CHRD1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CHRD1_MOUSE
• UniProt AC: Q9D1P4
• Protein Name: Cysteine and histidine-rich domain-containing protein 1
• Gene Name: Chordc1
• Organism: Mus musculus (Mouse).
• Sequence Length: 331
• Protein Description: Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis (By similarity)..
• Protein Sequence: MALLCYNRGCGQRFDPEANSDDACTYHPGVPVFHDALKGWSCCKRRTTDFSDFLSIVGCTKGRHNSEKPPEPVKPEVKTTEKKELSELKPKFQEHIIQAPKPVEAIKRPSPDEPMTNLELKISASLKQALDKLKLSSGSEEDKKEEDSDEIKIGTSCKNGGCSKTYQGLQSLEEVCVYHSGVPIFHEGMKYWSCCRRKTSDFNTFLAQEGCTRGKHVWTKKDAGKKVVPCRHDWHQTGGEVTISVYAKNSLPELSQVEANSTLLNVHIVFEGEKEFHQNVKLWGVIDVKRSYVTMTATKIEITMRKAEPMQWASLELPTTKKQEKQKDIAD

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	------MALLCYNRG ------CCEEECCCC	14.83	-
20	Phosphorylation	RFDPEANSDDACTYH CCCCCCCCCCCCCCC	43.87	-
24	S-palmitoylation	EANSDDACTYHPGVP CCCCCCCCCCCCCCC	5.09	28680068
25	Phosphorylation	ANSDDACTYHPGVPV CCCCCCCCCCCCCCC	26.95	-
26	Phosphorylation	NSDDACTYHPGVPVF CCCCCCCCCCCCCCC	13.10	-
47	Phosphorylation	WSCCKRRTTDFSDFL CCCCCCCCCCHHHHH	34.45	26824392
48	Phosphorylation	SCCKRRTTDFSDFLS CCCCCCCCCHHHHHH	32.98	25619855
51	Phosphorylation	KRRTTDFSDFLSIVG CCCCCCHHHHHHHHC	30.20	25619855
55	Phosphorylation	TDFSDFLSIVGCTKG CCHHHHHHHHCCCCC	18.41	25619855
59	S-nitrosocysteine	DFLSIVGCTKGRHNS HHHHHHCCCCCCCCC	2.17	-
59	S-nitrosylation	DFLSIVGCTKGRHNS HHHHHHCCCCCCCCC	2.17	21278135
59	Glutathionylation	DFLSIVGCTKGRHNS HHHHHHCCCCCCCCC	2.17	24333276
89	Acetylation	KKELSELKPKFQEHI HHHHHHHCHHHHHHH	41.95	23954790
89	Ubiquitination	KKELSELKPKFQEHI HHHHHHHCHHHHHHH	41.95	27667366
110	Phosphorylation	VEAIKRPSPDEPMTN HHHCCCCCCCCCCCC	49.36	25521595
116	Phosphorylation	PSPDEPMTNLELKIS CCCCCCCCCCCHHHC	47.57	28059163
125	Phosphorylation	LELKISASLKQALDK CCHHHCHHHHHHHHH	29.34	29176673
127	Ubiquitination	LKISASLKQALDKLK HHHCHHHHHHHHHHC	30.91	27667366
136	Phosphorylation	ALDKLKLSSGSEEDK HHHHHCCCCCCHHHC	30.94	27742792
137	Phosphorylation	LDKLKLSSGSEEDKK HHHHCCCCCCHHHCC	57.69	30635358
139	Phosphorylation	KLKLSSGSEEDKKEE HHCCCCCCHHHCCCC	39.50	26824392
148	Phosphorylation	EDKKEEDSDEIKIGT HHCCCCCCCCCEECC	40.18	27742792
198	Malonylation	YWSCCRRKTSDFNTF HHHHHCCCCCCHHHH	32.78	26320211
199	Phosphorylation	WSCCRRKTSDFNTFL HHHHCCCCCCHHHHH	31.55	25521595
200	Phosphorylation	SCCRRKTSDFNTFLA HHHCCCCCCHHHHHH	43.15	25521595
204	Phosphorylation	RKTSDFNTFLAQEGC CCCCCHHHHHHHCCC	21.73	28833060
306	Acetylation	KIEITMRKAEPMQWA EEEEEEEECCCCCCE	46.40	6568987

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

Oops, there are no upstream regulatory protein records of CHRD1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CHRD1_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CHRD1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PPP5_MOUSE	Ppp5c	physical	16083881
HS90B_MOUSE	Hsp90ab1	physical	16083881
HS90A_MOUSE	Hsp90aa1	physical	16083881
NOD1_MOUSE	Nod1	physical	16083881
PPP5_HUMAN	PPP5C	physical	23184943
SGT1_HUMAN	SUGT1	physical	23184943
CHRD1_MOUSE	Chordc1	physical	23184943
HS90B_HUMAN	HSP90AB1	physical	15642353

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47 AND THR-204, AND MASSSPECTROMETRY.
PubMed: 17242355