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Huntingtin (Huntington disease protein) (HD protein)

 HD_HUMAN                Reviewed;        3142 AA.
P42858; Q9UQB7;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
22-NOV-2017, entry version 185.
RecName: Full=Huntingtin;
AltName: Full=Huntington disease protein;
Short=HD protein;
Name=HTT; Synonyms=HD, IT15;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Retina;
PubMed=8458085;
Macdonald M., Ambrose C.M., Duyao M.P., Myers R.H., Lin C.S.,
Srinidhi J., Barnes G., Taylor S.A., James M., Groot N., McFarlane H.,
Jenkins B., Anderson M.A., Wexler N.S., Gusella J.F., Bates G.P.,
Baxendale S., Hummerich H., Kirby S., North M., Youngman S., Mott R.,
Zehetner G., Sedlacek Z., Poustka A., Frischauf A.-M., Lehrach H.,
Buckler A.J., Church D., Doucette-Stamm L., O'Donovan M.C.,
Riba-Ramirez L., Shah M., Stanton V.P., Strobel S.A., Draths K.M.,
Wales J.L., Dervan P., Housman D.E., Altherr M., Shiang R.,
Thompson L., Fielder T., Wasmuth J.J., Tagle D., Valdes J., Elmer L.,
Allard M., Castilla L., Swaroop M., Blanchard K., Collins F.S.,
Snell R., Holloway T., Gillespie K., Datson N., Shaw S., Harper P.S.;
"A novel gene containing a trinucleotide repeat that is expanded and
unstable on Huntington's disease chromosomes.";
Cell 72:971-983(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=11013077; DOI=10.1006/geno.2000.6317;
Matsuyama N., Hadano S., Onoe K., Osuga H., Shouguchi-Miyata J.,
Gondo Y., Ikeda J.-E.;
"Identification and characterization of the miniature pig Huntington's
disease gene homolog: evidence for conservation and polymorphism in
the CAG triplet repeat.";
Genomics 69:72-85(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-203.
PubMed=8197474; DOI=10.1007/BF02257483;
Ambrose C.M., Duyao M.P., Barnes G., Bates G.P., Lin C.S.,
Srinidhi J., Baxendale S., Hummerich H., Lehrach H., Altherr M.,
Wasmuth J., Buckler A., Church D., Housman D., Berks M., Micklem G.,
Durbin R., Dodge A., Read A., Gusella J.F., Macdonald M.E.;
"Structure and expression of the Huntington's disease gene: evidence
against simple inactivation due to an expanded CAG repeat.";
Somat. Cell Mol. Genet. 20:27-38(1994).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-88.
PubMed=7759106; DOI=10.1016/0888-7543(95)80014-D;
Lin B., Nasir J., Kalchman M.A., McDonald H., Zeisler J.,
Goldberg Y.P., Hayden M.R.;
"Structural analysis of the 5' region of mouse and human Huntington
disease genes reveals conservation of putative promoter region and
di- and trinucleotide polymorphisms.";
Genomics 25:707-715(1995).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 2561-3142, AND VARIANT ILE-2786.
TISSUE=Brain, Caudate nucleus, Frontal cortex, Muscle, and Retina;
PubMed=7903579; DOI=10.1093/hmg/2.10.1541;
Lin B., Rommens J.M., Graham R.K., Kalchman M., Macdonald H.,
Nasir J., Delaney A., Goldberg Y.P., Hayden M.R.;
"Differential 3' polyadenylation of the Huntington disease gene
results in two mRNA species with variable tissue expression.";
Hum. Mol. Genet. 2:1541-1545(1993).
[7]
SUBCELLULAR LOCATION.
PubMed=7647777; DOI=10.1038/ng0595-104;
Trottier Y., Devys D., Imbert G., Saudou F., An I., Lutz Y., Weber C.,
Agid Y., Hirsch E.C., Mandel J.-L.;
"Cellular localization of the Huntington's disease protein and
discrimination of the normal and mutated form.";
Nat. Genet. 10:104-110(1995).
[8]
CLEAVAGE BY APOPAIN.
PubMed=8696339; DOI=10.1038/ng0896-442;
Goldberg Y.P., Nicholson D.W., Rasper D.M., Kalchman M.A., Koide H.B.,
Graham R.K., Bromm M., Kazemi-Esfarjani P., Thornberry N.A.,
Vaillancourt J.P., Hayden M.R.;
"Cleavage of huntingtin by apopain, a proapoptotic cysteine protease,
is modulated by the polyglutamine tract.";
Nat. Genet. 13:442-449(1996).
[9]
INTERACTION WITH PRPF40A AND SETD2.
PubMed=9700202; DOI=10.1093/hmg/7.9.1463;
Faber P.W., Barnes G.T., Srinidhi J., Chen J., Gusella J.F.,
MacDonald M.E.;
"Huntingtin interacts with a family of WW domain proteins.";
Hum. Mol. Genet. 7:1463-1474(1998).
[10]
INTERACTION WITH PQBP1.
TISSUE=Brain;
PubMed=10332029; DOI=10.1093/hmg/8.6.977;
Waragai M., Lammers C.-H., Takeuchi S., Imafuku I., Udagawa Y.,
Kanazawa I., Kawabata M., Mouradian M.M., Okazawa H.;
"PQBP-1, a novel polyglutamine tract binding protein, inhibits
transcription activation by Brn-2 and affects cell survival.";
Hum. Mol. Genet. 8:977-987(1999).
[11]
INTERACTION WITH SETD2.
PubMed=10958656; DOI=10.1093/hmg/9.14.2175;
Passani L.A., Bedford M.T., Faber P.W., McGinnis K.M., Sharp A.H.,
Gusella J.F., Vonsattel J.-P., MacDonald M.E.;
"Huntingtin's WW domain partners in Huntington's disease post-mortem
brain fulfill genetic criteria for direct involvement in Huntington's
disease pathogenesis.";
Hum. Mol. Genet. 9:2175-2182(2000).
