dbPTM

APBB1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	APBB1_HUMAN
UniProt AC	O00213
Protein Name	Amyloid-beta A4 precursor protein-binding family B member 1
Gene Name	APBB1
Organism	Homo sapiens (Human).
Sequence Length	710
Subcellular Localization	Cell membrane. Cytoplasm. Nucleus. Cell projection, growth cone. Nucleus speckle. Colocalizes with TSHZ3 in axonal growth cone (By similarity). In normal conditions, it mainly localizes to the cytoplasm, while a small fraction is tethered to the cell
Protein 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 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	MSVPSSLSQSAINANSHGGPALSLPLPLHAAHNQLLNAKLQATAVGPKDLRSAMGEGGGPEPGPANAKWLKEGQNQLRRAATAHRDQNRNVTLTLAEEASQEPEMAPLGPKGLIHLYSELELSAHNAANRGLRGPGLIISTQEQGPDEGEEKAAGEAEEEEEDDDDEEEEEDLSSPPGLPEPLESVEAPPRPQALTDGPREHSKSASLLFGMRNSAASDEDSSWATLSQGSPSYGSPEDTDSFWNPNAFETDSDLPAGWMRVQDTSGTYYWHIPTGTTQWEPPGRASPSQGSSPQEESQLTWTGFAHGEGFEDGEFWKDEPSDEAPMELGLKEPEEGTLTFPAQSLSPEPLPQEEEKLPPRNTNPGIKCFAVRSLGWVEMTEEELAPGRSSVAVNNCIRQLSYHKNNLHDPMSGGWGEGKDLLLQLEDETLKLVEPQSQALLHAQPIISIRVWGVGRDSGRERDFAYVARDKLTQMLKCHVFRCEAPAKNIATSLHEICSKIMAERRNARCLVNGLSLDHSKLVDVPFQVEFPAPKNELVQKFQVYYLGNVPVAKPVGVDVINGALESVLSSSSREQWTPSHVSVAPATLTILHQQTEAVLGECRVRFLSFLAVGRDVHTFAFIMAAGPASFCCHMFWCEPNAASLSEAVQAACMLRYQKCLDARSQASTSCLPAPPAESVARRVGWTVRRGVQSLWGSLKPKRLGAHTP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
43	Phosphorylation	LNAKLQATAVGPKDL HHHHHHHEECCHHHH	14.65	22985185
48	Ubiquitination	QATAVGPKDLRSAMG HHEECCHHHHHHHHC	64.56	21890473
48 (in isoform 2)	Ubiquitination	-	64.56	21890473
48 (in isoform 1)	Ubiquitination	-	64.56	21890473
48	Ubiquitination	QATAVGPKDLRSAMG HHEECCHHHHHHHHC	64.56	2189047
92	Phosphorylation	RDQNRNVTLTLAEEA HHHCCCEEEEEEHHH	19.99	28555341
118	Phosphorylation	KGLIHLYSELELSAH HHHHHHHHHHHHHHH	41.90	24719451
175	Phosphorylation	EEEEDLSSPPGLPEP HHHHHHCCCCCCCCC	42.27	14697653
205	Phosphorylation	GPREHSKSASLLFGM CCCCCCCCHHHHHCC	26.55	28450419
207	Phosphorylation	REHSKSASLLFGMRN CCCCCCHHHHHCCCC	32.47	28450419
228	Phosphorylation	DSSWATLSQGSPSYG CCCCEECCCCCCCCC	28.30	-
239 (in isoform 3)	Phosphorylation	-	60.23	20058876
287	Phosphorylation	WEPPGRASPSQGSSP CCCCCCCCCCCCCCC	24.59	14697653
289	Phosphorylation	PPGRASPSQGSSPQE CCCCCCCCCCCCCHH	44.68	-
322	Phosphorylation	EFWKDEPSDEAPMEL CCCCCCCCCCCCCCC	46.14	27732954
345	Phosphorylation	TLTFPAQSLSPEPLP EEEEECCCCCCCCCC	32.68	27732954
347	Phosphorylation	TFPAQSLSPEPLPQE EEECCCCCCCCCCHH	32.25	22496350
459 (in isoform 2)	Phosphorylation	-	38.09	20058876
459	Phosphorylation	VWGVGRDSGRERDFA EEEECCCCCCCCCHH	38.09	20058876
478	Ubiquitination	DKLTQMLKCHVFRCE HHHHHHHCCEEEECC	19.56	-
517	Phosphorylation	RCLVNGLSLDHSKLV EEEECCEECCHHHCC	32.90	22617229
522	Ubiquitination	GLSLDHSKLVDVPFQ CEECCHHHCCCCCEE	49.46	-
536	Ubiquitination	QVEFPAPKNELVQKF EEEECCCCCHHHHEE	66.22	-
547	Phosphorylation	VQKFQVYYLGNVPVA HHEEEEEEECCCCCC	14.85	15031292
579	Phosphorylation	SSSREQWTPSHVSVA CCCCCCCCCCCEECC	18.01	-
610	Phosphorylation	ECRVRFLSFLAVGRD HHHHHHHHHHHCCCC	18.59	-
660	Ubiquitination	ACMLRYQKCLDARSQ HHHHHHHHHHHHHHH	28.03	-
666	O-linked_Glycosylation	QKCLDARSQASTSCL HHHHHHHHHCCCCCC	31.64	28657654
680	Phosphorylation	LPAPPAESVARRVGW CCCCCHHHHHHHHCH	24.15	28555341
695	Phosphorylation	TVRRGVQSLWGSLKP HHHHHHHHHHHCCCC	24.55	29978859
699	Phosphorylation	GVQSLWGSLKPKRLG HHHHHHHCCCCCCCC	22.95	29978859
709	Phosphorylation	PKRLGAHTP------ CCCCCCCCC------	30.11	30266825

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
175	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
228	S	Phosphorylation	Kinase	ATM	Q13315	PSP
228	S	Phosphorylation	Kinase	ATR	Q13535	PSP
287	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
347	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
547	Y	Phosphorylation	Kinase	ABL1	P00519	Uniprot
547	Y	Phosphorylation	Kinase	ABL-FAMILY	-	GPS
579	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
610	S	Phosphorylation	Kinase	SGK1	O00141	Uniprot
709	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	NEDD4L	Q96PU5	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
610	S	Phosphorylation		15031292
Phosphorylation at Ser-610 by SGK1 promotes its localization to the nucleus (By similarity).

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TFCP2_HUMAN	TFCP2	physical	9685356
EVL_HUMAN	EVL	physical	10945997
A4_HUMAN	APP	physical	8887653
A4_HUMAN	APP	physical	9045663
A4_HUMAN	APP	physical	8855266
APLP2_HUMAN	APLP2	physical	8855266
A4_HUMAN	APP	physical	10081969
APLP1_HUMAN	APLP1	physical	10081969
APLP2_HUMAN	APLP2	physical	10081969
A4_HUMAN	APP	physical	9837937
LRP1_HUMAN	LRP1	physical	9837937
TSH3_HUMAN	TSHZ3	physical	19343227
HDAC1_HUMAN	HDAC1	physical	19343227
CPSF6_HUMAN	CPSF6	physical	16055720
SET_HUMAN	SET	physical	15592452
NED4L_HUMAN	NEDD4L	physical	19381069
1433G_HUMAN	YWHAG	physical	16223726
KAT5_HUMAN	KAT5	physical	16223726
A4_HUMAN	APP	physical	16223726
APBB1_HUMAN	APBB1	physical	15044485
EGFR_HUMAN	EGFR	physical	16273093
ERBB2_HUMAN	ERBB2	physical	16273093
HTSF1_HUMAN	HTATSF1	physical	16055720
YBOX1_HUMAN	YBX1	physical	16055720
PQBP1_HUMAN	PQBP1	physical	16055720
TR150_HUMAN	THRAP3	physical	16055720
DDX17_HUMAN	DDX17	physical	16055720
DDX3X_HUMAN	DDX3X	physical	16055720
DDX46_HUMAN	DDX46	physical	16055720
DHX15_HUMAN	DHX15	physical	16055720
DHX9_HUMAN	DHX9	physical	16055720
HNRH1_HUMAN	HNRNPH1	physical	16055720
HNRPK_HUMAN	HNRNPK	physical	16055720
KHDR1_HUMAN	KHDRBS1	physical	16055720
FUBP2_HUMAN	KHSRP	physical	16055720
SPF45_HUMAN	RBM17	physical	16055720
CPSF7_HUMAN	CPSF7	physical	16055720
NONO_HUMAN	NONO	physical	16055720
PABP1_HUMAN	PABPC1	physical	16055720
PTBP1_HUMAN	PTBP1	physical	16055720
SF01_HUMAN	SF1	physical	16055720
SF3A1_HUMAN	SF3A1	physical	16055720
SF3A2_HUMAN	SF3A2	physical	16055720
SF3A3_HUMAN	SF3A3	physical	16055720
SF3B1_HUMAN	SF3B1	physical	16055720
SF3B2_HUMAN	SF3B2	physical	16055720
SF3B3_HUMAN	SF3B3	physical	16055720
