Reviewed, UniProtKB/Swiss-Prot P42858 (HD_HUMAN)

Names and origin

Protein names

Recommended name:
    Huntingtin
Alternative name(s):
    Huntington disease protein
      Short name=HD protein

Gene names

Name:	HTT
Synonyms:	HD, IT15

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	3144 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May play a role in microtubule-mediated transport or vesicle function.
Subunit structure	Binds SH3GLB1 By similarity. Interacts through its N-terminus with PRPF40A. Interacts with PQBP1, SETD2 and SYVN.
Subcellular location	Cytoplasm. Nucleus.
Tissue specificity	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.
Post-translational modification	Cleaved by apopain downstream of the polyglutamine stretch. The resulting amino-terminal fragment is cytotoxic and provokes apoptosis. Forms with expanded polyglutamine expansion are specifically ubiquitinated by SYVN1, which promotes their proteasomal degradation.
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.
Involvement in disease	Defects in HTT are the cause of Huntington disease (HD) [MIM:143100]. HD is an autosomal dominant 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 and symptoms progressively worsen leading to death in 10 to 20 years. Onset and clinical course depend on the degree of poly-Gln repeat expansion, longer expansions resulting in earlier onset and more severe clinical manifestations. HD affects 1 in 10,000 individuals of European origin. Neuropathology of Huntington disease displays a distinctive pattern with loss of neurons, especially in the caudate and putamen (striatum).
Sequence similarities	Belongs to the huntingtin family. Contains 10 HEAT repeats.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism Triplet repeat expansion
Disease	Disease mutation
Domain	Repeat
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	behavior Traceable author statement. Source: ProtInc induction of apoptosis Traceable author statement. Source: ProtInc organ morphogenesis Traceable author statement. Source: ProtInc pathogenesis Traceable author statement. Source: ProtInc
Cellular component	Golgi apparatus Inferred from direct assay. Source: UniProtKB nucleus Traceable author statement. Source: ProtInc soluble fraction Traceable author statement. Source: ProtInc
Molecular function	microtubule binding Traceable author statement. Source: ProtInc transcription corepressor activity Traceable author statement. Source: ProtInc transporter activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CHD3	Q12873	1	EBI-466029,EBI-523590
CREBBP	Q92793	1	EBI-466029,EBI-81215
CRMP1	Q14194	1	EBI-466029,EBI-473101
ECH1	Q13011	1	EBI-466029,EBI-711968
FEZ1	Q99689	1	EBI-466029,EBI-396435
GIT1	Q9Y2X7	5	EBI-466029,EBI-466061
IKBKAP	O95163	1	EBI-466029,EBI-347559
KIAA1377	Q9P2H0	1	EBI-466029,EBI-473176
MED31	Q9Y3C7	1	EBI-466029,EBI-394707
PFN2	P35080	1	EBI-466029,EBI-473138
PIAS4	Q8N2W9	1	EBI-466029,EBI-473160
SIN3A	Q96ST3	1	EBI-466029,EBI-347218
TP53	P04637	2	EBI-466029,EBI-366083
XRCC6	P12956	1	EBI-466029,EBI-353208
ZDHHC17	Q8IUH5	1	EBI-466029,EBI-524753