[12]
INTERACTION WITH SETD2.
PubMed=11461154; DOI=10.1006/mcne.2001.1004;
Rega S., Stiewe T., Chang D.-I., Pollmeier B., Esche H.,
Bardenheuer W., Marquitan G., Puetzer B.M.;
"Identification of the full-length huntingtin-interacting protein
p231HBP/HYPB as a DNA-binding factor.";
Mol. Cell. Neurosci. 18:68-79(2001).
[13]
NUCLEAR EXPORT SIGNAL.
PubMed=12783847; DOI=10.1093/hmg/ddg156;
Xia J., Lee D.H., Taylor J., Vandelft M., Truant R.;
"Huntingtin contains a highly conserved nuclear export signal.";
Hum. Mol. Genet. 12:1393-1403(2003).
[14]
INTERACTION WITH TPR, AND SUBCELLULAR LOCATION.
PubMed=15654337; DOI=10.1038/ng1503;
Cornett J., Cao F., Wang C.E., Ross C.A., Bates G.P., Li S.H.,
Li X.J.;
"Polyglutamine expansion of huntingtin impairs its nuclear export.";
Nat. Genet. 37:198-204(2005).
[15]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=16391387; DOI=10.1385/NMM:7:4:297;
Sayer J.A., Manczak M., Akileswaran L., Reddy P.H., Coghlan V.M.;
"Interaction of the nuclear matrix protein NAKAP with HypA and
huntingtin: implications for nuclear toxicity in Huntington's disease
pathogenesis.";
NeuroMolecular Med. 7:297-310(2005).
[16]
INTERACTION WITH SYVN, AND UBIQUITINATION.
PubMed=17141218; DOI=10.1016/j.yexcr.2006.10.031;
Yang H., Zhong X., Ballar P., Luo S., Shen Y., Rubinsztein D.C.,
Monteiro M.J., Fang S.;
"Ubiquitin ligase Hrd1 enhances the degradation and suppresses the
toxicity of polyglutamine-expanded huntingtin.";
Exp. Cell Res. 313:538-550(2007).
[17]
PHOSPHORYLATION AT SER-1179 AND SER-1199.
PubMed=17611284; DOI=10.1523/JNEUROSCI.1831-07.2007;
Anne S.L., Saudou F., Humbert S.;
"Phosphorylation of huntingtin by cyclin-dependent kinase 5 is induced
by DNA damage and regulates wild-type and mutant huntingtin toxicity
in neurons.";
J. Neurosci. 27:7318-7328(2007).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1870, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[20]
INTERACTION WITH PFN1.
PubMed=18573880; DOI=10.1128/MCB.00079-08;
Shao J., Welch W.J., Diprospero N.A., Diamond M.I.;
"Phosphorylation of profilin by ROCK1 regulates polyglutamine
aggregation.";
Mol. Cell. Biol. 28:5196-5208(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411; SER-1870 AND
SER-1874, 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).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432 AND SER-1874, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1870 AND SER-1874, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[25]
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).
[26]
ACETYLATION AT LYS-9; LYS-176; LYS-234; LYS-343 AND LYS-442.
PubMed=21685499; DOI=10.1074/mcp.M111.009829;
Cong X., Held J.M., Degiacomo F., Bonner A., Chen J.M., Schilling B.,
Czerwieniec G.A., Gibson B.W., Ellerby L.M.;
"Mass spectrometric identification of novel lysine acetylation sites
in huntingtin.";
Mol. Cell. Proteomics 0:0-0(2011).
[27]
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).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640; SER-643; SER-1199
AND SER-1874, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
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).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432, 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).
[30]
INTERACTION WITH ZDHHC17 AND ZDHHC13, AND MUTAGENESIS OF ILE-495;
GLN-498 AND PRO-499.
PubMed=26198635; DOI=10.1074/jbc.M115.657668;
Lemonidis K., Sanchez-Perez M.C., Chamberlain L.H.;
"Identification of a novel sequence motif recognized by the ankyrin
repeat domain of zDHHC17/13 S-acyltransferases.";
J. Biol. Chem. 290:21939-21950(2015).
[31]
INTERACTION WITH ZDHHC17.
PubMed=28882895; DOI=10.1074/jbc.M117.799650;
Lemonidis K., MacLeod R., Baillie G.S., Chamberlain L.H.;
"Peptide array based screening reveals a large number of proteins
interacting with the ankyrin repeat domain of the zDHHC17 S-
acyltransferase.";
J. Biol. Chem. 0:0-0(2017).
[32]
INTERACTION WITH ZDHHC17, AND MUTAGENESIS OF 498-GLN-PRO-499.
PubMed=28757145; DOI=10.1016/j.str.2017.06.018;
Verardi R., Kim J.S., Ghirlando R., Banerjee A.;
"Structural basis for substrate recognition by the ankyrin repeat
domain of human DHHC17 palmitoyltransferase.";
Structure 0:0-0(2017).
[33]
INVOLVEMENT IN LOMARS, AND VARIANT LOMARS LEU-2717.
PubMed=27329733; DOI=10.1038/ejhg.2016.74;
Rodan L.H., Cohen J., Fatemi A., Gillis T., Lucente D., Gusella J.,
Picker J.D.;
"A novel neurodevelopmental disorder associated with compound
heterozygous variants in the huntingtin gene.";
Eur. J. Hum. Genet. 24:1826-1827(2016).
[34]
VARIANT LOMARS LEU-703, AND VARIANT MET-1260.
