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P51111

- HD_RAT

UniProt

P51111 - HD_RAT

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Protein

Huntingtin

Gene

Htt

Organism
Rattus norvegicus (Rat)
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.

GO - Molecular functioni

  1. receptor binding Source: RGD
  2. transcription factor binding Source: RefGenome

GO - Biological processi

  1. central nervous system development Source: RGD
  2. mRNA transport Source: RGD
  3. negative regulation of cysteine-type endopeptidase activity Source: RGD
  4. organ development Source: RefGenome
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Huntingtin
Alternative name(s):
Huntington disease protein homolog
Short name:
HD protein homolog
Gene namesi
Name:Htt
Synonyms:Hd, Hdh
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi68337. Htt.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity
Note: Shuttles between cytoplasm and nucleus in a Ran GTPase-independent manner.

GO - Cellular componenti

  1. axon Source: RGD
  2. clathrin-coated vesicle Source: RGD
  3. cytoplasm Source: RefGenome
  4. cytosol Source: RGD
  5. dendrite Source: RGD
  6. neuronal cell body Source: RGD
  7. nucleus Source: RefGenome
  8. postsynaptic density Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 31103110HuntingtinPRO_0000083944Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N6-acetyllysineBy similarity
Modified residuei146 – 1461N6-acetyllysineBy similarity
Modified residuei204 – 2041N6-acetyllysineBy similarity
Modified residuei313 – 3131N6-acetyllysineBy similarity
Modified residuei402 – 4021PhosphoserineBy similarity
Modified residuei412 – 4121N6-acetyllysineBy similarity
Modified residuei1150 – 11501Phosphoserine; by CDK5By similarity
Modified residuei1170 – 11701Phosphoserine; by CDK5By similarity
Modified residuei1845 – 18451PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation at Ser-1150 and Ser-1170 by CDK5 in response to DNA damage in nuclei of neurons protects neurons against polyglutamine expansion as well as DNA damage mediated toxicity.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP51111.
PRIDEiP51111.

PTM databases

PhosphoSiteiP51111.

Expressioni

Tissue specificityi

Expressed to a high degree in all the regions of the brain of adults and in meiotic cells of the testis. In addition, very low levels are detected in various non-neuronal tissues (heart, muscle, liver, lung and kidney).

Developmental stagei

Identified at high levels in neuronal tissues of embryos as early as day 14.5. This expression remains constant in all further development stages (up to the adult). On the other hand the expression in non-neuronal tissues is down-regulated from stage 17.5 day old embryos.

Gene expression databases

GenevestigatoriP51111.

Interactioni

Subunit structurei

Interacts with PQBP1 and SETD2. Binds SH3GLB1 By similarity. Interacts with PFN1. Interacts with TPR; the interaction is inhibited by forms of Huntingtin with expanded polyglutamine stretch By similarity.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Itpr1P299944EBI-9674649,EBI-8614640

Protein-protein interaction databases

IntActiP51111. 1 interaction.
MINTiMINT-3375769.
STRINGi10116.ENSRNOP00000054971.

Structurei

3D structure databases

ProteinModelPortaliP51111.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati174 – 21138HEAT 1Add
BLAST
Repeati216 – 25338HEAT 2Add
BLAST
Repeati773 – 81038HEAT 3Add
BLAST
Repeati873 – 91139HEAT 4Add
BLAST
Repeati1395 – 143238HEAT 5Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi2363 – 237210Nuclear export signalBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi11 – 188Poly-Gln
Compositional biasi19 – 3820Poly-ProAdd
BLAST
Compositional biasi42 – 5110Poly-Pro
Compositional biasi1408 – 14114Poly-Thr
Compositional biasi2606 – 26116Poly-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.By similarity

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG82191.
HOGENOMiHOG000082472.
HOVERGENiHBG005953.
InParanoidiP51111.
PhylomeDBiP51111.

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.

