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P42858

- HD_HUMAN

UniProt

P42858 - HD_HUMAN

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Protein

Huntingtin

Gene

HTT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

May play a role in microtubule-mediated transport or vesicle function.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei511 – 5122Cleavage; by apopainSequence Analysis
Sitei528 – 5292Cleavage; by apopainSequence Analysis
Sitei550 – 5512Cleavage; by apopainSequence Analysis
Sitei587 – 5882Cleavage; by apopainSequence Analysis

GO - Molecular functioni

  1. beta-tubulin binding Source: UniProtKB
  2. diazepam binding Source: Ensembl
  3. dynactin binding Source: UniProtKB
  4. dynein intermediate chain binding Source: UniProtKB
  5. identical protein binding Source: IntAct
  6. ion channel binding Source: UniProtKB
  7. p53 binding Source: UniProtKB
  8. transcription factor binding Source: RefGenome

GO - Biological processi

  1. anterior/posterior pattern specification Source: Ensembl
  2. axon cargo transport Source: Ensembl
  3. cell aging Source: Ensembl
  4. citrulline metabolic process Source: Ensembl
  5. determination of adult lifespan Source: Ensembl
  6. dopamine receptor signaling pathway Source: Ensembl
  7. endoplasmic reticulum organization Source: Ensembl
  8. endosomal transport Source: Ensembl
  9. ER to Golgi vesicle-mediated transport Source: Ensembl
  10. establishment of mitotic spindle orientation Source: UniProtKB
  11. Golgi organization Source: UniProtKB
  12. grooming behavior Source: Ensembl
  13. hormone metabolic process Source: Ensembl
  14. insulin secretion Source: Ensembl
  15. iron ion homeostasis Source: Ensembl
  16. lactate biosynthetic process from pyruvate Source: Ensembl
  17. L-glutamate import Source: Ensembl
  18. locomotory behavior Source: Ensembl
  19. negative regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
  20. negative regulation of neuron apoptotic process Source: Ensembl
  21. neural plate formation Source: Ensembl
  22. neuron apoptotic process Source: Ensembl
  23. neuron development Source: Ensembl
  24. olfactory lobe development Source: Ensembl
  25. organ development Source: RefGenome
  26. paraxial mesoderm formation Source: Ensembl
  27. positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity Source: UniProtKB
  28. protein import into nucleus Source: Ensembl
  29. quinolinate biosynthetic process Source: Ensembl
  30. regulation of mitochondrial membrane permeability Source: Ensembl
  31. regulation of mitochondrial membrane potential Source: Ensembl
  32. regulation of protein phosphatase type 2A activity Source: dictyBase
  33. regulation of synaptic plasticity Source: Ensembl
  34. response to calcium ion Source: Ensembl
  35. retrograde vesicle-mediated transport, Golgi to ER Source: UniProtKB
  36. social behavior Source: Ensembl
  37. spermatogenesis Source: Ensembl
  38. striatum development Source: Ensembl
  39. urea cycle Source: Ensembl
  40. vesicle transport along microtubule Source: UniProtKB
  41. visual learning Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

SignaLinkiP42858.

Names & Taxonomyi

Protein namesi
Recommended name:
Huntingtin
Alternative name(s):
Huntington disease protein
Short name:
HD protein
Gene namesi
Name:HTT
Synonyms:HD, IT15
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:4851. HTT.

Subcellular locationi

Cytoplasm. Nucleus
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.

GO - Cellular componenti

  1. autophagic vacuole Source: UniProtKB
  2. axon Source: UniProtKB
  3. cytoplasm Source: UniProtKB
  4. cytoplasmic vesicle membrane Source: UniProtKB
  5. cytosol Source: UniProtKB
  6. dendrite Source: UniProtKB
  7. endoplasmic reticulum Source: UniProtKB
  8. Golgi apparatus Source: UniProtKB
  9. inclusion body Source: Ensembl
  10. late endosome Source: UniProtKB
  11. mitochondrion Source: Ensembl
  12. nucleus Source: UniProtKB
  13. protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.