PubMed=26740508; DOI=10.1136/jmedgenet-2015-103568;
Lopes F., Barbosa M., Ameur A., Soares G., de Sa J., Dias A.I.,
Oliveira G., Cabral P., Temudo T., Calado E., Cruz I.F., Vieira J.P.,
Oliveira R., Esteves S., Sauer S., Jonasson I., Syvaenen A.C.,
Gyllensten U., Pinto D., Maciel P.;
"Identification of novel genetic causes of Rett syndrome-like
phenotypes.";
J. Med. Genet. 53:190-199(2016).
[35]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 1-64, AND DOMAIN.
PubMed=19748341; DOI=10.1016/j.str.2009.08.002;
Kim M.W., Chelliah Y., Kim S.W., Otwinowski Z., Bezprozvanny I.;
"Secondary structure of Huntingtin amino-terminal region.";
Structure 17:1205-1212(2009).
-!- FUNCTION: May play a role in microtubule-mediated transport or
vesicle function.
-!- SUBUNIT: Interacts with PFN1 (PubMed:18573880). Interacts through
its N-terminus with PRPF40A (PubMed:9700202). Interacts with PQBP1
(PubMed:10332029). Interacts with SETD2 (PubMed:9700202,
PubMed:10958656, PubMed:11461154). Interacts with SH3GLB1 (By
similarity). Interacts with SYVN (PubMed:17141218). Interacts with
TPR; the interaction is inhibited by forms of Huntingtin with
expanded polyglutamine stretch (PubMed:15654337). Interacts with
ZDHHC13 (via ANK repeats) (PubMed:26198635). Interacts with
ZDHHC17 (via ANK repeats) (PubMed:26198635, PubMed:28882895,
PubMed:28757145). {ECO:0000250|UniProtKB:P42859,
ECO:0000269|PubMed:10332029, ECO:0000269|PubMed:10958656,
ECO:0000269|PubMed:11461154, ECO:0000269|PubMed:15654337,
ECO:0000269|PubMed:17141218, ECO:0000269|PubMed:18573880,
ECO:0000269|PubMed:26198635, ECO:0000269|PubMed:28757145,
ECO:0000269|PubMed:28882895, ECO:0000269|PubMed:9700202}.
-!- INTERACTION:
Self; NbExp=9; IntAct=EBI-466029, EBI-466029;
Q8N264:ARHGAP24; NbExp=3; IntAct=EBI-466029, EBI-988764;
Q9NRL2:BAZ1A; NbExp=4; IntAct=EBI-466029, EBI-927511;
Q14457:BECN1; NbExp=2; IntAct=EBI-466029, EBI-949378;
Q9P2H0:CEP126; NbExp=2; IntAct=EBI-466029, EBI-473176;
Q12873:CHD3; NbExp=3; IntAct=EBI-466029, EBI-523590;
P53618:COPB1; NbExp=3; IntAct=EBI-466029, EBI-359063;
Q92793:CREBBP; NbExp=2; IntAct=EBI-466029, EBI-81215;
Q14194:CRMP1; NbExp=2; IntAct=EBI-466029, EBI-473101;
P35222:CTNNB1; NbExp=5; IntAct=EBI-466029, EBI-491549;
Q13561:DCTN2; NbExp=6; IntAct=EBI-466029, EBI-715074;
Q9NVH1:DNAJC11; NbExp=3; IntAct=EBI-466029, EBI-1055336;
Q5F1R6:DNAJC21; NbExp=6; IntAct=EBI-466029, EBI-2654581;
Q9NNZ3:DNAJC4; NbExp=3; IntAct=EBI-466029, EBI-4397791;
O14645:DNALI1; NbExp=3; IntAct=EBI-466029, EBI-395638;
Q05193:DNM1; NbExp=3; IntAct=EBI-466029, EBI-713135;
Q14204:DYNC1H1; NbExp=5; IntAct=EBI-466029, EBI-356015;
O88485:Dync1i1 (xeno); NbExp=2; IntAct=EBI-466029, EBI-492834;
Q13011:ECH1; NbExp=2; IntAct=EBI-466029, EBI-711968;
Q2NKX8:ERCC6L; NbExp=2; IntAct=EBI-466029, EBI-1042535;
Q9UI08-2:EVL; NbExp=2; IntAct=EBI-466029, EBI-6448852;
Q99689:FEZ1; NbExp=5; IntAct=EBI-466029, EBI-396435;
Q8N3X1:FNBP4; NbExp=6; IntAct=EBI-466029, EBI-310600;
P02792:FTL; NbExp=2; IntAct=EBI-466029, EBI-713279;
Q9Y2X7:GIT1; NbExp=10; IntAct=EBI-466029, EBI-466061;
Q9H4A5:GOLPH3L; NbExp=2; IntAct=EBI-466029, EBI-4403434;
Q9Y5Q9:GTF3C3; NbExp=3; IntAct=EBI-466029, EBI-1054873;
P54257-2:HAP1; NbExp=8; IntAct=EBI-466029, EBI-9392340;
P54256:Hap1 (xeno); NbExp=3; IntAct=EBI-466029, EBI-994539;
Q9UBP5:HEY2; NbExp=2; IntAct=EBI-466029, EBI-750630;
O00291:HIP1; NbExp=4; IntAct=EBI-466029, EBI-473886;
P68431:HIST1H3D; NbExp=2; IntAct=EBI-466029, EBI-79722;
Q9NP66:HMG20A; NbExp=2; IntAct=EBI-466029, EBI-740641;
P09429:HMGB1; NbExp=13; IntAct=EBI-466029, EBI-389432;
O95163:IKBKAP; NbExp=4; IntAct=EBI-466029, EBI-347559;
