CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000026
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Amyloid beta A4 precursor protein-binding family B member 1 
Protein Synonyms/Alias
 Protein Fe65 
Gene Name
 APBB1 
Gene Synonyms/Alias
 FE65; RIR 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
48QATAVGPKDLRSAMGubiquitination[1]
522GLSLDHSKLVDVPFQubiquitination[2]
660ACMLRYQKCLDARSQubiquitination[2]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961
Functional Description
 Transcription coregulator that can have both coactivator and corepressor functions. Adapter protein that forms a transcriptionally active complex with the gamma-secretase-derived amyloid precursor protein (APP) intracellular domain. Plays a central role in the response to DNA damage by translocating to the nucleus and inducing apoptosis. 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. Required for histone H4 acetylation at double-strand breaks (DSBs). Its ability to specifically bind modified histones and chromatin modifying enzymes such as KAT5/TIP60, probably explains its trancription activation activity. Function in association with TSHZ3, SET and HDAC factors as a transcriptional repressor, that inhibits the expression of CASP4. Associates with chromatin in a region surrounding the CASP4 transcriptional start site(s). 
Sequence Annotation
 DOMAIN 253 285 WW.
 DOMAIN 370 509 PID 1.
 DOMAIN 542 699 PID 2.
 MOD_RES 547 547 Phosphotyrosine; by ABL1.
 MOD_RES 610 610 Phosphoserine; by SGK1 (By similarity).  
Keyword
 3D-structure; Activator; Alternative splicing; Apoptosis; Cell membrane; Cell projection; Chromatin regulator; Complete proteome; Cytoplasm; DNA damage; Membrane; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 710 AA 
Protein Sequence
MSVPSSLSQS AINANSHGGP ALSLPLPLHA AHNQLLNAKL QATAVGPKDL RSAMGEGGGP 60
EPGPANAKWL KEGQNQLRRA ATAHRDQNRN VTLTLAEEAS QEPEMAPLGP KGLIHLYSEL 120
ELSAHNAANR GLRGPGLIIS TQEQGPDEGE EKAAGEAEEE EEDDDDEEEE EDLSSPPGLP 180
EPLESVEAPP RPQALTDGPR EHSKSASLLF GMRNSAASDE DSSWATLSQG SPSYGSPEDT 240
DSFWNPNAFE TDSDLPAGWM RVQDTSGTYY WHIPTGTTQW EPPGRASPSQ GSSPQEESQL 300
TWTGFAHGEG FEDGEFWKDE PSDEAPMELG LKEPEEGTLT FPAQSLSPEP LPQEEEKLPP 360
RNTNPGIKCF AVRSLGWVEM TEEELAPGRS SVAVNNCIRQ LSYHKNNLHD PMSGGWGEGK 420
DLLLQLEDET LKLVEPQSQA LLHAQPIISI RVWGVGRDSG RERDFAYVAR DKLTQMLKCH 480
VFRCEAPAKN IATSLHEICS KIMAERRNAR CLVNGLSLDH SKLVDVPFQV EFPAPKNELV 540
QKFQVYYLGN VPVAKPVGVD VINGALESVL SSSSREQWTP SHVSVAPATL TILHQQTEAV 600
LGECRVRFLS FLAVGRDVHT FAFIMAAGPA SFCCHMFWCE PNAASLSEAV QAACMLRYQK 660
CLDARSQAST SCLPAPPAES VARRVGWTVR RGVQSLWGSL KPKRLGAHTP 710 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0030426; C:growth cone; IDA:UniProtKB.
 GO:0030027; C:lamellipodium; IDA:UniProtKB.
 GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0045202; C:synapse; IDA:UniProtKB.
 GO:0001540; F:beta-amyloid binding; IPI:UniProtKB.
 GO:0003682; F:chromatin binding; IDA:UniProtKB.
 GO:0008134; F:transcription factor binding; ISS:UniProtKB.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0007411; P:axon guidance; IEA:Compara.
 GO:0007409; P:axonogenesis; NAS:UniProtKB.
 GO:0007050; P:cell cycle arrest; ISS:UniProtKB.
 GO:0006302; P:double-strand break repair; IEA:Compara.
 GO:0030198; P:extracellular matrix organization; IEA:Compara.
 GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
 GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
 GO:0045665; P:negative regulation of neuron differentiation; IEA:Compara.
 GO:0050760; P:negative regulation of thymidylate synthase biosynthetic process; ISS:UniProtKB.
 GO:0001764; P:neuron migration; IEA:Compara.
 GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
 GO:0045739; P:positive regulation of DNA repair; IEA:Compara.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0006974; P:response to DNA damage stimulus; IDA:UniProtKB.
 GO:0007165; P:signal transduction; NAS:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0008542; P:visual learning; IEA:Compara. 
Interpro
 IPR011993; PH_like_dom.
 IPR006020; PTyr_interaction_dom.
 IPR001202; WW_dom. 
Pfam
 PF00640; PID
 PF00397; WW 
SMART
 SM00462; PTB
 SM00456; WW 
PROSITE
 PS01179; PID
 PS01159; WW_DOMAIN_1
 PS50020; WW_DOMAIN_2 
PRINTS