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 3144	3144	Huntingtin
Regions
	Repeat	206 – 243	38	HEAT 1
	Repeat	248 – 285	38	HEAT 2
	Repeat	318 – 362	45	HEAT 3
	Repeat	804 – 841	38	HEAT 4
	Repeat	904 – 942	39	HEAT 5
	Motif	2397 – 2406	10	Nuclear export signal By similarity
	Compositional bias	18 – 40	23	Poly-Gln
	Compositional bias	41 – 51	11	Poly-Pro
	Compositional bias	65 – 80	16	Poly-Pro
	Compositional bias	1439 – 1442	4	Poly-Thr
	Compositional bias	2343 – 2347	5	Poly-Glu
	Compositional bias	2640 – 2645	6	Poly-Glu
Sites
	Site	513 – 514	2	Cleavage; by apopain Potential
	Site	530 – 531	2	Cleavage; by apopain Potential
	Site	552 – 553	2	Cleavage; by apopain Potential
	Site	589 – 590	2	Cleavage; by apopain Potential
Amino acid modifications
	Modified residue	421	1	Phosphoserine
	Modified residue	434	1	Phosphoserine
	Modified residue	1876	1	Phosphoserine By similarity
Natural variations
	Natural variant	38 – 40	3	Missing
Experimental info
	Sequence conflict	825	1	C → S in BAA36753. Ref.2
	Sequence conflict	2788	1	V → I in AAA52702. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P42858-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 9D1BA8528929908F	FASTA	3,144	347,860
	10 20 30 40 50 60 MATLEKLMKA FESLKSFQQQ QQQQQQQQQQ QQQQQQQQQQ PPPPPPPPPP PQLPQPPPQA 70 80 90 100 110 120 QPLLPQPQPP PPPPPPPPGP AVAEEPLHRP KKELSATKKD RVNHCLTICE NIVAQSVRNS 130 140 150 160 170 180 PEFQKLLGIA MELFLLCSDD AESDVRMVAD ECLNKVIKAL MDSNLPRLQL ELYKEIKKNG 190 200 210 220 230 240 APRSLRAALW RFAELAHLVR PQKCRPYLVN LLPCLTRTSK RPEESVQETL AAAVPKIMAS 250 260 270 280 290 300 FGNFANDNEI KVLLKAFIAN LKSSSPTIRR TAAGSAVSIC QHSRRTQYFY SWLLNVLLGL 310 320 330 340 350 360 LVPVEDEHST LLILGVLLTL RYLVPLLQQQ VKDTSLKGSF GVTRKEMEVS PSAEQLVQVY 370 380 390 400 410 420 ELTLHHTQHQ DHNVVTGALE LLQQLFRTPP PELLQTLTAV GGIGQLTAAK EESGGRSRSG 430 440 450 460 470 480 SIVELIAGGG SSCSPVLSRK QKGKVLLGEE EALEDDSESR SDVSSSALTA SVKDEISGEL 490 500 510 520 530 540 AASSGVSTPG SAGHDIITEQ PRSQHTLQAD SVDLASCDLT SSATDGDEED ILSHSSSQVS 550 560 570 580 590 600 AVPSDPAMDL NDGTQASSPI SDSSQTTTEG PDSAVTPSDS SEIVLDGTDN QYLGLQIGQP 610 620 630 640 650 660 QDEDEEATGI LPDEASEAFR NSSMALQQAH LLKNMSHCRQ PSDSSVDKFV LRDEATEPGD 670 680 690 700 710 720 QENKPCRIKG DIGQSTDDDS APLVHCVRLL SASFLLTGGK NVLVPDRDVR VSVKALALSC 730 740 750 760 770 780 VGAAVALHPE SFFSKLYKVP LDTTEYPEEQ YVSDILNYID HGDPQVRGAT AILCGTLICS 790 800 810 820 830 840 ILSRSRFHVG DWMGTIRTLT GNTFSLADCI PLLRKTLKDE SSVTCKLACT AVRNCVMSLC 850 860 870 880 890 900 SSSYSELGLQ LIIDVLTLRN SSYWLVRTEL LETLAEIDFR LVSFLEAKAE NLHRGAHHYT 910 920 930 940 950 960 GLLKLQERVL NNVVIHLLGD EDPRVRHVAA ASLIRLVPKL FYKCDQGQAD PVVAVARDQS 970 980 990 1000 1010 1020 SVYLKLLMHE TQPPSHFSVS TITRIYRGYN LLPSITDVTM ENNLSRVIAA VSHELITSTT 1030 1040 1050 1060 1070 1080 RALTFGCCEA LCLLSTAFPV CIWSLGWHCG VPPLSASDES RKSCTVGMAT MILTLLSSAW 1090 1100 1110 1120 1130 1140 FPLDLSAHQD ALILAGNLLA ASAPKSLRSS WASEEEANPA ATKQEEVWPA LGDRALVPMV 1150 1160 1170 1180 1190 1200 EQLFSHLLKV INICAHVLDD VAPGPAIKAA LPSLTNPPSL SPIRRKGKEK EPGEQASVPL 1210 1220 1230 1240 1250 1260 SPKKGSEASA ASRQSDTSGP VTTSKSSSLG SFYHLPSYLK LHDVLKATHA NYKVTLDLQN 1270 1280 1290 1300 1310 1320 STEKFGGFLR SALDVLSQIL ELATLQDIGK CVEEILGYLK SCFSREPMMA TVCVQQLLKT 1330 1340 1350 1360 1370 1380 LFGTNLASQF DGLSSNPSKS QGRAQRLGSS SVRPGLYHYC FMAPYTHFTQ ALADASLRNM 1390 1400 1410 1420 1430 1440 VQAEQENDTS GWFDVLQKVS TQLKTNLTSV TKNRADKNAI HNHIRLFEPL VIKALKQYTT 1450 1460 1470 1480 1490 1500 TTCVQLQKQV LDLLAQLVQL RVNYCLLDSD QVFIGFVLKQ FEYIEVGQFR