Keywords - Diseasei

Disease mutation, Neurodegeneration

Organism-specific databases

MIMi143100. phenotype.
Orphaneti399. Huntington disease.
248111. Juvenile Huntington disease.
PharmGKBiPA164741646.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 31423142HuntingtinPRO_0000083942Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91N6-acetyllysine1 Publication
Modified residuei176 – 1761N6-acetyllysine1 Publication
Modified residuei234 – 2341N6-acetyllysine1 Publication
Modified residuei343 – 3431N6-acetyllysine1 Publication
Modified residuei411 – 4111Phosphoserine1 Publication
Modified residuei432 – 4321Phosphoserine1 Publication
Modified residuei442 – 4421N6-acetyllysine1 Publication
Modified residuei1179 – 11791Phosphoserine; by CDK51 Publication
Modified residuei1199 – 11991Phosphoserine; by CDK51 Publication
Modified residuei1870 – 18701Phosphoserine3 Publications
Modified residuei1874 – 18741Phosphoserine3 Publications

Post-translational modificationi

Cleaved by apopain downstream of the polyglutamine stretch. The resulting N-terminal fragment is cytotoxic and provokes apoptosis.
Forms with expanded polyglutamine expansion are specifically ubiquitinated by SYVN1, which promotes their proteasomal degradation.1 Publication
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.5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP42858.
PaxDbiP42858.
PRIDEiP42858.

PTM databases

PhosphoSiteiP42858.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiP42858.
CleanExiHS_HTT.
ExpressionAtlasiP42858. baseline and differential.
GenevestigatoriP42858.

Organism-specific databases

HPAiCAB002756.
HPA026114.

