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Myomegalin (Cardiomyopathy-associated protein 2) (Phosphodiesterase 4D-interacting protein)

 MYOME_HUMAN             Reviewed;        2346 AA.
Q5VU43; A0A0A0MRM0; A0A0C4DFQ0; A2RU15; E9PL24; O75042; O75065;
Q2YDC1; Q5VU42; Q5VU44; Q5VU45; Q5VU46; Q5VU47; Q5VU48; Q5VU49;
Q68DU2; Q6AZ93; Q6PK88; Q86T40; Q86TB2; Q8N3W0; Q8TAY9; Q9HCP2;
Q9HCP3; Q9HCP4; Q9HCP5;
23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
28-MAR-2018, sequence version 3.
12-SEP-2018, entry version 135.
RecName: Full=Myomegalin;
AltName: Full=Cardiomyopathy-associated protein 2;
AltName: Full=Phosphodiesterase 4D-interacting protein;
Name=PDE4DIP; Synonyms=CMYA2, KIAA0454, KIAA0477, MMGL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 10; 11 AND 12), TISSUE
SPECIFICITY, AND VARIANT THR-49.
TISSUE=Myocardium;
PubMed=11374908; DOI=10.1006/geno.2001.6527;
Soejima H., Kawamoto S., Akai J., Miyoshi O., Arai Y., Morohka T.,
Matsuo S., Niikawa N., Kimura A., Okubo K., Mukai T.;
"Isolation of novel heart-specific genes using the BodyMap database.";
Genomics 74:115-120(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 13), FUNCTION (ISOFORM 13),
INTERACTION WITH AKAP9; GAMMA-TUBULIN RING COMPLEX; MAPRE1 AND MAPRE3
(ISOFORM 13), SUBCELLULAR LOCATION (ISOFORM 13), AND MUTAGENESIS
(ISOFORM 13).
PubMed=25217626; DOI=10.1242/jcs.155408;
Wang Z., Zhang C., Qi R.Z.;
"A newly identified myomegalin isoform functions in Golgi microtubule
organization and ER-Golgi transport.";
J. Cell Sci. 127:4904-4917(2014).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Brain;
PubMed=9455484; DOI=10.1093/dnares/4.5.345;
Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
Nomura N., Ohara O.;
"Characterization of cDNA clones in size-fractionated cDNA libraries
from human brain.";
DNA Res. 4:345-349(1997).
[4]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 6 AND 7), AND
VARIANTS CYS-708; ILE-1013; THR-1066; GLU-1359; GLU-1736 AND SER-1742.
TISSUE=Amygdala, and Skeletal muscle;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS CYS-708
AND TRP-1396.
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 8 AND 9), AND
VARIANT THR-49.
TISSUE=Brain, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2261-2346 (ISOFORM 4).
TISSUE=Skeletal muscle;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
CHROMOSOMAL TRANSLOCATION WITH PDGFRB.
PubMed=12907457; DOI=10.1182/blood-2003-04-1150;
Wilkinson K., Velloso E.R.P., Lopes L.F., Lee C., Aster J.C.,
Shipp M.A., Aguiar R.C.T.;
"Cloning of the t(1;5)(q23;q33) in a myeloproliferative disorder
associated with eosinophilia: involvement of PDGFRB and response to
imatinib.";
Blood 102:4187-4190(2003).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-704, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252 (ISOFORMS 13 AND 2),
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[14]
FUNCTION (ISOFORM 13), SUBCELLULAR LOCATION (ISOFORM 13), AND
INTERACTION WITH AKAP9 AND CAMSAP2 (ISOFORM 13).
PubMed=27666745; DOI=10.1016/j.devcel.2016.08.009;
Wu J., de Heus C., Liu Q., Bouchet B.P., Noordstra I., Jiang K.,
Hua S., Martin M., Yang C., Grigoriev I., Katrukha E.A.,
Altelaar A.F., Hoogenraad C.C., Qi R.Z., Klumperman J., Akhmanova A.;
"Molecular pathway of microtubule organization at the Golgi
apparatus.";
Dev. Cell 39:44-60(2016).
[15]
FUNCTION (ISOFORM 13), INTERACTION WITH AKAP9; CAMSAP2; MAPRE1 AND
MAPRE3 (ISOFORM 13), AND MUTAGENESIS (ISOFORM 13).
