MYOME_HUMAN
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 03-AUG-2022, entry version 161.
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; Q13895: BYSL; NbExp=5; IntAct=EBI-1105124, EBI-358049;
CC Q5VU43; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-1105124, EBI-8643161;
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 Q5VU43-2; Q92619: ARHGAP45; NbExp=3; IntAct=EBI-9640281, EBI-2825900;
CC Q5VU43-2; Q13895: BYSL; NbExp=3; IntAct=EBI-9640281, EBI-358049;
CC Q5VU43-2; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-9640281, EBI-8643161;
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="http://atlasgeneticsoncology.org/Genes/PDE4DIP01q22ID180.html";
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 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; 193.
DR DIP; DIP-51263N; -.
DR IntAct; Q5VU43; 185.
DR MINT; Q5VU43; -.
DR STRING; 9606.ENSP00000358363; -.
DR GlyGen; Q5VU43; 2 sites, 1 O-linked glycan (2 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; Q5VU43; -.
DR PeptideAtlas; Q5VU43; -.
DR PRIDE; 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 Antibodypedia; 2152; 128 antibodies from 23 providers.
DR DNASU; 9659; -.
DR Ensembl; ENST00000313431.13; ENSP00000316434.9; ENSG00000178104.19. [Q5VU43-2]
DR Ensembl; ENST00000369347.8; ENSP00000358353.4; ENSG00000178104.19. [Q5VU43-11]
DR Ensembl; ENST00000369349.7; ENSP00000358355.3; ENSG00000178104.19. [Q5VU43-6]
DR Ensembl; ENST00000369351.7; ENSP00000358357.3; ENSG00000178104.19. [Q5VU43-7]
DR Ensembl; ENST00000369354.7; ENSP00000358360.3; ENSG00000178104.19. [Q5VU43-1]
DR Ensembl; ENST00000369356.8; ENSP00000358363.4; ENSG00000178104.19. [Q5VU43-4]
DR Ensembl; ENST00000529945.2; ENSP00000433392.1; ENSG00000178104.19. [Q5VU43-13]
DR Ensembl; ENST00000530472.5; ENSP00000482121.1; ENSG00000178104.19. [Q5VU43-8]
DR Ensembl; ENST00000618462.4; ENSP00000479409.1; ENSG00000178104.19. [Q5VU43-3]
DR GeneID; 9659; -.
DR KEGG; hsa:9659; -.
DR UCSC; uc001emb.3; human. [Q5VU43-1]
DR UCSC; uc057kja.1; human.
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 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; FILERMY; -.
DR OrthoDB; 15127at2759; -.
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; 344 hits in 1091 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 196 other tissues.
DR ExpressionAtlas; Q5VU43; baseline and differential.
DR Genevisible; Q5VU43; HS.
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 Pfam; PF07989; Cnn_1N; 1.
DR Pfam; PF06758; Olduvai; 1.
DR SMART; SM01148; DUF1220; 1.
DR PROSITE; PS51316; ODV; 1.
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; BAB17759/BAB17760/BAB17761/
FT BAB17762 and 7; 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