Interactioni

Subunit structurei

Binds SH3GLB1 (By similarity). Interacts through its N-terminus with PRPF40A. Interacts with PQBP1, SETD2 and SYVN. Interacts with PFN1. Interacts with TPR; the interaction is inhibited by forms of Huntingtin with expanded polyglutamine stretch.By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-466029,EBI-466029
ARHGAP24Q8N2643EBI-466029,EBI-988764
BAZ1AQ9NRL24EBI-466029,EBI-927511
CHD3Q128733EBI-466029,EBI-523590
COPB1P536183EBI-466029,EBI-359063
CREBBPQ927932EBI-466029,EBI-81215
CRMP1Q141942EBI-466029,EBI-473101
CTNNB1P352225EBI-466029,EBI-491549
DCTN2Q135616EBI-466029,EBI-715074
DNAJC11Q9NVH13EBI-466029,EBI-1055336
DNAJC21Q5F1R66EBI-466029,EBI-2654581
DNAJC4Q9NNZ33EBI-466029,EBI-4397791
DNALI1O146453EBI-466029,EBI-395638
DNM1Q051933EBI-466029,EBI-713135
DYNC1H1Q142043EBI-466029,EBI-356015
ECH1Q130112EBI-466029,EBI-711968
ERCC6LQ2NKX82EBI-466029,EBI-1042535
EVLQ9UI08-22EBI-466029,EBI-6448852
FEZ1Q996895EBI-466029,EBI-396435
FNBP4Q8N3X16EBI-466029,EBI-310600
FTLP027922EBI-466029,EBI-713279
GIT1Q9Y2X710EBI-466029,EBI-466061
GOLPH3LQ9H4A52EBI-466029,EBI-4403434
GTF3C3Q9Y5Q93EBI-466029,EBI-1054873
HAP1P54257-28EBI-466029,EBI-9392340
Hap1P542563EBI-466029,EBI-994539From a different organism.
HEY2Q9UBP52EBI-466029,EBI-750630
HIP1O002914EBI-466029,EBI-473886
HIST1H3DP684312EBI-466029,EBI-79722
HMG20AQ9NP662EBI-466029,EBI-740641
IKBKAPO951634EBI-466029,EBI-347559
Itpr1P299942EBI-466029,EBI-8614640From a different organism.
JAKMIP1Q96N164EBI-466029,EBI-2680803
KIAA1377Q9P2H02EBI-466029,EBI-473176
LDOC1O957515EBI-466029,EBI-740738
MAGEB6Q8N7X42EBI-466029,EBI-6447163
MBD1Q9UIS92EBI-466029,EBI-867196
MED15Q96RN53EBI-466029,EBI-394506
MED31Q9Y3C73EBI-466029,EBI-394707
MKRN2Q9H0003EBI-466029,EBI-2341005
MRE11AP499595EBI-466029,EBI-396513
MRFAP1L1Q96HT83EBI-466029,EBI-748896
MTSS1O433123EBI-466029,EBI-473954
NBR1Q145963EBI-466029,EBI-742698
NCOR1O753763EBI-466029,EBI-347233
NME4O007462EBI-466029,EBI-744871
NUPL1Q9BVL24EBI-466029,EBI-2811583
OPTNQ96CV97EBI-466029,EBI-748974
OSTF1Q928825EBI-466029,EBI-1051152
P4HA1P136745EBI-466029,EBI-1237386
PACSIN1Q9BY113EBI-466029,EBI-721769
PAK2Q131772EBI-466029,EBI-1045887
PFN2P350804EBI-466029,EBI-473138
PIAS4Q8N2W93EBI-466029,EBI-473160
PIBF1Q8WXW33EBI-466029,EBI-2558770
PIK3R1P279867EBI-466029,EBI-79464
PIK3R2O004596EBI-466029,EBI-346930
PIK3R3Q925696EBI-466029,EBI-79893
PKMP146183EBI-466029,EBI-353408
PPARGP372314EBI-466029,EBI-781384
PRPF40AO7540015EBI-466029,EBI-473291
RNF20Q5VTR23EBI-466029,EBI-2372238
RNF40O751503EBI-466029,EBI-744408
RPL4P365782EBI-466029,EBI-348313
SETD2Q9BYW24EBI-466029,EBI-945869
SH3GL3Q999639EBI-466029,EBI-473910
SNCAP378404EBI-466029,EBI-985879
SORBS1Q9BX664EBI-466029,EBI-433642
SRGAP1Q7Z6B74EBI-466029,EBI-2481729
SRGAP2O750443EBI-466029,EBI-1051034
SRGAP3O432954EBI-466029,EBI-368166
SRRTQ9BXP53EBI-466029,EBI-712721
TACC1O754104EBI-466029,EBI-624237
TANKQ928443EBI-466029,EBI-356349
TCERG1O147769EBI-466029,EBI-473271
TP53P046374EBI-466029,EBI-366083
TRAFD1O145455EBI-466029,EBI-1396921
UBAC1Q9BSL15EBI-466029,EBI-749370
UBE2KP610863EBI-466029,EBI-473850
USP9XQ930088EBI-466029,EBI-302524
WACQ9BTA95EBI-466029,EBI-749118
WBP4O755543EBI-466029,EBI-7251981
WDFY3Q8IZQ110EBI-466029,EBI-1569256
XAGE3Q8WTP93EBI-466029,EBI-6448284
XRCC6P129563EBI-466029,EBI-353208
ZDHHC17Q8IUH512EBI-466029,EBI-524753
ZFC3H1G3V1X12EBI-466029,EBI-6448783
ZFYVE19Q96K213EBI-466029,EBI-6448240
ZMAT2Q96NC02EBI-466029,EBI-2682299

Protein-protein interaction databases

BioGridi109314. 193 interactions.
DIPiDIP-32492N.
IntActiP42858. 335 interactions.
MINTiMINT-133355.
STRINGi9606.ENSP00000347184.