PubMed=28814570; DOI=10.1083/jcb.201701024;
Yang C., Wu J., de Heus C., Grigoriev I., Liv N., Yao Y., Smal I.,
Meijering E., Klumperman J., Qi R.Z., Akhmanova A.;
"EB1 and EB3 regulate microtubule minus end organization and Golgi
morphology.";
J. Cell Biol. 216:3179-3198(2017).
[16]
INTERACTION WITH AKAP9; CDK5RAP2; LGALS3BP AND MAPRE1 (ISOFORM 13),
SUBCELLULAR LOCATION (ISOFORM 13), IDENTIFICATION BY MASS SPECTROMETRY
(ISOFORM 13), MUTAGENESIS (ISOFORM 13), AND DOMAIN.
PubMed=29162697; DOI=10.1073/pnas.1705682114;
Bouguenina H., Salaun D., Mangon A., Muller L., Baudelet E.,
Camoin L., Tachibana T., Cianferani S., Audebert S.,
Verdier-Pinard P., Badache A.;
"EB1-binding-myomegalin protein complex promotes centrosomal
microtubules functions.";
Proc. Natl. Acad. Sci. U.S.A. 114:E10687-E10696(2017).
-!- FUNCTION: Functions as an anchor sequestering components of the
cAMP-dependent pathway to Golgi and/or centrosomes (By
similarity). {ECO:0000250|UniProtKB:Q9WUJ3}.
-!- FUNCTION: Isoform 13: Participates in microtubule dynamics,
promoting microtubule assembly. Depending upon the cell context,
may act at the level of the Golgi apparatus or that of the
centrosome (PubMed:25217626, PubMed:27666745, PubMed:28814570,
PubMed:29162697). In complex with AKAP9, recruits CAMSAP2 to the
Golgi apparatus and tethers non-centrosomal minus-end microtubules
to the Golgi, an important step for polarized cell movement
(PubMed:27666745, PubMed:28814570). In complex with AKAP9,
EB1/MAPRE1 and CDK5RAP2, contributes to microtubules nucleation
and extension from the centrosome to the cell periphery, a crucial
process for directed cell migration, mitotic spindle orientation
and cell-cycle progression (PubMed:29162697).
{ECO:0000269|PubMed:25217626, ECO:0000269|PubMed:27666745,
ECO:0000269|PubMed:28814570, ECO:0000269|PubMed:29162697}.
-!- SUBUNIT: Interacts with PDE4D (By similarity). Isoform 13
interacts with MAPRE1 and MAPRE3 (PubMed:25217626,
PubMed:28814570, PubMed:29162697). Isoform 13 forms a
pericentrosomal complex with AKAP9, CDK5RAP2 and EB1/MAPRE1;
within this complex, may mediate MAPRE1-binding to CDK5RAP2
(PubMed:29162697). Interaction of isoform 13 with AKAP9 stabilizes
both proteins (PubMed:25217626, PubMed:27666745). Isoform 13
interacts (via N-terminus) with CAMSAP2; this interaction is much
stronger in the presence of AKAP9 (PubMed:27666745). In complex
with AKAP9, Isoform 13 recruits CAMSAP2 to the Golgi apparatus
(PubMed:27666745, PubMed:28814570). Isoform 13 interacts with
unglycosylated LGALS3BP; this interaction may connect the
pericentrosomal complex to the gamma-tubulin ring complex (gamma-
TuRC) to promote microtubule assembly and acetylation
(PubMed:25217626, PubMed:29162697). {ECO:0000250|UniProtKB:Q9WUJ3,
ECO:0000269|PubMed:25217626, ECO:0000269|PubMed:27666745,
ECO:0000269|PubMed:28814570, ECO:0000269|PubMed:29162697}.
