ID KANK1_HUMAN Reviewed; 1352 AA. AC Q14678; A2A2W8; D3DRH3; Q5W0W0; Q8IY65; Q8WX74; DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 30-AUG-2005, sequence version 3. DT 24-JUN-2015, entry version 127. DE RecName: Full=KN motif and ankyrin repeat domain-containing protein 1; DE AltName: Full=Ankyrin repeat domain-containing protein 15; DE AltName: Full=Kidney ankyrin repeat-containing protein; GN Name=KANK1; Synonyms=ANKRD15, KANK, KIAA0172; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP ALA-464. RC TISSUE=Bone marrow; RX PubMed=8724849; DOI=10.1093/dnares/3.1.17; RA Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. V. RT The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by RT analysis of cDNA clones from human cell line KG-1."; RL DNA Res. 3:17-24(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., RA Rogers J., Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLN-432. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS RP LYS-206 AND GLN-432. RC TISSUE=Testis; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PUTATIVE FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=12133830; DOI=10.1074/jbc.M204244200; RA Sarkar S., Roy B.C., Hatano N., Aoyagi T., Gohji K., Kiyama R.; RT "A novel ankyrin repeat-containing gene (Kank) located at 9p24 is a RT growth suppressor of renal cell carcinoma."; RL J. Biol. Chem. 277:36585-36591(2002). RN [6] RP ALTERNATIVE PROMOTER USAGE (ISOFORM 2), AND TISSUE SPECIFICITY. RX PubMed=15823577; DOI=10.1016/j.bbrc.2005.03.106; RA Wang Y., Onishi Y., Kakinuma N., Roy B.C., Aoyagi T., Kiyama R.; RT "Alternative splicing of the human Kank gene produces two types of RT Kank protein."; RL Biochem. Biophys. Res. Commun. 330:1247-1253(2005). RN [7] RP INVOLVEMENT IN CPSQ2. RX PubMed=16301218; DOI=10.1093/hmg/ddi415; RA Lerer I., Sagi M., Meiner V., Cohen T., Zlotogora J., Abeliovich D.; RT "Deletion of the ANKRD15 gene at 9p24.3 causes parent-of-origin- RT dependent inheritance of familial cerebral palsy."; RL Hum. Mol. Genet. 14:3911-3920(2005). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CTNNB1, AND RP MUTAGENESIS OF LEU-43; ILE-52; 65-LYS--LYS-68; LEU-125; LEU-129; RP ILE-134; LEU-613; LEU-616; LEU-620; LEU-622; 979-LYS--LYS-981 AND RP 991-LYS-LYS-992. RX PubMed=16968744; DOI=10.1242/jcs.03169; RA Wang Y., Kakinuma N., Zhu Y., Kiyama R.; RT "Nucleo-cytoplasmic shuttling of human Kank protein accompanies RT intracellular translocation of beta-catenin."; RL J. Cell Sci. 119:4002-4010(2006). RN [9] RP FUNCTION, PHOSPHORYLATION AT SER-325, INTERACTION WITH YWHAB; YWHAG; RP YWHAE; YWHAH; YWHAQ; YWHAZ AND SFN, AND MUTAGENESIS OF SER-325. RX PubMed=18458160; DOI=10.1083/jcb.200707022; RA Kakinuma N., Roy B.C., Zhu Y., Wang Y., Kiyama R.; RT "Kank regulates RhoA-dependent formation of actin stress fibers and RT cell migration via 14-3-3 in PI3K-Akt signaling."; RL J. Cell Biol. 181:537-549(2008). RN [10] 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 [11] RP INTERACTION WITH KIF21A. RX PubMed=19559006; DOI=10.1016/j.bbrc.2009.06.109; RA Kakinuma N., Kiyama R.; RT "A major mutation of KIF21A associated with congenital fibrosis of the RT extraocular muscles type 1 (CFEOM1) enhances translocation of Kank1 to RT the membrane."; RL Biochem. Biophys. Res. Commun. 