Structurei

Secondary structure

1
3142
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1712Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D3Xmodel-A199-325[»]
2LD0NMR-A1-17[»]
2LD2NMR-A1-17[»]
3IO4X-ray3.63A/B/C1-64[»]
3IO6X-ray3.70A/B/C1-64[»]
3IORX-ray3.60A/B/C1-64[»]
3IOTX-ray3.50A/B/C1-64[»]
3IOUX-ray3.70A/B/C1-64[»]
3IOVX-ray3.70A/B/C1-64[»]
3IOWX-ray3.50A/B/C1-64[»]
3LRHX-ray2.60B/D/F/H/J/L/N/P5-18[»]
4FE8X-ray3.00A/B/C1-64[»]
4FEBX-ray2.80A/B/C1-64[»]
4FECX-ray3.00A/B/C1-64[»]
4FEDX-ray2.81A/B/C1-64[»]
ProteinModelPortaliP42858.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42858.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati204 – 24138HEAT 1Add
BLAST
Repeati246 – 28338HEAT 2Add
BLAST
Repeati316 – 36045HEAT 3Add
BLAST
Repeati802 – 83938HEAT 4Add
BLAST
Repeati902 – 94039HEAT 5Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni3 – 1311Sufficient for interaction with TPRAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi2395 – 240410Nuclear export signalBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi18 – 3821Poly-GlnAdd
BLAST
Compositional biasi39 – 4911Poly-ProAdd
BLAST
Compositional biasi63 – 7816Poly-ProAdd
BLAST
Compositional biasi1437 – 14404Poly-Thr
Compositional biasi2341 – 23455Poly-Glu
Compositional biasi2638 – 26436Poly-Glu

Domaini

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.1 Publication

Sequence similaritiesi

Belongs to the huntingtin family.Curated
Contains 5 HEAT repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG82191.
GeneTreeiENSGT00390000015863.
HOGENOMiHOG000082472.
HOVERGENiHBG005953.
InParanoidiP42858.
KOiK04533.
OMAiSDQVFIG.
OrthoDBiEOG7JQBMD.
PhylomeDBiP42858.
TreeFamiTF323608.

Family and domain databases

Gene3Di1.25.10.10. 4 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000091. Huntingtin.
IPR028426. Huntingtin_fam.
IPR024613. Huntingtin_middle-repeat.
[Graphical view]
PANTHERiPTHR10170. PTHR10170. 1 hit.
PfamiPF12372. DUF3652. 2 hits.
[Graphical view]
PRINTSiPR00375. HUNTINGTIN.
SUPFAMiSSF48371. SSF48371. 6 hits.

Sequencei

Sequence statusi: Complete.

