ID MYOME_HUMAN Reviewed; 2346 AA. AC Q5VU43; A0A0A0MRM0; A0A0C4DFQ0; A2RU15; E9PL24; O75042; O75065; Q2YDC1; AC Q5VU42; Q5VU44; Q5VU45; Q5VU46; Q5VU47; Q5VU48; Q5VU49; Q68DU2; Q6AZ93; AC Q6PK88; Q86T40; Q86TB2; Q8N3W0; Q8TAY9; Q9HCP2; Q9HCP3; Q9HCP4; Q9HCP5; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 28-MAR-2018, sequence version 3. DT 27-MAR-2024, entry version 170. DE RecName: Full=Myomegalin; DE AltName: Full=Cardiomyopathy-associated protein 2; DE AltName: Full=Phosphodiesterase 4D-interacting protein; GN Name=PDE4DIP; Synonyms=CMYA2, KIAA0454, KIAA0477, MMGL; 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 [MRNA] (ISOFORMS 10; 11 AND 12), TISSUE SPECIFICITY, RP AND VARIANT THR-49. RC TISSUE=Myocardium; RX PubMed=11374908; DOI=10.1006/geno.2001.6527; RA Soejima H., Kawamoto S., Akai J., Miyoshi O., Arai Y., Morohka T., RA Matsuo S., Niikawa N., Kimura A., Okubo K., Mukai T.; RT "Isolation of novel heart-specific genes using the BodyMap database."; RL Genomics 74:115-120(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 13), FUNCTION (ISOFORM 13), INTERACTION RP WITH AKAP9; GAMMA-TUBULIN RING COMPLEX; MAPRE1 AND MAPRE3 (ISOFORM 13), RP SUBCELLULAR LOCATION (ISOFORM 13), AND MUTAGENESIS (ISOFORM 13). RX PubMed=25217626; DOI=10.1242/jcs.155408; RA Wang Z., Zhang C., Qi R.Z.; RT "A newly identified myomegalin isoform functions in Golgi microtubule RT organization and ER-Golgi transport."; RL J. Cell Sci. 127:4904-4917(2014). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Brain; RX PubMed=9455484; DOI=10.1093/dnares/4.5.345; RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., RA Nomura N., Ohara O.; RT "Characterization of cDNA clones in size-fractionated cDNA libraries from RT human brain."; RL DNA Res. 4:345-349(1997). RN [4] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 6 AND 7), AND VARIANTS RP CYS-708; ILE-1013; THR-1066; GLU-1359; GLU-1736 AND SER-1742. RC TISSUE=Amygdala, and Skeletal muscle; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS CYS-708 AND RP TRP-1396. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 8 AND 9), AND VARIANT RP THR-49. 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2261-2346 (ISOFORM 4). RC TISSUE=Skeletal muscle; 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 [9] RP CHROMOSOMAL TRANSLOCATION WITH PDGFRB. RX PubMed=12907457; DOI=10.1182/blood-2003-04-1150; RA Wilkinson K., Velloso E.R.P., Lopes L.F., Lee C., Aster J.C., Shipp M.A., RA Aguiar R.C.T.; RT "Cloning of the t(1;5)(q23;q33) in a myeloproliferative disorder associated RT with eosinophilia: involvement of PDGFRB and response to imatinib."; RL Blood 102:4187-4190(2003). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-704, AND IDENTIFICATION BY RP 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252 (ISOFORMS 13 AND 2), AND RP 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 [14] RP FUNCTION (ISOFORM 13), SUBCELLULAR LOCATION (ISOFORM 13), AND INTERACTION RP WITH AKAP9 AND CAMSAP2 (ISOFORM 13). RX PubMed=27666745; DOI=10.1016/j.devcel.2016.08.009; RA Wu J., de Heus C., Liu Q., Bouchet B.P., Noordstra I., Jiang K., Hua S., RA Martin M., Yang C., Grigoriev I., Katrukha E.A., Altelaar A.F., RA Hoogenraad C.C., Qi R.Z., Klumperman J., Akhmanova A.; RT "Molecular pathway of microtubule organization at the Golgi apparatus."; RL Dev. Cell 39:44-60(2016). RN [15] RP FUNCTION (ISOFORM 13), INTERACTION WITH AKAP9; CAMSAP2; MAPRE1 AND MAPRE3 RP (ISOFORM 13), AND MUTAGENESIS (ISOFORM 13). RX PubMed=28814570; DOI=10.1083/jcb.201701024; RA Yang C., Wu J., de Heus C., Grigoriev I., Liv N., Yao Y., Smal I., RA Meijering E., Klumperman J., Qi R.Z., Akhmanova A.; RT "EB1 and EB3 regulate microtubule minus end organization and Golgi RT morphology."; RL J. Cell Biol. 216:3179-3198(2017). RN [16] RP INTERACTION WITH AKAP9; CDK5RAP2; LGALS3BP AND MAPRE1 (ISOFORM 13), RP SUBCELLULAR LOCATION (ISOFORM 13), IDENTIFICATION BY MASS SPECTROMETRY RP (ISOFORM 13), MUTAGENESIS (ISOFORM 13), AND DOMAIN. RX PubMed=29162697; DOI=10.1073/pnas.1705682114; RA Bouguenina H., Salaun D., Mangon A., Muller L., Baudelet E., Camoin L., RA Tachibana T., Cianferani S., Audebert S., Verdier-Pinard P., Badache A.; RT "EB1-binding-myomegalin protein complex promotes centrosomal microtubules RT functions."; RL Proc. Natl. Acad. Sci. U.S.A. 114:E10687-E10696(2017). CC -!