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Synaptotagmin-1 (Synaptotagmin I) (SytI) (p65)

 SYT1_HUMAN              Reviewed;         422 AA.
P21579; Q6AI31;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 1.
23-MAY-2018, entry version 190.
RecName: Full=Synaptotagmin-1;
AltName: Full=Synaptotagmin I;
Short=SytI;
AltName: Full=p65;
Name=SYT1; Synonyms=SVP65, SYT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1840599;
Perin M.S., Johnston P.A., Oezcelik T., Jahn R., Francke U.,
Suedhof T.C.;
"Structural and functional conservation of synaptotagmin (p65) in
Drosophila and humans.";
J. Biol. Chem. 266:615-622(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Amygdala, and Brain;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Hippocampus;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=PNS;
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).
[6]
INTERACTION WITH SCAMP5.
PubMed=19234194; DOI=10.4049/jimmunol.0802002;
Han C., Chen T., Yang M., Li N., Liu H., Cao X.;
"Human SCAMP5, a novel secretory carrier membrane protein, facilitates
calcium-triggered cytokine secretion by interaction with SNARE
machinery.";
J. Immunol. 182:2986-2996(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[8]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=23999003; DOI=10.1016/j.jdermsci.2013.07.010;
Yoo J.C., Lim T.Y., Park J.S., Hah Y.S., Park N., Hong S.G.,
Park J.Y., Yoon T.J.;
"SYT14L, especially its C2 domain, is involved in regulating
melanocyte differentiation.";
J. Dermatol. Sci. 72:246-251(2013).
[9]
VARIANT THR-368, AND POSSIBLE INVOLVEMENT IN NEURO-DEVELOPMENTAL
DISORDER.
PubMed=25705886; DOI=10.1172/JCI79765;
Baker K., Gordon S.L., Grozeva D., van Kogelenberg M., Roberts N.Y.,
Pike M., Blair E., Hurles M.E., Chong W.K., Baldeweg T., Kurian M.A.,
Boyd S.G., Cousin M.A., Raymond F.L.;
"Identification of a human synaptotagmin-1 mutation that perturbs
synaptic vesicle cycling.";
J. Clin. Invest. 125:1670-1678(2015).
-!- FUNCTION: May have a regulatory role in the membrane interactions
during trafficking of synaptic vesicles at the active zone of the
synapse. It binds acidic phospholipids with a specificity that
requires the presence of both an acidic head group and a diacyl
backbone. A Ca(2+)-dependent interaction between synaptotagmin and
putative receptors for activated protein kinase C has also been
reported. It can bind to at least three additional proteins in a
Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.
Plays a role in dendrite formation by melanocytes
(PubMed:23999003). {ECO:0000269|PubMed:23999003}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000250|UniProtKB:P21707};
Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2
domains. {ECO:0000250|UniProtKB:P21707};
-!- SUBUNIT: Homotetramer (Probable). Interacts with SCAMP5, STON2,
SV2A, SV2B, SV2C and RIMS1. Forms a complex with SV2B, syntaxin 1
and SNAP25 (By similarity). Interacts with PRRT2 (By similarity).
{ECO:0000250, ECO:0000250|UniProtKB:P46096, ECO:0000305}.
-!- INTERACTION:
O00305-2:CACNB4; NbExp=2; IntAct=EBI-524909, EBI-714855;
Q9Y6K9:IKBKG; NbExp=3; IntAct=EBI-524909, EBI-81279;
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
membrane {ECO:0000250|UniProtKB:P21707}; Single-pass membrane
protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle,
synaptic vesicle membrane {ECO:0000250|UniProtKB:P21707}; Single-
pass membrane protein {ECO:0000250|UniProtKB:P21707}. Cytoplasmic
vesicle, secretory vesicle, chromaffin granule membrane
{ECO:0000250|UniProtKB:P21707}; Single-pass membrane protein
{ECO:0000250|UniProtKB:P21707}. Cytoplasm
{ECO:0000250|UniProtKB:P21707}. Note=Synaptic vesicles and
chromaffin granules. {ECO:0000250|UniProtKB:P21707}.
-!- TISSUE SPECIFICITY: Expressed in melanocytes (PubMed:23999003).
{ECO:0000269|PubMed:23999003}.
-!- DOMAIN: The first C2 domain mediates Ca(2+)-dependent phospholipid
binding. {ECO:0000250|UniProtKB:P21707}.
-!- DOMAIN: The second C2 domain mediates interaction with SV2A and
probably with STN2. {ECO:0000250|UniProtKB:P21707}.
-!- DISEASE: Note=A SYT1 rare mutation has been found in a child with
a severe neuro-developmental disorder. The individual harboring
this variant shows early onset dyskinetic movement disorder,
severe motor delay and profound cognitive impairment, suggesting
that SYT1 may play a role in the pathogenesis of this neuro-
developmental disorder. {ECO:0000269|PubMed:25705886}.
-!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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EMBL; M55047; AAA60609.1; -; mRNA.
EMBL; AK094616; BAG52897.1; -; mRNA.
EMBL; AK126908; BAG54392.1; -; mRNA.
EMBL; CR627387; CAH10483.1; -; mRNA.
EMBL; CH471054; EAW97343.1; -; Genomic_DNA.
EMBL; BC058917; AAH58917.1; -; mRNA.
CCDS; CCDS9017.1; -.
PIR; A39052; BMHU1Y.
RefSeq; NP_001129277.1; NM_001135805.1.
RefSeq; NP_001129278.1; NM_001135806.1.
RefSeq; NP_005630.1; NM_005639.2.
RefSeq; XP_011537012.1; XM_011538710.1.
RefSeq; XP_016875398.1; XM_017019909.1.
UniGene; Hs.310545; -.
PDB; 2K45; NMR; -; A=141-268.
PDB; 2K4A; NMR; -; A=141-268.
PDB; 2K8M; NMR; -; A/D=141-268.
PDB; 2KI6; NMR; -; A/F=141-268.
PDB; 2LHA; NMR; -; A=271-422.
PDB; 2N1T; NMR; -; E=272-419.
PDB; 2R83; X-ray; 2.70 A; A/B=141-422.
PDB; 3F00; X-ray; 1.36 A; A=141-266.
PDB; 3F01; X-ray; 1.70 A; A=141-266.
PDB; 3F04; X-ray; 1.35 A; A=141-266.
PDB; 3F05; X-ray; 1.40 A; A=141-266.
PDB; 4ISQ; X-ray; 2.65 A; D/E/F=33-53.
PDB; 4V11; X-ray; 1.95 A; A=273-422.
PDBsum; 2K45; -.
PDBsum; 2K4A; -.
PDBsum; 2K8M; -.
PDBsum; 2KI6; -.
PDBsum; 2LHA; -.
PDBsum; 2N1T; -.
PDBsum; 2R83; -.
PDBsum; 3F00; -.
PDBsum; 3F01; -.
PDBsum; 3F04; -.
PDBsum; 3F05; -.
PDBsum; 4ISQ; -.
PDBsum; 4V11; -.
ProteinModelPortal; P21579; -.
SMR; P21579; -.
BioGrid; 112723; 41.
DIP; DIP-34042N; -.
ELM; P21579; -.
IntAct; P21579; 19.
MINT; P21579; -.
STRING; 9606.ENSP00000261205; -.
TCDB; 1.F.1.1.1; the synaptosomal vesicle fusion pore (svf-pore) family.
iPTMnet; P21579; -.
PhosphoSitePlus; P21579; -.
SwissPalm; P21579; -.
BioMuta; SYT1; -.
DMDM; 135086; -.
EPD; P21579; -.
PaxDb; P21579; -.
PeptideAtlas; P21579; -.
PRIDE; P21579; -.
Ensembl; ENST00000261205; ENSP00000261205; ENSG00000067715.
Ensembl; ENST00000393240; ENSP00000376932; ENSG00000067715.
Ensembl; ENST00000552744; ENSP00000447575; ENSG00000067715.
GeneID; 6857; -.
KEGG; hsa:6857; -.
UCSC; uc001sys.4; human.
CTD; 6857; -.
DisGeNET; 6857; -.
EuPathDB; HostDB:ENSG00000067715.13; -.
GeneCards; SYT1; -.
HGNC; HGNC:11509; SYT1.
HPA; HPA008394; -.
HPA; HPA064788; -.
MIM; 185605; gene.
neXtProt; NX_P21579; -.
OpenTargets; ENSG00000067715; -.
PharmGKB; PA36290; -.
eggNOG; ENOG410IT3Q; Eukaryota.
eggNOG; ENOG410Z15P; LUCA.
GeneTree; ENSGT00760000118973; -.
HOGENOM; HOG000232127; -.
HOVERGEN; HBG005010; -.
InParanoid; P21579; -.
KO; K15290; -.
OMA; HNATEPA; -.
OrthoDB; EOG091G0XMQ; -.
PhylomeDB; P21579; -.
TreeFam; TF315600; -.
Reactome; R-HSA-181429; Serotonin Neurotransmitter Release Cycle.
Reactome; R-HSA-181430; Norepinephrine Neurotransmitter Release Cycle.
Reactome; R-HSA-210500; Glutamate Neurotransmitter Release Cycle.
Reactome; R-HSA-212676; Dopamine Neurotransmitter Release Cycle.
Reactome; R-HSA-264642; Acetylcholine Neurotransmitter Release Cycle.
Reactome; R-HSA-5250958; Toxicity of botulinum toxin type B (BoNT/B).
Reactome; R-HSA-5250989; Toxicity of botulinum toxin type G (BoNT/G).
Reactome; R-HSA-6794361; Neurexins and neuroligins.
Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
Reactome; R-HSA-888590; GABA synthesis, release, reuptake and degradation.
ChiTaRS; SYT1; human.
EvolutionaryTrace; P21579; -.
GeneWiki; SYT1; -.
GenomeRNAi; 6857; -.
PMAP-CutDB; P21579; -.
PRO; PR:P21579; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000067715; -.
CleanEx; HS_SYT1; -.
ExpressionAtlas; P21579; baseline and differential.
Genevisible; P21579; HS.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0042584; C:chromaffin granule membrane; IEA:UniProtKB-SubCell.
GO; GO:0030665; C:clathrin-coated vesicle membrane; TAS:Reactome.
GO; GO:0060201; C:clathrin-sculpted acetylcholine transport vesicle membrane; TAS:Reactome.
GO; GO:0061202; C:clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane; TAS:Reactome.
GO; GO:0060203; C:clathrin-sculpted glutamate transport vesicle membrane; TAS:Reactome.
GO; GO:0070083; C:clathrin-sculpted monoamine transport vesicle membrane; TAS:Reactome.
GO; GO:0005829; C:cytosol; IDA:ARUK-UCL.
GO; GO:0031045; C:dense core granule; IEA:Ensembl.
GO; GO:0060076; C:excitatory synapse; IEA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0030285; C:integral component of synaptic vesicle membrane; IEA:Ensembl.
GO; GO:0043005; C:neuron projection; ISS:ParkinsonsUK-UCL.
GO; GO:0044306; C:neuron projection terminus; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl.
GO; GO:0031201; C:SNARE complex; IEA:Ensembl.
GO; GO:0008021; C:synaptic vesicle; TAS:UniProtKB.
GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
GO; GO:0005545; F:1-phosphatidylinositol binding; TAS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
GO; GO:0005544; F:calcium-dependent phospholipid binding; ISS:ParkinsonsUK-UCL.
GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl.
GO; GO:0005516; F:calmodulin binding; IEA:Ensembl.
GO; GO:0030276; F:clathrin binding; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IDA:MGI.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
GO; GO:0001786; F:phosphatidylserine binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0000149; F:SNARE binding; ISS:ParkinsonsUK-UCL.
GO; GO:0017075; F:syntaxin-1 binding; ISS:ParkinsonsUK-UCL.
