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Dynamin-2 (EC 3.6.5.5) (Dynamin UDNM)

 DYN2_MOUSE              Reviewed;         870 AA.
P39054; Q9DBE1;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
26-JUL-2002, sequence version 2.
27-SEP-2017, entry version 166.
RecName: Full=Dynamin-2;
EC=3.6.5.5;
AltName: Full=Dynamin UDNM;
Name=Dnm2; Synonyms=Dyn2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=NIH Swiss;
PubMed=9143510; DOI=10.1006/geno.1997.4634;
Klocke R., Augustin A., Ronsiek M., Stief A., van der Putten H.,
Jockusch H.;
"Dynamin genes Dnm1 and Dnm2 are located on proximal mouse chromosomes
2 and 9, respectively.";
Genomics 41:290-292(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Liver;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
PROTEIN SEQUENCE OF 45-54; 91-107; 114-142; 207-217; 230-237; 300-309;
370-376 AND 678-688, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[4]
INTERACTION WITH SH3BP4.
PubMed=16325581; DOI=10.1016/j.cell.2005.10.021;
Tosoni D., Puri C., Confalonieri S., Salcini A.E., De Camilli P.,
Tacchetti C., Di Fiore P.P.;
"TTP specifically regulates the internalization of the transferrin
receptor.";
Cell 123:875-888(2005).
[5]
INTERACTION WITH MYOF.
PubMed=17702744; DOI=10.1074/jbc.M704798200;
Bernatchez P.N., Acevedo L., Fernandez-Hernando C., Murata T.,
Chalouni C., Kim J., Erdjument-Bromage H., Shah V., Gratton J.-P.,
McNally E.M., Tempst P., Sessa W.C.;
"Myoferlin regulates vascular endothelial growth factor receptor-2
stability and function.";
J. Biol. Chem. 282:30745-30753(2007).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18923138; DOI=10.1091/mbc.E08-08-0890;
Liu Y.W., Surka M.C., Schroeter T., Lukiyanchuk V., Schmid S.L.;
"Isoform and splice-variant specific functions of dynamin-2 revealed
by analysis of conditional knock-out cells.";
Mol. Biol. Cell 19:5347-5359(2008).
[7]
FUNCTION, INTERACTION WITH PIK3C3, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF LYS-44.
PubMed=18425118; DOI=10.1038/ncb1718;
Kinchen J.M., Doukoumetzidis K., Almendinger J., Stergiou L.,
Tosello-Trampont A., Sifri C.D., Hengartner M.O., Ravichandran K.S.;
"A pathway for phagosome maturation during engulfment of apoptotic
cells.";
Nat. Cell Biol. 10:556-566(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
TISSUE SPECIFICITY.
PubMed=23092955; DOI=10.1038/ejhg.2012.226;
Koutsopoulos O.S., Kretz C., Weller C.M., Roux A., Mojzisova H.,
Boehm J., Koch C., Toussaint A., Heckel E., Stemkens D.,
Ter Horst S.A., Thibault C., Koch M., Mehdi S.Q., Bijlsma E.K.,
Mandel J.L., Vermot J., Laporte J.;
"Dynamin 2 homozygous mutation in humans with a lethal congenital
syndrome.";
Eur. J. Hum. Genet. 21:637-642(2013).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-299, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Microtubule-associated force-producing protein involved
in producing microtubule bundles and able to bind and hydrolyze
GTP. Plays a role in the regulation of neuron morphology, axon
growth and formation of neuronal growth cones (By similarity).
Plays an important role in vesicular trafficking processes, in
particular endocytosis. Involved in cytokinesis (PubMed:18923138).
Regulates maturation of apoptotic cell corpse-containing
phagosomes by recruiting PIK3C3 to the phagosome membrane
(PubMed:18425118). {ECO:0000250|UniProtKB:P39052,
ECO:0000269|PubMed:18425118, ECO:0000269|PubMed:18923138}.
-!- CATALYTIC ACTIVITY: GTP + H(2)O = GDP + phosphate.
-!- SUBUNIT: Interacts with SHANK1, SHANK2 and NOSTRIN. Interacts with
SNX9. Interacts with SNX33 (via SH3 domain). Interacts with MYO1E
(via SH3 domain). Interacts with CTTN and ACTN1 (By similarity).
Interacts with MYOF and SH3BP4 (PubMed:17702744, PubMed:16325581).
