ID   HD_MOUSE                Reviewed;        3119 AA.
AC   P42859;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   24-JAN-2024, entry version 196.
DE   RecName: Full=Huntingtin;
DE   AltName: Full=Huntington disease protein homolog;
DE            Short=HD protein homolog;
DE   Contains:
DE     RecName: Full=Huntingtin, myristoylated N-terminal fragment {ECO:0000250|UniProtKB:P42858};
GN   Name=Htt; Synonyms=Hd, Hdh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Spleen;
RX   PubMed=8162057; DOI=10.1093/hmg/3.1.85;
RA   Lin B., Nasir J., Macdonald H., Hutchinson G., Graham R.K., Rommens J.M.,
RA   Hayden M.R.;
RT   "Sequence of the murine Huntington disease gene: evidence for conservation,
RT   alternate splicing and polymorphism in a triplet (CCG) repeat.";
RL   Hum. Mol. Genet. 3:85-92(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND POLYMORPHISM.
RX   PubMed=8009370; DOI=10.1007/bf02290678;
RA   Barnes G.T., Duyao M.P., Ambrose C.M., McNeil S., Persichetti F.,
RA   Srinidhi J., Gusella J.F., Macdonald M.E.;
RT   "Mouse Huntington's disease gene homolog (Hdh).";
RL   Somat. Cell Mol. Genet. 20:87-97(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7647777; DOI=10.1038/ng0595-104;
RA   Trottier Y., Devys D., Imbert G., Saudou F., An I., Lutz Y., Weber C.,
RA   Agid Y., Hirsch E.C., Mandel J.-L.;
RT   "Cellular localization of the Huntington's disease protein and
RT   discrimination of the normal and mutated form.";
RL   Nat. Genet. 10:104-110(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-181.
RX   PubMed=7759106; DOI=10.1016/0888-7543(95)80014-d;
RA   Lin B., Nasir J., Kalchman M.A., McDonald H., Zeisler J., Goldberg Y.P.,
RA   Hayden M.R.;
RT   "Structural analysis of the 5' region of mouse and human Huntington disease
RT   genes reveals conservation of putative promoter region and di- and
RT   trinucleotide polymorphisms.";
RL   Genomics 25:707-715(1995).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11035034; DOI=10.1074/jbc.m008099200;
RA   Peters M.F., Ross C.A.;
RT   "Isolation of a 40-kDa Huntingtin-associated protein.";
RL   J. Biol. Chem. 276:3188-3194(2001).
RN   [6]
RP   INTERACTION WITH SH3GLB1.
RX   PubMed=12456676; DOI=10.1074/jbc.m208568200;
RA   Modregger J., Schmidt A.A., Ritter B., Huttner W.B., Plomann M.;
RT   "Characterization of endophilin B1b, a brain-specific membrane-associated
RT   lysophosphatidic acid acyl transferase with properties distinct from
RT   endophilin A1.";
RL   J. Biol. Chem. 278:4160-4167(2003).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-396; SER-398; SER-411 AND
RP   SER-1853, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [9]
RP   INTERACTION WITH ZDHHC17 AND ZDHHC13.
RX   PubMed=26198635; DOI=10.1074/jbc.m115.657668;
RA   Lemonidis K., Sanchez-Perez M.C., Chamberlain L.H.;
RT   "Identification of a novel sequence motif recognized by the ankyrin repeat
RT   domain of zDHHC17/13 S-acyltransferases.";
RL   J. Biol. Chem. 290:21939-21950(2015).
CC   -!- FUNCTION: [Huntingtin]: May play a role in microtubule-mediated
CC       transport or vesicle function. {ECO:0000250|UniProtKB:P42858}.
CC   -!- FUNCTION: [Huntingtin, myristoylated N-terminal fragment]: Promotes the
CC       formation of autophagic vesicles. {ECO:0000250|UniProtKB:P42858}.
CC   -!- SUBUNIT: Interacts with PFN1 (By similarity). Interacts through its N-
CC       terminus with PRPF40A (By similarity). Interacts with PQBP1 (By
CC       similarity). Interacts with SETD2 (By similarity). Interacts with
CC       SH3GLB1 (PubMed:12456676). Interacts with SYVN (By similarity).
