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HUMAN:HD

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Contents

Species (Taxon ID) Homo sapiens (Human). (taxon:9606)
Gene Name(s) HTT ( synonyms: HD, IT15 )
Protein Name(s)
  • Huntingtin
  • Huntington disease protein
  • HD protein
External Links
UniProt Identifier HD_HUMAN
UniProt Accessions P42858, Q9UQB7,
EMBL L12392, AB016794, Z49154, Z49155, Z49208, Z49769, Z68756, Z69649, L27350, L27351, L27352, L27353, L27354, L34020, L20431,
PIR A46068,
RefSeq NP_002102.4,
PDB 2D3X, 3IO4, 3IO6, 3IOR, 3IOT, 3IOU, 3IOV, 3IOW, 3LRH,
IntAct P42858,
Ensembl ENST00000355072,
Pfam PF02985,

Annotations

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0005794

Golgi apparatus

IDA: Inferred from Direct Assay

C

Source: UniProtKB

GO:0034399

nuclear periphery

IDA: Inferred from Direct Assay

C

Source: UniProtKB

GO:0005625

soluble fraction

TAS: Traceable Author Statement

C

Source: ProtInc

GO:0008017

microtubule binding

TAS: Traceable Author Statement

F

Source: ProtInc

GO:0003714

transcription corepressor activity

TAS: Traceable Author Statement

F

Source: ProtInc

GO:0005215

transporter activity

TAS: Traceable Author Statement

F

Source: ProtInc

GO:0006917

induction of apoptosis

TAS: Traceable Author Statement

P

Source: ProtInc

GO:0000132

establishment of mitotic spindle orientation

PMID:20696378[1]

IMP: Inferred from Mutant Phenotype

P

GO:0002039

p53 binding

PMID:10823891[2]

IPI: Inferred from Physical Interaction

UniProtKB:P04637

F

GO:0005488

binding

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR011989

F

GO:0005488

binding

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR016024

F

GO:0005515

protein binding

PMID:10823891[2]

IPI: Inferred from Physical Interaction

UniProtKB:P04637

F

GO:0005515

protein binding

PMID:10823891[2]

IPI: Inferred from Physical Interaction

UniProtKB:Q92793

F

GO:0005515

protein binding

PMID:10823891[2]

IPI: Inferred from Physical Interaction

UniProtKB:Q96ST3

F

GO:0005515

protein binding

PMID:15383276[3]

IPI: Inferred from Physical Interaction

UniProtKB:O95163

F

GO:0005515

protein binding

PMID:15383276[3]

IPI: Inferred from Physical Interaction

UniProtKB:P12956

F

GO:0005515

protein binding

PMID:15383276[3]

IPI: Inferred from Physical Interaction

UniProtKB:P35080

F

GO:0005515

protein binding

PMID:15383276[3]

IPI: Inferred from Physical Interaction

UniProtKB:Q12873

F

GO:0005515

protein binding

PMID:15383276[3]

IPI: Inferred from Physical Interaction

UniProtKB:Q13011

F

GO:0005515

protein binding

PMID:15383276[3]

IPI: Inferred from Physical Interaction

UniProtKB:Q14194

F

GO:0005515

protein binding

PMID:15383276[3]

IPI: Inferred from Physical Interaction

UniProtKB:Q8N2W9

F

GO:0005515

protein binding

PMID:15383276[3]

IPI: Inferred from Physical Interaction

UniProtKB:Q99689

F

GO:0005515

protein binding

PMID:15383276[3]

IPI: Inferred from Physical Interaction

UniProtKB:Q9P2H0

F

GO:0005515

protein binding

PMID:15383276[3]

IPI: Inferred from Physical Interaction

UniProtKB:Q9Y2X7

F

GO:0005515

protein binding

PMID:15383276[3]

IPI: Inferred from Physical Interaction

UniProtKB:Q9Y3C7

F

GO:0005515

protein binding

PMID:15603740[4]

IPI: Inferred from Physical Interaction

UniProtKB:Q8IUH5

F

GO:0005515

protein binding

PMID:20417604[5]

IPI: Inferred from Physical Interaction

UniProtKB:Q14596

F

GO:0005515

protein binding

PMID:20417604[5]

IPI: Inferred from Physical Interaction

UniProtKB:Q8IZQ1

F

GO:0005515

protein binding

PMID:20515468[6]

IPI: Inferred from Physical Interaction

UniProtKB:P54257

F

GO:0005515

protein binding

PMID:7477378[7]

IPI: Inferred from Physical Interaction

UniProtKB:P54257

F

GO:0005624

membrane fraction

PMID:7748555[8]

IDA: Inferred from Direct Assay

C

GO:0005634

nucleus

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000091

C

GO:0005634

nucleus

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0539

C

GO:0005634

nucleus

GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_SL:SL-0191

C

GO:0005634

nucleus

PMID:12783847[9]

IDA: Inferred from Direct Assay

C

GO:0005634

nucleus

PMID:17704510[10]

IDA: Inferred from Direct Assay

C

GO:0005634

nucleus

PMID:18029348[11]

IDA: Inferred from Direct Assay

C

GO:0005737

cytoplasm

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000091

C

GO:0005737

cytoplasm

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0963

C

GO:0005737

cytoplasm

GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_SL:SL-0086

C

GO:0005737

cytoplasm

PMID:15064418[12]

IDA: Inferred from Direct Assay

C

GO:0005737

cytoplasm

PMID:18029348[11]

IDA: Inferred from Direct Assay

C

GO:0005737

cytoplasm

PMID:7748555[8]

IDA: Inferred from Direct Assay

C

GO:0005770

late endosome

PMID:17704510[10]

IDA: Inferred from Direct Assay

C

GO:0005776

autophagic vacuole

PMID:17704510[10]

IDA: Inferred from Direct Assay

C

GO:0005783

endoplasmic reticulum

PMID:17704510[10]

IDA: Inferred from Direct Assay

C

GO:0005794

Golgi apparatus

PMID:15837803[13]

IDA: Inferred from Direct Assay

C

GO:0005829

cytosol

PMID:20515468[6]

IDA: Inferred from Direct Assay

C

GO:0006890

retrograde vesicle-mediated transport, Golgi to ER

PMID:20515468[6]

IMP: Inferred from Mutant Phenotype

P

GO:0006915

apoptosis

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0053

P

GO:0007030

Golgi organization

PMID:20515468[6]

IMP: Inferred from Mutant Phenotype

P

GO:0008134

transcription factor binding

GO_REF:0000033

PANTHER:PTHR10170_AN3

F

GO:0008219

cell death

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0523

P

GO:0030424

axon

PMID:7748555[8]

IDA: Inferred from Direct Assay

C

GO:0030425

dendrite

PMID:7748555[8]

IDA: Inferred from Direct Assay

C

GO:0030659

cytoplasmic vesicle membrane

PMID:7748555[8]

IDA: Inferred from Direct Assay

C

GO:0034452

dynactin binding

PMID:18922795[14]

IPI: Inferred from Physical Interaction

UniProtKB:Q14203

F

GO:0043234

protein complex

PMID:18922795[14]

IDA: Inferred from Direct Assay

C

GO:0045505

dynein intermediate chain binding

PMID:20515468[6]

IDA: Inferred from Direct Assay

F

GO:0047496

vesicle transport along microtubule

PMID:20515468[6]

IMP: Inferred from Mutant Phenotype

P

GO:0048487

beta-tubulin binding

PMID:11870213[15]

IDA: Inferred from Direct Assay

F

GO:0048513

organ development

GO_REF:0000033

PANTHER:PTHR10170_AN4

P

NOT

GO:0005730

nucleolus

PMID:18029348[11]

IDA: Inferred from Direct Assay

C


Notes

References

See Help:References for how to manage references in GONUTS.

  1. Godin JD et al. (2010) Huntingtin is required for mitotic spindle orientation and mammalian neurogenesis. Neuron 67: 392-406 PubMed GONUTS page
  2. 2.0 2.1 2.2 2.3 Steffan JS et al. (2000) The Huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription. Proc Natl Acad Sci U S A 97: 6763-8 PubMed GONUTS page
  3. 3.00 3.01 3.02 3.03 3.04 3.05 3.06 3.07 3.08 3.09 3.10 Goehler H et al. (2004) A protein interaction network links GIT1, an enhancer of huntingtin aggregation, to Huntington's disease. Mol Cell 15: 853-65 PubMed GONUTS page
  4. Huang K et al. (2004) Huntingtin-interacting protein HIP14 is a palmitoyl transferase involved in palmitoylation and trafficking of multiple neuronal proteins. Neuron 44: 977-86 PubMed GONUTS page
  5. 5.0 5.1 Filimonenko M et al. (2010) The selective macroautophagic degradation of aggregated proteins requires the PI3P-binding protein Alfy. Mol Cell 38: 265-79 PubMed GONUTS page
  6. 6.0 6.1 6.2 6.3 6.4 6.5 Pardo R et al. (2010) pARIS-htt: an optimised expression platform to study huntingtin reveals functional domains required for vesicular trafficking. Mol Brain 3: 17 PubMed GONUTS page
  7. Li XJ et al. (1995) A huntingtin-associated protein enriched in brain with implications for pathology. Nature 378: 398-402 PubMed GONUTS page
  8. 8.0 8.1 8.2 8.3 8.4 DiFiglia M et al. (1995) Huntingtin is a cytoplasmic protein associated with vesicles in human and rat brain neurons. Neuron 14: 1075-81 PubMed GONUTS page
  9. Xia J et al. (2003) Huntingtin contains a highly conserved nuclear export signal. Hum Mol Genet 12: 1393-403 PubMed GONUTS page
  10. 10.0 10.1 10.2 10.3 Atwal RS et al. (2007) Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity. Hum Mol Genet 16: 2600-15 PubMed GONUTS page
  11. 11.0 11.1 11.2 Barbe L et al. (2008) Toward a confocal subcellular atlas of the human proteome. Mol Cell Proteomics 7: 499-508 PubMed GONUTS page
  12. Steffan JS et al. (2004) SUMO modification of Huntingtin and Huntington's disease pathology. Science 304: 100-4 PubMed GONUTS page
  13. Sahlender DA et al. (2005) Optineurin links myosin VI to the Golgi complex and is involved in Golgi organization and exocytosis. J Cell Biol 169: 285-95 PubMed GONUTS page
  14. 14.0 14.1 Shimojo M (2008) Huntingtin regulates RE1-silencing transcription factor/neuron-restrictive silencer factor (REST/NRSF) nuclear trafficking indirectly through a complex with REST/NRSF-interacting LIM domain protein (RILP) and dynactin p150 Glued. J Biol Chem 283: 34880-6 PubMed GONUTS page
  15. Hoffner G et al. (2002) Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with beta-tubulin: relevance to Huntington's disease. J Cell Sci 115: 941-8 PubMed GONUTS page
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