-!- INTERACTION:
Q9H6F0:-; NbExp=3; IntAct=EBI-1105124, EBI-10307481;
Q8WTP8:AEN; NbExp=3; IntAct=EBI-1105124, EBI-8637627;
Q8R560:Ankrd1 (xeno); NbExp=2; IntAct=EBI-10769071, EBI-10817505;
Q13895:BYSL; NbExp=5; IntAct=EBI-1105124, EBI-358049;
Q9NX04:C1orf109; NbExp=3; IntAct=EBI-1105124, EBI-8643161;
Q9NVL8:CCDC198; NbExp=3; IntAct=EBI-1105124, EBI-10238351;
Q9NX63:CHCHD3; NbExp=3; IntAct=EBI-1105124, EBI-743375;
Q9H0A8:COMMD4; NbExp=4; IntAct=EBI-10769071, EBI-1550064;
A0A0S2Z3U4:EGR2; NbExp=3; IntAct=EBI-9640281, EBI-16431598;
P04764:Eno1 (xeno); NbExp=2; IntAct=EBI-10769071, EBI-915852;
P15429:Eno3 (xeno); NbExp=2; IntAct=EBI-10769071, EBI-10817548;
Q3B820:FAM161A; NbExp=3; IntAct=EBI-1105124, EBI-719941;
Q5TZK3:FAM74A6; NbExp=3; IntAct=EBI-1105124, EBI-10247271;
Q0D2H9:GOLGA8DP; NbExp=3; IntAct=EBI-1105124, EBI-10181276;
Q08AF8:GOLGA8G; NbExp=3; IntAct=EBI-1105124, EBI-10181260;
Q96CS2:HAUS1; NbExp=3; IntAct=EBI-1105124, EBI-2514791;
Q6P597:KLC3; NbExp=3; IntAct=EBI-1105124, EBI-1643885;
Q96BZ8:LENG1; NbExp=3; IntAct=EBI-1105124, EBI-726510;
P61968:LMO4; NbExp=3; IntAct=EBI-1105124, EBI-2798728;
Q15691:MAPRE1; NbExp=4; IntAct=EBI-1105124, EBI-1004115;
A9UHW6:MIF4GD; NbExp=3; IntAct=EBI-1105124, EBI-373498;
Q5JR59:MTUS2; NbExp=3; IntAct=EBI-1105124, EBI-742948;
Q14896:MYBPC3; NbExp=5; IntAct=EBI-10769071, EBI-704176;
P41227:NAA10; NbExp=3; IntAct=EBI-1105124, EBI-747693;
Q6NYC8:PPP1R18; NbExp=3; IntAct=EBI-1105124, EBI-2557469;
P09456:Prkar1a (xeno); NbExp=2; IntAct=EBI-10769071, EBI-916215;
P12368:Prkar2a (xeno); NbExp=2; IntAct=EBI-10769071, EBI-919521;
Q8WWY3:PRPF31; NbExp=6; IntAct=EBI-1105124, EBI-1567797;
Q14D33:RTP5; NbExp=3; IntAct=EBI-1105124, EBI-10217913;
Q9NUL5:RYDEN; NbExp=3; IntAct=EBI-1105124, EBI-10313866;
Q9BWG6:SCNM1; NbExp=3; IntAct=EBI-1105124, EBI-748391;
O00560:SDCBP; NbExp=3; IntAct=EBI-1105124, EBI-727004;
Q9H788:SH2D4A; NbExp=3; IntAct=EBI-1105124, EBI-747035;
Q9H788-2:SH2D4A; NbExp=3; IntAct=EBI-1105124, EBI-10308083;
P19429:TNNI3; NbExp=4; IntAct=EBI-10769071, EBI-704146;
P23693:Tnni3 (xeno); NbExp=2; IntAct=EBI-10769071, EBI-10817583;
Q08E77:UTP14C; NbExp=3; IntAct=EBI-1105124, EBI-10225961;
Q9BQ24:ZFYVE21; NbExp=3; IntAct=EBI-1105124, EBI-2849569;
Q9H9D4:ZNF408; NbExp=3; IntAct=EBI-1105124, EBI-347633;
Q9P0T4:ZNF581; NbExp=3; IntAct=EBI-1105124, EBI-745520;
Q16670:ZSCAN26; NbExp=3; IntAct=EBI-1105124, EBI-3920053;
-!- SUBCELLULAR LOCATION: Golgi apparatus
{ECO:0000269|PubMed:27666745}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000250|UniProtKB:Q9WUJ3}.
-!- SUBCELLULAR LOCATION: Isoform 13: Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000269|PubMed:29162697}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:29162697}. Golgi apparatus
{ECO:0000269|PubMed:25217626}. Note=Associated with the
microtubule network at the growing distal tip of microtubules
(PubMed:29162697). Targeting to the Golgi apparatus requires AKAP9
(PubMed:25217626). {ECO:0000269|PubMed:25217626,
ECO:0000269|PubMed:29162697}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=12;
Name=1;
IsoId=Q5VU43-1; Sequence=Displayed;
Name=2;
IsoId=Q5VU43-2; Sequence=VSP_028772, VSP_028779;
Note=Contains a phosphoserine at position 252.
