APBB1
entrez
322
canonical
uniprot
O00213
canonical
ensembl
ENSG00000166313
resolver
ensp
ENSP00000311912
resolver
ensp
ENSP00000433338
resolver
ensp
ENSP00000476442
resolver
ensp
ENSP00000476646
resolver
ensp
ENSP00000476846
resolver
ensp
ENSP00000476871
resolver
ensp
ENSP00000477069
resolver
ensp
ENSP00000477213
resolver
genesymbol
APBB1
resolver
genesymbol_syn
FE65
resolver
genesymbol_syn
RIR
resolver
hgnc
HGNC:581
resolver
uniprot
A1E379
resolver
uniprot
A6NH82
resolver
uniprot
A6NL69
resolver
uniprot
B7Z1J5
resolver
uniprot
B7Z1J6
resolver
uniprot
B7Z2Y0
resolver
uniprot
B7Z4M9
resolver
uniprot
D3DQT2
resolver
uniprot
Q7Z324
resolver
uniprot
Q96A93
resolver
uniprot
V9GYK0
resolver
uniprot
V9GYT4
resolver
uniprot_entry
APBB1_HUMAN
resolver
uniprot_entry
B7Z4M9_HUMAN
resolver
uniprot_sec
A1E379
resolver
uniprot_sec
A6NH82
resolver
uniprot_sec
A6NL69
resolver
uniprot_sec
B7Z1J5
resolver
uniprot_sec
B7Z1J6
resolver
uniprot_sec
B7Z2Y0
resolver
uniprot_sec
D3DQT2
resolver
uniprot_sec
Q7Z324
resolver
uniprot_sec
Q96A93
resolver
uniprot_sec
V9GYK0
resolver
uniprot_sec
V9GYT4
resolver
amino_acid_sequence
MSVPSSLSQSAINANSHGGPALSLPLPLHAAHNQLLNAKLQATAVGPKDLRSAMGEGGGPEPGPANAKWLKEGQNQLRRAATAHRDQNRNVTLTLAEEASQEPEMAPLGPKGLIHLYSELELSAHNAANRGLRGPGLIISTQEQGPDEGEEKAAGEAEEEEEDDDDEEEEEDLSSPPGLPEPLESVEAPPRPQALTDGPREHSKSASLLFGMRNSAASDEDSSWATLSQGSPSYGSPEDTDSFWNPNAFETDSDLPAGWMRVQDTSGTYYWHIPTGTTQWEPPGRASPSQGSSPQEESQLTWTGFAHGEGFEDGEFWKDEPSDEAPMELGLKEPEEGTLTFPAQSLSPEPLPQEEEKLPPRNTNPGIKCFAVRSLGWVEMTEEELAPGRSSVAVNNCIRQLSYHKNNLHDPMSGGWGEGKDLLLQLEDETLKLVEPQSQALLHAQPIISIRVWGVGRDSGRERDFAYVARDKLTQMLKCHVFRCEAPAKNIATSLHEICSKIMAERRNARCLVNGLSLDHSKLVDVPFQVEFPAPKNELVQKFQVYYLGNVPVAKPVGVDVINGALESVLSSSSREQWTPSHVSVAPATLTILHQQTEAVLGECRVRFLSFLAVGRDVHTFAFIMAAGPASFCCHMFWCEPNAASLSEAVQAACMLRYQKCLDARSQASTSCLPAPPAESVARRVGWTVRRGVQSLWGSLKPKRLGAHTP
uniprot
proteins
function
FUNCTION: Transcription coregulator that can have both coactivator and corepressor functions (PubMed:15031292, PubMed:18468999, PubMed:18922798, PubMed:25342469, PubMed:33938178). Adapter protein that forms a transcriptionally active complex with the gamma-secretase-derived amyloid precursor protein (APP) intracellular domain (PubMed:15031292, PubMed:18468999, PubMed:18922798, PubMed:25342469). Plays a central role in the response to DNA damage by translocating to the nucleus and inducing apoptosis (PubMed:15031292, PubMed:18468999, PubMed:18922798, PubMed:25342469). May act by specifically recognizing and binding histone H2AX phosphorylated on 'Tyr-142' (H2AXY142ph) at double-strand breaks (DSBs), recruiting other pro-apoptosis factors such as MAPK8/JNK1 (PubMed:19234442). Required for histone H4 acetylation at double-strand breaks (DSBs) (PubMed:19234442). Its ability to specifically bind modified histones and chromatin modifying enzymes such as KAT5/TIP60, probably explains its transcription activation activity (PubMed:33938178). Functions in association with TSHZ3, SET and HDAC factors as a transcriptional repressor, that inhibits the expression of CASP4 (PubMed:19343227). Associates with chromatin in a region surrounding the CASP4 transcriptional start site(s) (PubMed:19343227). Involved in hippocampal neurite branching and neuromuscular junction formation, as a result plays a role in spatial memory functioning (By similarity). Plays a role in the maintenance of lens transparency (By similarity). May play a role in muscle cell strength (By similarity). Acts as a molecular adapter that functions in neurite outgrowth by activating the RAC1-ARF6 axis upon insulin treatment (PubMed:36250347). {ECO:0000250|UniProtKB:Q9QXJ1, ECO:0000269|PubMed:15031292, ECO:0000269|PubMed:18468999, ECO:0000269|PubMed:18922798, ECO:0000269|PubMed:19234442, ECO:0000269|PubMed:19343227, ECO:0000269|PubMed:25342469, ECO:0000269|PubMed:33938178, ECO:0000269|PubMed:36250347}.