CC       Interacts with TPR; the interaction is inhibited by forms of Huntingtin
CC       with expanded polyglutamine stretch (By similarity). Interacts with
CC       ZDHHC13 (via ANK repeats) (PubMed:26198635). Interacts with ZDHHC17
CC       (via ANK repeats) (PubMed:26198635). Interacts with F8A1/F8A2/F8A3 (By
CC       similarity). Found in a complex with F8A1/F8A2/F8A3, HTT and RAB5A;
CC       mediates the recruitment of HTT by RAB5A (By similarity).
CC       {ECO:0000250|UniProtKB:P42858, ECO:0000269|PubMed:12456676,
CC       ECO:0000269|PubMed:26198635}.
CC   -!- INTERACTION:
CC       P42859; P70677: Casp3; NbExp=2; IntAct=EBI-5327353, EBI-1790419;
CC       P42859; Q02248: Ctnnb1; NbExp=3; IntAct=EBI-5327353, EBI-397872;
CC       P42859; Q8CIN4: Pak2; NbExp=2; IntAct=EBI-5327353, EBI-1559317;
CC       P42859; O70405: Ulk1; NbExp=4; IntAct=EBI-5327353, EBI-8390771;
CC   -!- SUBCELLULAR LOCATION: [Huntingtin]: Cytoplasm
CC       {ECO:0000269|PubMed:11035034}. Nucleus {ECO:0000250|UniProtKB:P42858}.
CC       Note=Shuttles between cytoplasm and nucleus in a Ran GTPase-independent
CC       manner. {ECO:0000250|UniProtKB:P42858}.
CC   -!- SUBCELLULAR LOCATION: [Huntingtin, myristoylated N-terminal fragment]:
CC       Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:P42858}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=P42859-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=P42859-2; Sequence=VSP_004282;
CC   -!- TISSUE SPECIFICITY: The highest level is seen throughout the brain, but
CC       it is also found in the stomach, heart, testis, adipose tissue, muscle,
CC       spleen, liver, and kidney.
CC   -!- DEVELOPMENTAL STAGE: Predominant expression in neuronal tissues at all
CC       developmental stages. In 14.5 day old embryos, it is also detected in
CC       non-neuronal tissues. This expression is down-regulated in later stages
CC       of development.
CC   -!- DOMAIN: The N-terminal Gln-rich and Pro-rich domain has great
CC       conformational flexibility and is likely to exist in a fluctuating
CC       equilibrium of alpha-helical, random coil, and extended conformations.
CC       {ECO:0000250|UniProtKB:P42858}.
CC   -!- PTM: Phosphorylation at Ser-1159 and Ser-1179 by CDK5 in response to
CC       DNA damage in nuclei of neurons protects neurons against polyglutamine
CC       expansion as well as DNA damage mediated toxicity.
CC       {ECO:0000250|UniProtKB:P42858}.
CC   -!- PTM: [Huntingtin]: Cleaved by caspases downstream of the polyglutamine
CC       stretch. {ECO:0000250|UniProtKB:P42858}.
CC   -!- PTM: [Huntingtin, myristoylated N-terminal fragment]: Myristoylated at
CC       Gly-530, following proteolytic cleavage at Asp-529.
CC       {ECO:0000250|UniProtKB:P42858}.
CC   -!- POLYMORPHISM: The poly-Gln region does not appear to be polymorphic,
CC       explaining the absence of a murine HD-like disorder (PubMed:8009370).
CC       {ECO:0000269|PubMed:8009370}.
CC   -!- MISCELLANEOUS: [Isoform Short]: Cannot be explained by a simple
CC       splicing event. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the huntingtin family. {ECO:0000305}.
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DR   EMBL; L23312; AAA37799.1; -; mRNA.
DR   EMBL; L23313; AAA37800.1; -; mRNA.
DR   EMBL; L28827; AAA89100.1; ALT_SEQ; mRNA.
DR   EMBL; U24233; AAC52218.1; -; mRNA.
DR   EMBL; AH003368; AAA91085.1; -; Genomic_DNA.