P42858-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATLEKLMKA FESLKSFQQQ QQQQQQQQQQ QQQQQQQQPP PPPPPPPPPQ
60 70 80 90 100
LPQPPPQAQP LLPQPQPPPP PPPPPPGPAV AEEPLHRPKK ELSATKKDRV
110 120 130 140 150
NHCLTICENI VAQSVRNSPE FQKLLGIAME LFLLCSDDAE SDVRMVADEC
160 170 180 190 200
LNKVIKALMD SNLPRLQLEL YKEIKKNGAP RSLRAALWRF AELAHLVRPQ
210 220 230 240 250
KCRPYLVNLL PCLTRTSKRP EESVQETLAA AVPKIMASFG NFANDNEIKV
260 270 280 290 300
LLKAFIANLK SSSPTIRRTA AGSAVSICQH SRRTQYFYSW LLNVLLGLLV
310 320 330 340 350
PVEDEHSTLL ILGVLLTLRY LVPLLQQQVK DTSLKGSFGV TRKEMEVSPS
360 370 380 390 400
AEQLVQVYEL TLHHTQHQDH NVVTGALELL QQLFRTPPPE LLQTLTAVGG
410 420 430 440 450
IGQLTAAKEE SGGRSRSGSI VELIAGGGSS CSPVLSRKQK GKVLLGEEEA
460 470 480 490 500
LEDDSESRSD VSSSALTASV KDEISGELAA SSGVSTPGSA GHDIITEQPR
510 520 530 540 550
SQHTLQADSV DLASCDLTSS ATDGDEEDIL SHSSSQVSAV PSDPAMDLND
560 570 580 590 600
GTQASSPISD SSQTTTEGPD SAVTPSDSSE IVLDGTDNQY LGLQIGQPQD
610 620 630 640 650
EDEEATGILP DEASEAFRNS SMALQQAHLL KNMSHCRQPS DSSVDKFVLR
660 670 680 690 700
DEATEPGDQE NKPCRIKGDI GQSTDDDSAP LVHCVRLLSA SFLLTGGKNV
710 720 730 740 750
LVPDRDVRVS VKALALSCVG AAVALHPESF FSKLYKVPLD TTEYPEEQYV
760 770 780 790 800
SDILNYIDHG DPQVRGATAI LCGTLICSIL SRSRFHVGDW MGTIRTLTGN
810 820 830 840 850
TFSLADCIPL LRKTLKDESS VTCKLACTAV RNCVMSLCSS SYSELGLQLI
860 870 880 890 900
IDVLTLRNSS YWLVRTELLE TLAEIDFRLV SFLEAKAENL HRGAHHYTGL
910 920 930 940 950
LKLQERVLNN VVIHLLGDED PRVRHVAAAS LIRLVPKLFY KCDQGQADPV
960 970 980 990 1000
VAVARDQSSV YLKLLMHETQ PPSHFSVSTI TRIYRGYNLL PSITDVTMEN
1010 1020 1030 1040 1050
NLSRVIAAVS HELITSTTRA LTFGCCEALC LLSTAFPVCI WSLGWHCGVP
1060 1070 1080 1090 1100
PLSASDESRK SCTVGMATMI LTLLSSAWFP LDLSAHQDAL ILAGNLLAAS
1110 1120 1130 1140 1150
APKSLRSSWA SEEEANPAAT KQEEVWPALG DRALVPMVEQ LFSHLLKVIN
1160 1170 1180 1190 1200
ICAHVLDDVA PGPAIKAALP SLTNPPSLSP IRRKGKEKEP GEQASVPLSP
1210 1220 1230 1240 1250
KKGSEASAAS RQSDTSGPVT TSKSSSLGSF YHLPSYLKLH DVLKATHANY
1260 1270 1280 1290 1300
KVTLDLQNST EKFGGFLRSA LDVLSQILEL ATLQDIGKCV EEILGYLKSC
1310 1320 1330 1340 1350
FSREPMMATV CVQQLLKTLF GTNLASQFDG LSSNPSKSQG RAQRLGSSSV
1360 1370 1380 1390 1400
RPGLYHYCFM APYTHFTQAL ADASLRNMVQ AEQENDTSGW FDVLQKVSTQ
1410 1420 1430 1440 1450
LKTNLTSVTK NRADKNAIHN HIRLFEPLVI KALKQYTTTT CVQLQKQVLD
1460 1470 1480 1490 1500
LLAQLVQLRV NYCLLDSDQV FIGFVLKQFE YIEVGQFRES EAIIPNIFFF
1510 1520 1530 1540 1550
LVLLSYERYH SKQIIGIPKI IQLCDGIMAS GRKAVTHAIP ALQPIVHDLF
1560 1570 1580 1590 1600
VLRGTNKADA GKELETQKEV VVSMLLRLIQ YHQVLEMFIL VLQQCHKENE
1610 1620 1630 1640 1650
DKWKRLSRQI ADIILPMLAK QQMHIDSHEA LGVLNTLFEI LAPSSLRPVD