uniprot
proteins
mass_dalton
77244
uniprot
proteins
mutagenesis
MUTAGEN 117; /note="Y->F: No effect on phosphorylation by ABL1."; /evidence="ECO:0000269|PubMed:15031292"; MUTAGEN 204; /note="K->Q: Mimics acetylation; leading to increased transcription activator activity; when associated with Q-701."; /evidence="ECO:0000269|PubMed:33938178"; MUTAGEN 204; /note="K->R: Abolished acetylation by KAT5, leading to decreased transcription activator activity; when associated with R-701."; /evidence="ECO:0000269|PubMed:33938178"; MUTAGEN 234; /note="Y->F: No effect on phosphorylation by ABL1."; /evidence="ECO:0000269|PubMed:15031292"; MUTAGEN 269..271; /note="YYW->AAA: Impairs transcriptional activation and inhibits binding to ABL1."; /evidence="ECO:0000269|PubMed:15031292"; MUTAGEN 269; /note="Y->F: No effect on phosphorylation by ABL1."; /evidence="ECO:0000269|PubMed:15031292"; MUTAGEN 270; /note="Y->F: No effect on phosphorylation by ABL1."; /evidence="ECO:0000269|PubMed:15031292"; MUTAGEN 403; /note="Y->F: No effect on phosphorylation by ABL1."; /evidence="ECO:0000269|PubMed:15031292"; MUTAGEN 459; /note="S->A: Loss of PKC-mediated phosphorylation."; /evidence="ECO:0000269|PubMed:36250347"; MUTAGEN 459; /note="S->E: Increased activation of the RAC1-ARF6 axis."; /evidence="ECO:0000269|PubMed:36250347"; MUTAGEN 467; /note="Y->F: No effect on phosphorylation by ABL1."; /evidence="ECO:0000269|PubMed:15031292"; MUTAGEN 546; /note="Y->F: No effect on phosphorylation by ABL1."; /evidence="ECO:0000269|PubMed:15031292"; MUTAGEN 547; /note="Y->F: Abrogates phosphorylation and stimulation of transcription by ABL1, and increases the interaction with RASD1/DEXRAS1."; /evidence="ECO:0000269|PubMed:15031292, ECO:0000269|PubMed:18922798"; MUTAGEN 658; /note="Y->F: No effect on phosphorylation by ABL1."; /evidence="ECO:0000269|PubMed:15031292"; MUTAGEN 701; /note="K->Q: Mimics acetylation; leading to increased transcription activator activity; when associated with Q-204."; /evidence="ECO:0000269|PubMed:33938178"; MUTAGEN 701; /note="K->R: Abolished acetylation by KAT5, leading to decreased transcription activator activity; when associated with R-204."; /evidence="ECO:0000269|PubMed:33938178
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-610 by SGK1 promotes its localization to the nucleus (By similarity). Phosphorylated following nuclear translocation (PubMed:15031292, PubMed:18922798). Phosphorylation at Tyr-547 by ABL1 enhances transcriptional activation activity and reduces the affinity for RASD1/DEXRAS1 (PubMed:15031292, PubMed:18922798). Phosphorylated at Ser-459 by PKC upon insulin activation (PubMed:36250347). {ECO:0000250|UniProtKB:P46933, ECO:0000269|PubMed:15031292, ECO:0000269|PubMed:18922798, ECO:0000269|PubMed:36250347}.; PTM: Acetylation at Lys-204 and Lys-701 by KAT5 promotes its transcription activator activity. {ECO:0000269|PubMed:33938178}.; PTM: Polyubiquitination by RNF157 leads to degradation by the proteasome (PubMed:25342469). {ECO:0000269|PubMed:25342469}.
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15031292
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
17512906
uniprot
proteins
pubmed
17686488
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18468999
uniprot
proteins
pubmed
18550529
uniprot
proteins
pubmed
18833287
uniprot
proteins
pubmed
18922798
uniprot
proteins
pubmed
19234442
uniprot
proteins
pubmed
19343227
uniprot
proteins
pubmed
21824145
uniprot
proteins
pubmed
25342469
uniprot
proteins
pubmed
33938178
uniprot
proteins
pubmed
36250347
uniprot
proteins
pubmed
8894693
uniprot
proteins
pubmed
9799084
uniprot
proteins
sequence_length
710
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18468999}. Cytoplasm {ECO:0000269|PubMed:18468999}. Nucleus {ECO:0000269|PubMed:15031292, ECO:0000269|PubMed:18468999, ECO:0000269|PubMed:18922798, ECO:0000269|PubMed:19343227}. Cell projection, growth cone {ECO:0000250|UniProtKB:P46933}. Nucleus speckle {ECO:0000269|PubMed:17512906}. Note=Colocalizes with TSHZ3 in axonal growth cone (By similarity). Colocalizes with TSHZ3 in the nucleus (PubMed:19343227). In normal conditions, it mainly localizes to the cytoplasm, while a small fraction is tethered to the cell membrane via its interaction with APP (PubMed:18468999). Following exposure to DNA damaging agents, it is released from cell membrane and translocates to the nucleus (PubMed:18468999). Nuclear translocation is under the regulation of APP (PubMed:18468999). Colocalizes with NEK6 at the nuclear speckles (PubMed:17512906). Phosphorylation at Ser-610 by SGK1 promotes its localization to the nucleus (By similarity). {ECO:0000250|UniProtKB:P46933, ECO:0000269|PubMed:17512906, ECO:0000269|PubMed:18468999, ECO:0000269|PubMed:19343227}.
uniprot
proteins