DR   PIR; I49729; I49729.
DR   BMRB; P42859; -.
DR   SMR; P42859; -.
DR   CORUM; P42859; -.
DR   DIP; DIP-41430N; -.
DR   IntAct; P42859; 22.
DR   MINT; P42859; -.
DR   STRING; 10090.ENSMUSP00000078945; -.
DR   ChEMBL; CHEMBL1250362; -.
DR   GlyGen; P42859; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P42859; -.
DR   PhosphoSitePlus; P42859; -.
DR   SwissPalm; P42859; -.
DR   EPD; P42859; -.
DR   jPOST; P42859; -.
DR   MaxQB; P42859; -.
DR   PaxDb; 10090-ENSMUSP00000078945; -.
DR   PeptideAtlas; P42859; -.
DR   ProteomicsDB; 269778; -. [P42859-1]
DR   ProteomicsDB; 269779; -. [P42859-2]
DR   Pumba; P42859; -.
DR   AGR; MGI:96067; -.
DR   MGI; MGI:96067; Htt.
DR   eggNOG; ENOG502QR1D; Eukaryota.
DR   InParanoid; P42859; -.
DR   PhylomeDB; P42859; -.
DR   ChiTaRS; Htt; mouse.
DR   PRO; PR:P42859; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P42859; Protein.
DR   GO; GO:0005776; C:autophagosome; ISO:MGI.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0005814; C:centriole; IDA:MGI.
DR   GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0005769; C:early endosome; ISO:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0016234; C:inclusion body; IDA:MGI.
DR   GO; GO:0005770; C:late endosome; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0071598; C:neuronal ribonucleoprotein granule; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0099524; C:postsynaptic cytosol; ISO:MGI.
DR   GO; GO:0099523; C:presynaptic cytosol; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0097060; C:synaptic membrane; ISO:MGI.
DR   GO; GO:0048487; F:beta-tubulin binding; ISO:MGI.
DR   GO; GO:0050809; F:diazepam binding; IMP:MGI.
DR   GO; GO:0034452; F:dynactin binding; ISO:MGI.
DR   GO; GO:0045505; F:dynein intermediate chain binding; ISO:MGI.
DR   GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0019900; F:kinase binding; ISO:MGI.
DR   GO; GO:0002039; F:p53 binding; ISO:MGI.
DR   GO; GO:0005522; F:profilin binding; ISO:MGI.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR   GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IMP:MGI.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR   GO; GO:0008306; P:associative learning; IMP:MGI.
DR   GO; GO:0008088; P:axo-dendritic transport; IMP:MGI.
DR   GO; GO:0007420; P:brain development; IMP:MGI.
DR   GO; GO:0090398; P:cellular senescence; IMP:MGI.
DR   GO; GO:0007417; P:central nervous system development; IMP:MGI.
DR   GO; GO:0000052; P:citrulline metabolic process; IMP:MGI.
DR   GO; GO:0008340; P:determination of adult lifespan; IMP:MGI.
DR   GO; GO:0007212; P:dopamine receptor signaling pathway; IMP:MGI.
DR   GO; GO:0007029; P:endoplasmic reticulum organization; IMP:MGI.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:MGI.
DR   GO; GO:0016197; P:endosomal transport; IMP:MGI.
DR   GO; GO:0000132; P:establishment of mitotic spindle orientation; ISO:MGI.
DR   GO; GO:0007369; P:gastrulation; IMP:MGI.
DR   GO; GO:0007030; P:Golgi organization; ISO:MGI.
DR   GO; GO:0007625; P:grooming behavior; IMP:MGI.
DR   GO; GO:0042445; P:hormone metabolic process; IMP:MGI.
DR   GO; GO:0030073; P:insulin secretion; IMP:MGI.
DR   GO; GO:0019244; P:lactate biosynthetic process from pyruvate; IMP:MGI.
DR   GO; GO:0007612; P:learning; IMP:MGI.
DR   GO; GO:0007611; P:learning or memory; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0007019; P:microtubule depolymerization; ISO:MGI.
DR   GO; GO:0099111; P:microtubule-based transport; IBA:GO_Central.
