APBB1_MOUSE - dbPTM
APBB1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID APBB1_MOUSE
UniProt AC Q9QXJ1
Protein Name Amyloid-beta A4 precursor protein-binding family B member 1
Gene Name Apbb1
Organism Mus musculus (Mouse).
Sequence Length 710
Subcellular Localization Cell membrane . Cytoplasm . Nucleus . Cell projection, growth cone. Nucleus speckle. Colocalizes with TSHZ3 in the nucleus and in axonal growth cone. Colocalizes with NEK6 at the nuclear speckles (By similarity). In normal conditions, it mainly local
Protein Description 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 transcription 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)..
Protein Sequence MSVPSSLSQSAINANSHGGPALSFPLPLHAAHNQLLNAKLQATAVVPKDLRSAMGEGSVPEPGPANAKWLKEGQNQLRRAATAHRDQNRNVTLTLAEEASQEAETAPLGPKGLMHLYSELELSAHNAANRGLHGSALIINTQEQGPDEGEEKAAGEAEEDDEDEEEEEEEEDLSSPPGLPEPLENVEVPSGPQALTDGPREHSKSASLLFGMRNSAASDEDSSWATLSQGSPSYGSPEDTDSFWNPNAFETDSDLPAGWMRVQDTSGTYYWHIPTGTTQWEPPGRASPSQGSSPQEESQLTWTGFAHQEGFEEGEFWKDEPSEEAPMELGLKDPEEATLSFPAQSLSPEPVPQEEEKLSQRNANPGIKCFAVRSLGWVEMTEEELAPGRSSVAVNNCIRQLSYHKNNLHDPMAGGWGEGKDLLLQLEDETLKLVEPQNQTLLHAQPIVSIRVWGVGRDSGSNRDFAYVARDKLTQMLKCHVFRCEAPAKNIATSLHEICSKIMSERRNARCLVNGLSLDHSKLVDVPFQVEFPAPKNELVQKFQVYYLGNVPVAKPVGVDVINGALESVLSSSSREQWTPSHVSVAPATLTILHQQTEAVLGECRVRFLSFLAVGRDVHTFAFIMAAGPASFCCHMFWCEPNAASLSEAVQAACMLRYQKCLDARSQTSTSCLPAPPAESVARRVGWTVRRGVQSLWGSLKPKRLGSQTP
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
48UbiquitinationQATAVVPKDLRSAMG
CEEEECCHHHHHHHC
58.7622790023
135PhosphorylationANRGLHGSALIINTQ
HHCCCCCCEEEEECC
14.7822817900
141PhosphorylationGSALIINTQEQGPDE
CCEEEEECCCCCCCC
24.0728066266
174PhosphorylationEEEEEDLSSPPGLPE
HHHHHHCCCCCCCCC
53.7929899451
205PhosphorylationGPREHSKSASLLFGM
CCCCCCCCHHHHHCC
26.5519060867
207PhosphorylationREHSKSASLLFGMRN
CCCCCCHHHHHCCCC
32.4729514104
231PhosphorylationWATLSQGSPSYGSPE
CEECCCCCCCCCCCC
11.7525338131
340PhosphorylationDPEEATLSFPAQSLS
CHHHCEEECCCCCCC
25.4828066266
345PhosphorylationTLSFPAQSLSPEPVP
EEECCCCCCCCCCCC
32.6828066266
347PhosphorylationSFPAQSLSPEPVPQE
ECCCCCCCCCCCCHH
32.2525521595
402PhosphorylationNNCIRQLSYHKNNLH
HHHHHHHHHCCCCCC
19.4928059163
403PhosphorylationNCIRQLSYHKNNLHD
HHHHHHHHCCCCCCC
25.9628059163
517PhosphorylationRCLVNGLSLDHSKLV
HHEECCEECCCHHCC
32.9022324799
521PhosphorylationNGLSLDHSKLVDVPF
CCEECCCHHCCCCCE
27.6122324799
547PhosphorylationVQKFQVYYLGNVPVA
HHEEEEEEECCCCCC
14.8515031292
610PhosphorylationECRVRFLSFLAVGRD
HHHHHHHHHHHCCCC
18.59-
666O-linked_GlycosylationQKCLDARSQTSTSCL
HHHHHCCCCCCCCCC
39.2655411933
699PhosphorylationGVQSLWGSLKPKRLG
HHHHHHHCCCCCCCC
22.9522817900
707PhosphorylationLKPKRLGSQTP----
CCCCCCCCCCC----
35.1622324799
709PhosphorylationPKRLGSQTP------
CCCCCCCCC------
32.4422324799

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
547YPhosphorylationKinaseABLP00520
PSP
547YPhosphorylationKinaseABL-FAMILY-GPS
610SPhosphorylationKinaseSGK1Q9WVC6
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
610SPhosphorylation

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Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of APBB1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
8894693
APLP1_HUMANAPLP1physical
8894693
APLP2_HUMANAPLP2physical
8894693
ENAH_MOUSEEnahphysical
9407065

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of APBB1_MOUSE

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Related Literatures of Post-Translational Modification

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