P51111-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKAFESLKSF QQQQQQQQPP PQPPPPPPPP PQPPQPPPQG QPPPPPPLPG
60 70 80 90 100
PAEEPLHRPK KELSATKKDR VNHCLTICEN IVAQSLRNSP EFQKLLGIAM
110 120 130 140 150
ELFLLCSDDA SRRRMVADEC LNKVIKALMD SNLPRLQLEL YKEIKKNGAP
160 170 180 190 200
RSLRAALWRF AELAHLVRPQ KCRPYLVNLL PCLTRTSKRP EESVQETLAA
210 220 230 240 250
AVPKIMASFG NFANDNEIKV LLKAFIANLK SSSPTVRRTA AGSAVSICQH
260 270 280 290 300
SRRTQYFYNW LLNVLLGLLV PMEEDHPTLL ILGVLLTLRC LVPLLQQQVK
310 320 330 340 350
DTSLKGSFGV TRKEMEVSPS AEQLVQVYEL TLHHTQHQDH NVVTGALELL
360 370 380 390 400
QQLFRTPPPE LLQALTTPGG LGQLTLVREE AGGRGRSGSI VELLAGGGSS
410 420 430 440 450
CSPVLSRKQK GKVLLGEEEA LEDDSESRSD VSSSAFAASV KSEIGGELAA
460 470 480 490 500
SSSGVSTPGS VGHDIITEQP RSQHTLQADS VDLSGCDLTS AATDGDEEDI
510 520 530 540 550
LSHSSSQFSA VPSDPAMDLN DGTQASSPIS DSSQTTTEGP DSAVTPSDSS
560 570 580 590 600
EIVLDGADSQ YLGVQIGQPQ EEDREAAGVL SGEVSDVFRN SSLALQQAHL
610 620 630 640 650
LERMGHSRQP SDSSVDKFVS KDEVAEAGDP ESKPCRIKGD IGQPNDDDSA
660 670 680 690 700
PLVHCVRLLS ASFLLTGEKK ALVPDRDVRV SVKALALSCI GAAVALHPES
710 720 730 740 750
FFSKLYKVPL STMESTEEQY VSDILNYIDH GDPQVRGATA ILCGTLVYSI
760 770 780 790 800
LSRSRLRVGD WLGTIRALTG NTFSLVDCIP LLQKTLKDES SVTCKLACTA
810 820 830 840 850
VRHCVLSLCS SSYSDLGLQL LIDMLPLKNS SYWLVRTELL ETLAEIDFRL
860 870 880 890 900
VSFLEAKAES LHRGPHHYTG FLKLQERVLN NVVIYLLGDE DPRVRHVAAT
910 920 930 940 950
TLTRLVPKLF YKCDQGQADP VEAVARDQSS VYLKLLMHET QPPSHFSVST
960 970 980 990 1000
ITRIYRGYSL LPSVTDVTME NNLSRVVAAV SHELITSTTR ALTFGCCEAL
1010 1020 1030 1040 1050
CVLSAAFPVC TWSLGWHCGV PPLSASDESR KSCTVGMASM ILTLLSSAWF
1060 1070 1080 1090 1100
PLDLSAIQDA LILAGNLLAA SAPKSLRSSW ASEEEGSSAA TRQEEIWPAL
1110 1120 1130 1140 1150
GDRTLVPMVE QLFSHLLKVI NICAHVLDDE TPGPAIKAAL PSLTNPPSLS
1160 1170 1180 1190 1200
PIRRKGKEKE PGEQTSTPMS PKKGGEASTA SRQSDTSGPV TASKSSSLGS
1210 1220 1230 1240 1250
FYHLPSYLRL HDVLKATHAN YKVTLDLQNS TEKFGGFLRS ALDVLSQILE
1260 1270 1280 1290 1300
LATLQDIGKC VEEVLGYLKS CFSREPMMAT VCVQQLLKTL FGTNLASQFD
1310 1320 1330 1340 1350
GLSSNPSKSQ CRAQRLGSSS VRPGLYHYCF MAPYTHFTQA LADASLRNMV
1360 1370 1380 1390 1400
QADQEHDASG WFDVLQKVSA QLKTNLTSVT KNRADKNAIH NHIRLFEPLV
1410 1420 1430 1440 1450
IKALKQYTTT TSVQLQKQVL DLLAQLVQLR VNYCLLDSDQ VFIGFVLKQF
1460 1470 1480 1490 1500
EYIEVGQFRE SEAIIPNIFF FLVLLSYERY HSKQIIGIPK IIQLCDGIMA
1510 1520 1530 1540 1550
SGRKAVTHAI PALQPIVHDL FVLRGTNKAD AGKELETQKE VVVSMLLRLI
1560 1570 1580 1590 1600
QYHQVLEMFI LVLQQCHKEN EDKWKRLSRQ VADIILPMLA KQQMHIDSHE