SF3B4_HUMAN	SF3B4	physical	16055720
SFPQ_HUMAN	SFPQ	physical	16055720
U2AF2_HUMAN	U2AF2	physical	16055720
WBP11_HUMAN	WBP11	physical	16055720
RL4_HUMAN	RPL4	physical	16055720
CYFP1_HUMAN	CYFIP1	physical	16055720
CYFP2_HUMAN	CYFIP2	physical	16055720
DIAP1_HUMAN	DIAPH1	physical	16055720
DIAP2_HUMAN	DIAPH2	physical	16055720
ENAH_HUMAN	ENAH	physical	16055720
EVL_HUMAN	EVL	physical	16055720
WIPF2_HUMAN	WIPF2	physical	16055720
ABI1_HUMAN	ABI1	physical	16055720
VASP_HUMAN	VASP	physical	16055720
WASP_HUMAN	WAS	physical	16055720
WASF2_HUMAN	WASF2	physical	16055720
WASL_HUMAN	WASL	physical	16055720
WIPF1_HUMAN	WIPF1	physical	16055720
CHERP_HUMAN	CHERP	physical	16055720
YLPM1_HUMAN	YLPM1	physical	16055720
CCD97_HUMAN	CCDC97	physical	16055720
A4_HUMAN	APP	physical	23663107
SART3_HUMAN	SART3	physical	25342469
KAT5_HUMAN	KAT5	physical	25342469
MGRN1_HUMAN	MGRN1	physical	25342469
A4_HUMAN	APP	physical	18096514
JAG1_HUMAN	JAG1	physical	26276215
JAG1_RAT	Jag1	physical	26276215
ENAH_HUMAN	ENAH	physical	17686488
BLM_HUMAN	BLM	physical	23572515
SYDE1_HUMAN	SYDE1	physical	28514442
APLP1_HUMAN	APLP1	physical	28514442
NEUL4_HUMAN	NEURL4	physical	28514442
APLP2_HUMAN	APLP2	physical	28514442
A4_HUMAN	APP	physical	28514442
HERC2_HUMAN	HERC2	physical	28514442
DCAKD_HUMAN	DCAKD	physical	28514442
SETX_HUMAN	SETX	physical	28514442
TAM41_HUMAN	TAMM41	physical	28514442

Drug and Disease Associations

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

Regulatory Network of APBB1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Dexras1 interacts with FE65 to regulate FE65-amyloid precursorprotein-dependent transcription."; Lau K.-F., Chan W.-M., Perkinton M.S., Tudor E.L., Chang R.C.C.,Chan H.-Y., McLoughlin D.M., Miller C.C.J.; J. Biol. Chem. 283:34728-34737(2008). Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-547,INTERACTION WITH RASD1, AND MUTAGENESIS OF TYR-547.	18922798 [Abstract]
"The c-Abl tyrosine kinase phosphorylates the Fe65 adaptor protein tostimulate Fe65/amyloid precursor protein nuclear signaling."; Perkinton M.S., Standen C.L., Lau K.F., Kesavapany S., Byers H.L.,Ward M., McLoughlin D.M., Miller C.C.; J. Biol. Chem. 279:22084-22091(2004). Cited for: FUNCTION, INTERACTION WITH ABL1, SUBCELLULAR LOCATION, PHOSPHORYLATIONAT TYR-547 BY ABL1, AND MUTAGENESIS OF TYR-117; TYR-234; TYR-269;TYR-270; TYR-403; TYR-467; 269-TYR--TRP-271; TYR-546 AND TYR-547.	15031292 [Abstract]

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