- FUNCTION: Functions as an anchor sequestering components of the cAMP- CC dependent pathway to Golgi and/or centrosomes (By similarity). CC {ECO:0000250|UniProtKB:Q9WUJ3}. CC -!- FUNCTION: [Isoform 13]: Participates in microtubule dynamics, promoting CC microtubule assembly. Depending upon the cell context, may act at the CC level of the Golgi apparatus or that of the centrosome CC (PubMed:25217626, PubMed:27666745, PubMed:28814570, PubMed:29162697). CC In complex with AKAP9, recruits CAMSAP2 to the Golgi apparatus and CC tethers non-centrosomal minus-end microtubules to the Golgi, an CC important step for polarized cell movement (PubMed:27666745, CC PubMed:28814570). In complex with AKAP9, EB1/MAPRE1 and CDK5RAP2, CC contributes to microtubules nucleation and extension from the CC centrosome to the cell periphery, a crucial process for directed cell CC migration, mitotic spindle orientation and cell-cycle progression CC (PubMed:29162697). {ECO:0000269|PubMed:25217626, CC ECO:0000269|PubMed:27666745, ECO:0000269|PubMed:28814570, CC ECO:0000269|PubMed:29162697}. CC -!- SUBUNIT: Interacts with PDE4D (By similarity). Isoform 13 interacts CC with MAPRE1 and MAPRE3 (PubMed:25217626, PubMed:28814570, CC PubMed:29162697). Isoform 13 forms a pericentrosomal complex with CC AKAP9, CDK5RAP2 and EB1/MAPRE1; within this complex, may mediate CC MAPRE1-binding to CDK5RAP2 (PubMed:29162697). Interaction of isoform 13 CC with AKAP9 stabilizes both proteins (PubMed:25217626, PubMed:27666745). CC Isoform 13 interacts (via N-terminus) with CAMSAP2; this interaction is CC much stronger in the presence of AKAP9 (PubMed:27666745). In complex CC with AKAP9, Isoform 13 recruits CAMSAP2 to the Golgi apparatus CC (PubMed:27666745, PubMed:28814570). Isoform 13 interacts with CC unglycosylated LGALS3BP; this interaction may connect the CC pericentrosomal complex to the gamma-tubulin ring complex (gamma-TuRC) CC to promote microtubule assembly and acetylation (PubMed:25217626, CC PubMed:29162697). {ECO:0000250|UniProtKB:Q9WUJ3, CC ECO:0000269|PubMed:25217626, ECO:0000269|PubMed:27666745, CC ECO:0000269|PubMed:28814570, ECO:0000269|PubMed:29162697}. CC -!- INTERACTION: CC Q5VU43; Q8WTP8: AEN; NbExp=3; IntAct=EBI-1105124, EBI-8637627; CC Q5VU43; Q9NX04: AIRIM; NbExp=3; IntAct=EBI-1105124, EBI-8643161; CC Q5VU43; Q13895: BYSL; NbExp=5; IntAct=EBI-1105124, EBI-358049; CC Q5VU43; Q9NVL8: CCDC198; NbExp=3; IntAct=EBI-1105124, EBI-10238351; CC Q5VU43; Q9NX63: CHCHD3; NbExp=3; IntAct=EBI-1105124, EBI-743375; CC Q5VU43; Q9NRI5: DISC1; NbExp=3; IntAct=EBI-1105124, EBI-529989; CC Q5VU43; Q3B820: FAM161A; NbExp=3; IntAct=EBI-1105124, EBI-719941; CC Q5VU43; Q5TZK3: FAM74A6; NbExp=3; IntAct=EBI-1105124, EBI-10247271; CC Q5VU43; Q0D2H9: GOLGA8DP; NbExp=3; IntAct=EBI-1105124, EBI-10181276; CC Q5VU43; Q08AF8: GOLGA8G; NbExp=3; IntAct=EBI-1105124, EBI-10181260; CC Q5VU43; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-1105124, EBI-2514791; CC Q5VU43; Q16891: IMMT; NbExp=2; IntAct=EBI-1105124, EBI-473801; CC Q5VU43; Q6P597: KLC3; NbExp=3; IntAct=EBI-1105124, EBI-1643885; CC Q5VU43; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-1105124, EBI-726510; CC Q5VU43; P61968: LMO4; NbExp=4; IntAct=EBI-1105124, EBI-2798728; CC Q5VU43; Q15691: MAPRE1; NbExp=5; IntAct=EBI-1105124, EBI-1004115; CC Q5VU43; A9UHW6: MIF4GD; NbExp=3; IntAct=EBI-1105124, EBI-373498; CC Q5VU43; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-1105124, EBI-742948; CC Q5VU43; P41227: NAA10; NbExp=3; IntAct=EBI-1105124, EBI-747693; CC Q5VU43; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-1105124, EBI-2557469; CC Q5VU43; Q8WWY3: PRPF31; NbExp=7; IntAct=EBI-1105124, EBI-1567797; CC Q5VU43; Q14D33: RTP5; NbExp=3; IntAct=EBI-1105124, EBI-10217913; CC Q5VU43; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-1105124, EBI-748391; CC Q5VU43; O00560: SDCBP; NbExp=4; IntAct=EBI-1105124, EBI-727004; CC Q5VU43; Q9H788: SH2D4A; NbExp=3; IntAct=EBI-1105124, EBI-747035; CC Q5VU43; Q9H788-2: SH2D4A; NbExp=3; IntAct=EBI-1105124, EBI-10308083; CC Q5VU43; Q9NUL5: SHFL; NbExp=3; IntAct=EBI-1105124, EBI-10313866; CC Q5VU43; Q08E77: UTP14C; NbExp=3; IntAct=EBI-1105124, EBI-10225961; CC Q5VU43; Q9BQ24: ZFYVE21; NbExp=3; IntAct=EBI-1105124, EBI-2849569; CC Q5VU43; Q9H9D4: ZNF408; NbExp=3; IntAct=EBI-1105124, EBI-347633; CC Q5VU43; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-1105124, EBI-745520; CC Q5VU43; Q16670: ZSCAN26; NbExp=3; IntAct=EBI-1105124, EBI-3920053; CC Q5VU43; Q9H6F0; NbExp=3; IntAct=EBI-1105124, EBI-10307481; CC Q5VU43; PRO_0000449630 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-1105124, EBI-25475888; CC Q5VU43-2; Q9NX04: AIRIM; NbExp=3; IntAct=EBI-9640281, EBI-8643161; CC Q5VU43-2; Q92619: ARHGAP45; NbExp=3; IntAct=EBI-9640281, EBI-2825900; CC Q5VU43-2; Q13895: BYSL; NbExp=3; IntAct=EBI-9640281, EBI-358049; CC Q5VU43-2; Q8IYE0: CCDC146; NbExp=3; IntAct=EBI-9640281, EBI-10749669; CC Q5VU43-2; E9PSE9: CCDC198; NbExp=3; IntAct=EBI-9640281, EBI-11748295; CC Q5VU43-2; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-9640281, EBI-5453285; CC Q5VU43-2; A0A0S2Z3U4: EGR2; NbExp=3; IntAct=EBI-9640281, EBI-16431598; CC Q5VU43-2; Q9Y247: FAM50B; NbExp=3; IntAct=EBI-9640281, EBI-742802; CC Q5VU43-2; P09067: HOXB5; NbExp=3; IntAct=EBI-9640281, EBI-3893317; CC Q5VU43-2; P31273: HOXC8; NbExp=3; IntAct=EBI-9640281, EBI-1752118; CC Q5VU43-2; Q96GY3: LIN37; NbExp=3; IntAct=EBI-9640281, EBI-748884; CC Q5VU43-2; Q9UPY8: MAPRE3; NbExp=3; IntAct=EBI-9640281, EBI-726739; CC Q5VU43-2; P52179-2: MYOM1; NbExp=3; IntAct=EBI-9640281, EBI-12010196; CC Q5VU43-2; P41227: NAA10; NbExp=3; IntAct=EBI-9640281, EBI-747693; CC Q5VU43-2; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-9640281, EBI-748391; CC Q5VU43-2; O00560: SDCBP; NbExp=4; IntAct=EBI-9640281, EBI-727004; CC Q5VU43-2; O43167: ZBTB24; NbExp=3; IntAct=EBI-9640281, EBI-744471; CC Q5VU43-2; Q9P1Z0: ZBTB4; NbExp=3; IntAct=EBI-9640281, EBI-2564133; CC Q5VU43-2; Q9BRR0: ZKSCAN3; NbExp=3; IntAct=EBI-9640281, EBI-1965777; CC Q5VU43-2; Q15973: ZNF124; NbExp=3; IntAct=EBI-9640281, EBI-2555767; CC Q5VU43-2; Q86VK4-3: ZNF410; NbExp=3; IntAct=EBI-9640281, EBI-11741890; CC Q5VU43-2; Q96IQ9: ZNF414; NbExp=3; IntAct=EBI-9640281, EBI-744257; CC Q5VU43-2; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-9640281, EBI-745520; CC Q5VU43-2; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-9640281, EBI-6427977; CC Q5VU43-2; Q9H7X3: ZNF696; NbExp=3; IntAct=EBI-9640281, EBI-11090299; CC Q5VU43-8; P28329-3: CHAT; NbExp=3; IntAct=EBI-25837868, EBI-25837549; CC Q5VU43-8; P22607: FGFR3; NbExp=3; IntAct=EBI-25837868, EBI-348399; CC Q5VU43-11; Q9H0A8: COMMD4; NbExp=4; IntAct=EBI-10769071, EBI-1550064; CC Q5VU43-11; Q14896: MYBPC3; NbExp=5; IntAct=EBI-10769071, EBI-704176; CC Q5VU43-11; P19429: TNNI3; NbExp=4; IntAct=EBI-10769071, EBI-704146; CC Q5VU43-11; Q8R560: Ankrd1; Xeno; NbExp=2; IntAct=EBI-10769071, EBI-10817505; CC Q5VU43-11; P04764: Eno1; Xeno; NbExp=2; IntAct=EBI-10769071, EBI-915852; CC Q5VU43-11; P15429: Eno3; Xeno; NbExp=2; IntAct=EBI-10769071, EBI-10817548; CC Q5VU43-11; P09456: Prkar1a; Xeno; NbExp=2; IntAct=EBI-10769071, EBI-916215; CC Q5VU43-11; P12368: Prkar2a; Xeno; NbExp=2; IntAct=EBI-10769071, EBI-919521; CC Q5VU43-11; P23693: Tnni3; Xeno; NbExp=2; IntAct=EBI-10769071, EBI-10817583; CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:27666745}. CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome CC {ECO:0000250|UniProtKB:Q9WUJ3}. CC -!- SUBCELLULAR LOCATION: [Isoform 13]: Cytoplasm, cytoskeleton, CC microtubule organizing center, centrosome CC {ECO:0000269|PubMed:29162697}. Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:29162697}. Golgi apparatus CC {ECO:0000269|PubMed:25217626}. Note=Associated with the microtubule CC network at the growing distal tip of microtubules (PubMed:29162697). CC Targeting to the Golgi apparatus requires AKAP9 (PubMed:25217626). CC {ECO:0000269|PubMed:25217626, ECO:0000269|PubMed:29162697}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=12; CC Name=1; CC IsoId=Q5VU43-1; Sequence=Displayed; CC Name=2; CC IsoId=Q5VU43-2; Sequence=VSP_028772, VSP_028779; CC Name=3; CC IsoId=Q5VU43-3; Sequence=VSP_028773, VSP_028781, VSP_028782; CC Name=4; CC IsoId=Q5VU43-4; Sequence=VSP_028783; CC Name=6; CC IsoId=Q5VU43-6; Sequence=VSP_028779; CC Name=7; CC IsoId=Q5VU43-7; Sequence=VSP_028778, VSP_028780; CC Name=8; CC IsoId=Q5VU43-8; Sequence=VSP_028774, VSP_028775; CC Name=9; CC IsoId=Q5VU43-9; Sequence=VSP_028774, VSP_028776, VSP_028777; CC Name=10; CC IsoId=Q5VU43-10; Sequence=VSP_028776, VSP_028777; CC Name=11; CC IsoId=Q5VU43-11; Sequence=VSP_028775; CC Name=12; CC IsoId=Q5VU43-12; Sequence=VSP_028773, VSP_028776, VSP_028777; CC Name=13; Synonyms=Myomegalin variant 8 {ECO:0000303|PubMed:25217626}, CC MMG {ECO:0000303|PubMed:27666745, ECO:0000303|PubMed:28814570}, MMG8 CC {ECO:0000303|PubMed:25217626}, Short myomegalin-like EB1 binding CC protein {ECO:0000303|PubMed:29162697}, SMYLE CC {ECO:0000303|PubMed:29162697}; CC IsoId=Q5VU43-13; Sequence=VSP_028772, VSP_059333, VSP_059334; CC -!- TISSUE SPECIFICITY: Highly expressed in adult and fetal heart, in CC skeletal muscle and, to a lower extent, in brain and placenta. CC {ECO:0000269|PubMed:11374908}. CC -!- DOMAIN: [Isoform 13]: Residues 1-150 are involved in AKAP9-binding. CC {ECO:0000269|PubMed:29162697}. CC -!- DISEASE: Note=A chromosomal aberration involving PDE4DIP may be the CC cause of a myeloproliferative disorder (MBD) associated with CC eosinophilia. Translocation t(1;5)(q23;q33) that forms a PDE4DIP-PDGFRB CC fusion protein. {ECO:0000269|PubMed:12907457}. CC -!- MISCELLANEOUS: [Isoform 13]: Mutagenesis at position 311-312:LP->AA CC (loss of MAPRE1- and MAPRE3-binding and loss of association with CC microtubule ends, no effect on AKAP9- and CDK5RAP2-binding, relocalizes CC from EB1/MAPRE1 microtubule ends to centrosomal area). CC {ECO:0000269|PubMed:25217626, ECO:0000269|PubMed:28814570, CC ECO:0000269|PubMed:29162697, ECO:0000305}. CC -!- CAUTION: Was initially reported to localize in the cytoplasm and CC nucleus (PubMed:11374908). However, many reports in different species CC have shown that it is associated with the Golgi apparatus and the CC centrosome. {ECO:0000269|PubMed:11374908, ECO:0000269|PubMed:27666745}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH04860.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=BAA32299.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAA32322.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAD91152.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=CAH18128.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/180/PDE4DIP01q22"; 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; AB042555; BAB17759.1; -; mRNA. DR EMBL; AB042556; BAB17760.1; -; mRNA. DR EMBL; AB042557; BAB17761.1; -; mRNA. DR EMBL; AB042558; BAB17762.1; -; mRNA. DR EMBL; AB007923; BAA32299.2; ALT_INIT; mRNA. DR EMBL; AB007946; BAA32322.2; ALT_INIT; mRNA. DR EMBL; HQ333476; ADO32613.1; -; mRNA. DR EMBL; AL831815; CAD38529.1; -; mRNA. DR EMBL; AL832024; CAD89923.1; -; mRNA. DR EMBL; AL833273; CAD91152.1; ALT_FRAME; mRNA. DR EMBL; CR749273; CAH18128.1; ALT_SEQ; mRNA. DR EMBL; AL590452; CAH72521.1; -; Genomic_DNA. DR EMBL; AL138791; CAH72521.1; JOINED; Genomic_DNA. DR EMBL; AL590452; CAH72522.1; -; Genomic_DNA. DR EMBL; AL138796; CAH72522.1; JOINED; Genomic_DNA. DR EMBL; AL590452; CAH72523.1; -; Genomic_DNA. DR EMBL; AL138796; CAH72523.1; JOINED; Genomic_DNA. DR EMBL; AL590452; CAH72524.1; -; Genomic_DNA. DR EMBL; AL138796; CAH72524.1; JOINED; Genomic_DNA. DR EMBL; AL590452; CAH72525.1; -; Genomic_DNA. DR EMBL; AL590452; CAH72526.1; -; Genomic_DNA. DR EMBL; AL138796; CAH72526.1; JOINED; Genomic_DNA. DR EMBL; AL590452; CAH72527.1; -; Genomic_DNA. DR EMBL; AL138796; CAH72527.1; JOINED; Genomic_DNA. DR EMBL; AL590452; CAH72528.1; -; Genomic_DNA. DR EMBL; AL138796; CAH72528.1; JOINED; Genomic_DNA. DR EMBL; AL138791; CAI22527.1; -; Genomic_DNA. DR EMBL; AL590452; CAI22527.1; JOINED; Genomic_DNA. DR EMBL; AL138796; CAI22822.1; -; Genomic_DNA. DR EMBL; AL590452; CAI22822.1; JOINED; Genomic_DNA. DR EMBL; AL138796; CAI22823.1; -; Genomic_DNA. DR EMBL; AL590452; CAI22823.1; JOINED; Genomic_DNA. DR EMBL; AL138796; CAI22824.1; -; Genomic_DNA. DR EMBL; AL590452; CAI22824.1; JOINED; Genomic_DNA. DR EMBL; AL138796; CAI22825.1; -; Genomic_DNA. DR