1610 1620 1630 1640 1650
ALGVLNTLFE ILAPSSLRPV DMLLRSMFIT PSTMASVSTV QLWISGILAI
1660 1670 1680 1690 1700
LRVLISQSTE DIVLSRIQEL SFSPYLISCP VINRLRDGDS NPTLGERSRG
1710 1720 1730 1740 1750
KQVKNLPEDT FSRFLLQLVG ILLEDIVTKQ LKVDMSEQQH TFYCQELGTL
1760 1770 1780 1790 1800
LMCLIHIFKS GMFRRITAAA TRLFTSDGCE GSFYTLDSLN ARVRAMVPTH
1810 1820 1830 1840 1850
PALVLLWCQI LLLINHTDHR WWAEVQQTPK RHSLSCTKSL NPQISAEEDS
1860 1870 1880 1890 1900
GSAAQLGMCN REIVRRGALI LFCDYVCQNL HDSEHLTWLI VNHIQDLISL
1910 1920 1930 1940 1950
SHEPPVQDFI SAIHRNSAAS GLFIQAIQSR CENLSTPTTL KKTLQCLEGI
1960 1970 1980 1990 2000
HLSQSGAVLT LYVDRLLGTP FRALARMVDT LACRRVEMLL AANLQSSMAQ
2010 2020 2030 2040 2050
LPEEELNRIQ EHLQNTGLAQ RHQRLYSLLD RFRLSTVQDS LSPLPPVTSH
2060 2070 2080 2090 2100
PLDGDGHTSL ETVNPDKDWY LQLVRSQCWT RSDSALLEGA ELVNRIPAED
2110 2120 2130 2140 2150
MSDFMMSSEF NLSLFAPCLS LGMSEIAGSQ KSPLFEAARR VTLDRVTNVV
2160 2170 2180 2190 2200
QQLPAVHQVF QPFLPTEPTA YWSKLNDLFG DTTSYQSLTT LARALAQYLV
2210 2220 2230 2240 2250
VLSKVPAPLH LPPEKEGHTV KFVVMTLEAL SWHLIHEQIP LSLDLQAGLD
2260 2270 2280 2290 2300
CCCLALQVPG LWGVLSSPEY VTHTCSLIHC VRFILEAIAV QPGDQLLGPE
2310 2320 2330 2340 2350
SRSHTPRAVR KEEVDSDIQN LSHITSACEM VADMVESLQS VLALGHKRNS
2360 2370 2380 2390 2400
TLPSFLTAVL KNIVVSLARL PLVNSYTRVP PLVWKLGWSP KPGGDFGTVF
2410 2420 2430 2440 2450
PEIPVEFLQE KEVLKEFIYR INTLGWTSRT QFEETWATLL GVLVTQPLVM
2460 2470 2480 2490 2500
EQEESPPEED TERTQIHVLA VQAITSLVLS AMAVPVAGNP AVSCLEQQPR
2510 2520 2530 2540 2550
NKPLKALDTR FGRKLSMIRG IVEQEIQEMV SQRENTATHH SHQAWDPVPS
2560 2570 2580 2590 2600
LLPATTGALI SHDKLLLQIN SEREPGNMSY KLGQVSIHSV WLGNNITPLR
2610 2620 2630 2640 2650
EEEWDEEEEE EADAPAPTSP PVSPVNSRKH RAGVDIHSCS QFLLELYSRW
2660 2670 2680 2690 2700
ILPSSAARRT PVILISEVVR SLLVVSDLFT DVPQFEMMYL TLTELRRVHP
2710 2720 2730 2740 2750
SEDEILIQYL VPATCKAAAV LGMDKTVAEP VSRLLESTLR STHLPSQIGA
2760 2770 2780 2790 2800
LHGILYVLEC DLLDDTVKQL IPVVSDYLLS NLKGIAHCVN IHSQQHVLVM
2810 2820 2830 2840 2850
CATAFYLMEN YPLDVGPEFS ASVIQMCGVM LSGSEESTPS VIYHCALRGL
2860 2870 2880 2890 2900
ERLLLSEQLS RLDTESLVKL SVDRVNVQSP HRAMAALGLM LTCMYTGKEK
2910 2920 2930 2940 2950
ASPGRASDPS PATPDSESVI VAMERVSVLF DRIRKGFPCE ARVVARILPQ
2960 2970 2980 2990 3000
FLDDFFPPQD VMNKVIGEFL SNQQPYPQFM ATVVYKVFQT LHSAGQSSMV
3010 3020 3030 3040 3050
RDWVMLSLSN FTQRTPVAMA MWSLSCFLVS ASTSPWVSAI LPHVISRMGK
3060 3070 3080 3090 3100
LEQVDVNLFC LVATDFYRHQ IEEEFDRRAF QSVFEVVAAP GSPYHRLLAC
3110
LQNVHKVTAC
Length:3,110
Mass (Da):343,762
Last modified:October 1, 1996 - v1
Checksum:i33C357E8FC141550
GO