GO; GO:0030348; F:syntaxin-3 binding; IEA:Ensembl.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; IBA:GO_Central.
GO; GO:0071277; P:cellular response to calcium ion; ISS:ParkinsonsUK-UCL.
GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
GO; GO:0005513; P:detection of calcium ion; TAS:UniProtKB.
GO; GO:0098746; P:fast, calcium ion-dependent exocytosis of neurotransmitter; ISS:ParkinsonsUK-UCL.
GO; GO:0014047; P:glutamate secretion; TAS:Reactome.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0007269; P:neurotransmitter secretion; TAS:UniProtKB.
GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; IEA:Ensembl.
GO; GO:1903861; P:positive regulation of dendrite extension; IDA:UniProtKB.
GO; GO:0050806; P:positive regulation of synaptic transmission; ISS:ParkinsonsUK-UCL.
GO; GO:0031340; P:positive regulation of vesicle fusion; IEA:Ensembl.
GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
GO; GO:0051260; P:protein homooligomerization; TAS:UniProtKB.
GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IBA:GO_Central.
GO; GO:0014059; P:regulation of dopamine secretion; IEA:Ensembl.
GO; GO:0017157; P:regulation of exocytosis; TAS:UniProtKB.
GO; GO:1903305; P:regulation of regulated secretory pathway; ISS:ParkinsonsUK-UCL.
GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; ISS:ParkinsonsUK-UCL.
GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
GO; GO:0048278; P:vesicle docking; IEA:Ensembl.
GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
Gene3D; 2.60.40.150; -; 2.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR001565; Synaptotagmin.
InterPro; IPR015428; Synaptotagmin1/2.
PANTHER; PTHR10024:SF239; PTHR10024:SF239; 1.
Pfam; PF00168; C2; 2.
PRINTS; PR00360; C2DOMAIN.
PRINTS; PR00399; SYNAPTOTAGMN.
SMART; SM00239; C2; 2.
PROSITE; PS50004; C2; 2.
1: Evidence at protein level;
3D-structure; Calcium; Cell junction; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Differentiation; Disease mutation; Glycoprotein;
Lipoprotein; Membrane; Metal-binding; Palmitate; Phosphoprotein;
Reference proteome; Repeat; Synapse; Transmembrane;
Transmembrane helix.
CHAIN 1 422 Synaptotagmin-1.
/FTId=PRO_0000183936.
TOPO_DOM 1 57 Vesicular. {ECO:0000255}.
TRANSMEM 58 80 Helical. {ECO:0000255}.
TOPO_DOM 81 422 Cytoplasmic. {ECO:0000255}.
DOMAIN 157 245 C2 1. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 287 378 C2 2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
REGION 136 382 Phospholipid binding. {ECO:0000305}.
METAL 172 172 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P21707}.
METAL 173 173 Calcium 1.
{ECO:0000250|UniProtKB:P21707}.
METAL 173 173 Calcium 2.
{ECO:0000250|UniProtKB:P21707}.
METAL 179 179 Calcium 1.
{ECO:0000250|UniProtKB:P21707}.
METAL 231 231 Calcium 1.
{ECO:0000250|UniProtKB:P21707}.
METAL 231 231 Calcium 2.
{ECO:0000250|UniProtKB:P21707}.
METAL 232 232 Calcium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P21707}.
METAL 233 233 Calcium 1.
{ECO:0000250|UniProtKB:P21707}.
METAL 233 233 Calcium 2.
{ECO:0000250|UniProtKB:P21707}.
METAL 233 233 Calcium 3.
{ECO:0000250|UniProtKB:P21707}.
METAL 236 236 Calcium 3.
{ECO:0000250|UniProtKB:P21707}.
METAL 237 237 Calcium 3; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P21707}.
METAL 239 239 Calcium 2.
{ECO:0000250|UniProtKB:P21707}.
METAL 239 239 Calcium 3.
{ECO:0000250|UniProtKB:P21707}.
MOD_RES 129 129 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 230 230 Phosphotyrosine.
{ECO:0000250|UniProtKB:P46096}.
