ID PKHA7_HUMAN Reviewed; 1121 AA. AC Q6IQ23; B4DK33; B4DWC3; Q86VZ7; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 2. DT 24-JAN-2024, entry version 161. DE RecName: Full=Pleckstrin homology domain-containing family A member 7; DE Short=PH domain-containing family A member 7; GN Name=PLEKHA7; 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 [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Synovium, and Thalamus; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, 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 [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=15144186; DOI=10.1021/ac035352d; RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., RA Peters E.C.; RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from RT human T cells using immobilized metal affinity chromatography and tandem RT mass spectrometry."; RL Anal. Chem. 76:2763-2772(2004). RN [5] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CAMSAP3 AND CTNND1. RX PubMed=19041755; DOI=10.1016/j.cell.2008.09.040; RA Meng W., Mushika Y., Ichii T., Takeichi M.; RT "Anchorage of microtubule minus ends to adherens junctions regulates RT epithelial cell-cell contacts."; RL Cell 135:948-959(2008). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-903 AND SER-907, 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 [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604; SER-612; SER-903; RP SER-907 AND SER-986, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-903 AND SER-907, 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612; SER-903 AND SER-907, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-536; SER-569; SER-604; RP SER-608; SER-612; SER-858; SER-860; SER-867; THR-870; SER-871; SER-903 AND RP SER-907, AND IDENTIFICATION 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., 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 [12] RP FUNCTION, INTERACTION WITH PDZD11 AND TSPAN33, AND SUBCELLULAR LOCATION. RX PubMed=30463011; DOI=10.1016/j.celrep.2018.10.088; RA Shah J., Rouaud F., Guerrera D., Vasileva E., Popov L.M., Kelley W.L., RA Rubinstein E., Carette J.E., Amieva M.R., Citi S.; RT "A Dock-and-Lock Mechanism Clusters ADAM10 at Cell-Cell Junctions to RT Promote alpha-Toxin Cytotoxicity."; RL Cell Rep. 25:2132-2147(2018). CC -!- FUNCTION: Required for zonula adherens biogenesis and maintenance CC (PubMed:19041755). Acts via its interaction with CAMSAP3, which anchors CC microtubules at their minus-ends to zonula adherens, leading to the CC recruitment of KIFC3 kinesin to the junctional site (PubMed:19041755). CC Mediates docking of ADAM10 to zonula adherens through a PDZD11- CC dependent interaction with the ADAM10-binding protein TSPAN33 CC (PubMed:30463011). {ECO:0000269|PubMed:19041755, CC ECO:0000269|PubMed:30463011}. CC -!- SUBUNIT: Interacts with CAMSAP3 and CTNND1 (PubMed:19041755). Interacts CC (via WW domains) with TSPAN33 (via cytoplasmic domain) and with PDZD11; CC the interaction with TSPAN33 is dependent on PDZD11 being bound to CC PLEKHA7 and facilitates the docking of ADAM10 to zonula adherens CC through interaction of TSPAN33 with ADAM10 (PubMed:30463011). CC {ECO:0000269|PubMed:19041755, ECO:0000269|PubMed:30463011}. CC -!- INTERACTION: CC Q6IQ23; Q9UKV8: AGO2; NbExp=7; IntAct=EBI-2125301, EBI-528269; CC Q6IQ23; P31947: SFN; NbExp=4; IntAct=EBI-2125301, EBI-476295; CC Q6IQ23; P62258: YWHAE; NbExp=6; IntAct=EBI-2125301, EBI-356498; CC Q6IQ23-2; Q9BPU9: B9D2; NbExp=3; IntAct=EBI-12069346, EBI-6958971; CC Q6IQ23-2; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-12069346, EBI-10175300; CC Q6IQ23-2; O95273: CCNDBP1; NbExp=3; IntAct=EBI-12069346, EBI-748961; CC Q6IQ23-2; Q86W67: FAM228A; NbExp=3; IntAct=EBI-12069346, EBI-12958227; CC Q6IQ23-2; P62993: GRB2; NbExp=3; IntAct=EBI-12069346, EBI-401755; CC