P29994:Itpr1 (xeno); NbExp=2; IntAct=EBI-466029, EBI-8614640;
Q96N16:JAKMIP1; NbExp=4; IntAct=EBI-466029, EBI-2680803;
O95751:LDOC1; NbExp=5; IntAct=EBI-466029, EBI-740738;
Q8N7X4:MAGEB6; NbExp=2; IntAct=EBI-466029, EBI-6447163;
Q9UIS9:MBD1; NbExp=2; IntAct=EBI-466029, EBI-867196;
Q96RN5:MED15; NbExp=3; IntAct=EBI-466029, EBI-394506;
Q9Y3C7:MED31; NbExp=3; IntAct=EBI-466029, EBI-394707;
Q9H000:MKRN2; NbExp=3; IntAct=EBI-466029, EBI-2341005;
P49959:MRE11; NbExp=5; IntAct=EBI-466029, EBI-396513;
Q96HT8:MRFAP1L1; NbExp=3; IntAct=EBI-466029, EBI-748896;
O43312:MTSS1; NbExp=3; IntAct=EBI-466029, EBI-473954;
Q14596:NBR1; NbExp=3; IntAct=EBI-466029, EBI-742698;
O75376:NCOR1; NbExp=3; IntAct=EBI-466029, EBI-347233;
O00746:NME4; NbExp=2; IntAct=EBI-466029, EBI-744871;
Q9BVL2:NUP58; NbExp=4; IntAct=EBI-466029, EBI-2811583;
Q96CV9:OPTN; NbExp=7; IntAct=EBI-466029, EBI-748974;
Q92882:OSTF1; NbExp=5; IntAct=EBI-466029, EBI-1051152;
P13674:P4HA1; NbExp=5; IntAct=EBI-466029, EBI-1237386;
Q9BY11:PACSIN1; NbExp=3; IntAct=EBI-466029, EBI-721769;
Q13177:PAK2; NbExp=2; IntAct=EBI-466029, EBI-1045887;
P35080:PFN2; NbExp=4; IntAct=EBI-466029, EBI-473138;
Q8N2W9:PIAS4; NbExp=3; IntAct=EBI-466029, EBI-473160;
Q8WXW3:PIBF1; NbExp=3; IntAct=EBI-466029, EBI-2558770;
P27986:PIK3R1; NbExp=7; IntAct=EBI-466029, EBI-79464;
O00459:PIK3R2; NbExp=6; IntAct=EBI-466029, EBI-346930;
Q92569:PIK3R3; NbExp=6; IntAct=EBI-466029, EBI-79893;
P14618:PKM; NbExp=3; IntAct=EBI-466029, EBI-353408;
P37231:PPARG; NbExp=4; IntAct=EBI-466029, EBI-781384;
O75400:PRPF40A; NbExp=15; IntAct=EBI-466029, EBI-473291;
Q5VTR2:RNF20; NbExp=3; IntAct=EBI-466029, EBI-2372238;
O75150:RNF40; NbExp=3; IntAct=EBI-466029, EBI-744408;
P36578:RPL4; NbExp=2; IntAct=EBI-466029, EBI-348313;
Q9BYW2:SETD2; NbExp=4; IntAct=EBI-466029, EBI-945869;
Q99963:SH3GL3; NbExp=9; IntAct=EBI-466029, EBI-473910;
P37840:SNCA; NbExp=4; IntAct=EBI-466029, EBI-985879;
Q9BX66:SORBS1; NbExp=4; IntAct=EBI-466029, EBI-433642;
Q13501:SQSTM1; NbExp=8; IntAct=EBI-466029, EBI-307104;
Q7Z6B7:SRGAP1; NbExp=4; IntAct=EBI-466029, EBI-2481729;
O75044:SRGAP2; NbExp=3; IntAct=EBI-466029, EBI-1051034;
O43295:SRGAP3; NbExp=4; IntAct=EBI-466029, EBI-368166;
Q9BXP5:SRRT; NbExp=3; IntAct=EBI-466029, EBI-712721;
O75410:TACC1; NbExp=4; IntAct=EBI-466029, EBI-624237;
Q92844:TANK; NbExp=3; IntAct=EBI-466029, EBI-356349;
O14776:TCERG1; NbExp=9; IntAct=EBI-466029, EBI-473271;
P04637:TP53; NbExp=4; IntAct=EBI-466029, EBI-366083;
O14545:TRAFD1; NbExp=5; IntAct=EBI-466029, EBI-1396921;
Q9BSL1:UBAC1; NbExp=5; IntAct=EBI-466029, EBI-749370;
P61086:UBE2K; NbExp=3; IntAct=EBI-466029, EBI-473850;
O75385:ULK1; NbExp=8; IntAct=EBI-466029, EBI-908831;
Q93008:USP9X; NbExp=8; IntAct=EBI-466029, EBI-302524;
Q9BTA9:WAC; NbExp=5; IntAct=EBI-466029, EBI-749118;
O75554:WBP4; NbExp=3; IntAct=EBI-466029, EBI-7251981;
Q8IZQ1:WDFY3; NbExp=10; IntAct=EBI-466029, EBI-1569256;
Q8WTP9:XAGE3; NbExp=3; IntAct=EBI-466029, EBI-6448284;
P12956:XRCC6; NbExp=3; IntAct=EBI-466029, EBI-353208;
Q8IUH5:ZDHHC17; NbExp=12; IntAct=EBI-466029, EBI-524753;
G3V1X1:ZFC3H1; NbExp=2; IntAct=EBI-466029, EBI-6448783;
Q96K21:ZFYVE19; NbExp=3; IntAct=EBI-466029, EBI-6448240;
Q96NC0:ZMAT2; NbExp=2; IntAct=EBI-466029, EBI-2682299;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15654337,
ECO:0000269|PubMed:7647777}. Nucleus {ECO:0000269|PubMed:15654337,
ECO:0000269|PubMed:16391387}. Note=The mutant Huntingtin protein
colocalizes with AKAP8L in the nuclear matrix of Huntington
disease neurons. Shuttles between cytoplasm and nucleus in a Ran
GTPase-independent manner. {ECO:0000269|PubMed:15654337}.