Interacts with PSTPIP1. Interacts with CTNND2 (By similarity). May
interact with PIK3C3 (PubMed:18425118). May be a component of a
complex composed of RAB5A (in GDP-bound form), DYN2 and PIK3C3
(PubMed:18425118). {ECO:0000250|UniProtKB:P39052,
ECO:0000250|UniProtKB:P50570, ECO:0000269|PubMed:16325581,
ECO:0000269|PubMed:17702744, ECO:0000305|PubMed:18425118}.
-!- INTERACTION:
Q7TQF7:Amph; NbExp=5; IntAct=EBI-642337, EBI-775139;
Q60598:Cttn; NbExp=2; IntAct=EBI-642337, EBI-397955;
Q01406:CTTN1 (xeno); NbExp=2; IntAct=EBI-642337, EBI-2530463;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P50570}.
Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P50570}. Cell
junction {ECO:0000250|UniProtKB:P39052}. Membrane, clathrin-coated
pit {ECO:0000250|UniProtKB:P39052}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density
{ECO:0000250|UniProtKB:P50570}. Cell junction, synapse
{ECO:0000250|UniProtKB:P50570}. Midbody
{ECO:0000250|UniProtKB:P50570}. Cell projection, phagocytic cup
{ECO:0000269|PubMed:18425118}. Cytoplasmic vesicle, phagosome
membrane {ECO:0000269|PubMed:18425118}; Peripheral membrane
protein {ECO:0000269|PubMed:18425118}. Note=Colocalizes with CTTN
at the basis of filopodia in hippocampus neuron growth zones.
Microtubule-associated. Also found in the postsynaptic density of
neuronal cells (By similarity). Co-localizes with PIK3C3 and RAB5A
to the nascent phagosome (PubMed:18425118).
{ECO:0000250|UniProtKB:P39052, ECO:0000250|UniProtKB:P50570,
ECO:0000269|PubMed:18425118}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P39054-1; Sequence=Displayed;
Name=2;
IsoId=P39054-2; Sequence=VSP_001326;
-!- TISSUE SPECIFICITY: Expressed in most tissues during embryonic
development, including the peripheral nervous system although no
expression is evident in skeletal muscle or heart.
{ECO:0000269|PubMed:23092955}.
-!- PTM: Phosphorylation at Ser-764 by CDK1 is greatly increased upon
mitotic entry. It regulates cytokinesis downstream of calcineurin,
and does not affect clathrin-mediated endocytosis.
Dephosphorylated by calcineurin/PP2 (By similarity).
Phosphorylated on tyrosine residues after activation of SRC (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:P39052}.
-!- DISRUPTION PHENOTYPE: Exhibits growth and cytokinesis defects.
{ECO:0000269|PubMed:18923138}.
-!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
superfamily. Dynamin/Fzo/YdjA family. {ECO:0000305}.
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EMBL; L31398; AAA40523.1; -; mRNA.
EMBL; AK005012; BAB23745.1; -; mRNA.
CCDS; CCDS57657.1; -. [P39054-1]
CCDS; CCDS57659.1; -. [P39054-2]
RefSeq; NP_001240822.1; NM_001253893.1. [P39054-1]
RefSeq; NP_001240823.1; NM_001253894.1.
RefSeq; NP_031897.2; NM_007871.2. [P39054-2]
UniGene; Mm.433257; -.
ProteinModelPortal; P39054; -.
SMR; P39054; -.
BioGrid; 199258; 8.
IntAct; P39054; 19.
MINT; MINT-1605893; -.
STRING; 10090.ENSMUSP00000133564; -.
iPTMnet; P39054; -.
PhosphoSitePlus; P39054; -.
REPRODUCTION-2DPAGE; IPI00131445; -.
MaxQB; P39054; -.
PaxDb; P39054; -.
PeptideAtlas; P39054; -.
PRIDE; P39054; -.
Ensembl; ENSMUST00000091087; ENSMUSP00000088616; ENSMUSG00000033335. [P39054-2]
Ensembl; ENSMUST00000172482; ENSMUSP00000133564; ENSMUSG00000033335. [P39054-1]
GeneID; 13430; -.
KEGG; mmu:13430; -.
UCSC; uc009olk.2; mouse. [P39054-2]
UCSC; uc029wxt.1; mouse. [P39054-1]
CTD; 1785; -.
MGI; MGI:109547; Dnm2.
eggNOG; KOG0446; Eukaryota.
eggNOG; COG0699; LUCA.
GeneTree; ENSGT00760000119213; -.
HOGENOM; HOG000161069; -.
HOVERGEN; HBG107833; -.
InParanoid; P39054; -.
KO; K01528; -.
PhylomeDB; P39054; -.
