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};
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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 Genevisible; Q6IQ23; HS.
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.
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
//