1660 1670 1680 1690 1700
MLLRSMFVTP NTMASVSTVQ LWISGILAIL RVLISQSTED IVLSRIQELS
1710 1720 1730 1740 1750
FSPYLISCTV INRLRDGDST STLEEHSEGK QIKNLPEETF SRFLLQLVGI
1760 1770 1780 1790 1800
LLEDIVTKQL KVEMSEQQHT FYCQELGTLL MCLIHIFKSG MFRRITAAAT
1810 1820 1830 1840 1850
RLFRSDGCGG SFYTLDSLNL RARSMITTHP ALVLLWCQIL LLVNHTDYRW
1860 1870 1880 1890 1900
WAEVQQTPKR HSLSSTKLLS PQMSGEEEDS DLAAKLGMCN REIVRRGALI
1910 1920 1930 1940 1950
LFCDYVCQNL HDSEHLTWLI VNHIQDLISL SHEPPVQDFI SAVHRNSAAS
1960 1970 1980 1990 2000
GLFIQAIQSR CENLSTPTML KKTLQCLEGI HLSQSGAVLT LYVDRLLCTP
2010 2020 2030 2040 2050
FRVLARMVDI LACRRVEMLL AANLQSSMAQ LPMEELNRIQ EYLQSSGLAQ
2060 2070 2080 2090 2100
RHQRLYSLLD RFRLSTMQDS LSPSPPVSSH PLDGDGHVSL ETVSPDKDWY
2110 2120 2130 2140 2150
VHLVKSQCWT RSDSALLEGA ELVNRIPAED MNAFMMNSEF NLSLLAPCLS
2160 2170 2180 2190 2200
LGMSEISGGQ KSALFEAARE VTLARVSGTV QQLPAVHHVF QPELPAEPAA
2210 2220 2230 2240 2250
YWSKLNDLFG DAALYQSLPT LARALAQYLV VVSKLPSHLH LPPEKEKDIV
2260 2270 2280 2290 2300
KFVVATLEAL SWHLIHEQIP LSLDLQAGLD CCCLALQLPG LWSVVSSTEF
2310 2320 2330 2340 2350
VTHACSLIYC VHFILEAVAV QPGEQLLSPE RRTNTPKAIS EEEEEVDPNT
2360 2370 2380 2390 2400
QNPKYITAAC EMVAEMVESL QSVLALGHKR NSGVPAFLTP LLRNIIISLA
2410 2420 2430 2440 2450
RLPLVNSYTR VPPLVWKLGW SPKPGGDFGT AFPEIPVEFL QEKEVFKEFI
2460 2470 2480 2490 2500
YRINTLGWTS RTQFEETWAT LLGVLVTQPL VMEQEESPPE EDTERTQINV
2510 2520 2530 2540 2550
LAVQAITSLV LSAMTVPVAG NPAVSCLEQQ PRNKPLKALD TRFGRKLSII
2560 2570 2580 2590 2600
RGIVEQEIQA MVSKRENIAT HHLYQAWDPV PSLSPATTGA LISHEKLLLQ
2610 2620 2630 2640 2650
INPERELGSM SYKLGQVSIH SVWLGNSITP LREEEWDEEE EEEADAPAPS
2660 2670 2680 2690 2700
SPPTSPVNSR KHRAGVDIHS CSQFLLELYS RWILPSSSAR RTPAILISEV
2710 2720 2730 2740 2750
VRSLLVVSDL FTERNQFELM YVTLTELRRV HPSEDEILAQ YLVPATCKAA
2760 2770 2780 2790 2800
AVLGMDKAVA EPVSRLLEST LRSSHLPSRV GALHGVLYVL ECDLLDDTAK
2810 2820 2830 2840 2850
QLIPVISDYL LSNLKGIAHC VNIHSQQHVL VMCATAFYLI ENYPLDVGPE
2860 2870 2880 2890 2900
FSASIIQMCG VMLSGSEEST PSIIYHCALR GLERLLLSEQ LSRLDAESLV
2910 2920 2930 2940 2950
KLSVDRVNVH SPHRAMAALG LMLTCMYTGK EKVSPGRTSD PNPAAPDSES
2960 2970 2980 2990 3000
VIVAMERVSV LFDRIRKGFP CEARVVARIL PQFLDDFFPP QDIMNKVIGE
3010 3020 3030 3040 3050
FLSNQQPYPQ FMATVVYKVF QTLHSTGQSS MVRDWVMLSL SNFTQRAPVA
3060 3070 3080 3090 3100
MATWSLSCFF VSASTSPWVA AILPHVISRM GKLEQVDVNL FCLVATDFYR
3110 3120 3130 3140
HQIEEELDRR AFQSVLEVVA APGSPYHRLL TCLRNVHKVT TC
Length:3,142
Mass (Da):347,603
Last modified:May 18, 2010 - v2
Checksum:iA267509E84D52F0D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti823 – 8231C → S in BAA36753. (PubMed:11013077)Curated