DR   GO; GO:0006839; P:mitochondrial transport; IMP:MGI.
DR   GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
DR   GO; GO:0051028; P:mRNA transport; ISO:MGI.
DR   GO; GO:0060586; P:multicellular organismal-level iron ion homeostasis; IMP:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IDA:MGI.
DR   GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
DR   GO; GO:0021990; P:neural plate formation; IMP:MGI.
DR   GO; GO:0022008; P:neurogenesis; IMP:MGI.
DR   GO; GO:0048666; P:neuron development; IMP:MGI.
DR   GO; GO:0021988; P:olfactory lobe development; IMP:MGI.
DR   GO; GO:0048341; P:paraxial mesoderm formation; IMP:MGI.
DR   GO; GO:0030072; P:peptide hormone secretion; IMP:MGI.
DR   GO; GO:1905337; P:positive regulation of aggrephagy; ISO:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR   GO; GO:1903599; P:positive regulation of autophagy of mitochondrion; ISO:MGI.
DR   GO; GO:0045724; P:positive regulation of cilium assembly; ISO:MGI.
DR   GO; GO:1904504; P:positive regulation of lipophagy; ISO:MGI.
DR   GO; GO:1905505; P:positive regulation of motile cilium assembly; IMP:MGI.
DR   GO; GO:1902857; P:positive regulation of non-motile cilium assembly; IMP:MGI.
DR   GO; GO:0099527; P:postsynapse to nucleus signaling pathway; IDA:SynGO.
DR   GO; GO:0031648; P:protein destabilization; ISO:MGI.
DR   GO; GO:0071539; P:protein localization to centrosome; IMP:MGI.
DR   GO; GO:0034504; P:protein localization to nucleus; IMP:MGI.
DR   GO; GO:0019805; P:quinolinate biosynthetic process; IMP:MGI.
DR   GO; GO:1905289; P:regulation of CAMKK-AMPK signaling cascade; ISO:MGI.
DR   GO; GO:2000479; P:regulation of cAMP-dependent protein kinase activity; IMP:ARUK-UCL.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:ARUK-UCL.
DR   GO; GO:1904580; P:regulation of intracellular mRNA localization; ISO:MGI.
DR   GO; GO:0043523; P:regulation of neuron apoptotic process; IMP:ARUK-UCL.
DR   GO; GO:1900180; P:regulation of protein localization to nucleus; IMP:ARUK-UCL.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
DR   GO; GO:0051592; P:response to calcium ion; IMP:MGI.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0035176; P:social behavior; IMP:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR   GO; GO:0021756; P:striatum development; IMP:MGI.
DR   GO; GO:0000050; P:urea cycle; IMP:MGI.
DR   GO; GO:0047496; P:vesicle transport along microtubule; IDA:MGI.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   GO; GO:0042297; P:vocal learning; ISO:MGI.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR048412; Htt_bridge.
DR   InterPro; IPR048413; Htt_C-HEAT_rpt.
DR   InterPro; IPR048411; Htt_N_HEAT_rpt-1.
DR   InterPro; IPR000091; Huntingtin.
DR   InterPro; IPR028426; Huntingtin_fam.
DR   InterPro; IPR024613; Huntingtin_N_HEAT_rpt-2.
DR   PANTHER; PTHR10170:SF10; HUNTINGTIN; 1.
DR   PANTHER; PTHR10170; HUNTINGTON DISEASE PROTEIN; 1.
DR   Pfam; PF20925; Htt_bridge; 1.
DR   Pfam; PF20927; Htt_C-HEAT; 1.
DR   Pfam; PF12372; Htt_N-HEAT; 1.
DR   Pfam; PF20926; Htt_N-HEAT_1; 1.
DR   PRINTS; PR00375; HUNTINGTIN.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
KW   Lipoprotein; Myristate; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat.