386:639-644(2009). RN [12] RP FUNCTION, AND INTERACTION WITH BAIAP2. RX PubMed=19171758; DOI=10.1083/jcb.200805147; RA Roy B.C., Kakinuma N., Kiyama R.; RT "Kank attenuates actin remodeling by preventing interaction between RT IRSp53 and Rac1."; RL J. Cell Biol. 184:253-267(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, AND IDENTIFICATION RP 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 [14] RP IDENTIFICATION BY 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [15] RP FUNCTION, AND INTERACTION WITH ARFGEF1. RX PubMed=22084092; DOI=10.1073/pnas.1117011108; RA Li C.C., Kuo J.C., Waterman C.M., Kiyama R., Moss J., Vaughan M.; RT "Effects of brefeldin A-inhibited guanine nucleotide-exchange (BIG) 1 RT and KANK1 proteins on cell polarity and directed migration during RT wound healing."; RL Proc. Natl. Acad. Sci. U.S.A. 108:19228-19233(2011). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, AND IDENTIFICATION RP 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., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION RP BY 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Involved in the control of cytoskeleton formation by CC regulating actin polymerization. Inhibits actin fiber formation CC and cell migration. Inhibits RhoA activity; the function involves CC phosphorylation through PI3K/Akt signaling and may depend on the CC competetive interaction with 14-3-3 adapter proteins to sequester CC them from active complexes. Inhibits the formation of lamellipodia CC but not of filopodia; the function may depend on the competetive CC interaction with BAIAP2 to block its association with activated CC RAC1. Inhibits fibronectin-mediated cell spreading; the function CC is partially mediated by BAIAP2. Inhibits neurite outgrowth. CC Involved in the establishment and persistence of cell polarity CC during directed cell movement in wound healing. In the nucleus, is CC involved in beta-catenin-dependent activation of transcription. CC Potential tumor suppressor for renal cell carcinoma. CC {ECO:0000269|PubMed:16968744, ECO:0000269|PubMed:18458160, CC ECO:0000269|PubMed:19171758, ECO:0000269|PubMed:22084092}. CC -!- SUBUNIT: Interacts with YWHAQ; the interaction requires KANK1 CC phosphorylation at Ser-325 and is enhanced by growth factor CC stimulation. Interacts with YWHAB, YWHAG, YWHAE, YWHAH, YWHAZ and CC SFN; the interaction requires KANK1 phosphorylation at Ser-325. CC Interacts with ARFGEF1; however, colocalization cannot be CC experimentally confirmed. Interacts with BAIAP2. Interacts (via CC ANK repeats 1-5) with KIF21A (via coiled coil region); KIF21A CC enhances translocation of KANK1 to the plasma membrane. Interacts CC with CTNNB1. {ECO:0000269|PubMed:16968744, CC ECO:0000269|PubMed:18458160, ECO:0000269|PubMed:19171758, CC ECO:0000269|PubMed:19559006, ECO:0000269|PubMed:22084092}. CC -!