{ECO:0000244|PubMed:24275569};
Name=3;
IsoId=Q5VU43-3; Sequence=VSP_028773, VSP_028781, VSP_028782;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q5VU43-4; Sequence=VSP_028783;
Name=6;
IsoId=Q5VU43-6; Sequence=VSP_028779;
Name=7;
IsoId=Q5VU43-7; Sequence=VSP_028778, VSP_028780;
Name=8;
IsoId=Q5VU43-8; Sequence=VSP_028774, VSP_028775;
Name=9;
IsoId=Q5VU43-9; Sequence=VSP_028774, VSP_028776, VSP_028777;
Name=10;
IsoId=Q5VU43-10; Sequence=VSP_028776, VSP_028777;
Name=11;
IsoId=Q5VU43-11; Sequence=VSP_028775;
Name=12;
IsoId=Q5VU43-12; Sequence=VSP_028773, VSP_028776, VSP_028777;
Name=13; Synonyms=Myomegalin variant 8
{ECO:0000303|PubMed:25217626}, MMG {ECO:0000303|PubMed:27666745,
ECO:0000303|PubMed:28814570}, MMG8 {ECO:0000303|PubMed:25217626},
Short myomegalin-like EB1 binding protein
{ECO:0000303|PubMed:29162697}, SMYLE
{ECO:0000303|PubMed:29162697};
IsoId=Q5VU43-13; Sequence=VSP_028772, VSP_059333, VSP_059334;
Note=Mutagenesis at position 311-312:LP->AA (loss of MAPRE1- and
MAPRE3-binding and loss of association with microtubule ends, no
effect on AKAP9- and CDK5RAP2-binding, relocalizes from
EB1/MAPRE1 microtubule ends to centrosomal area). Contains a
phosphoserine at position 252. {ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:25217626, ECO:0000269|PubMed:28814570,
ECO:0000269|PubMed:29162697};
-!- TISSUE SPECIFICITY: Highly expressed in adult and fetal heart, in
skeletal muscle and, to a lower extent, in brain and placenta.
{ECO:0000269|PubMed:11374908}.
-!- DOMAIN: Isoform 13: residues 1-150 are involved in AKAP9-binding.
{ECO:0000269|PubMed:29162697}.
-!- DISEASE: Note=A chromosomal aberration involving PDE4DIP may be
the cause of a myeloproliferative disorder (MBD) associated with
eosinophilia. Translocation t(1;5)(q23;q33) that forms a PDE4DIP-
PDGFRB fusion protein. {ECO:0000269|PubMed:12907457}.
-!- CAUTION: Was initially reported to localize in the cytoplasm and
nucleus (PubMed:11374908). However, many reports in different
species have shown that it is associated with the Golgi apparatus
and the centrosome. {ECO:0000269|PubMed:11374908,
ECO:0000269|PubMed:27666745}.
-!- SEQUENCE CAUTION:
Sequence=AAH04860.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAA32299.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAA32322.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAD91152.1; Type=Frameshift; Positions=1507; Evidence={ECO:0000305};
Sequence=CAH18128.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PDE4DIP01q22ID180.html";
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EMBL; AB042555; BAB17759.1; -; mRNA.
EMBL; AB042556; BAB17760.1; -; mRNA.
EMBL; AB042557; BAB17761.1; -; mRNA.
EMBL; AB042558; BAB17762.1; -; mRNA.
EMBL; AB007923; BAA32299.2; ALT_INIT; mRNA.
EMBL; AB007946; BAA32322.2; ALT_INIT; mRNA.
EMBL; HQ333476; ADO32613.1; -; mRNA.
EMBL; AL831815; CAD38529.1; -; mRNA.
EMBL; AL832024; CAD89923.1; -; mRNA.
EMBL; AL833273; CAD91152.1; ALT_FRAME; mRNA.
EMBL; CR749273; CAH18128.1; ALT_SEQ; mRNA.
EMBL; AL590452; CAH72521.1; -; Genomic_DNA.
EMBL; AL138791; CAH72521.1; JOINED; Genomic_DNA.
EMBL; AL590452; CAH72522.1; -; Genomic_DNA.
EMBL; AL138796; CAH72522.1; JOINED; Genomic_DNA.
EMBL; AL590452; CAH72523.1; -; Genomic_DNA.
EMBL; AL138796; CAH72523.1; JOINED; Genomic_DNA.
EMBL; AL590452; CAH72524.1; -; Genomic_DNA.
EMBL; AL138796; CAH72524.1; JOINED; Genomic_DNA.
EMBL; AL590452; CAH72525.1; -; Genomic_DNA.
EMBL; AL590452; CAH72526.1; -; Genomic_DNA.
EMBL; AL138796; CAH72526.1; JOINED; Genomic_DNA.
EMBL; AL590452; CAH72527.1; -; Genomic_DNA.
EMBL; AL138796; CAH72527.1; JOINED; Genomic_DNA.
EMBL; AL590452; CAH72528.1; -; Genomic_DNA.
EMBL; AL138796; CAH72528.1; JOINED; Genomic_DNA.
