NC2B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NC2B_HUMAN
• UniProt AC: Q01658
• Protein Name: Protein Dr1
• Gene Name: DR1
• Organism: Homo sapiens (Human).
• Sequence Length: 176
• Subcellular Localization: Nucleus.
• Protein Description: The association of the DR1/DRAP1 heterodimer with TBP results in a functional repression of both activated and basal transcription of class II genes. This interaction precludes the formation of a transcription-competent complex by inhibiting the association of TFIIA and/or TFIIB with TBP. Can bind to DNA on its own. Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4..
• Protein Sequence: MASSSGNDDDLTIPRAAINKMIKETLPNVRVANDARELVVNCCTEFIHLISSEANEICNKSEKKTISPEHVIQALESLGFGSYISEVKEVLQECKTVALKRRKASSRLENLGIPEEELLRQQQELFAKARQQQAELAQQEWLQMQQAAQQAQLAAASASASNQAGSSQDEEDDDDI

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
2	Acetylation	------MASSSGNDD ------CCCCCCCCC	20.37	22223895
3	Phosphorylation	-----MASSSGNDDD -----CCCCCCCCCC	24.60	25159151
4	Phosphorylation	----MASSSGNDDDL ----CCCCCCCCCCC	32.50	30108239
5	Phosphorylation	---MASSSGNDDDLT ---CCCCCCCCCCCC	38.84	19664995
20	Acetylation	IPRAAINKMIKETLP CCHHHHHHHHHHHCC	35.57	25953088
20	Ubiquitination	IPRAAINKMIKETLP CCHHHHHHHHHHHCC	35.57	-
23	Malonylation	AAINKMIKETLPNVR HHHHHHHHHHCCCCE	40.94	26320211
60	Acetylation	EANEICNKSEKKTIS HHHHHCCHHCCCCCC	56.43	26051181
60	Ubiquitination	EANEICNKSEKKTIS HHHHHCCHHCCCCCC	56.43	-
65	Phosphorylation	CNKSEKKTISPEHVI CCHHCCCCCCHHHHH	37.44	25627689
67	Phosphorylation	KSEKKTISPEHVIQA HHCCCCCCHHHHHHH	29.48	25159151
95	Acetylation	KEVLQECKTVALKRR HHHHHHHHHHHHHHH	45.33	26051181
95	Malonylation	KEVLQECKTVALKRR HHHHHHHHHHHHHHH	45.33	26320211
96	Phosphorylation	EVLQECKTVALKRRK HHHHHHHHHHHHHHH	23.75	-
105	Phosphorylation	ALKRRKASSRLENLG HHHHHHHHHHHHHCC	21.01	25159151
106	Phosphorylation	LKRRKASSRLENLGI HHHHHHHHHHHHCCC	45.83	25159151
128	Acetylation	QQQELFAKARQQQAE HHHHHHHHHHHHHHH	36.45	25953088
128	Ubiquitination	QQQELFAKARQQQAE HHHHHHHHHHHHHHH	36.45	-
157	Phosphorylation	QAQLAAASASASNQA HHHHHHHHHHHHCCC	20.31	18669648
159	Phosphorylation	QLAAASASASNQAGS HHHHHHHHHHCCCCC	29.72	25137130
161	Phosphorylation	AAASASASNQAGSSQ HHHHHHHHCCCCCCC	27.29	25137130
166	Phosphorylation	SASNQAGSSQDEEDD HHHCCCCCCCCCCCC	28.04	28348404
167	Phosphorylation	ASNQAGSSQDEEDDD HHCCCCCCCCCCCCC	40.51	28348404

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of NC2B_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NC2B_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 NC2B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DPOE3_HUMAN	POLE3	physical	16189514
NC2A_HUMAN	DRAP1	physical	8608938
KAT2B_HUMAN	KAT2B	physical	18838386
YETS2_HUMAN	YEATS2	physical	18838386
KAT2A_HUMAN	KAT2A	physical	18838386
TAD2A_HUMAN	TADA2A	physical	18838386
TADA3_HUMAN	TADA3	physical	18838386
MBIP1_HUMAN	MBIP	physical	18838386
WDR5_HUMAN	WDR5	physical	18838386
SGF29_HUMAN	CCDC101	physical	18838386
NC2A_HUMAN	DRAP1	physical	18838386
YETS2_HUMAN	YEATS2	physical	22939629
TTL12_HUMAN	TTLL12	physical	22863883
TBP_HUMAN	TBP	physical	25416956
DPOE3_HUMAN	POLE3	physical	25416956
SGF29_HUMAN	CCDC101	physical	26344197
CSN3_HUMAN	COPS3	physical	26344197
NC2A_HUMAN	DRAP1	physical	26344197

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

Acetylation

"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-3, AND MASS SPECTROMETRY.
PubMed: 19413330

Phosphorylation

"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-3, 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-166 AND SER-167, ANDMASS SPECTROMETRY.
PubMed: 18669648

"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND MASSSPECTROMETRY.
PubMed: 17287340