CHRC1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CHRC1_HUMAN
• UniProt AC: Q9NRG0
• Protein Name: Chromatin accessibility complex protein 1
• Gene Name: CHRAC1
• Organism: Homo sapiens (Human).
• Sequence Length: 131
• Subcellular Localization: Nucleus .
• Protein Description: Forms a complex with DNA polymerase epsilon subunit POLE3 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome remodeling activity of ISWI/SNF2H and ACF1..
• Protein Sequence: MADVVVGKDKGGEQRLISLPLSRIRVIMKSSPEVSSINQEALVLTAKATELFVQCLATYSYRHGSGKEKKVLTYSDLANTAQQSETFQFLADILPKKILASKYLKMLKEEKREEDEENDNDNESDHDEADS

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	------MADVVVGKD ------CCCEEEECC	20.50	22814378
8	Acetylation	MADVVVGKDKGGEQR CCCEEEECCCCCCEE	44.66	23749302
8	Ubiquitination	MADVVVGKDKGGEQR CCCEEEECCCCCCEE	44.66	33845483
60	Phosphorylation	VQCLATYSYRHGSGK HHHHHHCHHHCCCCC	16.01	24719451
67	Acetylation	SYRHGSGKEKKVLTY HHHCCCCCEEEEEEH	68.97	156597
102	2-Hydroxyisobutyrylation	PKKILASKYLKMLKE CHHHHHHHHHHHHHH	49.33	-
102	Acetylation	PKKILASKYLKMLKE CHHHHHHHHHHHHHH	49.33	19608861
102	Ubiquitination	PKKILASKYLKMLKE CHHHHHHHHHHHHHH	49.33	33845483
105	"N6,N6-dimethyllysine"	ILASKYLKMLKEEKR HHHHHHHHHHHHHHH	38.81	-
105	Methylation	ILASKYLKMLKEEKR HHHHHHHHHHHHHHH	38.81	23644510
108	"N6,N6-dimethyllysine"	SKYLKMLKEEKREED HHHHHHHHHHHHHHH	61.40	-
108	Methylation	SKYLKMLKEEKREED HHHHHHHHHHHHHHH	61.40	23644510
124	Phosphorylation	ENDNDNESDHDEADS CCCCCCCCCCCCCCC	46.64	22167270
131	Phosphorylation	SDHDEADS------- CCCCCCCC-------	49.52	22167270

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

Oops, there are no upstream regulatory protein records of CHRC1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CHRC1_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 CHRC1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BAZ1A_HUMAN	BAZ1A	physical	14759371
SMCA5_HUMAN	SMARCA5	physical	14759371
A4_HUMAN	APP	physical	21832049
SMCA5_HUMAN	SMARCA5	physical	22939629
XPC_HUMAN	XPC	physical	22939629
RPC9_HUMAN	CRCP	physical	22939629
IN80C_HUMAN	INO80C	physical	22939629
PURA2_HUMAN	ADSS	physical	22863883
CUTA_HUMAN	CUTA	physical	22863883
AATC_HUMAN	GOT1	physical	22863883
MTAP_HUMAN	MTAP	physical	22863883
NDKA_HUMAN	NME1	physical	22863883
PTN11_HUMAN	PTPN11	physical	22863883
RBBP7_HUMAN	RBBP7	physical	22863883
TALDO_HUMAN	TALDO1	physical	22863883
FAM9B_HUMAN	FAM9B	physical	25416956
DPOE3_HUMAN	POLE3	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, AND MASS SPECTROMETRY.
PubMed: 19413330

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-102, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"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-124, AND MASSSPECTROMETRY.
PubMed: 18669648