EMBL; AL138791; CAI22527.1; -; Genomic_DNA.
EMBL; AL590452; CAI22527.1; JOINED; Genomic_DNA.
EMBL; AL138796; CAI22822.1; -; Genomic_DNA.
EMBL; AL590452; CAI22822.1; JOINED; Genomic_DNA.
EMBL; AL138796; CAI22823.1; -; Genomic_DNA.
EMBL; AL590452; CAI22823.1; JOINED; Genomic_DNA.
EMBL; AL138796; CAI22824.1; -; Genomic_DNA.
EMBL; AL590452; CAI22824.1; JOINED; Genomic_DNA.
EMBL; AL138796; CAI22825.1; -; Genomic_DNA.
EMBL; AL590452; CAI22825.1; JOINED; Genomic_DNA.
EMBL; AL138796; CAI22826.1; -; Genomic_DNA.
EMBL; AL590452; CAI22826.1; JOINED; Genomic_DNA.
EMBL; AL138796; CAI22827.1; -; Genomic_DNA.
EMBL; AL590452; CAI22827.1; JOINED; Genomic_DNA.
EMBL; AC239802; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC245389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC239804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC004860; AAH04860.1; ALT_SEQ; mRNA.
EMBL; BC025406; AAH25406.1; -; mRNA.
EMBL; BC078660; AAH78660.1; -; mRNA.
EMBL; BC110294; AAI10295.1; -; mRNA.
EMBL; BC132717; AAI32718.1; -; mRNA.
EMBL; BC152439; AAI52440.1; -; mRNA.
EMBL; DA900724; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS72887.1; -. [Q5VU43-8]
CCDS; CCDS72888.1; -. [Q5VU43-3]
CCDS; CCDS72890.1; -. [Q5VU43-6]
CCDS; CCDS72891.1; -. [Q5VU43-1]
CCDS; CCDS72892.1; -. [Q5VU43-4]
CCDS; CCDS72893.1; -. [Q5VU43-11]
CCDS; CCDS72894.1; -. [Q5VU43-2]
PIR; T00069; T00069.
PIR; T00259; T00259.
RefSeq; NP_001002810.1; NM_001002810.3. [Q5VU43-11]
RefSeq; NP_001002811.2; NM_001002811.2. [Q5VU43-2]
RefSeq; NP_001002812.2; NM_001002812.2. [Q5VU43-6]
RefSeq; NP_001182189.1; NM_001195260.1.
RefSeq; NP_001182190.1; NM_001195261.1.
RefSeq; NP_001185761.2; NM_001198832.2. [Q5VU43-3]
RefSeq; NP_001185763.3; NM_001198834.3. [Q5VU43-4]
RefSeq; NP_055459.5; NM_014644.5. [Q5VU43-1]
RefSeq; NP_071754.3; NM_022359.5. [Q5VU43-8]
RefSeq; XP_016855361.1; XM_016999872.1.
RefSeq; XP_016855362.1; XM_016999873.1.
RefSeq; XP_016858514.1; XM_017003025.1.
RefSeq; XP_016858515.1; XM_017003026.1.
UniGene; Hs.584841; -.
UniGene; Hs.632434; -.
UniGene; Hs.657490; -.
UniGene; Hs.682380; -.
UniGene; Hs.721759; -.
UniGene; Hs.731111; -.
ProteinModelPortal; Q5VU43; -.
SMR; Q5VU43; -.
BioGrid; 115017; 143.
DIP; DIP-51263N; -.
IntAct; Q5VU43; 113.
MINT; Q5VU43; -.
STRING; 9606.ENSP00000358363; -.
iPTMnet; Q5VU43; -.
PhosphoSitePlus; Q5VU43; -.
BioMuta; PDE4DIP; -.
DMDM; 74747041; -.
EPD; Q5VU43; -.
PaxDb; Q5VU43; -.
PeptideAtlas; Q5VU43; -.
PRIDE; Q5VU43; -.
ProteomicsDB; 65374; -.
ProteomicsDB; 65375; -. [Q5VU43-10]
ProteomicsDB; 65376; -. [Q5VU43-11]
ProteomicsDB; 65377; -. [Q5VU43-12]
ProteomicsDB; 65378; -. [Q5VU43-2]
ProteomicsDB; 65379; -. [Q5VU43-3]
ProteomicsDB; 65380; -. [Q5VU43-4]
ProteomicsDB; 65381; -. [Q5VU43-6]
ProteomicsDB; 65382; -. [Q5VU43-7]
ProteomicsDB; 65383; -. [Q5VU43-8]
ProteomicsDB; 65384; -. [Q5VU43-9]
DNASU; 9659; -.