- INTERACTION: CC Q9UQB8:BAIAP2; NbExp=6; IntAct=EBI-2556221, EBI-525456; CC Q9UQB8-4:BAIAP2; NbExp=4; IntAct=EBI-6173812, EBI-6174091; CC P35222:CTNNB1; NbExp=2; IntAct=EBI-2556221, EBI-491549; CC Q7Z4S6:KIF21A; NbExp=3; IntAct=EBI-6173812, EBI-2691397; CC P62258:YWHAE; NbExp=3; IntAct=EBI-6173812, EBI-356498; CC P61981:YWHAG; NbExp=3; IntAct=EBI-6173812, EBI-359832; CC Q04917:YWHAH; NbExp=3; IntAct=EBI-6173812, EBI-306940; CC P27348:YWHAQ; NbExp=3; IntAct=EBI-6173812, EBI-359854; CC -!- SUBCELLULAR LOCATION: Cell projection, ruffle membrane CC {ECO:0000269|PubMed:12133830, ECO:0000269|PubMed:16968744}. CC Note=Colocalizes with KIF21A in membrane ruffles. CC -!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Nucleus. Note=Shuttles CC between the cytoplasm and nucleus. CC -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus. Cell CC projection, ruffle membrane. Note=Shuttles between the cytoplasm CC and nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter usage; Named isoforms=2; CC Name=1; Synonyms=Kank-L; CC IsoId=Q14678-1; Sequence=Displayed; CC Name=2; Synonyms=Kank-S; CC IsoId=Q14678-2; Sequence=VSP_043958; CC -!- TISSUE SPECIFICITY: Widely expressed. Isoform 1 is predominantly CC expressed in heart and kidney. Isoform 2 probably is widely CC expressed at basic levels. {ECO:0000269|PubMed:15823577}. CC -!- DISEASE: Cerebral palsy, spastic quadriplegic 2 (CPSQ2) CC [MIM:612900]: A non-progressive disorder of movement and/or CC posture resulting from defects in the developing central nervous CC system. Affected individuals manifest congenital hypotonia CC evolving over the first year to spastic quadriplegia with CC accompanying transient nystagmus and varying degrees of mental CC retardation. Neuroimaging shows brain atrophy and CC ventriculomegaly. {ECO:0000269|PubMed:16301218}. Note=The disease CC is caused by mutations affecting the gene represented in this CC entry. CC -!- SIMILARITY: Contains 5 ANK repeats. {ECO:0000255|PROSITE- CC ProRule:PRU00023}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA11489.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D79994; BAA11489.2; ALT_INIT; mRNA. DR EMBL; AL136979; CAH70388.1; -; Genomic_DNA. DR EMBL; AL136979; CAM13084.1; -; Genomic_DNA. DR EMBL; CH471071; EAW58821.1; -; Genomic_DNA. DR EMBL; CH471071; EAW58822.1; -; Genomic_DNA. DR EMBL; BC037495; AAH37495.1; -; mRNA. DR CCDS; CCDS34976.1; -. [Q14678-1] DR CCDS; CCDS6441.1; -. [Q14678-2] DR RefSeq; NP_001243805.1; NM_001256876.1. [Q14678-1] DR RefSeq; NP_001243806.1; NM_001256877.1. [Q14678-1] DR RefSeq; NP_055973.2; NM_015158.3. [Q14678-1] DR UniGene; Hs.306764; -. DR ProteinModelPortal; Q14678; -. DR SMR; Q14678; 1084-1325. DR BioGrid; 116798; 7. DR DIP; DIP-56491N; -. DR IntAct; Q14678; 14. DR MINT; MINT-7997401; -. DR STRING; 9606.ENSP00000371734; -. DR PhosphoSite; Q14678; -. DR BioMuta; KANK1; -. DR DMDM; 73920184; -. DR MaxQB; Q14678; -. DR PaxDb; Q14678; -. DR PRIDE; Q14678; -. DR Ensembl; ENST00000382293; ENSP00000371730; ENSG00000107104. [Q14678-2] DR Ensembl; ENST00000382297; ENSP00000371734; ENSG00000107104. [Q14678-1] DR Ensembl; ENST00000382303; ENSP00000371740; ENSG00000107104. [Q14678-1] DR Ensembl; ENST00000619269; ENSP00000477725; ENSG00000107104. [Q14678-1] DR GeneID; 23189; -. DR KEGG; hsa:23189; -. DR UCSC; uc003zgl.2; human. [Q14678-1] DR