakinuma N., Roy B.C., Zhu Y., Wang Y., Kiyama R.;
"Kank regulates RhoA-dependent formation of actin stress fibers and
cell migration via 14-3-3 in PI3K-Akt signaling.";
J. Cell Biol. 181:537-549(2008).
[10]
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).
[11]
INTERACTION WITH KIF21A.
PubMed=19559006; DOI=10.1016/j.bbrc.2009.06.109;
Kakinuma N., Kiyama R.;
"A major mutation of KIF21A associated with congenital fibrosis of the
extraocular muscles type 1 (CFEOM1) enhances translocation of Kank1 to
the membrane.";
Biochem. Biophys. Res. Commun. 386:639-644(2009).
[12]
FUNCTION, AND INTERACTION WITH BAIAP2.
PubMed=19171758; DOI=10.1083/jcb.200805147;
Roy B.C., Kakinuma N., Kiyama R.;
"Kank attenuates actin remodeling by preventing interaction between
IRSp53 and Rac1.";
J. Cell Biol. 184:253-267(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
FUNCTION, AND INTERACTION WITH ARFGEF1.
PubMed=22084092; DOI=10.1073/pnas.1117011108;
Li C.C., Kuo J.C., Waterman C.M., Kiyama R., Moss J., Vaughan M.;
"Effects of brefeldin A-inhibited guanine nucleotide-exchange (BIG) 1
and KANK1 proteins on cell polarity and directed migration during
wound healing.";
Proc. Natl. Acad. Sci. U.S.A. 108:19228-19233(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, 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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Involved in the control of cytoskeleton formation by
regulating actin polymerization. Inhibits actin fiber formation
and cell migration. Inhibits RhoA activity; the function involves
phosphorylation through PI3K/Akt signaling and may depend on the
competetive interaction with 14-3-3 adapter proteins to sequester
them from active complexes. Inhibits the formation of lamellipodia
but not of filopodia; the function may depend on the competetive
interaction with BAIAP2 to block its association with activated
RAC1. Inhibits fibronectin-mediated cell spreading; the function
is partially mediated by BAIAP2. Inhibits neurite outgrowth.
Involved in the establishment and persistence of cell polarity
during directed cell movement in wound healing. In the nucleus, is
involved in beta-catenin-dependent activation of transcription.
Potential tumor suppressor for renal cell carcinoma.
{ECO:0000269|PubMed:16968744, ECO:0000269|PubMed:18458160,
ECO:0000269|PubMed:19171758, ECO:0000269|PubMed:22084092}.
-!- SUBUNIT: Interacts with YWHAQ; the interaction requires KANK1
phosphorylation at Ser-325 and is enhanced by growth factor
stimulation. Interacts with YWHAB, YWHAG, YWHAE, YWHAH, YWHAZ and
SFN; the interaction requires KANK1 phosphorylation at Ser-325.
Interacts with ARFGEF1; however, colocalization cannot be
experimentally confirmed. Interacts with BAIAP2. Interacts (via
ANK repeats 1-5) with KIF21A (via coiled coil region); KIF21A
enhances translocation of KANK1 to the plasma membrane. Interacts
with CTNNB1. {ECO:0000269|PubMed:16968744,
ECO:0000269|PubMed:18458160, ECO:0000269|PubMed:19171758,
ECO:0000269|PubMed:19559006, ECO:0000269|PubMed:22084092}.
-!- INTERACTION:
Q9Y6D6:ARFGEF1; NbExp=8; IntAct=EBI-2556221, EBI-1044254;
Q9UQB8:BAIAP2; NbExp=6; IntAct=EBI-2556221, EBI-525456;
Q9UQB8-4:BAIAP2; NbExp=4; IntAct=EBI-6173812, EBI-6174091;
P35222:CTNNB1; NbExp=2; IntAct=EBI-2556221, EBI-491549;
Q7Z4S6:KIF21A; NbExp=5; IntAct=EBI-2556221, EBI-2691397;
P62258:YWHAE; NbExp=3; IntAct=EBI-6173812, EBI-356498;
P61981:YWHAG; NbExp=3; IntAct=EBI-6173812, EBI-359832;
Q04917:YWHAH; NbExp=3; IntAct=EBI-6173812, EBI-306940;
P27348:YWHAQ; NbExp=3; IntAct=EBI-6173812, EBI-359854;
-!- SUBCELLULAR LOCATION: Cell projection, ruffle membrane
{ECO:0000269|PubMed:12133830, ECO:0000269|PubMed:16968744}.
Note=Colocalizes with KIF21A in membrane ruffles.