EMBL; AL590452; CAI22825.1; JOINED; Genomic_DNA. DR EMBL; AL138796; CAI22826.1; -; Genomic_DNA. DR EMBL; AL590452; CAI22826.1; JOINED; Genomic_DNA. DR EMBL; AL138796; CAI22827.1; -; Genomic_DNA. DR EMBL; AL590452; CAI22827.1; JOINED; Genomic_DNA. DR EMBL; AC239802; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC245389; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC239804; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC004860; AAH04860.1; ALT_SEQ; mRNA. DR EMBL; BC025406; AAH25406.1; -; mRNA. DR EMBL; BC078660; AAH78660.1; -; mRNA. DR EMBL; BC110294; AAI10295.1; -; mRNA. DR EMBL; BC132717; AAI32718.1; -; mRNA. DR EMBL; BC152439; AAI52440.1; -; mRNA. DR EMBL; DA900724; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS72887.1; -. [Q5VU43-8] DR CCDS; CCDS72888.1; -. [Q5VU43-3] DR CCDS; CCDS72890.1; -. [Q5VU43-6] DR CCDS; CCDS72891.1; -. [Q5VU43-1] DR CCDS; CCDS72892.1; -. [Q5VU43-4] DR CCDS; CCDS72893.1; -. [Q5VU43-11] DR CCDS; CCDS72894.1; -. [Q5VU43-2] DR CCDS; CCDS91045.1; -. [Q5VU43-13] DR PIR; T00069; T00069. DR PIR; T00259; T00259. DR RefSeq; NP_001002810.1; NM_001002810.3. [Q5VU43-11] DR RefSeq; NP_001002811.2; NM_001002811.2. [Q5VU43-2] DR RefSeq; NP_001002812.2; NM_001002812.2. [Q5VU43-6] DR RefSeq; NP_001182189.1; NM_001195260.1. DR RefSeq; NP_001182190.1; NM_001195261.1. DR RefSeq; NP_001185761.2; NM_001198832.2. [Q5VU43-3] DR RefSeq; NP_001185763.3; NM_001198834.3. [Q5VU43-4] DR RefSeq; NP_055459.5; NM_014644.5. [Q5VU43-1] DR RefSeq; NP_071754.3; NM_022359.5. [Q5VU43-8] DR RefSeq; XP_016855361.1; XM_016999872.1. DR RefSeq; XP_016855362.1; XM_016999873.1. DR RefSeq; XP_016858514.1; XM_017003025.1. DR RefSeq; XP_016858515.1; XM_017003026.1. DR AlphaFoldDB; Q5VU43; -. DR SMR; Q5VU43; -. DR BioGRID; 115017; 202. DR DIP; DIP-51263N; -. DR IntAct; Q5VU43; 188. DR MINT; Q5VU43; -. DR STRING; 9606.ENSP00000358363; -. DR GlyCosmos; Q5VU43; 2 sites, 1 glycan. DR GlyGen; Q5VU43; 5 sites, 2 O-linked glycans (5 sites). DR iPTMnet; Q5VU43; -. DR PhosphoSitePlus; Q5VU43; -. DR BioMuta; PDE4DIP; -. DR DMDM; 74747041; -. DR EPD; Q5VU43; -. DR jPOST; Q5VU43; -. DR MassIVE; Q5VU43; -. DR MaxQB; Q5VU43; -. DR PaxDb; 9606-ENSP00000358363; -. DR PeptideAtlas; Q5VU43; -. DR ProteomicsDB; 21657; -. DR ProteomicsDB; 65374; -. [Q5VU43-1] DR ProteomicsDB; 65375; -. [Q5VU43-10] DR ProteomicsDB; 65376; -. [Q5VU43-11] DR ProteomicsDB; 65377; -. [Q5VU43-12] DR ProteomicsDB; 65378; -. [Q5VU43-2] DR ProteomicsDB; 65379; -. [Q5VU43-3] DR ProteomicsDB; 65380; -. [Q5VU43-4] DR ProteomicsDB; 65381; -. [Q5VU43-6] DR ProteomicsDB; 65382; -. [Q5VU43-7] DR ProteomicsDB; 65383; -. [Q5VU43-8] DR ProteomicsDB; 65384; -. [Q5VU43-9] DR Pumba; Q5VU43; -. DR Antibodypedia; 2152; 151 antibodies from 23 providers. DR DNASU; 9659; -. DR Ensembl; ENST00000313431.13; ENSP00000316434.9; ENSG00000178104.22. [Q5VU43-2] DR Ensembl; ENST00000369347.8; ENSP00000358353.4; ENSG00000178104.22. [Q5VU43-11] DR Ensembl; ENST00000369349.7; ENSP00000358355.3; ENSG00000178104.22. [Q5VU43-6] DR Ensembl; ENST00000369351.7; ENSP00000358357.3; ENSG00000178104.22. [Q5VU43-7] DR Ensembl; ENST00000369354.7; ENSP00000358360.3; ENSG00000178104.22. [Q5VU43-1] DR Ensembl; ENST00000369356.8; ENSP00000358363.4; ENSG00000178104.22. [Q5VU43-4] DR Ensembl; ENST00000529945.2; ENSP00000433392.1; ENSG00000178104.22. [Q5VU43-13] DR Ensembl; ENST00000530472.5; ENSP00000482121.1; ENSG00000178104.22. [Q5VU43-8] DR Ensembl; ENST00000618462.4; ENSP00000479409.1; ENSG00000178104.22. [Q5VU43-3] DR GeneID; 9659; -. DR KEGG; hsa:9659; -. DR UCSC; uc001emb.3; human. [Q5VU43-1] DR UCSC; uc057kja.1; human. DR AGR; HGNC:15580; -. DR CTD; 9659; -. DR DisGeNET; 9659; -. DR GeneCards; PDE4DIP; -. DR HGNC; HGNC:15580; PDE4DIP. DR HPA; ENSG00000178104; Group enriched (heart muscle, skeletal muscle, tongue). DR MalaCards; PDE4DIP; -. DR MIM; 608117; gene. DR neXtProt; NX_Q5VU43; -. DR OpenTargets; ENSG00000178104; -. DR PharmGKB; PA33131; -. DR VEuPathDB; HostDB:ENSG00000178104; -. DR eggNOG; ENOG502QPV2; Eukaryota. DR GeneTree; ENSGT00950000183190; -. DR HOGENOM; CLU_897036_0_0_1; -. DR InParanoid; Q5VU43; -. DR OMA; FMLERIY; -. DR OrthoDB; 5323352at2759; -. DR PhylomeDB; Q5VU43; -. DR TreeFam; TF329233; -. DR PathwayCommons; Q5VU43; -. DR SignaLink; Q5VU43; -. DR SIGNOR; Q5VU43; -. DR BioGRID-ORCS; 653513; 0 hits in 3 CRISPR screens. DR BioGRID-ORCS; 9659; 367 hits in 1161 CRISPR screens. DR ChiTaRS; PDE4DIP; human. DR GeneWiki; Myomegalin; -. DR GenomeRNAi; 9659; -. DR Pharos; Q5VU43; Tbio. DR PRO; PR:Q5VU43; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q5VU43; Protein. DR Bgee; ENSG00000178104; Expressed in apex of heart and 198 other cell types or tissues. DR ExpressionAtlas; Q5VU43; baseline and differential. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0030016; C:myofibril; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0019899; F:enzyme binding; ISS:UniProtKB. DR GO; GO:0060090; F:molecular adaptor activity; IDA:UniProtKB. DR GO; GO:0030953; P:astral microtubule organization; IMP:UniProtKB. DR GO; GO:0007098; P:centrosome cycle; IBA:GO_Central. DR GO; GO:0090063; P:positive regulation of microtubule nucleation; IMP:UniProtKB. DR GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB. DR GO; GO:1903358; P:regulation of Golgi organization; IDA:UniProtKB. DR InterPro; IPR012943; Cnn_1N. DR InterPro; IPR010630; Olduvai_dom. DR PANTHER; PTHR46501; MYOMEGALIN; 1. DR PANTHER; PTHR46501:SF2; MYOMEGALIN; 1. DR Pfam; PF07989; Cnn_1N; 1. DR Pfam; PF06758; Olduvai; 2. DR SMART; SM01148; DUF1220; 1. DR PROSITE; PS51316; ODV; 1. DR Genevisible; Q5VU43; HS. PE 1: Evidence at protein level; KW Alternative splicing; Chromosomal rearrangement; Coiled coil; Cytoplasm; KW Cytoskeleton; Golgi apparatus; Phosphoprotein; Reference proteome. FT CHAIN 1..2346 FT /note="Myomegalin" FT /id="PRO_0000307690" FT DOMAIN 1551..1642 FT /note="Olduvai" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00647" FT REGION 698..732 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1193..1214 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1591..1614 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1633..1690 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2081..2103 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2127..2156 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 41..132 FT /evidence="ECO:0000255" FT COILED 162..205 FT /evidence="ECO:0000255" FT COILED 238..318 FT /evidence="ECO:0000255" FT COILED 350..684 FT /evidence="ECO:0000255" FT COILED 743..936 FT /evidence="ECO:0000255" FT COILED 1002..1043 FT /evidence="ECO:0000255" FT COILED 1096..1124 FT /evidence="ECO:0000255" FT COILED 1212..1240 FT /evidence="ECO:0000255" FT COILED 1346..1385 FT /evidence="ECO:0000255" FT COILED 1431..1455 FT /evidence="ECO:0000255" FT COILED 1736..1760 FT /evidence="ECO:0000255" FT COILED 1840..2077 FT /evidence="ECO:0000255" FT COILED 2273..2312 FT /evidence="ECO:0000255" FT COMPBIAS 1644..1690 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2127..2142 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 742..743 FT /note="Breakpoint for insertion to form PDE4DIP-PDGFRB FT fusion protein" FT MOD_RES 704 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT VAR_SEQ 1..210 FT /note="MSNGYRTLSQHLNDLKKENFSLKLRIYFLEERMQQKYEASREDIYKRNIELK FT VEVESLKRELQDKKQHLDKTWADVENLNSQNEAELRRQFEERQQETEHVYELLENKIQL FT LQEESRLAKNEAARMAALVEAEKECNLELSEKLKGVTKNWEDVPGDQVKPDQYTEALAQ FT RDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEPTSME -> MKEICRICARELCGN FT QRRWIFHTASKLNLQVLLSHVLGKDVPRDGKAEFACSKCAFMLDRIYRFDTVIARIEAL FT SIERLQKLLLEKDRLKFCIASMYRKNNDDSGAEIKAGNGTVDMSVLPDARYSALLQEDF FT AYSGFECWVENEDQIQEPHSCHGSEGPGNRPRRCRGCAALRVADSDYEAICKVPRKVAR FT SISCGPSSRWSTSICTEEPALSEVGPPDLASTKVPPDGESMEEETPGSSVESLDASVQA FT SPPQQKDEETERSAKELGKCDCCSDDQAPQHGCNHKLELALSMIKGLDYKPIQSPRGSR FT LPIPVKSSLPGAKPGPSMTDGVSSGFLNRSLKPLYKTPVSYPLELSDLQELWDDLCEDY FT LPLR (in isoform 2 and isoform 13)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9455484" FT /id="VSP_028772" FT VAR_SEQ 1..10 FT /note="MSNGYRTLSQ -> MEQTWTRDYFAEDDGEMVPRTSHTAAFLSDTKDRGPPV FT QSQIWRSGEKVPFVQTYSLRAFEKPPQVQTQALRDFEK (in isoform 3 and FT isoform 12)" FT /evidence="ECO:0000303|PubMed:11374908, FT ECO:0000303|PubMed:9455484" FT /id="VSP_028773" FT VAR_SEQ 1..10 FT /note="MSNGYRTLSQ -> MKGTDSGSCCRRRCDFGCCCRASRRAHYTPYRSGDATR