FT   CHAIN           1..3119
FT                   /note="Huntingtin"
FT                   /id="PRO_0000083943"
FT   CHAIN           530..563
FT                   /note="Huntingtin, myristoylated N-terminal fragment"
FT                   /evidence="ECO:0000250|UniProtKB:P42858"
FT                   /id="PRO_0000447487"
FT   REPEAT          183..220
FT                   /note="HEAT 1"
FT   REPEAT          225..262
FT                   /note="HEAT 2"
FT   REPEAT          782..819
FT                   /note="HEAT 3"
FT   REPEAT          882..920
FT                   /note="HEAT 4"
FT   REPEAT          1404..1441
FT                   /note="HEAT 5"
FT   REGION          1..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          470..481
FT                   /note="Interaction with ZDHHC17"
FT                   /evidence="ECO:0000250|UniProtKB:P42858"
FT   REGION          495..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1146..1204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2610..2637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           2372..2381
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        24..61
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..558
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1186..1204
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            490..491
FT                   /note="Cleavage; by caspase-3"
FT                   /evidence="ECO:0000250|UniProtKB:P42858"
FT   SITE            507..508
FT                   /note="Cleavage; by caspase-3"
FT                   /evidence="ECO:0000255"
FT   SITE            529..530
FT                   /note="Cleavage; by caspase-3"
FT                   /evidence="ECO:0000250|UniProtKB:P42858"
FT   SITE            563..564
FT                   /note="Cleavage; by caspase-6"
FT                   /evidence="ECO:0000250|UniProtKB:P42858"
FT   MOD_RES         9
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P42858"
FT   MOD_RES         155
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P42858"
FT   MOD_RES         213
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P42858"
FT   MOD_RES         322
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P42858"
FT   MOD_RES         396
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         398
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         411
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         421
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P42858"
FT   MOD_RES         620
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42858"
FT   MOD_RES         623
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42858"
FT   MOD_RES         1159
FT                   /note="Phosphoserine; by CDK5"
FT                   /evidence="ECO:0000250|UniProtKB:P42858"
FT   MOD_RES         1179
FT                   /note="Phosphoserine; by CDK5"
FT                   /evidence="ECO:0000250|UniProtKB:P42858"
FT   MOD_RES         1853
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   LIPID           530
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250|UniProtKB:P42858"
FT   VAR_SEQ         1522..2001
FT                   /note="Missing (in isoform Short)"
FT                   /evidence="ECO:0000303|PubMed:8162057"
FT                   /id="VSP_004282"
FT   CONFLICT        2
FT                   /note="A -> G (in Ref. 1; AAA37799/AAA37800 and 4;