ESEAIIPNIF 1510 1520 1530 1540 1550 1560 FFLVLLSYER YHSKQIIGIP KIIQLCDGIM ASGRKAVTHA IPALQPIVHD LFVLRGTNKA 1570 1580 1590 1600 1610 1620 DAGKELETQK EVVVSMLLRL IQYHQVLEMF ILVLQQCHKE NEDKWKRLSR QIADIILPML 1630 1640 1650 1660 1670 1680 AKQQMHIDSH EALGVLNTLF EILAPSSLRP VDMLLRSMFV TPNTMASVST VQLWISGILA 1690 1700 1710 1720 1730 1740 ILRVLISQST EDIVLSRIQE LSFSPYLISC TVINRLRDGD STSTLEEHSE GKQIKNLPEE 1750 1760 1770 1780 1790 1800 TFSRFLLQLV GILLEDIVTK QLKVEMSEQQ HTFYCQELGT LLMCLIHIFK SGMFRRITAA 1810 1820 1830 1840 1850 1860 ATRLFRSDGC GGSFYTLDSL NLRARSMITT HPALVLLWCQ ILLLVNHTDY RWWAEVQQTP 1870 1880 1890 1900 1910 1920 KRHSLSSTKL LSPQMSGEEE DSDLAAKLGM CNREIVRRGA LILFCDYVCQ NLHDSEHLTW 1930 1940 1950 1960 1970 1980 LIVNHIQDLI SLSHEPPVQD FISAVHRNSA ASGLFIQAIQ SRCENLSTPT MLKKTLQCLE 1990 2000 2010 2020 2030 2040 GIHLSQSGAV LTLYVDRLLC TPFRVLARMV DILACRRVEM LLAANLQSSM AQLPMEELNR 2050 2060 2070 2080 2090 2100 IQEYLQSSGL AQRHQRLYSL LDRFRLSTMQ DSLSPSPPVS SHPLDGDGHV SLETVSPDKD 2110 2120 2130 2140 2150 2160 WYVHLVKSQC WTRSDSALLE GAELVNRIPA EDMNAFMMNS EFNLSLLAPC LSLGMSEISG 2170 2180 2190 2200 2210 2220 GQKSALFEAA REVTLARVSG TVQQLPAVHH VFQPELPAEP AAYWSKLNDL FGDAALYQSL 2230 2240 2250 2260 2270 2280 PTLARALAQY LVVVSKLPSH LHLPPEKEKD IVKFVVATLE ALSWHLIHEQ IPLSLDLQAG 2290 2300 2310 2320 2330 2340 LDCCCLALQL PGLWSVVSST EFVTHACSLI YCVHFILEAV AVQPGEQLLS PERRTNTPKA 2350 2360 2370 2380 2390 2400 ISEEEEEVDP NTQNPKYITA ACEMVAEMVE SLQSVLALGH KRNSGVPAFL TPLLRNIIIS 2410 2420 2430 2440 2450 2460 LARLPLVNSY TRVPPLVWKL GWSPKPGGDF GTAFPEIPVE FLQEKEVFKE FIYRINTLGW 2470 2480 2490 2500 2510 2520 TSRTQFEETW ATLLGVLVTQ PLVMEQEESP PEEDTERTQI NVLAVQAITS LVLSAMTVPV 2530 2540 2550 2560 2570 2580 AGNPAVSCLE QQPRNKPLKA LDTRFGRKLS IIRGIVEQEI QAMVSKRENI ATHHLYQAWD 2590 2600 2610 2620 2630 2640 PVPSLSPATT GALISHEKLL LQINPERELG SMSYKLGQVS IHSVWLGNSI TPLREEEWDE 2650 2660 2670 2680 2690 2700 EEEEEADAPA PSSPPTSPVN SRKHRAGVDI HSCSQFLLEL YSRWILPSSS ARRTPAILIS 2710 2720 2730 2740 2750 2760 EVVRSLLVVS DLFTERNQFE LMYVTLTELR RVHPSEDEIL AQYLVPATCK AAAVLGMDKA 2770 2780 2790 2800 2810 2820 VAEPVSRLLE STLRSSHLPS RVGALHGVLY VLECDLLDDT AKQLIPVISD YLLSNLKGIA 2830 2840 2850 2860 2870 2880 HCVNIHSQQH VLVMCATAFY LIENYPLDVG PEFSASIIQM CGVMLSGSEE STPSIIYHCA 2890 2900 2910 2920 2930 2940 LRGLERLLLS EQLSRLDAES LVKLSVDRVN VHSPHRAMAA LGLMLTCMYT GKEKVSPGRT 2950 2960 2970 2980 2990 3000 SDPNPAAPDS ESVIVAMERV SVLFDRIRKG FPCEARVVAR ILPQFLDDFF PPQDIMNKVI 3010 3020 3030 3040 3050 3060 GEFLSNQQPY PQFMATVVYK VFQTLHSTGQ SSMVRDWVML SLSNFTQRAP VAMATWSLSC 3070 3080 3090 3100 3110 3120 FFVSASTSPW VAAILPHVIS RMGKLEQVDV NLFCLVATDF YRHQIEEELD RRAFQSVLEV 3130 3140 VAAPGSPYHR LLTCLRNVHK VTTC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes." 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. Cell 72:971-983(1993) [PubMed: 8458085] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Retina.
[2]	"Identification and characterization of the miniature pig Huntington's disease gene homolog: evidence for conservation and polymorphism in the CAG triplet repeat." Matsuyama N., Hadano S., Onoe K., Osuga H., Shouguchi-Miyata J., Gondo Y., Ikeda J.-E. Genomics 69:72-85(2000) [PubMed: 11013077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[3]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." 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. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Structure and expression of the Huntington's disease gene: evidence against simple inactivation due to an expanded CAG repeat." 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. Somat. Cell Mol. Genet. 20:27-38(1994) [PubMed: 8197474] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-205.