FT TPQSPRQTPSRERRRPEPAGSWAAAAEEEEAAAAATPWMRDYFAEDDGEMVPRTSHTAA FT FLSDTKDRGPPVQSQIWRSGEKVPFVQTYSLRAFEKPPQVQTQALRDFEK (in FT isoform 8 and isoform 9)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_028774" FT VAR_SEQ 174..2346 FT /note="Missing (in isoform 8 and isoform 11)" FT /evidence="ECO:0000303|PubMed:11374908, FT ECO:0000303|PubMed:15489334" FT /id="VSP_028775" FT VAR_SEQ 174 FT /note="R -> I (in isoform 9, isoform 10 and isoform 12)" FT /evidence="ECO:0000303|PubMed:11374908, FT ECO:0000303|PubMed:15489334" FT /id="VSP_028776" FT VAR_SEQ 175..2346 FT /note="Missing (in isoform 9, isoform 10 and isoform 12)" FT /evidence="ECO:0000303|PubMed:11374908, FT ECO:0000303|PubMed:15489334" FT /id="VSP_028777" FT VAR_SEQ 940..953 FT /note="AAAGDDTEDTSTEF -> GELESVRIHHKHAY (in isoform 13)" FT /id="VSP_059333" FT VAR_SEQ 954..2346 FT /note="Missing (in isoform 13)" FT /id="VSP_059334" FT VAR_SEQ 968..988 FT /note="QLVKVALEKSLATVETQNPSF -> QVSQCQGLGLPGWTAHSPSEV (in FT isoform 7)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_028778" FT VAR_SEQ 970..2346 FT /note="Missing (in isoform 2 and isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:17974005, ECO:0000303|PubMed:9455484" FT /id="VSP_028779" FT VAR_SEQ 989..2346 FT /note="Missing (in isoform 7)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_028780" FT VAR_SEQ 1082..1191 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:9455484" FT /id="VSP_028781" FT VAR_SEQ 1695..1756 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:9455484" FT /id="VSP_028782" FT VAR_SEQ 2334..2346 FT /note="VKSLRALPCTPAL -> EPCKKRSHQKSLKQQERWACPPFVQLPIC (in FT isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_028783" FT VARIANT 13 FT /note="N -> S (in dbSNP:rs3010980)" FT /id="VAR_036627" FT VARIANT 25 FT /note="R -> L (in dbSNP:rs1664022)" FT /id="VAR_036628" FT VARIANT 49 FT /note="I -> T (in dbSNP:rs573724)" FT /evidence="ECO:0000269|PubMed:11374908, FT ECO:0000269|PubMed:15489334" FT /id="VAR_036629" FT VARIANT 143 FT /note="K -> E (in dbSNP:rs1747958)" FT /id="VAR_056951" FT VARIANT 150 FT /note="N -> S (in dbSNP:rs3010980)" FT /id="VAR_056952" FT VARIANT 167 FT /note="A -> T (in dbSNP:rs2590120)" FT /id="VAR_036630" FT VARIANT 171 FT /note="R -> K (in dbSNP:rs3121544)" FT /id="VAR_051204" FT VARIANT 391 FT /note="E -> A (in dbSNP:rs1324366)" FT /id="VAR_051205" FT VARIANT 410 FT /note="E -> V (in dbSNP:rs1061308)" FT /id="VAR_051206" FT VARIANT 482 FT /note="H -> R (in dbSNP:rs1698681)" FT /id="VAR_051207" FT VARIANT 681 FT /note="R -> H (in dbSNP:rs1629011)" FT /id="VAR_051208" FT VARIANT 708 FT /note="R -> C (in dbSNP:rs1628172)" FT /evidence="ECO:0000269|PubMed:16710414, FT ECO:0000269|PubMed:17974005" FT /id="VAR_051209" FT VARIANT 1013 FT /note="F -> I (in dbSNP:rs1698624)" FT /evidence="ECO:0000269|PubMed:17974005" FT /id="VAR_051210" FT VARIANT 1066 FT /note="A -> T (in dbSNP:rs1698647)" FT /evidence="ECO:0000269|PubMed:17974005" FT /id="VAR_051211" FT VARIANT 1359 FT /note="K -> E (in dbSNP:rs1747958)" FT /evidence="ECO:0000269|PubMed:17974005" FT /id="VAR_051212" FT VARIANT 1396 FT /note="R -> W (in dbSNP:rs2798901)" FT /id="VAR_080232" FT VARIANT 1736 FT /note="V -> E (in dbSNP:rs1778159)" FT /evidence="ECO:0000269|PubMed:17974005" FT /id="VAR_051213" FT VARIANT 1742 FT /note="A -> S (in dbSNP:rs1698605)" FT /evidence="ECO:0000269|PubMed:17974005" FT /id="VAR_051214" FT CONFLICT 33 FT /note="M -> T (in Ref. 5; CAD89923)" FT /evidence="ECO:0000305" FT CONFLICT 98 FT /note="T -> M (in Ref. 1; BAB17761/BAB17762)" FT /evidence="ECO:0000305" FT CONFLICT 109 FT /note="I -> M (in Ref. 1; FT BAB17759/BAB17760/BAB17761/BAB17762 and 7; FT AAH25406/AAI10295)" FT /evidence="ECO:0000305" FT CONFLICT 401 FT /note="R -> Q (in Ref. 5; CAD91152)" FT /evidence="ECO:0000305" FT CONFLICT 643 FT /note="M -> V (in Ref. 5; CAD91152)" FT /evidence="ECO:0000305" FT CONFLICT 776 FT /note="L -> P (in Ref. 5; CAD91152)" FT /evidence="ECO:0000305" FT CONFLICT 783 FT /note="M -> I (in Ref. 5; CAD38529 and 7; AAI32718)" FT /evidence="ECO:0000305" FT CONFLICT 830 FT /note="L -> P (in Ref. 5; CAD91152)" FT /evidence="ECO:0000305" FT CONFLICT 863 FT /note="L -> P (in