dbPTM

CHRD1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CHRD1_HUMAN
UniProt AC	Q9UHD1
Protein Name	Cysteine and histidine-rich domain-containing protein 1
Gene Name	CHORDC1
Organism	Homo sapiens (Human).
Sequence Length	332
Subcellular Localization
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..
Protein Sequence	MALLCYNRGCGQRFDPETNSDDACTYHPGVPVFHDALKGWSCCKRRTTDFSDFLSIVGCTKGRHNSEKPPEPVKPEVKTTEKKELCELKPKFQEHIIQAPKPVEAIKRPSPDEPMTNLELKISASLKQALDKLKLSSGNEENKKEEDNDEIKIGTSCKNGGCSKTYQGLESLEEVCVYHSGVPIFHEGMKYWSCCRRKTSDFNTFLAQEGCTKGKHMWTKKDAGKKVVPCRHDWHQTGGEVTISVYAKNSLPELSRVEANSTLLNVHIVFEGEKEFDQNVKLWGVIDVKRSYVTMTATKIEITMRKAEPMQWASLELPAAKKQEKQKDATTD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MALLCYNRG ------CCEEECCCC	14.83	22814378
8	Methylation	MALLCYNRGCGQRFD CCEEECCCCCCCCCC	18.46	-
18	Phosphorylation	GQRFDPETNSDDACT CCCCCCCCCCCCCCC	45.47	28348404
18	Ubiquitination	GQRFDPETNSDDACT CCCCCCCCCCCCCCC	45.47	27667366
20	Phosphorylation	RFDPETNSDDACTYH CCCCCCCCCCCCCCC	44.26	25159151
20	Ubiquitination	RFDPETNSDDACTYH CCCCCCCCCCCCCCC	44.26	27667366
25	Phosphorylation	TNSDDACTYHPGVPV CCCCCCCCCCCCCCC	26.95	28348404
26	Phosphorylation	NSDDACTYHPGVPVF CCCCCCCCCCCCCCC	13.10	27642862
29	Ubiquitination	DACTYHPGVPVFHDA CCCCCCCCCCCCHHH	24.05	27667366
38	2-Hydroxyisobutyrylation	PVFHDALKGWSCCKR CCCHHHHCCCCCCCC	61.12	-
38	Acetylation	PVFHDALKGWSCCKR CCCHHHHCCCCCCCC	61.12	27452117
41	Phosphorylation	HDALKGWSCCKRRTT HHHHCCCCCCCCCCC	20.50	-
44	2-Hydroxyisobutyrylation	LKGWSCCKRRTTDFS HCCCCCCCCCCCCHH	49.60	-
47	Phosphorylation	WSCCKRRTTDFSDFL CCCCCCCCCCHHHHH	34.45	30266825
48	Phosphorylation	SCCKRRTTDFSDFLS CCCCCCCCCHHHHHH	32.98	30266825
51	Phosphorylation	KRRTTDFSDFLSIVG CCCCCCHHHHHHHHC	30.20	10571178
55	Phosphorylation	TDFSDFLSIVGCTKG CCHHHHHHHHCCCCC	18.41	23403867
55	Ubiquitination	TDFSDFLSIVGCTKG CCHHHHHHHHCCCCC	18.41	33845483
59	Glutathionylation	DFLSIVGCTKGRHNS HHHHHHCCCCCCCCC	2.17	22555962
60	Phosphorylation	FLSIVGCTKGRHNSE HHHHHCCCCCCCCCC	30.52	23403867
64	Ubiquitination	VGCTKGRHNSEKPPE HCCCCCCCCCCCCCC	51.33	29967540
66	Phosphorylation	CTKGRHNSEKPPEPV CCCCCCCCCCCCCCC	40.65	28555341
68	Ubiquitination	KGRHNSEKPPEPVKP CCCCCCCCCCCCCCC	66.74	33845483
70	Ubiquitination	RHNSEKPPEPVKPEV CCCCCCCCCCCCCCC	70.37	27667366
72	Ubiquitination	NSEKPPEPVKPEVKT CCCCCCCCCCCCCCC	45.25	21890473
72 (in isoform 2)	Ubiquitination	-	45.25	21890473