[5]	"Structural analysis of the 5' region of mouse and human Huntington disease genes reveals conservation of putative promoter region and di- and trinucleotide polymorphisms." Lin B., Nasir J., Kalchman M.A., McDonald H., Zeisler J., Goldberg Y.P., Hayden M.R. Genomics 25:707-715(1995) [PubMed: 7759106] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-90.
[6]	"Differential 3' polyadenylation of the Huntington disease gene results in two mRNA species with variable tissue expression." Lin B., Rommens J.M., Graham R.K., Kalchman M., Macdonald H., Nasir J., Delaney A., Goldberg Y.P., Hayden M.R. Hum. Mol. Genet. 2:1541-1545(1993) [PubMed: 7903579] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2563-3144. Tissue: Brain, Caudate nucleus, Frontal cortex, Muscle and Retina.
[7]	"Cellular localization of the Huntington's disease protein and discrimination of the normal and mutated form." Trottier Y., Devys D., Imbert G., Saudou F., An I., Lutz Y., Weber C., Agid Y., Hirsch E.C., Mandel J.-L. Nat. Genet. 10:104-110(1995) [PubMed: 7647777] [Abstract] Cited for: SUBCELLULAR LOCATION.
[8]	"Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract." 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. Nat. Genet. 13:442-449(1996) [PubMed: 8696339] [Abstract] Cited for: CLEAVAGE BY APOPAIN.
[9]	"Huntingtin interacts with a family of WW domain proteins." Faber P.W., Barnes G.T., Srinidhi J., Chen J., Gusella J.F., MacDonald M.E. Hum. Mol. Genet. 7:1463-1474(1998) [PubMed: 9700202] [Abstract] Cited for: INTERACTION WITH PRPF40A AND SETD2.
[10]	"PQBP-1, a novel polyglutamine tract binding protein, inhibits transcription activation by Brn-2 and affects cell survival." Waragai M., Lammers C.-H., Takeuchi S., Imafuku I., Udagawa Y., Kanazawa I., Kawabata M., Mouradian M.M., Okazawa H. Hum. Mol. Genet. 8:977-987(1999) [PubMed: 10332029] [Abstract] Cited for: INTERACTION WITH PQBP1. Tissue: Brain.
[11]	"Huntingtin's WW domain partners in Huntington's disease post-mortem brain fulfill genetic criteria for direct involvement in Huntington's disease pathogenesis." Passani L.A., Bedford M.T., Faber P.W., McGinnis K.M., Sharp A.H., Gusella J.F., Vonsattel J.-P., MacDonald M.E. Hum. Mol. Genet. 9:2175-2182(2000) [PubMed: 10958656] [Abstract] Cited for: INTERACTION WITH SETD2.
[12]	"Identification of the full-length huntingtin-interacting protein p231HBP/HYPB as a DNA-binding factor." Rega S., Stiewe T., Chang D.-I., Pollmeier B., Esche H., Bardenheuer W., Marquitan G., Puetzer B.M. Mol. Cell. Neurosci. 18:68-79(2001) [PubMed: 11461154] [Abstract] Cited for: INTERACTION WITH SETD2.
[13]	"Huntingtin contains a highly conserved nuclear export signal." Xia J., Lee D.H., Taylor J., Vandelft M., Truant R. Hum. Mol. Genet. 12:1393-1403(2003) [PubMed: 12783847] [Abstract] Cited for: NUCLEAR EXPORT SIGNAL.
[14]	"Ubiquitin ligase Hrd1 enhances the degradation and suppresses the toxicity of polyglutamine-expanded huntingtin." Yang H., Zhong X., Ballar P., Luo S., Shen Y., Rubinsztein D.C., Monteiro M.J., Fang S. Exp. Cell Res. 313:538-550(2007) [PubMed: 17141218] [Abstract] Cited for: INTERACTION WITH SYVN, UBIQUITINATION.
[15]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421 AND SER-434, MASS SPECTROMETRY. Tissue: Platelet.
+	Additional computationally mapped references.