Polymorphismi

The poly-Gln region does not appear to be polymorphic, explaining the absence of a rodent HD-like disorder.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U18650 mRNA. Translation: AAA90987.1. Sequence problems.
U01022 mRNA. Translation: AAC52133.1.
PIRiS40522.
UniGeneiRn.11193.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U18650 mRNA. Translation: AAA90987.1 . Sequence problems.
U01022 mRNA. Translation: AAC52133.1 .
PIRi S40522.
UniGenei Rn.11193.

3D structure databases

ProteinModelPortali P51111.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P51111. 1 interaction.
MINTi MINT-3375769.
STRINGi 10116.ENSRNOP00000054971.

Chemistry

ChEMBLi CHEMBL2439943.

PTM databases

PhosphoSitei P51111.

Proteomic databases

PaxDbi P51111.
PRIDEi P51111.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

RGDi 68337. Htt.

Phylogenomic databases

eggNOGi NOG82191.
HOGENOMi HOG000082472.
HOVERGENi HBG005953.
InParanoidi P51111.
PhylomeDBi P51111.

Miscellaneous databases

PROi P51111.

Gene expression databases

Genevestigatori P51111.

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. "Expression of the Huntington disease gene in rodents: cloning the rat homologue and evidence for downregulation in non-neuronal tissues during development."
    Schmitt I., Baechner D., Megow D., Henklein P., Boulter J., Hameister H., Epplen J.T., Riess O.
    Hum. Mol. Genet. 4:1173-1182(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. Lubec G., Kang S.U., Lubec S.
    Submitted (SEP-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 356-384; 429-441; 767-795; 1760-1772; 1832-1838 AND 2875-2898, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  3. "Widespread expression of the human and rat Huntington's disease gene in brain and nonneural tissues."
    Strong T.V., Tagle D.A., Valdes J.M., Elmer L.W., Boehm K., Swaroop M., Kaatz K.W., Collins F.S., Albin R.L.
    Nat. Genet. 5:259-265(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1773-1926.
    Tissue: Brain.

Entry informationi

Entry nameiHD_RAT
AccessioniPrimary (citable) accession number: P51111
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3