Polymorphismi

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti18 – 181Q → QQQ.
VAR_005268
Natural varianti893 – 8931G → R.
Corresponds to variant rs363075 [ dbSNP | Ensembl ].
VAR_060170
Natural varianti1064 – 10641V → I.
Corresponds to variant rs35892913 [ dbSNP | Ensembl ].
VAR_060171
Natural varianti1091 – 10911I → M.
Corresponds to variant rs1143646 [ dbSNP | Ensembl ].
VAR_060172
Natural varianti1173 – 11731T → A.
Corresponds to variant rs3025843 [ dbSNP | Ensembl ].
VAR_060173
Natural varianti1260 – 12601T → M.
Corresponds to variant rs34315806 [ dbSNP | Ensembl ].
VAR_060174
Natural varianti1382 – 13821E → A.
Corresponds to variant rs3025837 [ dbSNP | Ensembl ].
VAR_054017
Natural varianti1385 – 13851N → H.
Corresponds to variant rs3025837 [ dbSNP | Ensembl ].
VAR_060175
Natural varianti1720 – 17201T → N.
Corresponds to variant rs363125 [ dbSNP | Ensembl ].
VAR_060176
Natural varianti2113 – 21131D → Y.
Corresponds to variant rs1143648 [ dbSNP | Ensembl ].
VAR_060177
Natural varianti2309 – 23091Y → H.
Corresponds to variant rs362331 [ dbSNP | Ensembl ].
VAR_060178
Natural varianti2786 – 27861V → I.1 Publication
Corresponds to variant rs362272 [ dbSNP | Ensembl ].
VAR_060179

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA46068.
RefSeqiNP_002102.4. NM_002111.7.
UniGeneiHs.518450.

Genome annotation databases

EnsembliENST00000355072; ENSP00000347184; ENSG00000197386.
GeneIDi3064.
KEGGihsa:3064.
UCSCiuc021xkv.1. human.

Polymorphism databases

DMDMi296434520.

Keywords - Coding sequence diversityi

Polymorphism, Triplet repeat expansion

Cross-referencesi

Web resourcesi

Wikipedia

Huntingtin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi A46068.
RefSeqi NP_002102.4. NM_002111.7.
UniGenei Hs.518450.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2D3X model - A 199-325 [» ]
2LD0 NMR - A 1-17 [» ]
2LD2 NMR - A 1-17 [» ]
3IO4 X-ray 3.63 A/B/C 1-64 [» ]
3IO6 X-ray 3.70 A/B/C 1-64 [» ]
3IOR X-ray 3.60 A/B/C 1-64 [» ]
3IOT X-ray 3.50 A/B/C 1-64 [» ]
3IOU X-ray 3.70 A/B/C 1-64 [» ]
3IOV X-ray 3.70 A/B/C 1-64 [» ]
3IOW X-ray 3.50 A/B/C 1-64 [» ]
3LRH X-ray 2.60 B/D/F/H/J/L/N/P 5-18 [» ]
4FE8 X-ray 3.00 A/B/C 1-64 [» ]
4FEB X-ray 2.80 A/B/C 1-64 [» ]
4FEC X-ray 3.00 A/B/C 1-64 [» ]
4FED X-ray 2.81 A/B/C 1-64 [» ]
ProteinModelPortali P42858.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109314. 193 interactions.
DIPi DIP-32492N.
IntActi P42858. 335 interactions.
MINTi MINT-133355.
STRINGi 9606.ENSP00000347184.

Chemistry

BindingDBi P42858.
ChEMBLi CHEMBL5514.

PTM databases

PhosphoSitei P42858.

Polymorphism databases

DMDMi 296434520.

Proteomic databases

MaxQBi P42858.
PaxDbi P42858.
PRIDEi P42858.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000355072 ; ENSP00000347184 ; ENSG00000197386 .
GeneIDi 3064.
KEGGi hsa:3064.
UCSCi uc021xkv.1. human.