TreeFam; TF300362; -.
BRENDA; 3.6.5.5; 3474.
Reactome; R-MMU-166016; Toll Like Receptor 4 (TLR4) Cascade.
Reactome; R-MMU-190873; Gap junction degradation.
Reactome; R-MMU-196025; Formation of annular gap junctions.
Reactome; R-MMU-203641; NOSTRIN mediated eNOS trafficking.
Reactome; R-MMU-2132295; MHC class II antigen presentation.
Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
Reactome; R-MMU-437239; Recycling pathway of L1.
Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
ChiTaRS; Dnm2; mouse.
PRO; PR:P39054; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000033335; -.
CleanEx; MM_DNM2; -.
ExpressionAtlas; P39054; baseline and differential.
Genevisible; P39054; MM.
GO; GO:0030054; C:cell junction; ISS:UniProtKB.
GO; GO:0005813; C:centrosome; IEA:Ensembl.
GO; GO:0045334; C:clathrin-coated endocytic vesicle; IEA:Ensembl.
GO; GO:0005905; C:clathrin-coated pit; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005768; C:endosome; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
GO; GO:0030426; C:growth cone; IEA:Ensembl.
GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
GO; GO:0005874; C:microtubule; ISO:MGI.
GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0001917; C:photoreceptor inner segment; IDA:MGI.
GO; GO:0014069; C:postsynaptic density of dendrite; IEA:UniProtKB-SubCell.
GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
GO; GO:0031749; F:D2 dopamine receptor binding; IEA:Ensembl.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
GO; GO:0050998; F:nitric-oxide synthase binding; IEA:Ensembl.
GO; GO:0036312; F:phosphatidylinositol 3-kinase regulatory subunit binding; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
GO; GO:0050699; F:WW domain binding; IEA:Ensembl.
GO; GO:0035904; P:aorta development; IMP:MGI.
GO; GO:0071245; P:cellular response to carbon monoxide; IEA:Ensembl.
GO; GO:1903351; P:cellular response to dopamine; IEA:Ensembl.
GO; GO:0071732; P:cellular response to nitric oxide; IEA:Ensembl.
GO; GO:0071481; P:cellular response to X-ray; IEA:Ensembl.
GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
GO; GO:0003374; P:dynamin family protein polymerization involved in mitochondrial fission; IBA:GO_Central.
GO; GO:0002031; P:G-protein coupled receptor internalization; IEA:Ensembl.
GO; GO:0006893; P:Golgi to plasma membrane transport; IEA:Ensembl.
GO; GO:0044351; P:macropinocytosis; IEA:Ensembl.
GO; GO:0061025; P:membrane fusion; IBA:GO_Central.
GO; GO:0000266; P:mitochondrial fission; IBA:GO_Central.
GO; GO:1903526; P:negative regulation of membrane tubulation; ISO:MGI.
GO; GO:1902856; P:negative regulation of non-motile cilium assembly; IEA:Ensembl.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
GO; GO:0010592; P:positive regulation of lamellipodium assembly; IEA:Ensembl.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
GO; GO:0050766; P:positive regulation of phagocytosis; IEA:Ensembl.
GO; GO:1903408; P:positive regulation of sodium:potassium-exchanging ATPase activity; IEA:Ensembl.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
GO; GO:0031623; P:receptor internalization; ISO:MGI.
GO; GO:0006898; P:receptor-mediated endocytosis; ISS:UniProtKB.
GO; GO:0030516; P:regulation of axon extension; ISS:UniProtKB.
GO; GO:1903358; P:regulation of Golgi organization; IEA:Ensembl.
GO; GO:0035020; P:regulation of Rac protein signal transduction; IEA:Ensembl.
GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
GO; GO:0009416; P:response to light stimulus; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0033572; P:transferrin transport; ISO:MGI.
GO; GO:0003281; P:ventricular septum development; IMP:MGI.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR027188; DNM2.
InterPro; IPR000375; Dynamin_central.
InterPro; IPR001401; Dynamin_GTPase.
InterPro; IPR019762; Dynamin_GTPase_CS.
InterPro; IPR022812; Dynamin_SF.
InterPro; IPR030381; G_DYNAMIN_dom.
InterPro; IPR003130; GED.
InterPro; IPR020850; GED_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR011993; PH_dom-like.
InterPro; IPR001849; PH_domain.
PANTHER; PTHR11566; PTHR11566; 1.
PANTHER; PTHR11566:SF94; PTHR11566:SF94; 1.
Pfam; PF01031; Dynamin_M; 1.
Pfam; PF00350; Dynamin_N; 1.