-!- TISSUE SPECIFICITY: Expressed in the brain cortex (at protein
level). Widely expressed with the highest level of expression in
the brain (nerve fibers, varicosities, and nerve endings). In the
brain, the regions where it can be mainly found are the cerebellar
cortex, the neocortex, the striatum, and the hippocampal
formation. {ECO:0000269|PubMed:16391387}.
-!- DOMAIN: The N-terminal Gln-rich and Pro-rich domain has great
conformational flexibility and is likely to exist in a fluctuating
equilibrium of alpha-helical, random coil, and extended
conformations. {ECO:0000269|PubMed:19748341}.
-!- PTM: Cleaved by apopain downstream of the polyglutamine stretch.
The resulting N-terminal fragment is cytotoxic and provokes
apoptosis.
-!- PTM: Forms with expanded polyglutamine expansion are specifically
ubiquitinated by SYVN1, which promotes their proteasomal
degradation. {ECO:0000269|PubMed:17141218}.
-!- PTM: Phosphorylation at Ser-1179 and Ser-1199 by CDK5 in response
to DNA damage in nuclei of neurons protects neurons against
polyglutamine expansion as well as DNA damage mediated toxicity.
{ECO:0000269|PubMed:17611284}.
-!- POLYMORPHISM: The poly-Gln region of HTT is highly polymorphic (10
to 35 repeats) in the normal population and is expanded to about
36-120 repeats in Huntington disease patients. The repeat length
usually increases in successive generations, but contracts also on
occasion. The adjacent poly-Pro region is also polymorphic and
varies between 7-12 residues. Polyglutamine expansion leads to
elevated susceptibility to apopain cleavage and likely result in
accelerated neuronal apoptosis (PubMed:8696339).
{ECO:0000269|PubMed:8696339}.
-!- DISEASE: Huntington disease (HD) [MIM:143100]: A neurodegenerative
disorder characterized by involuntary movements (chorea), general
motor impairment, psychiatric disorders and dementia. Onset of the
disease occurs usually in the third or fourth decade of life.
Onset and clinical course depend on the degree of poly-Gln repeat
expansion, longer expansions resulting in earlier onset and more
severe clinical manifestations. Neuropathology of Huntington
disease displays a distinctive pattern with loss of neurons,
especially in the caudate and putamen. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- DISEASE: Lopes-Maciel-Rodan syndrome (LOMARS) [MIM:617435]: An
autosomal recessive neurodevelopmental disorder characterized by
developmental regression in infancy, delayed psychomotor
development, severe intellectual disability, and cerebral and
cerebellar atrophy. Additional features include swallowing
problems, dystonia, bradykinesia, and continuous manual
stereotypies without chorea. Some patients manifest seizures.
{ECO:0000269|PubMed:26740508, ECO:0000269|PubMed:27329733}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the huntingtin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Huntingtin entry;
URL="https://en.wikipedia.org/wiki/Huntingtin";
-----------------------------------------------------------------------
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EMBL; L12392; AAB38240.1; -; mRNA.
EMBL; AB016794; BAA36753.1; -; mRNA.
EMBL; Z49154; CAA89024.1; -; Genomic_DNA.
EMBL; Z49155; CAA89025.1; -; Genomic_DNA.
EMBL; Z49208; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z49769; CAA89839.1; -; Genomic_DNA.
EMBL; Z68756; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z69649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L27350; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L27351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L27352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L27353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L27354; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L34020; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L20431; AAA52702.1; -; mRNA.
PIR; A46068; A46068.
RefSeq; NP_002102.4; NM_002111.8.
UniGene; Hs.518450; -.
PDB; 2D3X; Model; -; A=199-325.
PDB; 2LD0; NMR; -; A=1-17.
PDB; 2LD2; NMR; -; A=1-17.
PDB; 3IO4; X-ray; 3.63 A; A/B/C=1-64.
PDB; 3IO6; X-ray; 3.70 A; A/B/C=1-64.
PDB; 3IOR; X-ray; 3.60 A; A/B/C=1-64.
PDB; 3IOT; X-ray; 3.50 A; A/B/C=1-64.
PDB; 3IOU; X-ray; 3.70 A; A/B/C=1-64.
PDB; 3IOV; X-ray; 3.70 A; A/B/C=1-64.
PDB; 3IOW; X-ray; 3.50 A; A/B/C=1-64.
PDB; 3LRH; X-ray; 2.60 A; B/D/F/H/J/L/N/P=5-18.
PDB; 4FE8; X-ray; 3.00 A; A/B/C=1-64.
PDB; 4FEB; X-ray; 2.80 A; A/B/C=1-64.
PDB; 4FEC; X-ray; 3.00 A; A/B/C=1-64.
PDB; 4FED; X-ray; 2.81 A; A/B/C=1-64.
PDB; 4RAV; X-ray; 2.50 A; E/F=1-17.
PDBsum; 2D3X; -.
PDBsum; 2LD0; -.
PDBsum; 2LD2; -.
PDBsum; 3IO4; -.
PDBsum; 3IO6; -.
PDBsum; 3IOR; -.
PDBsum; 3IOT; -.
PDBsum; 3IOU; -.
PDBsum; 3IOV; -.
PDBsum; 3IOW; -.
PDBsum; 3LRH; -.
PDBsum; 4FE8; -.
PDBsum; 4FEB; -.
PDBsum; 4FEC; -.
PDBsum; 4FED; -.
PDBsum; 4RAV; -.
ProteinModelPortal; P42858; -.
SMR; P42858; -.
BioGrid; 109314; 226.
CORUM; P42858; -.
DIP; DIP-32492N; -.
ELM; P42858; -.
IntAct; P42858; 362.
MINT; MINT-133355; -.
