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P51111

- HD_RAT

UniProt

P51111 - HD_RAT

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Protein

Huntingtin

Gene
Htt, Hd, Hdh
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. protein binding Source: RGD
  2. receptor binding Source: RGD
  3. 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-acetyllysine By similarity
Modified residuei146 – 1461N6-acetyllysine By similarity
Modified residuei204 – 2041N6-acetyllysine By similarity
Modified residuei313 – 3131N6-acetyllysine By similarity
Modified residuei402 – 4021Phosphoserine By similarity
Modified residuei412 – 4121N6-acetyllysine By similarity
Modified residuei1150 – 11501Phosphoserine; by CDK5 By similarity
Modified residuei1170 – 11701Phosphoserine; by CDK5 By similarity
Modified residuei1845 – 18451Phosphoserine By 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.

Protein-protein interaction databases

MINTiMINT-3375769.
STRINGi10116.ENSRNOP00000054971.

Structurei

3D structure databases

ProteinModelPortaliP51111.

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 signal By 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.
Contains 5 HEAT repeats.

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

MKAFESLKSF QQQQQQQQPP PQPPPPPPPP PQPPQPPPQG QPPPPPPLPG     50
PAEEPLHRPK KELSATKKDR VNHCLTICEN IVAQSLRNSP EFQKLLGIAM 100
ELFLLCSDDA SRRRMVADEC LNKVIKALMD SNLPRLQLEL YKEIKKNGAP 150
RSLRAALWRF AELAHLVRPQ KCRPYLVNLL PCLTRTSKRP EESVQETLAA 200
AVPKIMASFG NFANDNEIKV LLKAFIANLK SSSPTVRRTA AGSAVSICQH 250
SRRTQYFYNW LLNVLLGLLV PMEEDHPTLL ILGVLLTLRC LVPLLQQQVK 300
DTSLKGSFGV TRKEMEVSPS AEQLVQVYEL TLHHTQHQDH NVVTGALELL 350
QQLFRTPPPE LLQALTTPGG LGQLTLVREE AGGRGRSGSI VELLAGGGSS 400
CSPVLSRKQK GKVLLGEEEA LEDDSESRSD VSSSAFAASV KSEIGGELAA 450
SSSGVSTPGS VGHDIITEQP RSQHTLQADS VDLSGCDLTS AATDGDEEDI 500
LSHSSSQFSA VPSDPAMDLN DGTQASSPIS DSSQTTTEGP DSAVTPSDSS 550
EIVLDGADSQ YLGVQIGQPQ EEDREAAGVL SGEVSDVFRN SSLALQQAHL 600
LERMGHSRQP SDSSVDKFVS KDEVAEAGDP ESKPCRIKGD IGQPNDDDSA 650
PLVHCVRLLS ASFLLTGEKK ALVPDRDVRV SVKALALSCI GAAVALHPES 700
FFSKLYKVPL STMESTEEQY VSDILNYIDH GDPQVRGATA ILCGTLVYSI 750
LSRSRLRVGD WLGTIRALTG NTFSLVDCIP LLQKTLKDES SVTCKLACTA 800
VRHCVLSLCS SSYSDLGLQL LIDMLPLKNS SYWLVRTELL ETLAEIDFRL 850
VSFLEAKAES LHRGPHHYTG FLKLQERVLN NVVIYLLGDE DPRVRHVAAT 900
TLTRLVPKLF YKCDQGQADP VEAVARDQSS VYLKLLMHET QPPSHFSVST 950
ITRIYRGYSL LPSVTDVTME NNLSRVVAAV SHELITSTTR ALTFGCCEAL 1000
CVLSAAFPVC TWSLGWHCGV PPLSASDESR KSCTVGMASM ILTLLSSAWF 1050
PLDLSAIQDA LILAGNLLAA SAPKSLRSSW ASEEEGSSAA TRQEEIWPAL 1100
GDRTLVPMVE QLFSHLLKVI NICAHVLDDE TPGPAIKAAL PSLTNPPSLS 1150
