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P42858

- HD_HUMAN

UniProt

P42858 - HD_HUMAN

Protein

Huntingtin

Gene

HTT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (18 May 2010)
      Previous versions | rss
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    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. p53 binding Source: UniProtKB
    7. protein 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. protein import into nucleus Source: Ensembl
    28. quinolinate biosynthetic process Source: Ensembl
    29. regulation of mitochondrial membrane permeability Source: Ensembl
    30. regulation of mitochondrial membrane potential Source: Ensembl
    31. regulation of protein phosphatase type 2A activity Source: dictyBase
    32. regulation of synaptic plasticity Source: Ensembl
    33. response to calcium ion Source: Ensembl
    34. retrograde vesicle-mediated transport, Golgi to ER Source: UniProtKB
    35. social behavior Source: Ensembl
    36. spermatogenesis Source: Ensembl
    37. striatum development Source: Ensembl
    38. urea cycle Source: Ensembl
    39. vesicle transport along microtubule Source: UniProtKB
    40. visual learning Source: Ensembl

    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: GOC
    12. nucleus Source: UniProtKB
    13. protein complex Source: UniProtKB

    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

    ArrayExpressiP42858.
    BgeeiP42858.
    CleanExiHS_HTT.
    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
    HAP1P54257-24EBI-466029,EBI-9392340
    Hap1P542562EBI-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
    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. 184 interactions.
    DIPiDIP-32492N.
    IntActiP42858. 334 interactions.
    MINTiMINT-133355.
    STRINGi9606.ENSP00000347184.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MATLEKLMKA FESLKSFQQQ QQQQQQQQQQ QQQQQQQQPP PPPPPPPPPQ     50
    LPQPPPQAQP LLPQPQPPPP PPPPPPGPAV AEEPLHRPKK ELSATKKDRV 100
    NHCLTICENI VAQSVRNSPE FQKLLGIAME LFLLCSDDAE SDVRMVADEC 150
    LNKVIKALMD SNLPRLQLEL YKEIKKNGAP RSLRAALWRF AELAHLVRPQ 200
    KCRPYLVNLL PCLTRTSKRP EESVQETLAA AVPKIMASFG NFANDNEIKV 250
    LLKAFIANLK SSSPTIRRTA AGSAVSICQH SRRTQYFYSW LLNVLLGLLV 300
    PVEDEHSTLL ILGVLLTLRY LVPLLQQQVK DTSLKGSFGV TRKEMEVSPS 350
    AEQLVQVYEL TLHHTQHQDH NVVTGALELL QQLFRTPPPE LLQTLTAVGG 400
    IGQLTAAKEE SGGRSRSGSI VELIAGGGSS CSPVLSRKQK GKVLLGEEEA 450
    LEDDSESRSD VSSSALTASV KDEISGELAA SSGVSTPGSA GHDIITEQPR 500
    SQHTLQADSV DLASCDLTSS ATDGDEEDIL SHSSSQVSAV PSDPAMDLND 550
    GTQASSPISD SSQTTTEGPD SAVTPSDSSE IVLDGTDNQY LGLQIGQPQD 600
    EDEEATGILP DEASEAFRNS SMALQQAHLL KNMSHCRQPS DSSVDKFVLR 650
    DEATEPGDQE NKPCRIKGDI GQSTDDDSAP LVHCVRLLSA SFLLTGGKNV 700
    LVPDRDVRVS VKALALSCVG AAVALHPESF FSKLYKVPLD TTEYPEEQYV 750
    SDILNYIDHG DPQVRGATAI LCGTLICSIL SRSRFHVGDW MGTIRTLTGN 800
    TFSLADCIPL LRKTLKDESS VTCKLACTAV RNCVMSLCSS SYSELGLQLI 850
    IDVLTLRNSS YWLVRTELLE TLAEIDFRLV SFLEAKAENL HRGAHHYTGL 900
    LKLQERVLNN VVIHLLGDED PRVRHVAAAS LIRLVPKLFY KCDQGQADPV 950
    VAVARDQSSV YLKLLMHETQ PPSHFSVSTI TRIYRGYNLL PSITDVTMEN 1000
    NLSRVIAAVS HELITSTTRA LTFGCCEALC LLSTAFPVCI WSLGWHCGVP 1050
    PLSASDESRK SCTVGMATMI LTLLSSAWFP LDLSAHQDAL ILAGNLLAAS 1100
    APKSLRSSWA SEEEANPAAT KQEEVWPALG DRALVPMVEQ LFSHLLKVIN 1150
    ICAHVLDDVA PGPAIKAALP SLTNPPSLSP IRRKGKEKEP GEQASVPLSP 1200
    KKGSEASAAS RQSDTSGPVT TSKSSSLGSF YHLPSYLKLH DVLKATHANY 1250
    KVTLDLQNST EKFGGFLRSA LDVLSQILEL ATLQDIGKCV EEILGYLKSC 1300
    FSREPMMATV CVQQLLKTLF GTNLASQFDG LSSNPSKSQG RAQRLGSSSV 1350
    RPGLYHYCFM APYTHFTQAL ADASLRNMVQ AEQENDTSGW FDVLQKVSTQ 1400
    LKTNLTSVTK NRADKNAIHN HIRLFEPLVI KALKQYTTTT CVQLQKQVLD 1450
    LLAQLVQLRV NYCLLDSDQV FIGFVLKQFE YIEVGQFRES EAIIPNIFFF 1500
    LVLLSYERYH SKQIIGIPKI IQLCDGIMAS GRKAVTHAIP ALQPIVHDLF 1550
    VLRGTNKADA GKELETQKEV VVSMLLRLIQ YHQVLEMFIL VLQQCHKENE 1600
    DKWKRLSRQI ADIILPMLAK QQMHIDSHEA LGVLNTLFEI LAPSSLRPVD 1650
    MLLRSMFVTP NTMASVSTVQ LWISGILAIL RVLISQSTED IVLSRIQELS 1700
    FSPYLISCTV INRLRDGDST STLEEHSEGK QIKNLPEETF SRFLLQLVGI 1750
    LLEDIVTKQL KVEMSEQQHT FYCQELGTLL MCLIHIFKSG MFRRITAAAT 1800
    RLFRSDGCGG SFYTLDSLNL RARSMITTHP ALVLLWCQIL LLVNHTDYRW 1850
    WAEVQQTPKR HSLSSTKLLS PQMSGEEEDS DLAAKLGMCN REIVRRGALI 1900
    LFCDYVCQNL HDSEHLTWLI VNHIQDLISL SHEPPVQDFI SAVHRNSAAS 1950
    GLFIQAIQSR CENLSTPTML KKTLQCLEGI HLSQSGAVLT LYVDRLLCTP 2000
    FRVLARMVDI LACRRVEMLL AANLQSSMAQ LPMEELNRIQ EYLQSSGLAQ 2050
    RHQRLYSLLD RFRLSTMQDS LSPSPPVSSH PLDGDGHVSL ETVSPDKDWY 2100
    VHLVKSQCWT RSDSALLEGA ELVNRIPAED MNAFMMNSEF NLSLLAPCLS 2150
    LGMSEISGGQ KSALFEAARE VTLARVSGTV QQLPAVHHVF QPELPAEPAA 2200
    YWSKLNDLFG DAALYQSLPT LARALAQYLV VVSKLPSHLH LPPEKEKDIV 2250
    KFVVATLEAL SWHLIHEQIP LSLDLQAGLD CCCLALQLPG LWSVVSSTEF 2300
    VTHACSLIYC VHFILEAVAV QPGEQLLSPE RRTNTPKAIS EEEEEVDPNT 2350
    QNPKYITAAC EMVAEMVESL QSVLALGHKR NSGVPAFLTP LLRNIIISLA 2400
    RLPLVNSYTR VPPLVWKLGW SPKPGGDFGT AFPEIPVEFL QEKEVFKEFI 2450
    YRINTLGWTS RTQFEETWAT LLGVLVTQPL VMEQEESPPE EDTERTQINV 2500
    LAVQAITSLV LSAMTVPVAG NPAVSCLEQQ PRNKPLKALD TRFGRKLSII 2550
    RGIVEQEIQA MVSKRENIAT HHLYQAWDPV PSLSPATTGA LISHEKLLLQ 2600
    INPERELGSM SYKLGQVSIH SVWLGNSITP LREEEWDEEE EEEADAPAPS 2650
    SPPTSPVNSR KHRAGVDIHS CSQFLLELYS RWILPSSSAR RTPAILISEV 2700
    VRSLLVVSDL FTERNQFELM YVTLTELRRV HPSEDEILAQ YLVPATCKAA 2750
    AVLGMDKAVA EPVSRLLEST LRSSHLPSRV GALHGVLYVL ECDLLDDTAK 2800
    QLIPVISDYL LSNLKGIAHC VNIHSQQHVL VMCATAFYLI ENYPLDVGPE 2850
    FSASIIQMCG VMLSGSEEST PSIIYHCALR GLERLLLSEQ LSRLDAESLV 2900
    KLSVDRVNVH SPHRAMAALG LMLTCMYTGK EKVSPGRTSD PNPAAPDSES 2950
    VIVAMERVSV LFDRIRKGFP CEARVVARIL PQFLDDFFPP QDIMNKVIGE 3000
    FLSNQQPYPQ FMATVVYKVF QTLHSTGQSS MVRDWVMLSL SNFTQRAPVA 3050
    MATWSLSCFF VSASTSPWVA AILPHVISRM GKLEQVDVNL FCLVATDFYR 3100
    HQIEEELDRR AFQSVLEVVA APGSPYHRLL TCLRNVHKVT TC 3142
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 184 interactions.
    DIPi DIP-32492N.
    IntActi P42858. 334 interactions.
    MINTi MINT-133355.
    STRINGi 9606.ENSP00000347184.

    Chemistry

    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.
    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

    ArrayExpressi P42858.
    Bgeei P42858.
    CleanExi HS_HTT.
    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

    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: October 1, 2014
    This is version 152 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