Q6IQ23-2; O75031: HSF2BP; NbExp=3; IntAct=EBI-12069346, EBI-7116203; CC Q6IQ23-2; P24592: IGFBP6; NbExp=3; IntAct=EBI-12069346, EBI-947015; CC Q6IQ23-2; Q6UWQ7-2: IGFL2; NbExp=3; IntAct=EBI-12069346, EBI-18115692; CC Q6IQ23-2; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-12069346, EBI-1216080; CC Q6IQ23-2; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-12069346, EBI-11750983; CC Q6IQ23-2; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-12069346, EBI-14066006; CC Q6IQ23-2; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-12069346, EBI-79165; CC Q6IQ23-2; O60437: PPL; NbExp=3; IntAct=EBI-12069346, EBI-368321; CC Q6IQ23-2; Q96NR8: RDH12; NbExp=3; IntAct=EBI-12069346, EBI-3916363; CC Q6IQ23-2; Q15669: RHOH; NbExp=3; IntAct=EBI-12069346, EBI-1244971; CC Q6IQ23-2; Q9NZ72: STMN3; NbExp=3; IntAct=EBI-12069346, EBI-725557; CC Q6IQ23-2; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-12069346, EBI-3650647; CC Q6IQ23-2; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-12069346, EBI-744794; CC Q6IQ23-2; Q9UDW3: ZMAT5; NbExp=3; IntAct=EBI-12069346, EBI-7850213; CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction CC {ECO:0000269|PubMed:19041755, ECO:0000269|PubMed:30463011}. Cytoplasm CC {ECO:0000269|PubMed:19041755}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome {ECO:0000269|PubMed:19041755}. CC Note=Localizes to zonula adherens, recruited via its interaction with CC CTNND1. {ECO:0000269|PubMed:19041755}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q6IQ23-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6IQ23-2; Sequence=VSP_025592; CC Name=3; CC IsoId=Q6IQ23-3; Sequence=VSP_039543, VSP_025592; CC -!- SEQUENCE CAUTION: CC Sequence=AAH33239.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAG62985.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AK296371; BAG59045.1; -; mRNA. DR EMBL; AK301465; BAG62985.1; ALT_INIT; mRNA. DR EMBL; AC026639; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC116533; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC127033; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC033239; AAH33239.1; ALT_INIT; mRNA. DR EMBL; BC071599; AAH71599.1; -; mRNA. DR CCDS; CCDS31434.1; -. [Q6IQ23-1] DR RefSeq; NP_001316559.1; NM_001329630.1. DR RefSeq; NP_001316560.1; NM_001329631.1. [Q6IQ23-2] DR RefSeq; NP_778228.3; NM_175058.4. [Q6IQ23-1] DR PDB; 7KJO; X-ray; 1.45 A; A/B=164-298. DR PDB; 7KJZ; X-ray; 2.43 A; A/B=164-298. DR PDB; 7KK7; X-ray; 2.80 A; A/B=164-285. DR PDBsum; 7KJO; -. DR PDBsum; 7KJZ; -. DR PDBsum; 7KK7; -. DR AlphaFoldDB; Q6IQ23; -. DR SMR; Q6IQ23; -. DR BioGRID; 126828; 119. DR CORUM; Q6IQ23; -. DR IntAct; Q6IQ23; 622. DR MINT; Q6IQ23; -. DR STRING; 9606.ENSP00000435389; -. DR ChEMBL; CHEMBL4296241; -. DR CarbonylDB; Q6IQ23; -. DR GlyGen; Q6IQ23; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q6IQ23; -. DR PhosphoSitePlus; Q6IQ23; -. DR BioMuta; PLEKHA7; -. DR DMDM; 215273867; -. DR EPD; Q6IQ23; -. DR jPOST; Q6IQ23; -. DR MassIVE; Q6IQ23; -. DR MaxQB; Q6IQ23; -. DR PaxDb; 9606-ENSP00000347883; -. DR PeptideAtlas; Q6IQ23; -. DR ProteomicsDB; 66479; -. [Q6IQ23-1] DR ProteomicsDB; 66480; -. [Q6IQ23-2] DR ProteomicsDB; 66481; -. [Q6IQ23-3] DR Pumba; Q6IQ23; -. DR Antibodypedia; 42457; 141 antibodies from 20 providers. DR DNASU; 144100; -. DR Ensembl; ENST00000355661.7; ENSP00000347883.2; ENSG00000166689.18. [Q6IQ23-1] DR GeneID; 144100; -. DR KEGG; hsa:144100; -. DR UCSC; uc001mmo.4; human. [Q6IQ23-1] DR AGR; HGNC:27049; -. DR CTD; 144100; -. DR DisGeNET; 144100; -. DR GeneCards; PLEKHA7; -. DR HGNC; HGNC:27049; PLEKHA7. DR HPA; ENSG00000166689; Low tissue specificity. DR MIM; 612686; gene. DR neXtProt; NX_Q6IQ23; -. DR OpenTargets; ENSG00000166689; -. DR PharmGKB; PA134894945; -. DR VEuPathDB; HostDB:ENSG00000166689; -. DR eggNOG; KOG0940; Eukaryota. DR