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Nucleus. Note=Shuttles
between the cytoplasm and nucleus.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus. Cell
projection, ruffle membrane. Note=Shuttles between the cytoplasm
and nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage; Named isoforms=2;
Name=1; Synonyms=Kank-L;
IsoId=Q14678-1; Sequence=Displayed;
Name=2; Synonyms=Kank-S;
IsoId=Q14678-2; Sequence=VSP_043958;
-!- TISSUE SPECIFICITY: Widely expressed. Isoform 1 is predominantly
expressed in heart and kidney. Isoform 2 probably is widely
expressed at basic levels. {ECO:0000269|PubMed:15823577}.
-!- DISEASE: Cerebral palsy, spastic quadriplegic 2 (CPSQ2)
[MIM:612900]: A non-progressive disorder of movement and/or
posture resulting from defects in the developing central nervous
system. Affected individuals manifest congenital hypotonia
evolving over the first year to spastic quadriplegia with
accompanying transient nystagmus and varying degrees of mental
retardation. Neuroimaging shows brain atrophy and
ventriculomegaly. {ECO:0000269|PubMed:16301218}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- SEQUENCE CAUTION:
Sequence=BAA11489.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; D79994; BAA11489.2; ALT_INIT; mRNA.
EMBL; AL136979; CAH70388.1; -; Genomic_DNA.
EMBL; AL136979; CAM13084.1; -; Genomic_DNA.
EMBL; CH471071; EAW58821.1; -; Genomic_DNA.
EMBL; CH471071; EAW58822.1; -; Genomic_DNA.
EMBL; BC037495; AAH37495.1; -; mRNA.
CCDS; CCDS34976.1; -. [Q14678-1]
CCDS; CCDS6441.1; -. [Q14678-2]
RefSeq; NP_001243805.1; NM_001256876.1. [Q14678-1]
RefSeq; NP_001243806.1; NM_001256877.1. [Q14678-1]
RefSeq; NP_055973.2; NM_015158.3. [Q14678-1]
RefSeq; XP_016870003.1; XM_017014514.1. [Q14678-1]
RefSeq; XP_016870004.1; XM_017014515.1. [Q14678-1]
RefSeq; XP_016870016.1; XM_017014527.1. [Q14678-2]
RefSeq; XP_016870017.1; XM_017014528.1. [Q14678-2]
RefSeq; XP_016870018.1; XM_017014529.1. [Q14678-2]
RefSeq; XP_016870019.1; XM_017014530.1. [Q14678-2]
UniGene; Hs.306764; -.
ProteinModelPortal; Q14678; -.
SMR; Q14678; -.
BioGrid; 116798; 12.
DIP; DIP-56491N; -.
IntAct; Q14678; 17.
MINT; MINT-7997401; -.
STRING; 9606.ENSP00000371734; -.
iPTMnet; Q14678; -.
PhosphoSitePlus; Q14678; -.
SwissPalm; Q14678; -.
BioMuta; KANK1; -.
DMDM; 73920184; -.
EPD; Q14678; -.
MaxQB; Q14678; -.
PaxDb; Q14678; -.
PeptideAtlas; Q14678; -.
PRIDE; Q14678; -.
Ensembl; ENST00000382293; ENSP00000371730; ENSG00000107104. [Q14678-2]
Ensembl; ENST00000382297; ENSP00000371734; ENSG00000107104. [Q14678-1]
Ensembl; ENST00000382303; ENSP00000371740; ENSG00000107104. [Q14678-1]
Ensembl; ENST00000619269; ENSP00000477725; ENSG00000107104. [Q14678-1]
GeneID; 23189; -.
KEGG; hsa:23189; -.
UCSC; uc003zgl.3; human. [Q14678-1]
CTD; 23189; -.
DisGeNET; 23189; -.
EuPathDB; HostDB:ENSG00000107104.18; -.
GeneCards; KANK1; -.
HGNC; HGNC:19309; KANK1.
HPA; HPA005539; -.
HPA; HPA056090; -.
MalaCards; KANK1; -.
MIM; 607704; gene.
MIM; 612900; phenotype.
neXtProt; NX_Q14678; -.
OpenTargets; ENSG00000107104; -.
Orphanet; 210141; Inherited congenital spastic tetraplegia.
PharmGKB; PA162392554; -.
eggNOG; KOG0514; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00530000063448; -.
HOGENOM; HOG000230897; -.
HOVERGEN; HBG050511; -.
InParanoid; Q14678; -.
OrthoDB; EOG091G0D3F; -.
PhylomeDB; Q14678; -.
TreeFam; TF324499; -.
ChiTaRS; KANK1; human.
GeneWiki; ANKRD15; -.
GenomeRNAi; 23189; -.
PRO; PR:Q14678; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000107104; -.
CleanEx; HS_KANK1; -.
ExpressionAtlas; Q14678; baseline and differential.
Genevisible; Q14678; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; IDA:UniProtKB.
GO; GO:0030837; P:negative regulation of actin filament polymerization; IDA:UniProtKB.
GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IMP:UniProtKB.
GO; GO:2000393; P:negative regulation of lamellipodium morphogenesis; IDA:UniProtKB.
GO; GO:0010977; P:negative regulation of neuron projection development; IDA:UniProtKB.
GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IMP:UniProtKB.
GO; GO:1900028; P:negative regulation of ruffle assembly; IDA:UniProtKB.
GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; IDA:UniProtKB.
GO; GO:0035413; P:positive regulation of catenin import into nucleus; IMP:UniProtKB.
GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IDA:UniProtKB.
GO; GO:0090303; P:positive regulation of wound healing; IMP:UniProtKB.
GO; GO:2000114; P:regulation of establishment of cell polarity; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00204; ANK; 2.
Gene3D; 1.25.40.20; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR021939; KN_motif.
Pfam; PF12796; Ank_2; 2.
Pfam; PF12075; KN_motif; 1.
SMART; SM00248; ANK; 6.
SUPFAM; SSF48403; SSF48403; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 3.
1: Evidence at protein level;
Alternative promoter usage; ANK repeat; Cell membrane;
Cell projection; Coiled coil; Complete proteome; Cytoplasm; Membrane;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Transcription; Transcription regulation; Tumor suppressor.
CHAIN 1 1352 KN motif and ankyrin repeat domain-
containing protein 1.
/FTId=PRO_0000066911.
REPEAT 1161 1191 ANK 1.
REPEAT 1195 1228 ANK 2.
REPEAT 1233 1262 ANK 3.
REPEAT 1266 1298 ANK 4.
REPEAT 1300 1329 ANK 5.
REGION 291 467 Interaction with KIF21A.
{ECO:0000269|PubMed:19559006}.
REGION 1156 1308 Interaction with KIF21A.
{ECO:0000269|PubMed:19559006}.
COILED 258 316 {ECO:0000255}.
COILED 361 395 {ECO:0000255}.
COILED 446 500 {ECO:0000255}.
MOTIF 43 52 Nuclear export signal 1 (NES 1).
MOTIF 65 68 Nuclear localization signal 1 (NLS 1).
MOTIF 125 134 Nuclear export signal 2 (NES 2).
MOTIF 613 622 Nuclear export signal 3 (NES 3).
MOTIF 979 992 Nuclear localization signal 2 (NLS 2).
MOD_RES 186 186 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 325 325 Phosphoserine; by PKB.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:18458160}.
VAR_SEQ 1 158 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_043958.
VARIANT 206 206 N -> K (in dbSNP:rs17857145).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_026212.
VARIANT 210 210 H -> Q (in dbSNP:rs28374506).
/FTId=VAR_048298.
VARIANT 321 321 K -> R (in dbSNP:rs17857159).
/FTId=VAR_048299.
VARIANT 432 432 E -> Q (in dbSNP:rs4465020).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.3}.
/FTId=VAR_026213.
VARIANT 464 464 S -> A (in dbSNP:rs912174).
{ECO:0000269|PubMed:8724849}.
/FTId=VAR_016697.
VARIANT 664 664 A -> V (in dbSNP:rs3824421).
/FTId=VAR_048300.
VARIANT 667 667 R -> H (in dbSNP:rs3824420).
/FTId=VAR_048301.
VARIANT 901 901 N -> S (in dbSNP:rs12352313).
/FTId=VAR_048302.
VARIANT 1055 1055 I -> T (in dbSNP:rs34832656).
/FTId=VAR_048303.
MUTAGEN 43 43 L->A: Nuclear localization; when
associated A-52; A-125; A-129; A-134; A-
613; A-616; A-620 and A-622.
{ECO:0000269|PubMed:16968744}.
MUTAGEN 52 52 I->A: Nuclear localization; when
associated A-43; A-125; A-129; A-134; A-
613; A-616; A-620 and A-622.
{ECO:0000269|PubMed:16968744}.
MUTAGEN 65 68 KRRK->AAAA: Enhanced cytoplasmic
localization; when associated with 979-
A--A-981 and 991-A-A-992.
{ECO:0000269|PubMed:16968744}.
MUTAGEN 125 125 L->A: Nuclear localization; when
associated A-43; A-52; A-129; A-134; A-
613; A-616; A-620 and A-622.
{ECO:0000269|PubMed:16968744}.
MUTAGEN 129 129 L->A: Nuclear localization; when
associated A-43; A-52; A-125; A-134; A-
613; A-616; A-620 and A-622.
{ECO:0000269|PubMed:16968744}.
MUTAGEN 134 134 I->A: Nuclear localization; when
associated A-43; A-52; A-125; A-129; A-
613; A-616; A-620 and A-622.
{ECO:0000269|PubMed:16968744}.
MUTAGEN 325 325 S->A: Abolishes phosphorylation by PKB.