STRING; 9606.ENSP00000347184; -.
BindingDB; P42858; -.
ChEMBL; CHEMBL5514; -.
iPTMnet; P42858; -.
PhosphoSitePlus; P42858; -.
SwissPalm; P42858; -.
BioMuta; HTT; -.
DMDM; 296434520; -.
EPD; P42858; -.
MaxQB; P42858; -.
PaxDb; P42858; -.
PeptideAtlas; P42858; -.
PRIDE; P42858; -.
Ensembl; ENST00000355072; ENSP00000347184; ENSG00000197386.
GeneID; 3064; -.
KEGG; hsa:3064; -.
UCSC; uc062uto.1; human.
CTD; 3064; -.
DisGeNET; 3064; -.
EuPathDB; HostDB:ENSG00000197386.10; -.
GeneCards; HTT; -.
GeneReviews; HTT; -.
HGNC; HGNC:4851; HTT.
HPA; CAB002756; -.
HPA; HPA026114; -.
MalaCards; HTT; -.
MIM; 143100; phenotype.
MIM; 613004; gene.
MIM; 617435; phenotype.
neXtProt; NX_P42858; -.
OpenTargets; ENSG00000197386; -.
Orphanet; 399; Huntington disease.
Orphanet; 248111; Juvenile Huntington disease.
PharmGKB; PA164741646; -.
eggNOG; ENOG410IDZV; Eukaryota.
eggNOG; ENOG410XSEC; LUCA.
GeneTree; ENSGT00390000015863; -.
HOGENOM; HOG000082472; -.
HOVERGEN; HBG005953; -.
InParanoid; P42858; -.
KO; K04533; -.
OMA; PIRRKGK; -.
OrthoDB; EOG091G004G; -.
PhylomeDB; P42858; -.
TreeFam; TF323608; -.
SignaLink; P42858; -.
SIGNOR; P42858; -.
ChiTaRS; HTT; human.
EvolutionaryTrace; P42858; -.
GeneWiki; Huntingtin; -.
GenomeRNAi; 3064; -.
PRO; PR:P42858; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000197386; -.
CleanEx; HS_HTT; -.
ExpressionAtlas; P42858; baseline and differential.
Genevisible; P42858; HS.
GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:0005814; C:centriole; IDA:SYSCILIA_CCNET.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0016234; C:inclusion body; IMP:CAFA.
GO; GO:0005770; C:late endosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IMP:CAFA.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0048487; F:beta-tubulin binding; IDA:UniProtKB.
GO; GO:0034452; F:dynactin binding; IPI:UniProtKB.
GO; GO:0045505; F:dynein intermediate chain binding; IDA:UniProtKB.
GO; GO:0031072; F:heat shock protein binding; IPI:CAFA.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0044325; F:ion channel binding; IDA:UniProtKB.
GO; GO:0019900; F:kinase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0005319; F:lipid transporter activity; IEA:InterPro.
GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
GO; GO:0005522; F:profilin binding; IPI:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IBA:GO_Central.
GO; GO:0048513; P:animal organ development; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB.
GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:1905337; P:positive regulation of aggrephagy; IMP:ParkinsonsUK-UCL.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:CAFA.
GO; GO:1903599; P:positive regulation of autophagy of mitochondrion; IMP:ParkinsonsUK-UCL.
GO; GO:0045724; P:positive regulation of cilium assembly; IMP:SYSCILIA_CCNET.
GO; GO:0031587; P:positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; IDA:UniProtKB.
GO; GO:1904504; P:positive regulation of lipophagy; IMP:ParkinsonsUK-UCL.
GO; GO:0031648; P:protein destabilization; IMP:CAFA.
GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IMP:dictyBase.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IMP:UniProtKB.
GO; GO:0047496; P:vesicle transport along microtubule; IMP:UniProtKB.
GO; GO:0042297; P:vocal learning; IMP:AgBase.
Gene3D; 1.25.10.10; -; 2.
Gene3D; 1.25.10.20; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR000091; Huntingtin.
InterPro; IPR028426; Huntingtin_fam.
InterPro; IPR024613; Huntingtin_middle-repeat.
InterPro; IPR011030; Lipovitellin_superhlx_dom.
PANTHER; PTHR10170; PTHR10170; 1.
Pfam; PF12372; DUF3652; 1.
PRINTS; PR00375; HUNTINGTIN.
SUPFAM; SSF48371; SSF48371; 6.
1: Evidence at protein level;
3D-structure; Acetylation; Apoptosis; Complete proteome; Cytoplasm;
Disease mutation; Mental retardation; Neurodegeneration; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Triplet repeat expansion; Ubl conjugation.
CHAIN 1 3142 Huntingtin.
/FTId=PRO_0000083942.
REPEAT 204 241 HEAT 1.
REPEAT 246 283 HEAT 2.
REPEAT 316 360 HEAT 3.
REPEAT 802 839 HEAT 4.
REPEAT 902 940 HEAT 5.
REGION 3 13 Sufficient for interaction with TPR.
{ECO:0000269|PubMed:15654337}.
REGION 491 502 Interaction with ZDHHC17.
{ECO:0000269|PubMed:28757145}.
MOTIF 2395 2404 Nuclear export signal. {ECO:0000250}.
COMPBIAS 18 38 Poly-Gln.
COMPBIAS 39 49 Poly-Pro.
COMPBIAS 63 78 Poly-Pro.
COMPBIAS 1437 1440 Poly-Thr.
COMPBIAS 2341 2345 Poly-Glu.
COMPBIAS 2638 2643 Poly-Glu.
SITE 511 512 Cleavage; by apopain. {ECO:0000255}.
SITE 528 529 Cleavage; by apopain. {ECO:0000255}.
SITE 550 551 Cleavage; by apopain. {ECO:0000255}.