GeneTree; ENSGT00940000155817; -. DR HOGENOM; CLU_008216_1_0_1; -. DR InParanoid; Q6IQ23; -. DR OrthoDB; 4609983at2759; -. DR PhylomeDB; Q6IQ23; -. DR TreeFam; TF329090; -. DR PathwayCommons; Q6IQ23; -. DR SignaLink; Q6IQ23; -. DR SIGNOR; Q6IQ23; -. DR BioGRID-ORCS; 144100; 11 hits in 1152 CRISPR screens. DR ChiTaRS; PLEKHA7; human. DR GenomeRNAi; 144100; -. DR Pharos; Q6IQ23; Tbio. DR PRO; PR:Q6IQ23; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q6IQ23; Protein. DR Bgee; ENSG00000166689; Expressed in sural nerve and 142 other cell types or tissues. DR ExpressionAtlas; Q6IQ23; baseline and differential. DR GO; GO:0030054; C:cell junction; IDA:HPA. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0046930; C:pore complex; IMP:UniProtKB. DR GO; GO:0005915; C:zonula adherens; IDA:UniProtKB. DR GO; GO:0070097; F:delta-catenin binding; IDA:UniProtKB. DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; ISS:ARUK-UCL. DR GO; GO:0090136; P:epithelial cell-cell adhesion; IMP:UniProtKB. DR GO; GO:0046931; P:pore complex assembly; IMP:UniProtKB. DR GO; GO:0045218; P:zonula adherens maintenance; IMP:UniProtKB. DR CDD; cd13248; PH_PEPP1_2_3; 1. DR CDD; cd00890; Prefoldin; 1. DR CDD; cd00201; WW; 1. DR Gene3D; 2.20.70.10; -; 2. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR040392; PKHA4-7_PH. DR InterPro; IPR001202; WW_dom. DR InterPro; IPR036020; WW_dom_sf. DR PANTHER; PTHR12752; PHOSPHOINOSITOL 3-PHOSPHATE-BINDING PROTEIN; 1. DR PANTHER; PTHR12752:SF4; PLECKSTRIN HOMOLOGY DOMAIN-CONTAINING FAMILY A MEMBER 7; 1. DR Pfam; PF00169; PH; 1. DR SMART; SM00233; PH; 1. DR SMART; SM00456; WW; 2. DR SUPFAM; SSF50729; PH domain-like; 1. DR SUPFAM; SSF51045; WW domain; 2. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS01159; WW_DOMAIN_1; 1. DR PROSITE; PS50020; WW_DOMAIN_2; 2. DR Genevisible; Q6IQ23; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell junction; Coiled coil; Cytoplasm; KW Cytoskeleton; Phosphoprotein; Reference proteome; Repeat. FT CHAIN 1..1121 FT /note="Pleckstrin homology domain-containing family A FT member 7" FT /id="PRO_0000287692" FT DOMAIN 9..42 FT /note="WW 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224" FT DOMAIN 54..87 FT /note="WW 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224" FT DOMAIN 164..282 FT /note="PH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT REGION 105..137 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 299..514 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 538..696 FT /note="Interaction with CTNND1" FT /evidence="ECO:0000269|PubMed:19041755" FT REGION 547..632 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 841..876 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 888..971 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1003..1028 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1082..1121 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 700..801 FT /evidence="ECO:0000255" FT COILED 1067..1094 FT /evidence="ECO:0000255" FT COMPBIAS 110..131 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 313..365 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 447..484 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 499..514 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 567..585 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 586..600 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 607..626 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 844..873 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 922..942 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 950..971 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1082..1097 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 536 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 545 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q3UIL6" FT