ARI3A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ARI3A_HUMAN
• UniProt AC: Q99856
• Protein Name: AT-rich interactive domain-containing protein 3A
• Gene Name: ARID3A
• Organism: Homo sapiens (Human).
• Sequence Length: 593
• Subcellular Localization: Nucleus . Cytoplasm . Shuttles between nucleus and cytoplasm.
• Protein Description: Transcription factor which may be involved in the control of cell cycle progression by the RB1/E2F1 pathway and in B-cell differentiation..
• Protein Sequence: MKLQAVMETLLQRQQRARQELEARQQLPPDPPAAPPGRARAAPDEDREPESARMQRAQMAALAAMRAAAAGLGHPASPGGSEDGPPGSEEEDAAREGTPGSPGRGREGPGEEHFEDMASDEDMKPKWEEEEMEEDLGEDEEEEEEDYEDEEEEEDEEGLGPPGPASLGTTALFPRKAQPPQAFRGDGVPRVLGGQERPGPGPAHPGGAAHVAPQLQPPDHGDWTYEEQFKQLYELDGDPKRKEFLDDLFSFMQKRGTPVNRIPIMAKQVLDLFMLYVLVTEKGGLVEVINKKLWREITKGLNLPTSITSAAFTLRTQYMKYLYPYECEKRGLSNPNELQAAIDSNRREGRRQSFGGSLFAYSPGGAHGMLSSPKLPVSSLGLAASTNGSSITPAPKIKKEEDSAIPITVPGRLPVSLAGHPVVAAQAAAVQAAAAQAAVAAQAAALEQLREKLESAEPPEKKMALVADEQQRLMQRALQQNFLAMAAQLPMSIRINSQASESRQDSAVNLTGTNGSNSISMSVEINGIMYTGVLFAQPPAPTPTSAPNKGGGGGGGSSSNAGGRGGNTGTSGGQAGPAGLSTPSTSTSNNSLP