Ref. 5; CAD38529)" FT /evidence="ECO:0000305" FT CONFLICT 1266 FT /note="K -> E (in Ref. 5; CAH18128)" FT /evidence="ECO:0000305" FT CONFLICT 1286 FT /note="E -> G (in Ref. 5; CAD91152)" FT /evidence="ECO:0000305" FT CONFLICT 1356 FT /note="K -> R (in Ref. 5; CAD91152)" FT /evidence="ECO:0000305" FT CONFLICT 1397 FT /note="K -> E (in Ref. 5; CAD91152)" FT /evidence="ECO:0000305" FT CONFLICT 1454 FT /note="K -> E (in Ref. 5; CAH18128)" FT /evidence="ECO:0000305" FT CONFLICT 1504 FT /note="R -> Q (in Ref. 5; CAH18128)" FT /evidence="ECO:0000305" FT CONFLICT 1598 FT /note="H -> R (in Ref. 5; CAH18128)" FT /evidence="ECO:0000305" FT CONFLICT 1610 FT /note="T -> P (in Ref. 5; CAH18128)" FT /evidence="ECO:0000305" FT CONFLICT 1727 FT /note="L -> P (in Ref. 5; CAH18128)" FT /evidence="ECO:0000305" FT CONFLICT 1757 FT /note="A -> T (in Ref. 5; CAH18128)" FT /evidence="ECO:0000305" FT CONFLICT 1867 FT /note="R -> C (in Ref. 5; CAH18128)" FT /evidence="ECO:0000305" FT CONFLICT 1910 FT /note="D -> E (in Ref. 5; CAH18128)" FT /evidence="ECO:0000305" FT CONFLICT 2001 FT /note="E -> G (in Ref. 5; CAH18128)" FT /evidence="ECO:0000305" FT CONFLICT 2088 FT /note="Missing (in Ref. 5; CAH18128)" FT /evidence="ECO:0000305" FT CONFLICT 2291 FT /note="R -> Q (in Ref. 5; CAH18128)" FT /evidence="ECO:0000305" FT CONFLICT 2317 FT /note="Q -> R (in Ref. 5; CAH18128)" FT /evidence="ECO:0000305" FT MOD_RES Q5VU43-2:252 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES Q5VU43-13:252 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" SQ SEQUENCE 2346 AA; 265103 MW; 8A29AA1514759B0C CRC64; MSNGYRTLSQ HLNDLKKENF SLKLRIYFLE ERMQQKYEAS REDIYKRNIE LKVEVESLKR ELQDKKQHLD KTWADVENLN SQNEAELRRQ FEERQQETEH VYELLENKIQ LLQEESRLAK NEAARMAALV EAEKECNLEL SEKLKGVTKN WEDVPGDQVK PDQYTEALAQ RDKRIEELNQ SLAAQERLVE QLSREKQQLL HLLEEPTSME VQPMTEELLK QQKLNSHETT ITQQSVSDSH LAELQEKIQQ TEATNKILQE KLNEMSYELK CAQESSQKQD GTIQNLKETL KSRERETEEL YQVIEGQNDT MAKLREMLHQ SQLGQLHSSE GTSPAQQQVA LLDLQSALFC SQLEIQKLQR VVRQKERQLA DAKQCVQFVE AAAHESEQQK EASWKHNQEL RKALQQLQEE LQNKSQQLRA WEAEKYNEIR TQEQNIQHLN HSLSHKEQLL QEFRELLQYR DNSDKTLEAN EMLLEKLRQR IHDKAVALER AIDEKFSALE EKEKELRQLR LAVRERDHDL ERLRDVLSSN EATMQSMESL LRAKGLEVEQ LSTTCQNLQW LKEEMETKFS RWQKEQESII QQLQTSLHDR NKEVEDLSAT LLCKLGPGQS EIAEELCQRL QRKERMLQDL LSDRNKQVLE HEMEIQGLLQ SVSTREQESQ AAAEKLVQAL MERNSELQAL RQYLGGRDSL MSQAPISNQQ AEVTPTGRLG KQTDQGSMQI PSRDDSTSLT AKEDVSIPRS TLGDLDTVAG LEKELSNAKE ELELMAKKER ESQMELSALQ SMMAVQEEEL QVQAADMESL TRNIQIKEDL IKDLQMQLVD PEDIPAMERL TQEVLLLREK VASVESQGQE ISGNRRQQLL LMLEGLVDER SRLNEALQAE RQLYSSLVKF HAHPESSERD RTLQVELEGA QVLRSRLEEV LGRSLERLNR LETLAAIGGA AAGDDTEDTS TEFTDSIEEE AAHHSHQQLV KVALEKSLAT VETQNPSFSP PSPMGGDSNR CLQEEMLHLR AEFHQHLEEK RKAEEELKEL KAQIEEAGFS SVSHIRNTML SLCLENAELK EQMGEAMSDG WEIEEDKEKG EVMVETVVTK EGLSESSLQA EFRKLQGKLK NAHNIINLLK EQLVLSSKEG NSKLTPELLV HLTSTIERIN TELVGSPGKH QHQEEGNVTV RPFPRPQSLD LGATFTVDAH QLDNQSQPRD PGPQSAFSLP GSTQHLRSQL SQCKQRYQDL QEKLLLSEAT VFAQANELEK YRVMLTGESL VKQDSKQIQV DLQDLGYETC GRSENEAERE ETTSPECEEH NSLKEMVLME GLCSEQGRRG STLASSSERK PLENQLGKQE EFRVYGKSEN ILVLRKDIKD LKAQLQNANK VIQNLKSRVR SLSVTSDYSS SLERPRKLRA VGTLEGSSPH SVPDEDEGWL SDGTGAFYSP GLQAKKDLES LIQRVSQLEA QLPKNGLEEK LAEELRSASW PGKYDSLIQD QARELSYLRQ KIREGRGICY LITRHAKDTV KSFEDLLRSN DIDYYLGQSF REQLAQGSQL TERLTSKLST KDHKSEKDQA GLEPLALRLS RELQEKEKVI EVLQAKLDAR SLTPSSSHAL SDSHRSPSST SFLSDELEAC SDMDIVSEYT HYEEKKASPS HSDSIHHSSH SAVLSSKPSS TSASQGAKAE SNSNPISLPT PQNTPKEANQ AHSGFHFHSI PKLASLPQAP LPSAPSSFLP FSPTGPLLLG CCETPVVSLA EAQQELQMLQ KQLGESASTV PPASTATLLS NDLEADSSYY LNSAQPHSPP RGTIELGRIL EPGYLGSSGK WDVMRPQKGS VSGDLSSGSS VYQLNSKPTG ADLLEEHLGE IRNLRQRLEE SICINDRLRE QLEHRLTSTA RGRGSTSNFY SQGLESIPQL CNENRVLRED NRRLQAQLSH VSREHSQETE SLREALLSSR SHLQELEKEL EHQKVERQQL LEDLREKQQE VLHFREERLS LQENDSRLQH KLVLLQQQCE EKQQLFESLQ SELQIYEALY GNSKKGLKAY SLDACHQIPL SSDLSHLVAE VRALRGQLEQ SIQGNNCLRL QLQQQLESGA GKASLSPSSI NQNFPASTDP GNKQLLLQDS AVSPPVRDVG MNSPALVFPS SASSTPGSET PIINRANGLG LDTSPVMKTP PKLEGDATDG SFANKHGRHV IGHIDDYSAL RQQIAEGKLL VKKIVSLVRS ACSFPGLEAQ GTEVLGSKGI HELRSSTSAL HHALEESASL LTMFWRAALP STHIPVLPGK VGESTERELL ELRTKVSKQE RLLQSTTEHL KNANQQKESM EQFIVSQLTR THDVLKKART NLEVKSLRAL PCTPAL //