FT                   AAA91085)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        29
FT                   /note="A -> P (in Ref. 2; AAA89100)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        116
FT                   /note="N -> D (in Ref. 2; AAA89100 and 4; AAA91085)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        138
FT                   /note="M -> L (in Ref. 1; AAA37799/AAA37800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        521
FT                   /note="S -> P (in Ref. 1; AAA37799/AAA37800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        524
FT                   /note="A -> P (in Ref. 1; AAA37799/AAA37800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        533
FT                   /note="A -> P (in Ref. 1; AAA37799/AAA37800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        607
FT                   /note="A -> T (in Ref. 1; AAA37799/AAA37800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        769
FT                   /note="D -> E (in Ref. 2; AAA89100)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        972
FT                   /note="S -> R (in Ref. 1; AAA37799/AAA37800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1106
FT                   /note="W -> C (in Ref. 1; AAA37799/AAA37800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1240
FT                   /note="T -> N (in Ref. 1; AAA37799/AAA37800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1384
FT                   /note="N -> T (in Ref. 1; AAA37799/AAA37800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1827
FT                   /note="H -> Y (in Ref. 1; AAA37799)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1979..1980
FT                   /note="PF -> SS (in Ref. 1; AAA37799)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2062
FT                   /note="D -> G (in Ref. 1; AAA37799/AAA37800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2570
FT                   /note="S -> N (in Ref. 1; AAA37799/AAA37800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2866
FT                   /note="E -> V (in Ref. 1; AAA37799/AAA37800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2877
FT                   /note="V -> G (in Ref. 1; AAA37799/AAA37800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2882
FT                   /note="D -> G (in Ref. 1; AAA37799/AAA37800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2887
FT                   /note="Q -> H (in Ref. 1; AAA37799/AAA37800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2915
FT                   /note="A -> T (in Ref. 1; AAA37799/AAA37800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3025
FT                   /note="P -> S (in Ref. 3; AAC52218)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3062..3063
FT                   /note="QV -> LM (in Ref. 1; AAA37799/AAA37800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3095..3096
FT                   /note="VV -> EE (in Ref. 1; AAA37799/AAA37800)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   3119 AA;  344690 MW;  ECA42B5916F50F4F CRC64;
     MATLEKLMKA FESLKSFQQQ QQQQPPPQAP PPPPPPPPQP PQPPPQGQPP PPPPPLPGPA
     EEPLHRPKKE LSATKKDRVN HCLTICENIV AQSLRNSPEF QKLLGIAMEL FLLCSNDAES
     DVRMVADECL NKVIKALMDS NLPRLQLELY KEIKKNGAPR SLRAALWRFA ELAHLVRPQK
     CRPYLVNLLP CLTRTSKRPE ESVQETLAAA VPKIMASFGN FANDNEIKVL LKAFIANLKS