Organism-specific databases

CTDi 3064.
GeneCardsi GC04P003076.
GeneReviewsi HTT.
HGNCi HGNC:4851. HTT.
HPAi CAB002756.
HPA026114.
MIMi 143100. phenotype.
613004. gene.
neXtProti NX_P42858.
Orphaneti 399. Huntington disease.
248111. Juvenile Huntington disease.
PharmGKBi PA164741646.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG82191.
GeneTreei ENSGT00390000015863.
HOGENOMi HOG000082472.
HOVERGENi HBG005953.
InParanoidi P42858.
KOi K04533.
OMAi SDQVFIG.
OrthoDBi EOG7JQBMD.
PhylomeDBi P42858.
TreeFami TF323608.

Enzyme and pathway databases

SignaLinki P42858.

Miscellaneous databases

ChiTaRSi HTT. human.
EvolutionaryTracei P42858.
GeneWikii Huntingtin.
GenomeRNAii 3064.
NextBioi 12121.
PROi P42858.
SOURCEi Search...

Gene expression databases

Bgeei P42858.
CleanExi HS_HTT.
ExpressionAtlasi P42858. baseline and differential.
Genevestigatori P42858.

Family and domain databases

Gene3Di 1.25.10.10. 4 hits.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000091. Huntingtin.
IPR028426. Huntingtin_fam.
IPR024613. Huntingtin_middle-repeat.
[Graphical view ]
PANTHERi PTHR10170. PTHR10170. 1 hit.
Pfami PF12372. DUF3652. 2 hits.
[Graphical view ]
PRINTSi PR00375. HUNTINGTIN.
SUPFAMi SSF48371. SSF48371. 6 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-203.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-88.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2561-3142, VARIANT ILE-2786.
    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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY APOPAIN.
  9. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEAR EXPORT SIGNAL.
  14. "Polyglutamine expansion of huntingtin impairs its nuclear export."
    Cornett J., Cao F., Wang C.E., Ross C.A., Bates G.P., Li S.H., Li X.J.
    Nat. Genet. 37:198-204(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TPR, SUBCELLULAR LOCATION.
  15. "Interaction of the nuclear matrix protein NAKAP with HypA and huntingtin: implications for nuclear toxicity in Huntington's disease pathogenesis."
    Sayer J.A., Manczak M., Akileswaran L., Reddy P.H., Coghlan V.M.
    NeuroMolecular Med. 7:297-310(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  16. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SYVN, UBIQUITINATION.
  17. "Phosphorylation of huntingtin by cyclin-dependent kinase 5 is induced by DNA damage and regulates wild-type and mutant huntingtin toxicity in neurons."
    Anne S.L., Saudou F., Humbert S.
    J. Neurosci. 27:7318-7328(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-1179 AND SER-1199.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  19. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1870, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "Phosphorylation of profilin by ROCK1 regulates polyglutamine aggregation."
    Shao J., Welch W.J., Diprospero N.A., Diamond M.I.
    Mol. Cell. Biol. 28:5196-5208(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PFN1.
  21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411; SER-1870 AND SER-1874, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432 AND SER-1874, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  24. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1870 AND SER-1874, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "Mass spectrometric identification of novel lysine acetylation sites in huntingtin."
    Cong X., Held J.M., Degiacomo F., Bonner A., Chen J.M., Schilling B., Czerwieniec G.A., Gibson B.W., Ellerby L.M.
    Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-9; LYS-176; LYS-234; LYS-343 AND LYS-442.
  27. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "Secondary structure of Huntingtin amino-terminal region."
    Kim M.W., Chelliah Y., Kim S.W., Otwinowski Z., Bezprozvanny I.
    Structure 17:1205-1212(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 1-64, DOMAIN.

Entry informationi

Entry nameiHD_HUMAN
AccessioniPrimary (citable) accession number: P42858
Secondary accession number(s): Q9UQB7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: May 18, 2010
Last modified: November 26, 2014
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3