74	Acetylation	EKPPEPVKPEVKTTE CCCCCCCCCCCCCCC	46.29	26051181
74	Ubiquitination	EKPPEPVKPEVKTTE CCCCCCCCCCCCCCC	46.29	33845483
79	Phosphorylation	PVKPEVKTTEKKELC CCCCCCCCCCCHHHH	45.42	28555341
82	Ubiquitination	PEVKTTEKKELCELK CCCCCCCCHHHHHCC	49.83	29967540
83	2-Hydroxyisobutyrylation	EVKTTEKKELCELKP CCCCCCCHHHHHCCH	50.08	-
83	Ubiquitination	EVKTTEKKELCELKP CCCCCCCHHHHHCCH	50.08	29967540
86	Glutathionylation	TTEKKELCELKPKFQ CCCCHHHHHCCHHHH	6.37	22555962
88	Ubiquitination	EKKELCELKPKFQEH CCHHHHHCCHHHHHH	12.88	29967540
89	Acetylation	KKELCELKPKFQEHI CHHHHHCCHHHHHHH	24.70	23749302
89	Malonylation	KKELCELKPKFQEHI CHHHHHCCHHHHHHH	24.70	26320211
89	Ubiquitination	KKELCELKPKFQEHI CHHHHHCCHHHHHHH	24.70	27667366
91	Acetylation	ELCELKPKFQEHIIQ HHHHCCHHHHHHHCC	59.08	23236377
91	Ubiquitination	ELCELKPKFQEHIIQ HHHHCCHHHHHHHCC	59.08	22817900
91 (in isoform 1)	Ubiquitination	-	59.08	21890473
101	Acetylation	EHIIQAPKPVEAIKR HHHCCCCCCHHHCCC	65.79	26051181
101	Ubiquitination	EHIIQAPKPVEAIKR HHHCCCCCCHHHCCC	65.79	29967540
102	Ubiquitination	HIIQAPKPVEAIKRP HHCCCCCCHHHCCCC	28.28	32015554
107	Acetylation	PKPVEAIKRPSPDEP CCCHHHCCCCCCCCC	66.36	26051181
107	Ubiquitination	PKPVEAIKRPSPDEP CCCHHHCCCCCCCCC	66.36	29967540
108	Ubiquitination	KPVEAIKRPSPDEPM CCHHHCCCCCCCCCC	30.71	32015554
110	Phosphorylation	VEAIKRPSPDEPMTN HHHCCCCCCCCCCCC	49.36	28464451
113	Ubiquitination	IKRPSPDEPMTNLEL CCCCCCCCCCCCCCH	40.11	27667366
115	Sulfoxidation	RPSPDEPMTNLELKI CCCCCCCCCCCCHHH	3.50	21406390
115	Ubiquitination	RPSPDEPMTNLELKI CCCCCCCCCCCCHHH	3.50	27667366
116	Phosphorylation	PSPDEPMTNLELKIS CCCCCCCCCCCHHHC	47.57	20068231
121	Ubiquitination	PMTNLELKISASLKQ CCCCCCHHHCHHHHH	25.82	32015554
124	Ubiquitination	NLELKISASLKQALD CCCHHHCHHHHHHHH	23.50	33845483
125	Phosphorylation	LELKISASLKQALDK CCHHHCHHHHHHHHH	29.34	28464451
125	Ubiquitination	LELKISASLKQALDK CCHHHCHHHHHHHHH	29.34	33845483
127	Acetylation	LKISASLKQALDKLK HHHCHHHHHHHHHHC	30.91	25953088
127	Succinylation	LKISASLKQALDKLK HHHCHHHHHHHHHHC	30.91	23954790
127	Ubiquitination	LKISASLKQALDKLK HHHCHHHHHHHHHHC	30.91	32015554
132	2-Hydroxyisobutyrylation	SLKQALDKLKLSSGN HHHHHHHHHCCCCCC	48.66	-
132	Acetylation	SLKQALDKLKLSSGN HHHHHHHHHCCCCCC	48.66	25953088
132	Ubiquitination	SLKQALDKLKLSSGN HHHHHHHHHCCCCCC	48.66	27667366
133	Ubiquitination	LKQALDKLKLSSGNE HHHHHHHHCCCCCCC	7.24	33845483
134	Ubiquitination	KQALDKLKLSSGNEE HHHHHHHCCCCCCCC	52.65	27667366