Web resources

GeneReviews

Wikipedia

Huntingtin entry

Cross-references

Sequence databases

EMBLGenBankDDBJ

L12392 mRNA. Translation: AAB38240.1.
AB016794 mRNA. Translation: BAA36753.1.
Z49154 Genomic DNA. Translation: CAA89024.1.
Z49155 Genomic DNA. Translation: CAA89025.1.
Z49208 Genomic DNA. No translation available.
Z49769 Genomic DNA. Translation: CAA89839.1.
Z68756 Genomic DNA. No translation available.
Z69649 Genomic DNA. No translation available.
L27350 Genomic DNA. No translation available.
L27351 Genomic DNA. No translation available.
L27352 Genomic DNA. No translation available.
L27353 Genomic DNA. No translation available.
L27354 Genomic DNA. No translation available.
L34020 Genomic DNA. No translation available.
L20431 mRNA. Translation: AAA52702.1.

PIR

A46068.

RefSeq

NP_002102.4.

UniGene

Hs.518450

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2D3X	model	-	A	201-327	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P42858.

PTM databases

PhosphoSite

P42858.

Genome annotation databases

Ensembl

ENSG00000197386. Homo sapiens. [Contig view]

GeneID

3064.

KEGG

hsa:3064.

Organism-specific databases

H-InvDB

HIX0004042.

HGNC

HGNC:4851. HTT.

HPA

CAB002756.

MIM

143100. gene+phenotype.

Orphanet

399. Huntington disease.

PharmGKB

PA29225.

GenAtlas

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GeneCards

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Phylogenomic databases