dbPTM

APBA3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	APBA3_HUMAN
UniProt AC	O96018
Protein Name	Amyloid-beta A4 precursor protein-binding family A member 3
Gene Name	APBA3
Organism	Homo sapiens (Human).
Sequence Length	575
Subcellular Localization	Cytoplasm, perinuclear region .
Protein Description	May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP-beta. May enhance the activity of HIF1A in macrophages by inhibiting the activity of HIF1AN..
Protein Sequence	MDFPTISRSPSGPPAMDLEGPRDILVPSEDLTPDSQWDPMPGGPGSLSRMELDESSLQELVQQFEALPGDLVGPSPGGAPCPLHIATGHGLASQEIADAHGLLSAEAGRDDLLGLLHCEECPPSQTGPEEPLEPAPRLLQPPEDPDEDSDSPEWVEGASAEQEGSRSSSSSPEPWLETVPLVTPEEPPAGAQSPETLASYPAPQEVPGPCDHEDLLDGVIFGARYLGSTQLVSERNPPTSTRMAQAREAMDRVKAPDGETQPMTEVDLFVSTKRIKVLTADSQEAMMDHALHTISYTADIGCVLVLMARRRLARRPAPQDHGRRLYKMLCHVFYAEDAQLIAQAIGQAFAAAYSQFLRESGIDPSQVGVHPSPGACHLHNGDLDHFSNSDNCREVHLEKRRGEGLGVALVESGWGSLLPTAVIANLLHGGPAERSGALSIGDRLTAINGTSLVGLPLAACQAAVRETKSQTSVTLSIVHCPPVTTAIIHRPHAREQLGFCVEDGIICSLLRGGIAERGGIRVGHRIIEINGQSVVATPHARIIELLTEAYGEVHIKTMPAATYRLLTGQEQPVYL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDFPTISR -------CCCCCCCC	12.36	22814378
5	Phosphorylation	---MDFPTISRSPSG ---CCCCCCCCCCCC	31.42	26074081
7	Phosphorylation	-MDFPTISRSPSGPP -CCCCCCCCCCCCCC	29.23	26074081
9	Phosphorylation	DFPTISRSPSGPPAM CCCCCCCCCCCCCCC	19.34	23401153
11	Phosphorylation	PTISRSPSGPPAMDL CCCCCCCCCCCCCCC	66.24	29255136
28	Phosphorylation	PRDILVPSEDLTPDS CCCEEECCCCCCCCC	35.94	28348404
32	Phosphorylation	LVPSEDLTPDSQWDP EECCCCCCCCCCCCC	37.05	28348404
35	Phosphorylation	SEDLTPDSQWDPMPG CCCCCCCCCCCCCCC	34.08	28857561
46	Phosphorylation	PMPGGPGSLSRMELD CCCCCCCCCCCCCCC	26.72	28857561
48	Phosphorylation	PGGPGSLSRMELDES CCCCCCCCCCCCCHH	31.14	28857561
171	Phosphorylation	GSRSSSSSPEPWLET CCCCCCCCCCCCCCC	34.92	-
225	Phosphorylation	GVIFGARYLGSTQLV HHEEEHHHCCCCCHH	18.19	-
229	Phosphorylation	GARYLGSTQLVSERN EHHHCCCCCHHCCCC	24.91	-
233	Phosphorylation	LGSTQLVSERNPPTS CCCCCHHCCCCCCCH	39.16	-
372	Phosphorylation	SQVGVHPSPGACHLH HHCCCCCCCCCCCCC	22.53	18691976
445	Phosphorylation	LSIGDRLTAINGTSL CCCCCCEEEECCCCC	26.78	19690332
450	Phosphorylation	RLTAINGTSLVGLPL CEEEECCCCCCCHHH	17.88	19690332
517	Methylation	LRGGIAERGGIRVGH HCCCHHHHCCEEECC	39.35	-

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
5	T	Phosphorylation	Kinase	MTOR	P42345	PSP
7	S	Phosphorylation	Kinase	MTOR	P42345	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of APBA3_HUMAN !!

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 APBA3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EGFR_HUMAN	EGFR	physical	16273093
UBB_HUMAN	UBB	physical	26186194
TBK1_HUMAN	TBK1	physical	26186194
NFX1_HUMAN	NFX1	physical	28514442
SCAI_HUMAN	SCAI	physical	28514442
ACSM1_HUMAN	ACSM1	physical	28514442
AZI2_HUMAN	AZI2	physical	28514442
NECA3_HUMAN	NECAB3	physical	28514442
ZKSC1_HUMAN	ZKSCAN1	physical	28514442
SCAFB_HUMAN	SCAF11	physical	28514442
PKP4_HUMAN	PKP4	physical	28514442
I13R1_HUMAN	IL13RA1	physical	28514442
ODPAT_HUMAN	PDHA2	physical	28514442
TBK1_HUMAN	TBK1	physical	28514442
CTR9_HUMAN	CTR9	physical	28514442
TAM41_HUMAN	TAMM41	physical	28514442
TJAP1_HUMAN	TJAP1	physical	28514442
PKN3_HUMAN	PKN3	physical	28514442
RPGF6_HUMAN	RAPGEF6	physical	28514442
APLP2_HUMAN	APLP2	physical	28514442
SYFB_HUMAN	FARSB	physical	28514442
DUS11_HUMAN	DUSP11	physical	28514442
CSTN1_HUMAN	CLSTN1	physical	28514442
RTF2_HUMAN	RTFDC1	physical	28514442
A4_HUMAN	APP	physical	28514442
CQ080_HUMAN	C17orf80	physical	28514442
ALR_HUMAN	GFER	physical	28514442
PI42C_HUMAN	PIP4K2C	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 APBA3_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND MASSSPECTROMETRY.	19369195 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-372, AND MASSSPECTROMETRY.	18691976 [Abstract]