136	Phosphorylation	ALDKLKLSSGNEENK HHHHHCCCCCCCCCC	34.31	25159151
137	Phosphorylation	LDKLKLSSGNEENKK HHHHCCCCCCCCCCC	56.95	25159151
143	Ubiquitination	SSGNEENKKEEDNDE CCCCCCCCCCCCCCC	65.91	33845483
144	Ubiquitination	SGNEENKKEEDNDEI CCCCCCCCCCCCCCE	77.30	33845483
152	Ubiquitination	EEDNDEIKIGTSCKN CCCCCCEEECCCCCC	32.79	33845483
175	Ubiquitination	GLESLEEVCVYHSGV CHHCHHHHEECCCCC	1.63	21890473
178	Phosphorylation	SLEEVCVYHSGVPIF CHHHHEECCCCCEEE	5.78	-
179	Ubiquitination	LEEVCVYHSGVPIFH HHHHEECCCCCEEEC	9.55	29967540
194	Ubiquitination	EGMKYWSCCRRKTSD CCHHHHHHHCCCCCC	0.98	33845483
198	Acetylation	YWSCCRRKTSDFNTF HHHHHCCCCCCHHHH	32.78	20167786
198	Ubiquitination	YWSCCRRKTSDFNTF HHHHHCCCCCCHHHH	32.78	29967540
199	Phosphorylation	WSCCRRKTSDFNTFL HHHHCCCCCCHHHHH	31.55	30266825
200	Phosphorylation	SCCRRKTSDFNTFLA HHHCCCCCCHHHHHH	43.15	30266825
204	Phosphorylation	RKTSDFNTFLAQEGC CCCCCHHHHHHHCCC	21.73	30266825
212	Phosphorylation	FLAQEGCTKGKHMWT HHHHCCCCCCCCCEE	54.40	23403867
213	Ubiquitination	LAQEGCTKGKHMWTK HHHCCCCCCCCCEEE	70.77	33845483
215	Acetylation	QEGCTKGKHMWTKKD HCCCCCCCCCEEECC	31.66	26051181
215	Ubiquitination	QEGCTKGKHMWTKKD HCCCCCCCCCEEECC	31.66	-
220	Acetylation	KGKHMWTKKDAGKKV CCCCCEEECCCCCEE	32.89	20167786
237	Phosphorylation	CRHDWHQTGGEVTIS CCCCCCCCCCEEEEE	33.98	21406692
242	Phosphorylation	HQTGGEVTISVYAKN CCCCCEEEEEEEECC	11.84	21406692
244	Phosphorylation	TGGEVTISVYAKNSL CCCEEEEEEEECCCC	10.34	21406692
246	Phosphorylation	GEVTISVYAKNSLPE CEEEEEEEECCCCCC	12.69	21406692
270	Ubiquitination	LLNVHIVFEGEKEFD EEEEEEEECCCCEEC	11.18	23000965
270 (in isoform 2)	Ubiquitination	-	11.18	21890473
289	2-Hydroxyisobutyrylation	LWGVIDVKRSYVTMT EEEEEEEECCEEEEE	31.70	-
289	Acetylation	LWGVIDVKRSYVTMT EEEEEEEECCEEEEE	31.70	25953088
289	Ubiquitination	LWGVIDVKRSYVTMT EEEEEEEECCEEEEE	31.70	23000965
289 (in isoform 1)	Ubiquitination	-	31.70	21890473
291	Phosphorylation	GVIDVKRSYVTMTAT EEEEEECCEEEEEEE	20.45	28152594
292	Nitration	VIDVKRSYVTMTATK EEEEECCEEEEEEEE	12.17	-
292	Phosphorylation	VIDVKRSYVTMTATK EEEEECCEEEEEEEE	12.17	28152594
294	Phosphorylation	DVKRSYVTMTATKIE EEECCEEEEEEEEEE	10.69	28152594
295	Sulfoxidation	VKRSYVTMTATKIEI EECCEEEEEEEEEEE	1.39	30846556
296	Phosphorylation	KRSYVTMTATKIEIT ECCEEEEEEEEEEEE	23.08	28152594
298	Phosphorylation	SYVTMTATKIEITMR CEEEEEEEEEEEEEE	24.32	28152594
302	Ubiquitination	MTATKIEITMRKAEP EEEEEEEEEEEECCC	4.11	32015554