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
7	Sulfoxidation	-MKLQAVMETLLQRQ -CHHHHHHHHHHHHH	3.50	21406390
77	Phosphorylation	AGLGHPASPGGSEDG HCCCCCCCCCCCCCC	28.64	19664994
81	Phosphorylation	HPASPGGSEDGPPGS CCCCCCCCCCCCCCC	38.13	19664994
88	Phosphorylation	SEDGPPGSEEEDAAR CCCCCCCCHHHHHHH	47.83	19664994
98	Phosphorylation	EDAAREGTPGSPGRG HHHHHHCCCCCCCCC	21.52	23898821
101	Phosphorylation	AREGTPGSPGRGREG HHHCCCCCCCCCCCC	25.94	23401153
119	Phosphorylation	EHFEDMASDEDMKPK HHHHHHCCCCCCCCC	34.59	22617229
211	Ubiquitination	HPGGAAHVAPQLQPP CCCCCCCCCCCCCCC	7.73	24816145
233	Phosphorylation	EEQFKQLYELDGDPK HHHHHHHHHCCCCHH	16.38	30266825
240	Ubiquitination	YELDGDPKRKEFLDD HHCCCCHHHHHHHHH	79.45	29967540
276	Phosphorylation	VLDLFMLYVLVTEKG HHHHHHHHHHHHCCC	4.67	22817900
309	Phosphorylation	NLPTSITSAAFTLRT CCCCHHHHHHHHHHH	18.87	-
313	Phosphorylation	SITSAAFTLRTQYMK HHHHHHHHHHHHHHH	15.59	24719451
327	S-palmitoylation	KYLYPYECEKRGLSN HHHCCHHHHHCCCCC	6.53	19214191
329	Ubiquitination	LYPYECEKRGLSNPN HCCHHHHHCCCCCHH	64.52	29967540
333	Phosphorylation	ECEKRGLSNPNELQA HHHHCCCCCHHHHHH	53.73	30243723
344	Phosphorylation	ELQAAIDSNRREGRR HHHHHHHCCCCCCCH	26.56	30243723
353	Phosphorylation	RREGRRQSFGGSLFA CCCCCHHHCCCCEEE	24.85	22617229
357	Phosphorylation	RRQSFGGSLFAYSPG CHHHCCCCEEEECCC	22.24	23898821
361	Phosphorylation	FGGSLFAYSPGGAHG CCCCEEEECCCCCCC	14.20	28450419
362	Phosphorylation	GGSLFAYSPGGAHGM CCCEEEECCCCCCCC	17.40	25218447
371	Phosphorylation	GGAHGMLSSPKLPVS CCCCCCCCCCCCCHH	35.38	28450419
372	Phosphorylation	GAHGMLSSPKLPVSS CCCCCCCCCCCCHHH	23.30	28450419
379	O-linked_Glycosylation	SPKLPVSSLGLAAST CCCCCHHHCCEECCC	27.04	30620550
398	Sumoylation	ITPAPKIKKEEDSAI CCCCCCCCCCCCCCC	61.33	-
398	Sumoylation	ITPAPKIKKEEDSAI CCCCCCCCCCCCCCC	61.33	28112733
399	Sumoylation	TPAPKIKKEEDSAIP CCCCCCCCCCCCCCC	70.57	28112733
408	O-linked_Glycosylation	EDSAIPITVPGRLPV CCCCCCCCCCCCCCC	18.46	30620550
408	Phosphorylation	EDSAIPITVPGRLPV CCCCCCCCCCCCCCC	18.46	-
452	Sumoylation	ALEQLREKLESAEPP HHHHHHHHHHHCCCC	51.63	-
452	Ubiquitination	ALEQLREKLESAEPP HHHHHHHHHHHCCCC	51.63	29967540
452	Sumoylation	ALEQLREKLESAEPP HHHHHHHHHHHCCCC	51.63	25218447
462	Sumoylation	SAEPPEKKMALVADE HCCCCHHHHHHHHHH	27.95	28112733
462	Ubiquitination	SAEPPEKKMALVADE HCCCCHHHHHHHHHH	27.95	24816145
462	Sumoylation	SAEPPEKKMALVADE HCCCCHHHHHHHHHH	27.95	-
463	Sulfoxidation	AEPPEKKMALVADEQ CCCCHHHHHHHHHHH	5.30	21406390
492	Phosphorylation	MAAQLPMSIRINSQA HHHCCCCEEEECCCC	13.53	-
568	Phosphorylation	AGGRGGNTGTSGGQA CCCCCCCCCCCCCCC	45.15	-
582	Phosphorylation	AGPAGLSTPSTSTSN CCCCCCCCCCCCCCC	26.71	22817900
584	Phosphorylation	PAGLSTPSTSTSNNS CCCCCCCCCCCCCCC	34.77	-
591	Phosphorylation	STSTSNNSLP----- CCCCCCCCCC-----	46.39	-

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
-	K	Ubiquitination	E3 ubiquitin ligase	ICP0	P08393	PMID:32416261

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ARI3A_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ARI3A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BTK_HUMAN	BTK	physical	15203319
UBC_HUMAN	UBC	physical	21248039
SP100_HUMAN	SP100	physical	15017387
UB2E3_HUMAN	UBE2E3	physical	15017387
PML_HUMAN	PML	physical	15017387
P53_HUMAN	TP53	physical	15017387
E2F2_HUMAN	E2F2	physical	15017387
E2F4_HUMAN	E2F4	physical	15017387
A4_HUMAN	APP	physical	21832049
TTC32_HUMAN	TTC32	physical	25416956
NT2NL_HUMAN	NOTCH2NL	physical	25416956
ARI3C_HUMAN	ARID3C	physical	28514442
ARI3B_HUMAN	ARID3B	physical	28514442
HERC2_HUMAN	HERC2	physical	28514442
PCGF3_HUMAN	PCGF3	physical	27173435
NISCH_HUMAN	NISCH	physical	27173435

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-81 AND SER-88,AND MASS SPECTROMETRY.
PubMed: 19690332

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-81 AND SER-88,AND MASS SPECTROMETRY.
PubMed: 19413330

"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-77; SER-81 AND SER-88,AND MASS SPECTROMETRY.
PubMed: 18669648

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-81 AND SER-88,AND MASS SPECTROMETRY.
PubMed: 17081983

"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81 AND SER-88, AND MASSSPECTROMETRY.
PubMed: 15302935