MOD_RES 569 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 604 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:24275569" FT MOD_RES 608 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 612 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 858 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 860 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 867 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 870 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 871 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 903 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 907 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 986 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT VAR_SEQ 1..447 FT /note="MAAATVGRDTLPEHWSYGVCRDGRVFFINDQLRCTTWLHPRTGEPVNSGHMI FT RSDLPRGWEEGFTEEGASYFIDHNQQTTAFRHPVTGQFSPENSEFILQEEPNPHMSKQD FT RNQRPSSMVSETSTAGTASTLEAKPGPKIIKSSSKVHSFGKRDQAIRRNPNVPVVVRGW FT LHKQDSSGMRLWKRRWFVLADYCLFYYKDSREEAVLGSIPLPSYVISPVAPEDRISRKY FT SFKAVHTGMRALIYNSSTAGSQAEQSGMRTYYFSADTQEDMNAWVRAMNQAAQVLSRSS FT LKRDMEKVERQAVPQANHTESCHECGRVGPGHTRDCPHRGHDDIVNFERQEQEGEQYRS FT QRDPLEGKRDRSKARSPYSPAEEDALFMDLPTGPRGQQAQPQRAEKNGMLPASYGPGEQ FT NGTGGYQRAFPPRTNPEKHSQRKSNLAQVEHWARAQKGDSR -> MFPKACRTLAWLPD FT PFLPFLL (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_039543" FT VAR_SEQ 915 FT /note="V -> VQ (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_025592" FT VARIANT 241 FT /note="L -> I (in dbSNP:rs35908144)" FT /id="VAR_032346" FT VARIANT 248 FT /note="A -> V (in dbSNP:rs16933529)" FT /id="VAR_032347" FT VARIANT 279 FT /note="Q -> R (in dbSNP:rs369819)" FT /id="VAR_032348" FT VARIANT 689 FT /note="S -> R (in dbSNP:rs61133161)" FT /id="VAR_061517" FT VARIANT 693 FT /note="V -> I (in dbSNP:rs34556458)" FT /id="VAR_032349" FT CONFLICT 494 FT /note="D -> N (in Ref. 1; BAG62985)" FT /evidence="ECO:0000305" FT CONFLICT 981 FT /note="L -> P (in Ref. 3; AAH71599)" FT /evidence="ECO:0000305" FT STRAND 165..174 FT /evidence="ECO:0007829|PDB:7KJO" FT STRAND 176..179 FT /evidence="ECO:0007829|PDB:7KK7" FT STRAND 182..190 FT /evidence="ECO:0007829|PDB:7KJO" FT STRAND 193..199 FT /evidence="ECO:0007829|PDB:7KJO" FT STRAND 204..210 FT /evidence="ECO:0007829|PDB:7KJO" FT STRAND 214..218 FT /evidence="ECO:0007829|PDB:7KJO" FT HELIX 221..223 FT /evidence="ECO:0007829|PDB:7KJO" FT STRAND 230..235 FT /evidence="ECO:0007829|PDB:7KJO" FT STRAND 259..263 FT /evidence="ECO:0007829|PDB:7KJO" FT HELIX 267..281 FT /evidence="ECO:0007829|PDB:7KJO" SQ SEQUENCE 1121 AA; 127135 MW; 93F616CF3EF9E5C2 CRC64; MAAATVGRDT LPEHWSYGVC RDGRVFFIND QLRCTTWLHP RTGEPVNSGH MIRSDLPRGW EEGFTEEGAS YFIDHNQQTT AFRHPVTGQF SPENSEFILQ EEPNPHMSKQ DRNQRPSSMV SETSTAGTAS TLEAKPGPKI IKSSSKVHSF GKRDQAIRRN PNVPVVVRGW LHKQDSSGMR LWKRRWFVLA DYCLFYYKDS REEAVLGSIP LPSYVISPVA PEDRISRKYS FKAVHTGMRA LIYNSSTAGS QAEQSGMRTY YFSADTQEDM NAWVRAMNQA AQVLSRSSLK RDMEKVERQA VPQANHTESC HECGRVGPGH TRDCPHRGHD DIVNFERQEQ EGEQYRSQRD PLEGKRDRSK ARSPYSPAEE DALFMDLPTG PRGQQAQPQR AEKNGMLPAS YGPGEQNGTG GYQRAFPPRT NPEKHSQRKS NLAQVEHWAR AQKGDSRSLP LDQTLPRQGP GQSLSFPENY QTLPKSTRHP SGGSSPPPRN LPSDYKYAQD RASHLKMSSE ERRAHRDGTV WQLYEWQQRQ QFRHGSPTAP ICLGSPEFTD QGRSRSMLEV PRSISVPPSP SDIPPPGPPR VFPPRRPHTP AERVTVKPPD QRRSVDISLG DSPRRARGHA VKNSSHVDRR SMPSMGYMTH TVSAPSLHGK SADDTYLQLK KDLEYLDLKM TGRDLLKDRS LKPVKIAESD TDVKLSIFCE QDRVLQDLED KIRALKENKD QLESVLEVLH RQMEQYRDQP QHLEKIAYQQ KLLQEDLVHI RAELSRESTE MENAWNEYLK LENDVEQLKQ TLQEQHRRAF FFQEKSQIQK DLWRIEDVTA GLSANKENFR ILVESVKNPE RKTVPLFPHP PVPSLSTSES KPPPQPSPPT SPVRTPLEVR LFPQLQTYVP YRPHPPQLRK VTSPLQSPTK AKPKVEDEAP PRPPLPELYS PEDQPPAVPP LPREATIIRH TSVRGLKRQS DERKRDRELG QCVNGDSRVE LRSYVSEPEL ATLSGDMAQP SLGLVGPESR YQTLPGRGLS GSTSRLQQSS TIAPYVTLRR GLNAESSKAT FPRPKSALER LYSGDHQRGK MSAEEQLERM KRHQKALVRE RKRTLGQGER TGLPSSRYLS RPLPGDLGSV C //