MOD_RES 265 265 Phosphoserine.
{ECO:0000250|UniProtKB:P46096}.
MOD_RES 343 343 Phosphoserine.
{ECO:0000250|UniProtKB:P21707}.
MOD_RES 345 345 Phosphoserine.
{ECO:0000250|UniProtKB:P21707}.
LIPID 75 75 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P21707}.
LIPID 76 76 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P21707}.
LIPID 78 78 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P21707}.
LIPID 80 80 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P21707}.
LIPID 83 83 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P21707}.
CARBOHYD 25 25 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 368 368 I -> T (probable disease-associated
mutation found in a patient with an early
onset dyskinetic movement disorder,
severe motor delay and profound cognitive
impairment).
{ECO:0000269|PubMed:25705886}.
/FTId=VAR_072911.
HELIX 37 47 {ECO:0000244|PDB:4ISQ}.
STRAND 145 153 {ECO:0000244|PDB:3F04}.
TURN 154 157 {ECO:0000244|PDB:3F04}.
STRAND 158 167 {ECO:0000244|PDB:3F04}.
HELIX 173 175 {ECO:0000244|PDB:3F04}.
STRAND 180 188 {ECO:0000244|PDB:3F04}.
STRAND 206 213 {ECO:0000244|PDB:3F04}.
HELIX 217 220 {ECO:0000244|PDB:3F04}.
STRAND 224 231 {ECO:0000244|PDB:3F04}.
STRAND 234 236 {ECO:0000244|PDB:3F04}.
STRAND 239 247 {ECO:0000244|PDB:3F04}.
HELIX 248 250 {ECO:0000244|PDB:3F04}.
STRAND 257 262 {ECO:0000244|PDB:3F04}.
STRAND 276 284 {ECO:0000244|PDB:4V11}.
TURN 285 288 {ECO:0000244|PDB:4V11}.
STRAND 289 299 {ECO:0000244|PDB:4V11}.
STRAND 304 307 {ECO:0000244|PDB:2N1T}.
STRAND 311 319 {ECO:0000244|PDB:4V11}.
STRAND 322 328 {ECO:0000244|PDB:4V11}.
STRAND 333 337 {ECO:0000244|PDB:2LHA}.
STRAND 339 347 {ECO:0000244|PDB:4V11}.
HELIX 350 352 {ECO:0000244|PDB:4V11}.
TURN 353 355 {ECO:0000244|PDB:4V11}.
STRAND 357 364 {ECO:0000244|PDB:4V11}.
STRAND 367 369 {ECO:0000244|PDB:4V11}.
STRAND 373 380 {ECO:0000244|PDB:4V11}.
HELIX 385 396 {ECO:0000244|PDB:4V11}.
STRAND 402 407 {ECO:0000244|PDB:4V11}.
HELIX 411 417 {ECO:0000244|PDB:4V11}.
SEQUENCE 422 AA; 47573 MW; 467F7C58E411AFA9 CRC64;
MVSESHHEAL AAPPVTTVAT VLPSNATEPA SPGEGKEDAF SKLKEKFMNE LHKIPLPPWA
LIAIAIVAVL LVLTCCFCIC KKCLFKKKNK KKGKEKGGKN AINMKDVKDL GKTMKDQALK
DDDAETGLTD GEEKEEPKEE EKLGKLQYSL DYDFQNNQLL VGIIQAAELP ALDMGGTSDP
YVKVFLLPDK KKKFETKVHR KTLNPVFNEQ FTFKVPYSEL GGKTLVMAVY DFDRFSKHDI
IGEFKVPMNT VDFGHVTEEW RDLQSAEKEE QEKLGDICFS LRYVPTAGKL TVVILEAKNL
KKMDVGGLSD PYVKIHLMQN GKRLKKKKTT IKKNTLNPYY NESFSFEVPF EQIQKVQVVV
TVLDYDKIGK NDAIGKVFVG YNSTGAELRH WSDMLANPRR PIAQWHTLQV EEEVDAMLAV
KK


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