SITE 587 588 Cleavage; by apopain. {ECO:0000255}.
MOD_RES 9 9 N6-acetyllysine.
{ECO:0000269|PubMed:21685499}.
MOD_RES 176 176 N6-acetyllysine.
{ECO:0000269|PubMed:21685499}.
MOD_RES 234 234 N6-acetyllysine.
{ECO:0000269|PubMed:21685499}.
MOD_RES 343 343 N6-acetyllysine.
{ECO:0000269|PubMed:21685499}.
MOD_RES 411 411 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 417 417 Phosphoserine.
{ECO:0000250|UniProtKB:P42859}.
MOD_RES 419 419 Phosphoserine.
{ECO:0000250|UniProtKB:P42859}.
MOD_RES 432 432 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
MOD_RES 442 442 N6-acetyllysine.
{ECO:0000269|PubMed:21685499}.
MOD_RES 640 640 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 643 643 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1179 1179 Phosphoserine; by CDK5.
{ECO:0000269|PubMed:17611284}.
MOD_RES 1199 1199 Phosphoserine; by CDK5.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:17611284}.
MOD_RES 1870 1870 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231}.
MOD_RES 1874 1874 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
VARIANT 18 18 Q -> QQQ.
/FTId=VAR_005268.
VARIANT 703 703 P -> L (in LOMARS).
{ECO:0000269|PubMed:26740508}.
/FTId=VAR_079026.
VARIANT 893 893 G -> R (in dbSNP:rs363075).
/FTId=VAR_060170.
VARIANT 1064 1064 V -> I (in dbSNP:rs35892913).
/FTId=VAR_060171.
VARIANT 1091 1091 I -> M (in dbSNP:rs1143646).
/FTId=VAR_060172.
VARIANT 1173 1173 T -> A (in dbSNP:rs3025843).
/FTId=VAR_060173.
VARIANT 1260 1260 T -> M (found in a patient with Rett
syndrome-like phenotype; unknown
pathological significance;
dbSNP:rs34315806).
{ECO:0000269|PubMed:26740508}.
/FTId=VAR_060174.
VARIANT 1382 1382 E -> A (in dbSNP:rs3025837).
/FTId=VAR_054017.
VARIANT 1385 1385 N -> H (in dbSNP:rs3025837).
/FTId=VAR_060175.
VARIANT 1720 1720 T -> N (in dbSNP:rs363125).
/FTId=VAR_060176.
VARIANT 2113 2113 D -> Y (in dbSNP:rs1143648).
/FTId=VAR_060177.
VARIANT 2309 2309 Y -> H (in dbSNP:rs362331).
/FTId=VAR_060178.
VARIANT 2717 2717 F -> L (in LOMARS).
{ECO:0000269|PubMed:27329733}.
/FTId=VAR_079027.
VARIANT 2786 2786 V -> I (in dbSNP:rs362272).
{ECO:0000269|PubMed:7903579}.
/FTId=VAR_060179.
MUTAGEN 495 495 I->A: Inhibits interaction with ZDHHC13
and ZDHHC17.
{ECO:0000269|PubMed:26198635}.
MUTAGEN 498 499 QP->AA: Abolishes interaction with
ZDHHC17. {ECO:0000269|PubMed:28757145}.
MUTAGEN 498 498 Q->A: Inhibits interaction with ZDHHC13
and ZDHHC17.
{ECO:0000269|PubMed:26198635}.
MUTAGEN 499 499 P->A: Inhibits interaction with ZDHHC13
and ZDHHC17.
{ECO:0000269|PubMed:26198635}.
CONFLICT 823 823 C -> S (in Ref. 2; BAA36753).
{ECO:0000305}.
HELIX 4 10 {ECO:0000244|PDB:4RAV}.
STRAND 13 15 {ECO:0000244|PDB:4RAV}.
HELIX 23 26 {ECO:0000244|PDB:3IOT}.
TURN 30 32 {ECO:0000244|PDB:3IOT}.
SEQUENCE 3142 AA; 347603 MW; A267509E84D52F0D CRC64;
MATLEKLMKA FESLKSFQQQ QQQQQQQQQQ QQQQQQQQPP PPPPPPPPPQ LPQPPPQAQP
LLPQPQPPPP PPPPPPGPAV AEEPLHRPKK ELSATKKDRV NHCLTICENI VAQSVRNSPE
FQKLLGIAME LFLLCSDDAE SDVRMVADEC LNKVIKALMD SNLPRLQLEL YKEIKKNGAP
RSLRAALWRF AELAHLVRPQ KCRPYLVNLL PCLTRTSKRP EESVQETLAA AVPKIMASFG
NFANDNEIKV LLKAFIANLK SSSPTIRRTA AGSAVSICQH SRRTQYFYSW LLNVLLGLLV