Abolishes interaction with YWHAB; YWHAG;
YWHAE; YWHAH; YWHAQ; YWHAZ and SFN.
{ECO:0000269|PubMed:18458160}.
MUTAGEN 613 613 L->A: Nuclear localization; when
associated A-43; A-52; A-125; A-129; A-
134; A-616; A-620 and A-622.
{ECO:0000269|PubMed:16968744}.
MUTAGEN 616 616 L->A: Nuclear localization; when
associated A-43; A-52; A-125; A-129; A-
134; A-613; A-620 and A-622.
{ECO:0000269|PubMed:16968744}.
MUTAGEN 620 620 L->A: Nuclear localization; when
associated A-43; A-52; A-125; A-129; A-
134; A-613; A-616 and A-622.
{ECO:0000269|PubMed:16968744}.
MUTAGEN 622 622 L->A: Nuclear localization; when
associated A-43; A-52; A-125; A-129; A-
134; A-613; A-616 and A-620.
{ECO:0000269|PubMed:16968744}.
MUTAGEN 979 981 KKK->AAA: Enhanced cytoplasmic
localization; when associated with 65-A--
A-68 and 991-A-A-992.
{ECO:0000269|PubMed:16968744}.
MUTAGEN 991 992 KK->AA: Enhanced cytoplasmic
localization; when associated with 65-A--
68 and 979-A--A-981.
{ECO:0000269|PubMed:16968744}.
SEQUENCE 1352 AA; 147289 MW; 0C3993143391363B CRC64;
MAHTTKVNGS ASGKAGDILS GDQDKEQKDP YFVETPYGYQ LDLDFLKYVD DIQKGNTIKR
LNIQKRRKPS VPCPEPRTTS GQQGIWTSTE SLSSSNSDDN KQCPNFLIAR SQVTSTPISK
PPPPLETSLP FLTIPENRQL PPPSPQLPKH NLHVTKTLME TRRRLEQERA TMQMTPGEFR
RPRLASFGGM GTTSSLPSFV GSGNHNPAKH QLQNGYQGNG DYGSYAPAAP TTSSMGSSIR
HSPLSSGIST PVTNVSPMHL QHIREQMAIA LKRLKELEEQ VRTIPVLQVK ISVLQEEKRQ
LVSQLKNQRA ASQINVCGVR KRSYSAGNAS QLEQLSRARR SGGELYIDYE EEEMETVEQS
TQRIKEFRQL TADMQALEQK IQDSSCEASS ELRENGECRS VAVGAEENMN DIVVYHRGSR
SCKDAAVGTL VEMRNCGVSV TEAMLGVMTE ADKEIELQQQ TIESLKEKIY RLEVQLRETT
HDREMTKLKQ ELQAAGSRKK VDKATMAQPL VFSKVVEAVV QTRDQMVGSH MDLVDTCVGT
SVETNSVGIS CQPECKNKVV GPELPMNWWI VKERVEMHDR CAGRSVEMCD KSVSVEVSVC
ETGSNTEESV NDLTLLKTNL NLKEVRSIGC GDCSVDVTVC SPKECASRGV NTEAVSQVEA
AVMAVPRTAD QDTSTDLEQV HQFTNTETAT LIESCTNTCL STLDKQTSTQ TVETRTVAVG
EGRVKDINSS TKTRSIGVGT LLSGHSGFDR PSAVKTKESG VGQININDNY LVGLKMRTIA
CGPPQLTVGL TASRRSVGVG DDPVGESLEN PQPQAPLGMM TGLDHYIERI QKLLAEQQTL
LAENYSELAE AFGEPHSQMG SLNSQLISTL SSINSVMKSA STEELRNPDF QKTSLGKITG
NYLGYTCKCG GLQSGSPLSS QTSQPEQEVG TSEGKPISSL DAFPTQEGTL SPVNLTDDQI
AAGLYACTNN ESTLKSIMKK KDGNKDSNGA KKNLQFVGIN GGYETTSSDD SSSDESSSSE
SDDECDVIEY PLEEEEEEED EDTRGMAEGH HAVNIEGLKS ARVEDEMQVQ ECEPEKVEIR
ERYELSEKML SACNLLKNTI NDPKALTSKD MRFCLNTLQH EWFRVSSQKS AIPAMVGDYI
AAFEAISPDV LRYVINLADG NGNTALHYSV SHSNFEIVKL LLDADVCNVD HQNKAGYTPI
MLAALAAVEA EKDMRIVEEL FGCGDVNAKA SQAGQTALML AVSHGRIDMV KGLLACGADV
NIQDDEGSTA LMCASEHGHV EIVKLLLAQP GCNGHLEDND GSTALSIALE AGHKDIAVLL
YAHVNFAKAQ SPGTPRLGRK TSPGPTHRGS FD


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