CTD; 23189; -. DR GeneCards; GC09P000474; -. DR HGNC; HGNC:19309; KANK1. DR HPA; HPA005539; -. DR MIM; 607704; gene. DR MIM; 612900; phenotype. DR neXtProt; NX_Q14678; -. DR Orphanet; 210141; Inherited congenital spastic tetraplegia. DR PharmGKB; PA162392554; -. DR eggNOG; COG0666; -. DR GeneTree; ENSGT00530000063448; -. DR HOGENOM; HOG000230897; -. DR HOVERGEN; HBG050511; -. DR InParanoid; Q14678; -. DR OMA; MTGLDHY; -. DR OrthoDB; EOG7NW687; -. DR PhylomeDB; Q14678; -. DR TreeFam; TF324499; -. DR ChiTaRS; KANK1; human. DR GeneWiki; ANKRD15; -. DR GenomeRNAi; 23189; -. DR NextBio; 44663; -. DR PRO; PR:Q14678; -. DR Proteomes; UP000005640; Chromosome 9. DR Bgee; Q14678; -. DR CleanEx; HS_KANK1; -. DR ExpressionAtlas; Q14678; baseline and differential. DR Genevisible; Q14678; HS. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB. DR GO; GO:0008013; F:beta-catenin binding; IDA:UniProtKB. DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IDA:UniProtKB. DR GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB. DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IMP:UniProtKB. DR GO; GO:2000393; P:negative regulation of lamellipodium morphogenesis; IDA:UniProtKB. DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:UniProtKB. DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IMP:UniProtKB. DR GO; GO:1900028; P:negative regulation of ruffle assembly; IDA:UniProtKB. DR GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; IDA:UniProtKB. DR GO; GO:0035413; P:positive regulation of catenin import into nucleus; IMP:UniProtKB. DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IDA:UniProtKB. DR GO; GO:0090303; P:positive regulation of wound healing; IMP:UniProtKB. DR GO; GO:2000114; P:regulation of establishment of cell polarity; IMP:UniProtKB. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.25.40.20; -; 1. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR020683; Ankyrin_rpt-contain_dom. DR InterPro; IPR021939; KN_motif. DR Pfam; PF00023; Ank; 3. DR Pfam; PF12075; KN_motif; 1. DR SMART; SM00248; ANK; 6. DR SUPFAM; SSF48403; SSF48403; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 3. PE 1: Evidence at protein level; KW Alternative promoter usage; ANK repeat; Cell membrane; KW Cell projection; Coiled coil; Complete proteome; Cytoplasm; Membrane; KW Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; KW Transcription; Transcription regulation; Tumor suppressor. FT CHAIN 1 1352 KN motif and ankyrin repeat domain- FT containing protein 1. FT /FTId=PRO_0000066911. FT REPEAT 1161 1191 ANK 1. FT REPEAT 1195 1228 ANK 2. FT REPEAT 1233 1262 ANK 3. FT REPEAT 1266 1298 ANK 4. FT REPEAT 1300 1329 ANK 5. FT REGION 291 467 Interaction with KIF21A. FT REGION 1156 1308 Interaction with KIF21A. FT COILED 258 316 {ECO:0000255}. FT COILED 361 395 {ECO:0000255}. FT COILED 446 500 {ECO:0000255}. FT MOTIF 43 52 Nuclear export signal 1 (NES 1). FT MOTIF 65 68 Nuclear localization signal 1 (NLS 1). FT MOTIF 125 134 Nuclear export signal 2 (NES 2). FT MOTIF 613 622 Nuclear export signal 3 (NES 3). FT MOTIF 979 992 Nuclear localization signal 2 (NLS 2). FT MOD_RES 186 186 Phosphoserine. FT {ECO:0000269|PubMed:24275569}. FT MOD_RES 325 325 Phosphoserine; by PKB. FT {ECO:0000269|PubMed:18458160, FT ECO:0000269|PubMed:19690332, FT ECO:0000269|PubMed:21406692}. FT VAR_SEQ 1 158 Missing (in isoform 2). {ECO:0000305}. FT /FTId=VSP_043958. FT VARIANT 206 206 N -> K (in dbSNP:rs17857145). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_026212. FT VARIANT 210 210 H -> Q (in dbSNP:rs28374506). FT /FTId=VAR_048298. FT VARIANT 321 321 K -> R (in dbSNP:rs17857159). FT /FTId=VAR_048299. FT VARIANT 432 432 E -> Q (in dbSNP:rs4465020). FT {ECO:0000269|PubMed:15489334, FT ECO:0000269|Ref.3}. FT /FTId=VAR_026213. FT VARIANT 464 464 S -> A (in dbSNP:rs912174). FT {ECO:0000269|PubMed:8724849}. FT /FTId=VAR_016697. FT VARIANT 664 664 A -> V (in dbSNP:rs3824421). FT /FTId=VAR_048300. FT VARIANT 667 667 R -> H (in dbSNP:rs3824420). FT /FTId=VAR_048301. FT VARIANT 901 901 N -> S (in dbSNP:rs12352313). FT /FTId=VAR_048302. FT VARIANT 1055 1055 I -> T (in dbSNP:rs34832656). FT /FTId=VAR_048303. FT MUTAGEN 43 43 L->A: Nuclear localization; when FT associated A-52; A-125; A-129; A-134; A- FT 613; A-616; A-620 and A-622. FT {ECO:0000269|PubMed:16968744}. FT MUTAGEN 52 52 I->A: Nuclear localization; when FT associated A-43; A-125; A-129; A-134; A- FT 613; A-616; A-620 and A-622. FT {ECO:0000269|PubMed:16968744}. FT MUTAGEN 65 68 KRRK->AAAA: Enhanced cytoplasmic FT localization; when associated with 979- FT A--A-981 and 991-A-A-992. FT {ECO:0000269|PubMed:16968744}. FT MUTAGEN 125 125 L->A: Nuclear localization; when FT associated A-43; A-52; A-129; A-134; A- FT 613; A-616; A-620 and A-622. FT {ECO:0000269|PubMed:16968744}. FT MUTAGEN 129 129 L->A: Nuclear localization; when FT associated A-43; A-52; A-125; A-134; A- FT 613; A-616; A-620 and A-622. FT {ECO:0000269|PubMed:16968744}. FT MUTAGEN 134 134 I->A: Nuclear localization; when FT associated A-43; A-52; A-125; A-129; A- FT 613; A-616; A-620 and A-622. FT {ECO:0000269|PubMed:16968744}. FT MUTAGEN 325 325 S->A: Abolishes phosphorylation by PKB. FT Abolishes interaction with YWHAB; YWHAG; FT YWHAE; YWHAH; YWHAQ; YWHAZ and SFN. FT {ECO:0000269|PubMed:18458160}. FT MUTAGEN 613 613 L->A: Nuclear localization; when FT associated A-43; A-52; A-125; A-129; A- FT 134; A-616; A-620 and A-622. FT {ECO:0000269|PubMed:16968744}. FT MUTAGEN 616 616 L->A: Nuclear localization; when FT associated A-43; A-52; A-125; A-129; A- FT 134; A-613; A-620 and A-622. FT {ECO:0000269|PubMed:16968744}. FT MUTAGEN 620 620 L->A: Nuclear localization; when FT associated A-43; A-52; A-125; A-129; A- FT 134; A-613; A-616 and A-622. FT {ECO:0000269|PubMed:16968744}. FT MUTAGEN 622 622 L->A: Nuclear localization; when FT associated A-43; A-52; A-125; A-129; A- FT 134; A-613; A-616 and A-620. FT {ECO:0000269|PubMed:16968744}. FT MUTAGEN 979 981 KKK->AAA: Enhanced cytoplasmic FT localization; when associated with 65-A-- FT A-68 and 991-A-A-992. FT {ECO:0000269|PubMed:16968744}. FT MUTAGEN 991 992 KK->AA: Enhanced cytoplasmic FT localization; when associated with 65-A-- FT 68 and 979-A--A-981. FT {ECO:0000269|PubMed:16968744}. SQ 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 //