dbPAF Protein Information


Tag Content
dbPAF ID dbPAF-0000032
Uniprot Accession O00213; APBB1_HUMAN; A1E379; A6NH82; A6NL69; B7Z1J5; B7Z1J6; B7Z2Y0; D3DQT2; Q7Z324; Q96A93; V9GYK0; V9GYT4;
Genbank Protein ID NP_001155.1; NP_001244248.1; NP_001244249.1; NP_001244250.1; NP_001244252.1; NP_001244254.1; NP_001244255.1; NP_663722.1; XP_006718278.2; XP_011518342.1; XP_011518343.1;
Genbank Nucleotide ID NM_001164.4; NM_001257319.2; NM_001257320.2; NM_001257321.2; NM_001257323.2; NM_001257325.2; NM_001257326.2; NM_145689.2; XM_006718215.2; XM_011520040.1; XM_011520041.1;
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;
Organism Homo sapiens(Human)
NCBI Taxa ID 9606
Functional Description
(View all)
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).
Phosphorylation Sites
dbPAF PTMs: 10
PositionPeptidesSourceReferences ( PMIDs )
175EEEEDLSSPPGLPEPdbPTM 3.0;Phospho.ELM 9.0;PhosphoSitePlus14697653; 16381945; 23193290; 22135298
228DSSWATLSQGSPSYGPhosphoSitePlus22135298
287WEPPGRASPSQGSSPdbPTM 3.0;Phospho.ELM 9.0;PhosphoSitePlus14697653; 16381945; 23193290; 22135298
347TFPAQSLSPEPLPQEdbPTM 3.0;Phospho.ELM 9.0;PhosphoPep 2.0;PhosphoSitePlus14697653; 16381945; 23193290; 19060867; 22135298
459VWGVGRDSGRERDFAdbPTM 3.0;HPRD 9;PhosphoSitePlus20058876; 16381945; 23193290; 18988627; 22135298
547VQKFQVYYLGNVPVAdbPTM 3.0;PhosphoSitePlus15031292; 18922798; 16381945; 23193290; 22135298
610ECRVRFLSFLAVGRDPhosphoSitePlus22135298
695TVRRGVQSLWGSLKPPhosphoSitePlus22135298
699GVQSLWGSLKPKRLGPhosphoSitePlus22135298
709PKRLGAHTP------dbPTM 3.0;Phospho.ELM 9.0;PhosphoSitePlus14697653; 16381945; 23193290; 22135298
Sequence
(Fasta)
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 711
Keyword

KW-0002--3D-structure
KW-0010--Activator
KW-0025--Alternative splicing
KW-0053--Apoptosis
KW-1003--Cell membrane
KW-0966--Cell projection
KW-0156--Chromatin regulator
KW-0181--Complete proteome
KW-0963--Cytoplasm
KW-0227--DNA damage
KW-0472--Membrane
KW-0539--Nucleus
KW-0597--Phosphoprotein
KW-0621--Polymorphism
KW-1185--Reference proteome
KW-0677--Repeat
KW-0678--Repressor
KW-0804--Transcription
KW-0805--Transcription regulation

Interpro

IPR011993--PH/PTB_dom
IPR006020--PTB/PI_dom
IPR001202--WW_dom

PROSITE

PS01179--PID
PS01159--WW_DOMAIN_1
PS50020--WW_DOMAIN_2

Pfam

PF00640--PID

Gene Ontology

GO:0005737--C:cytoplasm
GO:0030426--C:growth cone
GO:0030027--C:lamellipodium
GO:0016607--C:nuclear speck
GO:0005654--C:nucleoplasm
GO:0005634--C:nucleus
GO:0005886--C:plasma membrane
GO:0045202--C:synapse
GO:0001540--F:beta-amyloid binding
GO:0003682--F:chromatin binding
GO:0042393--F:histone binding
GO:0070064--F:proline-rich region binding
GO:0008134--F:transcription factor binding
GO:0006915--P:apoptotic process
GO:0007409--P:axonogenesis
GO:0007050--P:cell cycle arrest
GO:0006974--P:cellular response to DNA damage stimulus
GO:0006281--P:DNA repair
GO:0006302--P:double-strand break repair
GO:0043967--P:histone H4 acetylation
GO:0030308--P:negative regulation of cell growth
GO:0050760--P:negative regulation of thymidylate synthase biosynthetic process
GO:0043065--P:positive regulation of apoptotic process
GO:0045893--P:positive regulation of transcription, DNA-templated
GO:0006355--P:regulation of transcription, DNA-templated
GO:0007165--P:signal transduction
GO:0006351--P:transcription, DNA-templated