Ensembl; ENST00000313431; ENSP00000316434; ENSG00000178104. [Q5VU43-2]
Ensembl; ENST00000369347; ENSP00000358353; ENSG00000178104. [Q5VU43-11]
Ensembl; ENST00000369349; ENSP00000358355; ENSG00000178104. [Q5VU43-6]
Ensembl; ENST00000369351; ENSP00000358357; ENSG00000178104. [Q5VU43-7]
Ensembl; ENST00000369354; ENSP00000358360; ENSG00000178104. [Q5VU43-1]
Ensembl; ENST00000369356; ENSP00000358363; ENSG00000178104. [Q5VU43-4]
Ensembl; ENST00000529945; ENSP00000433392; ENSG00000178104. [Q5VU43-13]
Ensembl; ENST00000530472; ENSP00000482121; ENSG00000178104. [Q5VU43-8]
Ensembl; ENST00000618462; ENSP00000479409; ENSG00000178104. [Q5VU43-3]
GeneID; 653513; -.
GeneID; 9659; -.
KEGG; hsa:653513; -.
KEGG; hsa:9659; -.
UCSC; uc001emb.3; human. [Q5VU43-1]
UCSC; uc057kja.1; human.
CTD; 9659; -.
DisGeNET; 653513; -.
DisGeNET; 9659; -.
EuPathDB; HostDB:ENSG00000178104.19; -.
GeneCards; PDE4DIP; -.
H-InvDB; HIX0178151; -.
HGNC; HGNC:15580; PDE4DIP.
HPA; HPA008162; -.
HPA; HPA012678; -.
MIM; 608117; gene.
neXtProt; NX_Q5VU43; -.
OpenTargets; ENSG00000178104; -.
PharmGKB; PA33131; -.
eggNOG; ENOG410J2NR; Eukaryota.
eggNOG; ENOG411281S; LUCA.
GeneTree; ENSGT00530000063845; -.
HOVERGEN; HBG108166; -.
InParanoid; Q5VU43; -.
KO; K16549; -.
OMA; YECWSER; -.
PhylomeDB; Q5VU43; -.
TreeFam; TF329233; -.
SIGNOR; Q5VU43; -.
ChiTaRS; PDE4DIP; human.
GeneWiki; Myomegalin; -.
GenomeRNAi; 9659; -.
PRO; PR:Q5VU43; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000178104; Expressed in 227 organ(s), highest expression level in gastrocnemius.
ExpressionAtlas; Q5VU43; baseline and differential.
Genevisible; Q5VU43; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0030016; C:myofibril; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; ISS:UniProtKB.
GO; GO:0032947; F:protein-containing complex scaffold activity; IDA:UniProtKB.
GO; GO:0030953; P:astral microtubule organization; IMP:UniProtKB.
GO; GO:0034622; P:cellular protein-containing complex assembly; ISS:UniProtKB.
GO; GO:0090063; P:positive regulation of microtubule nucleation; IMP:UniProtKB.
GO; GO:1903358; P:regulation of Golgi organization; IDA:UniProtKB.
InterPro; IPR012943; Cnn_1N.
InterPro; IPR010630; NBPF_dom.
Pfam; PF07989; Cnn_1N; 1.
Pfam; PF06758; DUF1220; 1.
SMART; SM01148; DUF1220; 1.
PROSITE; PS51316; NBPF; 1.
1: Evidence at protein level;
Alternative splicing; Chromosomal rearrangement; Coiled coil;
Complete proteome; Cytoplasm; Cytoskeleton; Golgi apparatus;
Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 2346 Myomegalin.
/FTId=PRO_0000307690.
DOMAIN 1551 1642 NBPF. {ECO:0000255|PROSITE-
ProRule:PRU00647}.
COILED 41 132 {ECO:0000255}.
COILED 162 205 {ECO:0000255}.
COILED 238 318 {ECO:0000255}.
COILED 350 684 {ECO:0000255}.
COILED 743 936 {ECO:0000255}.
COILED 1002 1043 {ECO:0000255}.
COILED 1096 1124 {ECO:0000255}.
COILED 1212 1240 {ECO:0000255}.
COILED 1346 1385 {ECO:0000255}.
COILED 1431 1455 {ECO:0000255}.
COILED 1736 1760 {ECO:0000255}.
COILED 1840 2077 {ECO:0000255}.
COILED 2273 2312 {ECO:0000255}.
SITE 742 743 Breakpoint for insertion to form PDE4DIP-
PDGFRB fusion protein.
MOD_RES 704 704 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
VAR_SEQ 1 210 MSNGYRTLSQHLNDLKKENFSLKLRIYFLEERMQQKYEASR
EDIYKRNIELKVEVESLKRELQDKKQHLDKTWADVENLNSQ
NEAELRRQFEERQQETEHVYELLENKIQLLQEESRLAKNEA
ARMAALVEAEKECNLELSEKLKGVTKNWEDVPGDQVKPDQY
TEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEE
PTSME -> MKEICRICARELCGNQRRWIFHTASKLNLQVL
LSHVLGKDVPRDGKAEFACSKCAFMLDRIYRFDTVIARIEA
LSIERLQKLLLEKDRLKFCIASMYRKNNDDSGAEIKAGNGT
VDMSVLPDARYSALLQEDFAYSGFECWVENEDQIQEPHSCH
GSEGPGNRPRRCRGCAALRVADSDYEAICKVPRKVARSISC
GPSSRWSTSICTEEPALSEVGPPDLASTKVPPDGESMEEET
PGSSVESLDASVQASPPQQKDEETERSAKELGKCDCCSDDQ
APQHGCNHKLELALSMIKGLDYKPIQSPRGSRLPIPVKSSL
PGAKPGPSMTDGVSSGFLNRSLKPLYKTPVSYPLELSDLQE
LWDDLCEDYLPLR (in isoform 2 and isoform
13). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9455484}.
/FTId=VSP_028772.
VAR_SEQ 1 10 MSNGYRTLSQ -> MEQTWTRDYFAEDDGEMVPRTSHTAAF
LSDTKDRGPPVQSQIWRSGEKVPFVQTYSLRAFEKPPQVQT
QALRDFEK (in isoform 3 and isoform 12).
{ECO:0000303|PubMed:11374908,
ECO:0000303|PubMed:9455484}.
/FTId=VSP_028773.
VAR_SEQ 1 10 MSNGYRTLSQ -> MKGTDSGSCCRRRCDFGCCCRASRRAH
YTPYRSGDATRTPQSPRQTPSRERRRPEPAGSWAAAAEEEE
AAAAATPWMRDYFAEDDGEMVPRTSHTAAFLSDTKDRGPPV
QSQIWRSGEKVPFVQTYSLRAFEKPPQVQTQALRDFEK
(in isoform 8 and isoform 9).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_028774.
VAR_SEQ 174 2346 Missing (in isoform 8 and isoform 11).
{ECO:0000303|PubMed:11374908,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_028775.
VAR_SEQ 174 174 R -> I (in isoform 9, isoform 10 and
isoform 12).
{ECO:0000303|PubMed:11374908,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_028776.
VAR_SEQ 175 2346 Missing (in isoform 9, isoform 10 and
isoform 12).
{ECO:0000303|PubMed:11374908,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_028777.
VAR_SEQ 940 953 AAAGDDTEDTSTEF -> GELESVRIHHKHAY (in
isoform 13).
/FTId=VSP_059333.
VAR_SEQ 954 2346 Missing (in isoform 13).
/FTId=VSP_059334.
VAR_SEQ 968 988 QLVKVALEKSLATVETQNPSF -> QVSQCQGLGLPGWTAH
SPSEV (in isoform 7).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_028778.
VAR_SEQ 970 2346 Missing (in isoform 2 and isoform 6).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005,
ECO:0000303|PubMed:9455484}.
/FTId=VSP_028779.
VAR_SEQ 989 2346 Missing (in isoform 7).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_028780.
VAR_SEQ 1082 1191 Missing (in isoform 3).
{ECO:0000303|PubMed:9455484}.
/FTId=VSP_028781.
VAR_SEQ 1695 1756 Missing (in isoform 3).
{ECO:0000303|PubMed:9455484}.
/FTId=VSP_028782.
VAR_SEQ 2334 2346 VKSLRALPCTPAL -> EPCKKRSHQKSLKQQERWACPPFV
QLPIC (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_028783.
VARIANT 13 13 N -> S (in dbSNP:rs3010980).
/FTId=VAR_036627.
VARIANT 25 25 R -> L (in dbSNP:rs1664022).
/FTId=VAR_036628.
VARIANT 49 49 I -> T (in dbSNP:rs573724).
{ECO:0000269|PubMed:11374908,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_036629.
VARIANT 143 143 K -> E (in dbSNP:rs1747958).
/FTId=VAR_056951.
VARIANT 150 150 N -> S (in dbSNP:rs3010980).
/FTId=VAR_056952.
VARIANT 167 167 A -> T (in dbSNP:rs2590120).
/FTId=VAR_036630.
VARIANT 171 171 R -> K (in dbSNP:rs3121544).
/FTId=VAR_051204.
VARIANT 391 391 E -> A (in dbSNP:rs1324366).
/FTId=VAR_051205.
VARIANT 410 410 E -> V (in dbSNP:rs1061308).
/FTId=VAR_051206.
VARIANT 482 482 H -> R (in dbSNP:rs1698681).
/FTId=VAR_051207.
VARIANT 681 681 R -> H (in dbSNP:rs1629011).
/FTId=VAR_051208.
VARIANT 708 708 R -> C (in dbSNP:rs1628172).
{ECO:0000269|PubMed:16710414,
ECO:0000269|PubMed:17974005}.
/FTId=VAR_051209.
VARIANT 1013 1013 F -> I (in dbSNP:rs1698624).
{ECO:0000269|PubMed:17974005}.
/FTId=VAR_051210.
VARIANT 1066 1066 A -> T (in dbSNP:rs1698647).
{ECO:0000269|PubMed:17974005}.
/FTId=VAR_051211.
VARIANT 1359 1359 K -> E (in dbSNP:rs1747958).
{ECO:0000269|PubMed:17974005}.
/FTId=VAR_051212.
VARIANT 1396 1396 R -> W (in dbSNP:rs2798901).
/FTId=VAR_080232.
VARIANT 1736 1736 V -> E (in dbSNP:rs1778159).
{ECO:0000269|PubMed:17974005}.
/FTId=VAR_051213.
VARIANT 1742 1742 A -> S (in dbSNP:rs1698605).
{ECO:0000269|PubMed:17974005}.
/FTId=VAR_051214.
CONFLICT 33 33 M -> T (in Ref. 5; CAD89923).
{ECO:0000305}.
CONFLICT 98 98 T -> M (in Ref. 1; BAB17761/BAB17762).
{ECO:0000305}.
CONFLICT 109 109 I -> M (in Ref. 1; BAB17759/BAB17760/
BAB17761/BAB17762 and 7; AAH25406/
AAI10295). {ECO:0000305}.
CONFLICT 401 401 R -> Q (in Ref. 5; CAD91152).
{ECO:0000305}.
CONFLICT 643 643 M -> V (in Ref. 5; CAD91152).
{ECO:0000305}.
CONFLICT 776 776 L -> P (in Ref. 5; CAD91152).
{ECO:0000305}.
CONFLICT 783 783 M -> I (in Ref. 5; CAD38529 and 7;
AAI32718). {ECO:0000305}.
CONFLICT 830 830 L -> P (in Ref. 5; CAD91152).
{ECO:0000305}.
CONFLICT 863 863 L -> P (in Ref. 5; CAD38529).
{ECO:0000305}.
CONFLICT 1266 1266 K -> E (in Ref. 5; CAH18128).
{ECO:0000305}.
CONFLICT 1286 1286 E -> G (in Ref. 5; CAD91152).
{ECO:0000305}.
CONFLICT 1356 1356 K -> R (in Ref. 5; CAD91152).
{ECO:0000305}.
CONFLICT 1397 1397 K -> E (in Ref. 5; CAD91152).
{ECO:0000305}.
CONFLICT 1454 1454 K -> E (in Ref. 5; CAH18128).
{ECO:0000305}.
CONFLICT 1504 1504 R -> Q (in Ref. 5; CAH18128).
{ECO:0000305}.
CONFLICT 1598 1598 H -> R (in Ref. 5; CAH18128).
{ECO:0000305}.
CONFLICT 1610 1610 T -> P (in Ref. 5; CAH18128).
{ECO:0000305}.
CONFLICT 1727 1727 L -> P (in Ref. 5; CAH18128).
{ECO:0000305}.
CONFLICT 1757 1757 A -> T (in Ref. 5; CAH18128).
{ECO:0000305}.
CONFLICT 1867 1867 R -> C (in Ref. 5; CAH18128).
{ECO:0000305}.
CONFLICT 1910 1910 D -> E (in Ref. 5; CAH18128).
{ECO:0000305}.
CONFLICT 2001 2001 E -> G (in Ref. 5; CAH18128).
{ECO:0000305}.
CONFLICT 2088 2088 Missing (in Ref. 5; CAH18128).
{ECO:0000305}.
CONFLICT 2291 2291 R -> Q (in Ref. 5; CAH18128).
{ECO:0000305}.
CONFLICT 2317 2317 Q -> R (in Ref. 5; CAH18128).
{ECO:0000305}.
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


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