PVEDEHSTLL ILGVLLTLRY LVPLLQQQVK DTSLKGSFGV TRKEMEVSPS AEQLVQVYEL
TLHHTQHQDH NVVTGALELL QQLFRTPPPE LLQTLTAVGG IGQLTAAKEE SGGRSRSGSI
VELIAGGGSS CSPVLSRKQK GKVLLGEEEA LEDDSESRSD VSSSALTASV KDEISGELAA
SSGVSTPGSA GHDIITEQPR SQHTLQADSV DLASCDLTSS ATDGDEEDIL SHSSSQVSAV
PSDPAMDLND GTQASSPISD SSQTTTEGPD SAVTPSDSSE IVLDGTDNQY LGLQIGQPQD
EDEEATGILP DEASEAFRNS SMALQQAHLL KNMSHCRQPS DSSVDKFVLR DEATEPGDQE
NKPCRIKGDI GQSTDDDSAP LVHCVRLLSA SFLLTGGKNV LVPDRDVRVS VKALALSCVG
AAVALHPESF FSKLYKVPLD TTEYPEEQYV SDILNYIDHG DPQVRGATAI LCGTLICSIL
SRSRFHVGDW MGTIRTLTGN TFSLADCIPL LRKTLKDESS VTCKLACTAV RNCVMSLCSS
SYSELGLQLI IDVLTLRNSS YWLVRTELLE TLAEIDFRLV SFLEAKAENL HRGAHHYTGL
LKLQERVLNN VVIHLLGDED PRVRHVAAAS LIRLVPKLFY KCDQGQADPV VAVARDQSSV
YLKLLMHETQ PPSHFSVSTI TRIYRGYNLL PSITDVTMEN NLSRVIAAVS HELITSTTRA
LTFGCCEALC LLSTAFPVCI WSLGWHCGVP PLSASDESRK SCTVGMATMI LTLLSSAWFP
LDLSAHQDAL ILAGNLLAAS APKSLRSSWA SEEEANPAAT KQEEVWPALG DRALVPMVEQ
LFSHLLKVIN ICAHVLDDVA PGPAIKAALP SLTNPPSLSP IRRKGKEKEP GEQASVPLSP
KKGSEASAAS RQSDTSGPVT TSKSSSLGSF YHLPSYLKLH DVLKATHANY KVTLDLQNST
EKFGGFLRSA LDVLSQILEL ATLQDIGKCV EEILGYLKSC FSREPMMATV CVQQLLKTLF
GTNLASQFDG LSSNPSKSQG RAQRLGSSSV RPGLYHYCFM APYTHFTQAL ADASLRNMVQ
AEQENDTSGW FDVLQKVSTQ LKTNLTSVTK NRADKNAIHN HIRLFEPLVI KALKQYTTTT
CVQLQKQVLD LLAQLVQLRV NYCLLDSDQV FIGFVLKQFE YIEVGQFRES EAIIPNIFFF
LVLLSYERYH SKQIIGIPKI IQLCDGIMAS GRKAVTHAIP ALQPIVHDLF VLRGTNKADA
GKELETQKEV VVSMLLRLIQ YHQVLEMFIL VLQQCHKENE DKWKRLSRQI ADIILPMLAK
QQMHIDSHEA LGVLNTLFEI LAPSSLRPVD MLLRSMFVTP NTMASVSTVQ LWISGILAIL
RVLISQSTED IVLSRIQELS FSPYLISCTV INRLRDGDST STLEEHSEGK QIKNLPEETF
SRFLLQLVGI LLEDIVTKQL KVEMSEQQHT FYCQELGTLL MCLIHIFKSG MFRRITAAAT
RLFRSDGCGG SFYTLDSLNL RARSMITTHP ALVLLWCQIL LLVNHTDYRW WAEVQQTPKR
HSLSSTKLLS PQMSGEEEDS DLAAKLGMCN REIVRRGALI LFCDYVCQNL HDSEHLTWLI
VNHIQDLISL SHEPPVQDFI SAVHRNSAAS GLFIQAIQSR CENLSTPTML KKTLQCLEGI
HLSQSGAVLT LYVDRLLCTP FRVLARMVDI LACRRVEMLL AANLQSSMAQ LPMEELNRIQ
EYLQSSGLAQ RHQRLYSLLD RFRLSTMQDS LSPSPPVSSH PLDGDGHVSL ETVSPDKDWY
VHLVKSQCWT RSDSALLEGA ELVNRIPAED MNAFMMNSEF NLSLLAPCLS LGMSEISGGQ
KSALFEAARE VTLARVSGTV QQLPAVHHVF QPELPAEPAA YWSKLNDLFG DAALYQSLPT
LARALAQYLV VVSKLPSHLH LPPEKEKDIV KFVVATLEAL SWHLIHEQIP LSLDLQAGLD
CCCLALQLPG LWSVVSSTEF VTHACSLIYC VHFILEAVAV QPGEQLLSPE RRTNTPKAIS
EEEEEVDPNT QNPKYITAAC EMVAEMVESL QSVLALGHKR NSGVPAFLTP LLRNIIISLA
RLPLVNSYTR VPPLVWKLGW SPKPGGDFGT AFPEIPVEFL QEKEVFKEFI YRINTLGWTS
RTQFEETWAT LLGVLVTQPL VMEQEESPPE EDTERTQINV LAVQAITSLV LSAMTVPVAG
NPAVSCLEQQ PRNKPLKALD TRFGRKLSII RGIVEQEIQA MVSKRENIAT HHLYQAWDPV
PSLSPATTGA LISHEKLLLQ INPERELGSM SYKLGQVSIH SVWLGNSITP LREEEWDEEE
EEEADAPAPS SPPTSPVNSR KHRAGVDIHS CSQFLLELYS RWILPSSSAR RTPAILISEV
VRSLLVVSDL FTERNQFELM YVTLTELRRV HPSEDEILAQ YLVPATCKAA AVLGMDKAVA
EPVSRLLEST LRSSHLPSRV GALHGVLYVL ECDLLDDTAK QLIPVISDYL LSNLKGIAHC
VNIHSQQHVL VMCATAFYLI ENYPLDVGPE FSASIIQMCG VMLSGSEEST PSIIYHCALR
GLERLLLSEQ LSRLDAESLV KLSVDRVNVH SPHRAMAALG LMLTCMYTGK EKVSPGRTSD
PNPAAPDSES VIVAMERVSV LFDRIRKGFP CEARVVARIL PQFLDDFFPP QDIMNKVIGE
FLSNQQPYPQ FMATVVYKVF QTLHSTGQSS MVRDWVMLSL SNFTQRAPVA MATWSLSCFF
VSASTSPWVA AILPHVISRM GKLEQVDVNL FCLVATDFYR HQIEEELDRR AFQSVLEVVA
APGSPYHRLL TCLRNVHKVT TC


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