310	Sulfoxidation	TMRKAEPMQWASLEL EEEECCCCCHHHCCC	3.80	28183972
314	Phosphorylation	AEPMQWASLELPAAK CCCCCHHHCCCCHHH	21.29	25159151
321	Acetylation	SLELPAAKKQEKQKD HCCCCHHHHHHHHHC	58.03	25953088
321	Ubiquitination	SLELPAAKKQEKQKD HCCCCHHHHHHHHHC	58.03	32015554

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
Oops, there are no upstream regulatory protein records of CHRD1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CHRD1_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 CHRD1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CHRD1_HUMAN	CHORDC1	physical	20360068
BCCIP_HUMAN	BCCIP	physical	22863883
XPO2_HUMAN	CSE1L	physical	22863883
KYNU_HUMAN	KYNU	physical	22863883
6PGD_HUMAN	PGD	physical	22863883
DHSO_HUMAN	SORD	physical	22863883
SGT1_HUMAN	SUGT1	physical	22863883
HS90B_HUMAN	HSP90AB1	physical	25036637
HS90A_HUMAN	HSP90AA1	physical	25036637
FKBP4_HUMAN	FKBP4	physical	25036637
TBA1B_HUMAN	TUBA1B	physical	25036637
XPO5_HUMAN	XPO5	physical	25036637
TOM34_HUMAN	TOMM34	physical	25036637
SYTM_HUMAN	TARS2	physical	25036637
EDRF1_HUMAN	EDRF1	physical	26186194
ASPD_HUMAN	ASPDH	physical	26344197
TTC37_HUMAN	TTC37	physical	26344197
CAN2_HUMAN	CAPN2	physical	26496610
HS90A_HUMAN	HSP90AA1	physical	26496610
HS90B_HUMAN	HSP90AB1	physical	26496610
DDR2_HUMAN	DDR2	physical	26496610
SSRG_HUMAN	SSR3	physical	26496610
STX3_HUMAN	STX3	physical	26496610
1433B_HUMAN	YWHAB	physical	26496610
ADAS_HUMAN	AGPS	physical	26496610
REPS2_HUMAN	REPS2	physical	26496610
PLPHP_HUMAN	PROSC	physical	26496610
KDM4B_HUMAN	KDM4B	physical	26496610
WDR70_HUMAN	WDR70	physical	26496610
SYIM_HUMAN	IARS2	physical	26496610
CDCA3_HUMAN	CDCA3	physical	26496610
NSRP1_HUMAN	NSRP1	physical	26496610
ARI5B_HUMAN	ARID5B	physical	26496610
DPY30_HUMAN	DPY30	physical	26496610
RM55_HUMAN	MRPL55	physical	26496610
CE120_HUMAN	CEP120	physical	26496610
PLBL2_HUMAN	PLBD2	physical	26496610
EDRF1_HUMAN	EDRF1	physical	28514442
TTC4_HUMAN	TTC4	physical	28514442
PRCC_HUMAN	PRCC	physical	27173435
SEP11_HUMAN	SEPT11	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.

Regulatory Network of CHRD1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-200, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"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-200, AND MASS SPECTROMETRY.	19413330 [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 THR-47 AND SER-51, AND MASSSPECTROMETRY.	18669648 [Abstract]