PIRRKGKEKE PGEQTSTPMS PKKGGEASTA SRQSDTSGPV TASKSSSLGS 1200
FYHLPSYLRL HDVLKATHAN YKVTLDLQNS TEKFGGFLRS ALDVLSQILE 1250
LATLQDIGKC VEEVLGYLKS CFSREPMMAT VCVQQLLKTL FGTNLASQFD 1300
GLSSNPSKSQ CRAQRLGSSS VRPGLYHYCF MAPYTHFTQA LADASLRNMV 1350
QADQEHDASG WFDVLQKVSA QLKTNLTSVT KNRADKNAIH NHIRLFEPLV 1400
IKALKQYTTT TSVQLQKQVL DLLAQLVQLR VNYCLLDSDQ VFIGFVLKQF 1450
EYIEVGQFRE SEAIIPNIFF FLVLLSYERY HSKQIIGIPK IIQLCDGIMA 1500
SGRKAVTHAI PALQPIVHDL FVLRGTNKAD AGKELETQKE VVVSMLLRLI 1550
QYHQVLEMFI LVLQQCHKEN EDKWKRLSRQ VADIILPMLA KQQMHIDSHE 1600
ALGVLNTLFE ILAPSSLRPV DMLLRSMFIT PSTMASVSTV QLWISGILAI 1650
LRVLISQSTE DIVLSRIQEL SFSPYLISCP VINRLRDGDS NPTLGERSRG 1700
KQVKNLPEDT FSRFLLQLVG ILLEDIVTKQ LKVDMSEQQH TFYCQELGTL 1750
LMCLIHIFKS GMFRRITAAA TRLFTSDGCE GSFYTLDSLN ARVRAMVPTH 1800
PALVLLWCQI LLLINHTDHR WWAEVQQTPK RHSLSCTKSL NPQISAEEDS 1850
GSAAQLGMCN REIVRRGALI LFCDYVCQNL HDSEHLTWLI VNHIQDLISL 1900
SHEPPVQDFI SAIHRNSAAS GLFIQAIQSR CENLSTPTTL KKTLQCLEGI 1950
HLSQSGAVLT LYVDRLLGTP FRALARMVDT LACRRVEMLL AANLQSSMAQ 2000
LPEEELNRIQ EHLQNTGLAQ RHQRLYSLLD RFRLSTVQDS LSPLPPVTSH 2050
PLDGDGHTSL ETVNPDKDWY LQLVRSQCWT RSDSALLEGA ELVNRIPAED 2100
MSDFMMSSEF NLSLFAPCLS LGMSEIAGSQ KSPLFEAARR VTLDRVTNVV 2150
QQLPAVHQVF QPFLPTEPTA YWSKLNDLFG DTTSYQSLTT LARALAQYLV 2200
VLSKVPAPLH LPPEKEGHTV KFVVMTLEAL SWHLIHEQIP LSLDLQAGLD 2250
CCCLALQVPG LWGVLSSPEY VTHTCSLIHC VRFILEAIAV QPGDQLLGPE 2300
SRSHTPRAVR KEEVDSDIQN LSHITSACEM VADMVESLQS VLALGHKRNS 2350
TLPSFLTAVL KNIVVSLARL PLVNSYTRVP PLVWKLGWSP KPGGDFGTVF 2400
PEIPVEFLQE KEVLKEFIYR INTLGWTSRT QFEETWATLL GVLVTQPLVM 2450
EQEESPPEED TERTQIHVLA VQAITSLVLS AMAVPVAGNP AVSCLEQQPR 2500
NKPLKALDTR FGRKLSMIRG IVEQEIQEMV SQRENTATHH SHQAWDPVPS 2550
LLPATTGALI SHDKLLLQIN SEREPGNMSY KLGQVSIHSV WLGNNITPLR 2600
EEEWDEEEEE EADAPAPTSP PVSPVNSRKH RAGVDIHSCS QFLLELYSRW 2650
ILPSSAARRT PVILISEVVR SLLVVSDLFT DVPQFEMMYL TLTELRRVHP 2700
SEDEILIQYL VPATCKAAAV LGMDKTVAEP VSRLLESTLR STHLPSQIGA 2750
LHGILYVLEC DLLDDTVKQL IPVVSDYLLS NLKGIAHCVN IHSQQHVLVM 2800
CATAFYLMEN YPLDVGPEFS ASVIQMCGVM LSGSEESTPS VIYHCALRGL 2850
ERLLLSEQLS RLDTESLVKL SVDRVNVQSP HRAMAALGLM LTCMYTGKEK 2900
ASPGRASDPS PATPDSESVI VAMERVSVLF DRIRKGFPCE ARVVARILPQ 2950
FLDDFFPPQD VMNKVIGEFL SNQQPYPQFM ATVVYKVFQT LHSAGQSSMV 3000
RDWVMLSLSN FTQRTPVAMA MWSLSCFLVS ASTSPWVSAI LPHVISRMGK 3050
LEQVDVNLFC LVATDFYRHQ IEEEFDRRAF QSVFEVVAAP GSPYHRLLAC 3100
LQNVHKVTAC 3110
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

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: June 11, 2014
This is version 103 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

Similar proteinsi