APBB1_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: APBB1_RAT
• UniProt AC: P46933
• Protein Name: Amyloid-beta A4 precursor protein-binding family B member 1
• Gene Name: Apbb1
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 711
• Subcellular Localization: Cell membrane. Cytoplasm. Nucleus. Cell projection, growth cone. Nucleus speckle. In normal conditions, it mainly localizes to the cytoplasm, while a small fraction is tethered to the cell membrane via its interaction with APP. Following exposure to
• 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: MSVPSSLSQSAINANSHGGPALSFPFPLHAAHNQLLNAKLQATAVVPKDLRSAMGEGSVPEPGPANAKWLKEGQNQLRRAATAHRDQNRNVTLTLAEEASQEAETAPLGPKGLMHLYSELELSAHNAANRGLHGSALIINTQGLGPDEGEEKAAGEVEEEDEDEEEEDEEEEDLSSPQGLPEPLENVEVPSGPQVLTDGPREHSKSASLLFGMRNSAASDEDSSWATLSQGSPSYGSPEDTDSFWNPNAFETDSDLPAGWMRVQDTSGTYYWHIPTGTTQWEPPGRASPSQGNSPQEESQLTWTGFAHQEGFEEGEFWKDEPSEEAPMELGLKDPEEGTLPFSAQSLSPEPVPQEEENLPQRNANPGIKCFAVRSLGWVEMTEEELAPGRSSVAVNNCIRQLSYHKNNLHDPMSGGWGEGKDLLLQLEDETLKLVEPQNQTLLHAQPIVSIRVWGVGRDSGRERDFAYVARDKLTQMLKCHVFRCEAPAKNIATSLHEICSKIMSERRNARCLVNGLSLDHSKLVDVPFQVEFPAPKNELVQKFQVYYLGNVPVAKPVGVDVINGALESVLSSSSREQWTPSHVSVAPATLTILHQQTEAVLGECRVRFLSFLAVGRDVHTFAFIMAAGPASFCCHMFWCEPNAASLSEAVQAACMLRYQKCLDARSQTSTSCLPAPPAESVARRVGWTVRRGVQSLWGSLKPKRLGSQTP

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
135	Phosphorylation	ANRGLHGSALIINTQ HHCCCCCCEEEEECC	14.78	-
206	Phosphorylation	GPREHSKSASLLFGM CCCCCCCCHHHHHCC	26.55	28432305
208	Phosphorylation	REHSKSASLLFGMRN CCCCCCHHHHHCCCC	32.47	28432305
348	Phosphorylation	PFSAQSLSPEPVPQE CCCCCCCCCCCCCHH	32.25	30240740
518	Phosphorylation	RCLVNGLSLDHSKLV HHEECCEECCCHHCC	32.90	27097102
548	Phosphorylation	VQKFQVYYLGNVPVA HHEEEEEEECCCCCC	14.85	-
611	Phosphorylation	ECRVRFLSFLAVGRD HHHHHHHHHHHCCCC	18.59	19282473
708	Phosphorylation	LKPKRLGSQTP---- CCCCCCCCCCC----	35.16	28551015
710	Phosphorylation	PKRLGSQTP------ CCCCCCCCC------	32.44	25403869

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
548	Y	Phosphorylation	Kinase	ABL1	-	Uniprot
611	S	Phosphorylation	Kinase	SGK1	O00141	PSP
611	S	Phosphorylation	Kinase	SGK1	Q06226	Uniprot
611	S	Phosphorylation	Kinase	SGK-FAMILY	-	GPS
611	S	Phosphorylation	Kinase	SGK_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
611	S	Phosphorylation	Phosphorylation at Ser-611 by SGK1 promotes its localization to the nucleus.	18304449

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of APBB1_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	9045663
NED4L_HUMAN	NEDD4L	physical	19381069
ENAH_HUMAN	ENAH	physical	10358088

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Regulation Fe65 localization to the nucleus by SGK1 phosphorylationof its Ser566 residue.";
Lee E.J., Chun J., Hyun S., Ahn H.R., Jeong J.M., Hong S.K.,Hong J.T., Chang I.K., Jeon H.Y., Han Y.S., Auh C.K., Park J.I.,Kang S.S.;
BMB Rep. 41:41-47(2008).
Cited for: PHOSPHORYLATION AT SER-611, AND SUBCELLULAR LOCATION.
PubMed: 18304449