     SSPTVRRTAA GSAVSICQHS RRTQYFYNWL LNVLLGLLVP MEEEHSTLLI LGVLLTLRCL
     VPLLQQQVKD TSLKGSFGVT RKEMEVSPST EQLVQVYELT LHHTQHQDHN VVTGALELLQ
     QLFRTPPPEL LQALTTPGGL GQLTLVQEEA RGRGRSGSIV ELLAGGGSSC SPVLSRKQKG
     KVLLGEEEAL EDDSESRSDV SSSAFAASVK SEIGGELAAS SGVSTPGSVG HDIITEQPRS
     QHTLQADSVD LSGCDLTSAA TDGDEEDILS HSSSQFSAVP SDPAMDLNDG TQASSPISDS
     SQTTTEGPDS AVTPSDSSEI VLDGADSQYL GMQIGQPQED DEEGAAGVLS GEVSDVFRNS
     SLALQQAHLL ERMGHSRQPS DSSIDKYVTR DEVAEASDPE SKPCRIKGDI GQPNDDDSAP
     LVHCVRLLSA SFLLTGEKKA LVPDRDVRVS VKALALSCIG AAVALHPESF FSRLYKVPLN
     TTESTEEQYV SDILNYIDHG DPQVRGATAI LCGTLVYSIL SRSRLRVGDW LGNIRTLTGN
     TFSLVDCIPL LQKTLKDESS VTCKLACTAV RHCVLSLCSS SYSDLGLQLL IDMLPLKNSS
     YWLVRTELLD TLAEIDFRLV SFLEAKAESL HRGAHHYTGF LKLQERVLNN VVIYLLGDED
     PRVRHVAATS LTRLVPKLFY KCDQGQADPV VAVARDQSSV YLKLLMHETQ PPSHFSVSTI
     TRIYRGYSLL PSITDVTMEN NLSRVVAAVS HELITSTTRA LTFGCCEALC LLSAAFPVCT
     WSLGWHCGVP PLSASDESRK SCTVGMASMI LTLLSSAWFP LDLSAHQDAL ILAGNLLAAS
     APKSLRSSWT SEEEANSAAT RQEEIWPALG DRTLVPLVEQ LFSHLLKVIN ICAHVLDDVT
     PGPAIKAALP SLTNPPSLSP IRRKGKEKEP GEQASTPMSP KKVGEASAAS RQSDTSGPVT
     ASKSSSLGSF YHLPSYLKLH DVLKATHANY KVTLDLQNST EKFGGFLRSA LDVLSQILEL
     ATLQDIGKCV EEVLGYLKSC FSREPMMATV CVQQLLKTLF GTNLASQFDG LSSNPSKSQC
     RAQRLGSSSV RPGLYHYCFM APYTHFTQAL ADASLRNMVQ AEQERDASGW FDVLQKVSAQ
     LKTNLTSVTK NRADKNAIHN HIRLFEPLVI KALKQYTTTT SVQLQKQVLD LLAQLVQLRV
     NYCLLDSDQV FIGFVLKQFE YIEVGQFRES EAIIPNIFFF LVLLSYERYH SKQIIGIPKI
     IQLCDGIMAS GRKAVTHAIP ALQPIVHDLF VLRGTNKADA GKELETQKEV VVSMLLRLIQ
     YHQVLEMFIL VLQQCHKENE DKWKRLSRQV ADIILPMLAK QQMHIDSHEA LGVLNTLFEI
     LAPSSLRPVD MLLRSMFITP STMASVSTVQ LWISGILAIL RVLISQSTED IVLCRIQELS
     FSPHLLSCPV INRLRGGGGN VTLGECSEGK QKSLPEDTFS RFLLQLVGIL LEDIVTKQLK
     VDMSEQQHTF YCQELGTLLM CLIHIFKSGM FRRITAAATR LFTSDGCEGS FYTLESLNAR
     VRSMVPTHPA LVLLWCQILL LINHTDHRWW AEVQQTPKRH SLSCTKSLNP QKSGEEEDSG
     SAAQLGMCNR EIVRRGALIL FCDYVCQNLH DSEHLTWLIV NHIQDLISLS HEPPVQDFIS
     AIHRNSAASG LFIQAIQSRC ENLSTPTTLK KTLQCLEGIH LSQSGAVLTL YVDRLLGTPF
     RALARMVDTL ACRRVEMLLA ANLQSSMAQL PEEELNRIQE HLQNSGLAQR HQRLYSLLDR
     FRLSTVQDSL SPLPPVTSHP LDGDGHTSLE TVSPDKDWYL QLVRSQCWTR SDSALLEGAE
     LVNRIPAEDM NDFMMSSEFN LSLLAPCLSL GMSEIANGQK SPLFEAARGV ILNRVTSVVQ
     QLPAVHQVFQ PFLPIEPTAY WNKLNDLLGD TTSYQSLTIL ARALAQYLVV LSKVPAHLHL
     PPEKEGDTVK FVVMTVEALS WHLIHEQIPL SLDLQAGLDC CCLALQVPGL WGVLSSPEYV
     THACSLIHCV RFILEAIAVQ PGDQLLGPES RSHTPRAVRK EEVDSDIQNL SHVTSACEMV
     ADMVESLQSV LALGHKRNST LPSFLTAVLK NIVISLARLP LVNSYTRVPP LVWKLGWSPK
     PGGDFGTVFP EIPVEFLQEK EILKEFIYRI NTLGWTNRTQ FEETWATLLG VLVTQPLVME
     QEESPPEEDT ERTQIHVLAV QAITSLVLSA MTVPVAGNPA VSCLEQQPRN KPLKALDTRF
     GRKLSMIRGI VEQEIQEMVS QRENTATHHS HQAWDPVPSL LPATTGALIS HDKLLLQINP
     EREPGNMSYK LGQVSIHSVW LGNNITPLRE EEWDEEEEEE SDVPAPTSPP VSPVNSRKHR
     AGVDIHSCSQ FLLELYSRWI LPSSAARRTP VILISEVVRS LLVVSDLFTE RTQFEMMYLT
     LTELRRVHPS EDEILIQYLV PATCKAAAVL GMDKTVAEPV SRLLESTLRS SHLPSQIGAL
     HGILYVLECD LLDDTAKQLI PVVSDYLLSN LKGIAHCVNI HSQQHVLVMC ATAFYLMENY
     PLDVGPEFSA SVIQMCGVML SGSEESTPSI IYHCALRGLE RLLLSEQLSR LDTESLVKLS
     VDRVNVQSPH RAMAALGLML TCMYTGKEKA SPGRASDPSP ATPDSESVIV AMERVSVLFD
     RIRKGFPCEA RVVARILPQF LDDFFPPQDV MNKVIGEFLS NQQPYPQFMA TVVYKVFQTL
     HSAGQSSMVR DWVMLSLSNF TQRTPVAMAM WSLSCFLVSA STSPWVSAIL PHVISRMGKL
     EQVDVNLFCL VATDFYRHQI EEEFDRRAFQ SVFEVVAAPG SPYHRLLACL QNVHKVTTC
//