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2LP1

The solution NMR structure of the transmembrane C-terminal domain of the amyloid precursor protein (C99)

Functional Information from GO Data
ChainGOidnamespacecontents
A0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00320
Number of Residues8
DetailsAPP_INTRA Amyloid precursor protein (APP) intracellular domain signature. GYENPTYK
ChainResidueDetails
AGLY756-LYS763

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsTRANSMEM: Helical => ECO:0000305|PubMed:22584060, ECO:0000305|PubMed:22654059, ECO:0000305|PubMed:30630874
ChainResidueDetails
AILE702-MET722

site_idSWS_FT_FI2
Number of Residues47
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
ALEU723-ASN770

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:11274207, ECO:0000269|PubMed:26898943
ChainResidueDetails
AHIS677
AHIS685

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:10413512, ECO:0000305|PubMed:11274207
ChainResidueDetails
ATYR681

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10413512, ECO:0000269|PubMed:11274207, ECO:0000269|PubMed:26898943
ChainResidueDetails
AHIS684

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Cleavage; by beta-secretase => ECO:0000305|PubMed:11851430
ChainResidueDetails
AMET671

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Cleavage; by caspase-6; when associated with variant 670-N-L-671
ChainResidueDetails
AASP672

site_idSWS_FT_FI8
Number of Residues1
DetailsSITE: Cleavage; by ACE => ECO:0000269|PubMed:11604391, ECO:0000269|PubMed:16154999
ChainResidueDetails
AASP678

site_idSWS_FT_FI9
Number of Residues1
DetailsSITE: Cleavage; by alpha-secretase => ECO:0000305|PubMed:11851430
ChainResidueDetails
ALYS687

site_idSWS_FT_FI10
Number of Residues1
DetailsSITE: Cleavage; by theta-secretase => ECO:0000269|PubMed:16816112
ChainResidueDetails
APHE690

site_idSWS_FT_FI11
Number of Residues1
DetailsSITE: Implicated in free radical propagation => ECO:0000250
ChainResidueDetails
AGLY704

site_idSWS_FT_FI12
Number of Residues1
DetailsSITE: Susceptible to oxidation => ECO:0000269|PubMed:10535332
ChainResidueDetails
AMET706

site_idSWS_FT_FI13
Number of Residues1
DetailsSITE: Cleavage; by gamma-secretase; site 1 => ECO:0000305|PubMed:11851430
ChainResidueDetails
AVAL711

site_idSWS_FT_FI14
Number of Residues1
DetailsSITE: Cleavage; by gamma-secretase; site 2 => ECO:0000305|PubMed:11851430
ChainResidueDetails
AALA713

site_idSWS_FT_FI15
Number of Residues1
DetailsSITE: Cleavage; by gamma-secretase; site 3 => ECO:0000269|PubMed:11851430, ECO:0000305|PubMed:30630874
ChainResidueDetails
ALEU720

site_idSWS_FT_FI16
Number of Residues1
DetailsSITE: Cleavage; by caspase-6, caspase-8 or caspase-9 => ECO:0000269|PubMed:10319819
ChainResidueDetails
AASP739

site_idSWS_FT_FI17
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P08592
ChainResidueDetails
ATHR729

site_idSWS_FT_FI18
Number of Residues1
DetailsMOD_RES: Phosphoserine; by APP-kinase I => ECO:0000250|UniProtKB:P08592
ChainResidueDetails
ASER730

site_idSWS_FT_FI19
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CDK5 and MAPK10 => ECO:0000269|PubMed:28720718, ECO:0000269|PubMed:8131745, ECO:0007744|PubMed:24275569
ChainResidueDetails
ATHR743

site_idSWS_FT_FI20
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:11877420
ChainResidueDetails
ATYR757

site_idSWS_FT_FI21
Number of Residues1
DetailsCARBOHYD: O-linked (HexNAc...) tyrosine; partial => ECO:0000269|PubMed:22576872
ChainResidueDetails
ATYR681

site_idSWS_FT_FI22
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P08592
ChainResidueDetails
ALYS763

223166

PDB entries from 2024-07-31

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