Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6YEJ

Cryo-EM structure of the Full-length disease type human Huntingtin

Functional Information from GO Data
ChainGOidnamespacecontents
A0000132biological_processestablishment of mitotic spindle orientation
A0002039molecular_functionp53 binding
A0005515molecular_functionprotein binding
A0005522molecular_functionprofilin binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005768cellular_componentendosome
A0005769cellular_componentearly endosome
A0005770cellular_componentlate endosome
A0005776cellular_componentautophagosome
A0005783cellular_componentendoplasmic reticulum
A0005794cellular_componentGolgi apparatus
A0005814cellular_componentcentriole
A0005829cellular_componentcytosol
A0006890biological_processretrograde vesicle-mediated transport, Golgi to endoplasmic reticulum
A0006915biological_processapoptotic process
A0007030biological_processGolgi organization
A0016234cellular_componentinclusion body
A0019900molecular_functionkinase binding
A0030424cellular_componentaxon
A0030425cellular_componentdendrite
A0030659cellular_componentcytoplasmic vesicle membrane
A0031072molecular_functionheat shock protein binding
A0031587biological_processpositive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity
A0031648biological_processprotein destabilization
A0032991cellular_componentprotein-containing complex
A0034452molecular_functiondynactin binding
A0042297biological_processvocal learning
A0042802molecular_functionidentical protein binding
A0043065biological_processpositive regulation of apoptotic process
A0043666biological_processregulation of phosphoprotein phosphatase activity
A0044325molecular_functiontransmembrane transporter binding
A0045505molecular_functiondynein intermediate chain binding
A0045724biological_processpositive regulation of cilium assembly
A0047496biological_processvesicle transport along microtubule
A0048471cellular_componentperinuclear region of cytoplasm
A0048487molecular_functionbeta-tubulin binding
A0099111biological_processmicrotubule-based transport
A0099523cellular_componentpresynaptic cytosol
A0099524cellular_componentpostsynaptic cytosol
A1901526biological_processpositive regulation of mitophagy
A1904504biological_processpositive regulation of lipophagy
A1905289biological_processregulation of CAMKK-AMPK signaling cascade
A1905337biological_processpositive regulation of aggrephagy
A2000479biological_processregulation of cAMP-dependent protein kinase activity
A2001237biological_processnegative regulation of extrinsic apoptotic signaling pathway
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Cleavage; by caspase-3 => ECO:0000269|PubMed:9535906
ChainResidueDetails
AASP562

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by caspase-3 => ECO:0000255
ChainResidueDetails
AASP579
AASP638

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Cleavage; by caspase-3 => ECO:0000269|PubMed:29802276
ChainResidueDetails
AASP601

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Cleavage; by caspase-6 => ECO:0000269|PubMed:10770929
ChainResidueDetails
AASP635

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:21685499
ChainResidueDetails
ALYS227
ALYS285
ALYS394
ALYS493

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER462

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P42859
ChainResidueDetails
ASER468
ASER470

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER483

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER691
ASER694

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CDK5 => ECO:0000269|PubMed:17611284
ChainResidueDetails
ASER1230

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CDK5 => ECO:0000269|PubMed:17611284, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER1250

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231
ChainResidueDetails
ASER1921

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER1925

site_idSWS_FT_FI14
Number of Residues1
DetailsLIPID: N-myristoyl glycine => ECO:0000269|PubMed:24459296, ECO:0000269|PubMed:29802276
ChainResidueDetails
AGLY602

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon