Q92624 · APBP2_HUMAN
- ProteinAmyloid protein-binding protein 2
- GeneAPPBP2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids585 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (PubMed:29775578, PubMed:29779948).
The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms (PubMed:29775578, PubMed:29779948).
The CRL2(APPBP2) complex specifically recognizes proteins with a -Arg-Xaa-Xaa-Gly degron at the C-terminus, leading to their ubiquitination and degradation (PubMed:29775578, PubMed:29779948).
The CRL2(APPBP2) complex mediates ubiquitination and degradation of truncated SELENOV selenoproteins produced by failed UGA/Sec decoding, which end with a -Arg-Xaa-Xaa-Gly degron (PubMed:26138980).
May play a role in intracellular protein transport: may be involved in the translocation of APP along microtubules toward the cell surface (PubMed:9843960).
The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms (PubMed:29775578, PubMed:29779948).
The CRL2(APPBP2) complex specifically recognizes proteins with a -Arg-Xaa-Xaa-Gly degron at the C-terminus, leading to their ubiquitination and degradation (PubMed:29775578, PubMed:29779948).
The CRL2(APPBP2) complex mediates ubiquitination and degradation of truncated SELENOV selenoproteins produced by failed UGA/Sec decoding, which end with a -Arg-Xaa-Xaa-Gly degron (PubMed:26138980).
May play a role in intracellular protein transport: may be involved in the translocation of APP along microtubules toward the cell surface (PubMed:9843960).
Activity regulation
E3 ubiquitin-protein ligase activity of the CRL2(APPBP2) complex is inhibited by APP.
Pathway
Protein modification; protein ubiquitination.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | Cul2-RING ubiquitin ligase complex | |
Cellular Component | cytoplasm | |
Cellular Component | cytoplasmic vesicle membrane | |
Cellular Component | microtubule | |
Cellular Component | microtubule associated complex | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | microtubule motor activity | |
Molecular Function | ubiquitin-like ligase-substrate adaptor activity | |
Biological Process | intracellular protein transport | |
Biological Process | intracellular transport | |
Biological Process | proteasome-mediated ubiquitin-dependent protein catabolic process | |
Biological Process | protein ubiquitination |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAmyloid protein-binding protein 2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ92624
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Peripheral membrane protein
Note: Associated with membranes and microtubules.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_052606 | 561 | in dbSNP:rs34146848 | |||
Sequence: S → N |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 382 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000106259 | 1-585 | Amyloid protein-binding protein 2 | |||
Sequence: MAAVELEWIPETLYNTAISAVVDNYIRSRRDIRSLPENIQFDVYYKLYQQGRLCQLGSEFCELEVFAKVLRALDKRHLLHHCFQALMDHGVKVASVLAYSFSRRCSYIAESDAAVKEKAIQVGFVLGGFLSDAGWYSDAEKVFLSCLQLCTLHDEMLHWFRAVECCVRLLHVRNGNCKYHLGEETFKLAQTYMDKLSKHGQQANKAALYGELCALLFAKSHYDEAYKWCIEAMKEITAGLPVKVVVDVLRQASKACVVKREFKKAEQLIKHAVYLARDHFGSKHPKYSDTLLDYGFYLLNVDNICQSVAIYQAALDIRQSVFGGKNIHVATAHEDLAYSSYVHQYSSGKFDNALFHAERAIGIITHILPEDHLLLASSKRVKALILEEIAIDCHNKETEQRLLQEAHDLHLSSLQLAKKAFGEFNVQTAKHYGNLGRLYQSMRKFKEAEEMHIKAIQIKEQLLGQEDYEVALSVGHLASLYNYDMNQYENAEKLYLRSIAIGKKLFGEGYSGLEYDYRGLIKLYNSIGNYEKVFEYHNVLSNWNRLRDRQYSVTDALEDVSTSPQSTEEVVQSFLISQNVEGPSC |
Post-translational modification
Rapidly degraded by the proteasome upon overexpression of a C-terminal fragment of APP.
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Component of a CRL2 E3 ubiquitin-protein ligase complex, also named ECS (Elongin BC-CUL2/5-SOCS-box protein) complex, composed of CUL2, Elongin BC (ELOB and ELOC), RBX1 and substrate-specific adapter APPBP2 (PubMed:29775578, PubMed:29779948).
Interacts with APP; APP interaction inhibits the E3 ubiquitin-protein ligase activity of the CRL2(APPBP2) complex (PubMed:29775578, PubMed:9843960).
Interacts with APP; APP interaction inhibits the E3 ubiquitin-protein ligase activity of the CRL2(APPBP2) complex (PubMed:29775578, PubMed:9843960).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 50-83 | TPR 1 | ||||
Sequence: QGRLCQLGSEFCELEVFAKVLRALDKRHLLHHCF | ||||||
Repeat | 120-153 | TPR 2 | ||||
Sequence: IQVGFVLGGFLSDAGWYSDAEKVFLSCLQLCTLH | ||||||
Repeat | 206-239 | TPR 3 | ||||
Sequence: AALYGELCALLFAKSHYDEAYKWCIEAMKEITAG | ||||||
Repeat | 288-321 | TPR 4 | ||||
Sequence: SDTLLDYGFYLLNVDNICQSVAIYQAALDIRQSV | ||||||
Repeat | 333-367 | TPR 5 | ||||
Sequence: HEDLAYSSYVHQYSSGKFDNALFHAERAIGIITHI | ||||||
Repeat | 429-462 | TPR 6 | ||||
Sequence: AKHYGNLGRLYQSMRKFKEAEEMHIKAIQIKEQL | ||||||
Repeat | 471-505 | TPR 7 | ||||
Sequence: ALSVGHLASLYNYDMNQYENAEKLYLRSIAIGKKL | ||||||
Repeat | 514-547 | TPR 8 | ||||
Sequence: EYDYRGLIKLYNSIGNYEKVFEYHNVLSNWNRLR |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length585
- Mass (Da)66,853
- Last updated2004-07-19 v2
- Checksum849A120807DA2438
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 296 | in Ref. 1; AAC83973 | ||||
Sequence: F → L | ||||||
Sequence conflict | 325 | in Ref. 1; AAC83973 | ||||
Sequence: K → R | ||||||
Sequence conflict | 340 | in Ref. 1; AAC83973 | ||||
Sequence: S → C | ||||||
Sequence conflict | 354 | in Ref. 1; AAC83973 | ||||
Sequence: L → V | ||||||
Sequence conflict | 369 | in Ref. 1; AAC83973 | ||||
Sequence: P → R | ||||||
Sequence conflict | 542 | in Ref. 1; AAC83973 | ||||
Sequence: N → K |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF017782 EMBL· GenBank· DDBJ | AAC83973.1 EMBL· GenBank· DDBJ | mRNA | ||
D86981 EMBL· GenBank· DDBJ | BAA13217.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK292227 EMBL· GenBank· DDBJ | BAF84916.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471179 EMBL· GenBank· DDBJ | EAW51406.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC018121 EMBL· GenBank· DDBJ | AAH18121.1 EMBL· GenBank· DDBJ | mRNA |