Pfam; PF02212; GED; 1.
Pfam; PF00169; PH; 1.
PRINTS; PR00195; DYNAMIN.
SMART; SM00053; DYNc; 1.
SMART; SM00302; GED; 1.
SMART; SM00233; PH; 1.
SUPFAM; SSF50729; SSF50729; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00410; G_DYNAMIN_1; 1.
PROSITE; PS51718; G_DYNAMIN_2; 1.
PROSITE; PS51388; GED; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell junction; Cell membrane;
Cell projection; Coated pit; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Cytoskeleton; Direct protein sequencing;
Endocytosis; GTP-binding; Hydrolase; Membrane; Microtubule;
Motor protein; Nucleotide-binding; Phagocytosis; Phosphoprotein;
Postsynaptic cell membrane; Reference proteome; Synapse.
CHAIN 1 870 Dynamin-2.
/FTId=PRO_0000206571.
DOMAIN 28 294 Dynamin-type G.
DOMAIN 519 625 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 653 744 GED. {ECO:0000255|PROSITE-
ProRule:PRU00720}.
NP_BIND 38 46 GTP. {ECO:0000250|UniProtKB:O00429}.
NP_BIND 205 211 GTP. {ECO:0000250|UniProtKB:O00429}.
NP_BIND 236 239 GTP. {ECO:0000250|UniProtKB:O00429}.
COMPBIAS 747 866 Pro-rich.
MOD_RES 299 299 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 598 598 N6-acetyllysine.
{ECO:0000250|UniProtKB:P50570}.
MOD_RES 755 755 Phosphothreonine.
{ECO:0000250|UniProtKB:P50570}.
MOD_RES 764 764 Phosphoserine; by CDK1.
{ECO:0000250|UniProtKB:P39052}.
VAR_SEQ 516 519 Missing (in isoform 2).
{ECO:0000303|PubMed:9143510}.
/FTId=VSP_001326.
MUTAGEN 44 44 K->A: Apoptotic cell corpse-containing
phagosomes fail to mature into acidic
phagosomes. Loss of PIK3C3 and RAB5A
recruitment to phagosomes.
{ECO:0000269|PubMed:18425118}.
CONFLICT 297 298 RS -> HG (in Ref. 1; AAA40523).
{ECO:0000305}.
CONFLICT 848 870 SRRAPAAPSRPTIIRPAEPSLLD -> RRPPPLAPARPFF
(in Ref. 2; BAB23745). {ECO:0000305}.
SEQUENCE 870 AA; 98145 MW; E80864AF94B8F778 CRC64;
MGNRGMEELI PLVNKLQDAF SSIGQSCHLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG
SGIVTRRPLI LQLIFSKTEY AEFLHCKSKK FTDFDEVRQE IEAETDRVTG TNKGISPVPI
NLRVYSPHVL NLTLIDLPGI TKVPVGDQPP DIEYQIKDMI LQFISRESSL ILAVTPANMD
LANSDALKLA KEVDPQGLRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK
DIEGKKDIRA ALAAERKFFL SHPAYRHMAD RMGTPHLQKT LNQQLTNHIR ESLPTLRSKL
QSQLLSLEKE VEEYKNFRPD DPTRKTKALL QMVQQFGVDF EKRIEGSGDQ VDTLELSGGA
RINRIFHERF PFELVKMEFD EKDLRREISY AIKNIHGVRT GLFTPDLAFE AIVKKQVVKL
KEPCLKCVDL VIQELISTVR QCTSKLSSYP RLREETERIV TTYIREREGR TKDQILLLID
IEQSYINTNH EDFIGFANAQ QRSTQLNKKR AIPNQGEILV IRRGWLTINN ISLMKGGSKE
YWFVLTAESL SWYKDEEEKE KKYMLPLDNL KIRDVEKGFM SNKHVFAIFN TEQRNVYKDL
RQIELACDSQ EDVDSWKASF LRAGVYPEKD QAENEDGAQE NTFSMDPQLE RQVETIRNLV
DSYVAIINKS IRDLMPKTIM HLMINNTKAF IHHELLAYLY SSADQSSLME ESAEQAQRRD
DMLRMYHALK EALNIIGDIS TSTVSTPVPP PVDDTWLQNT SGHSPTPQRR PVSSVHPPGR
PPAVRGPTPG PPLIPMPVGA TSSFSAPPIP SRPGPQSVFA NNDPFSAPPQ IPSRPARIPP
GIPPGVPSRR APAAPSRPTI IRPAEPSLLD


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