dbPTM

HXC10_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HXC10_HUMAN
UniProt AC	Q9NYD6
Protein Name	Homeobox protein Hox-C10
Gene Name	HOXC10
Organism	Homo sapiens (Human).
Sequence Length	342
Subcellular Localization	Nucleus.
Protein Description	Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis..
Protein Sequence	MTCPRNVTPNSYAEPLAAPGGGERYSRSAGMYMQSGSDFNCGVMRGCGLAPSLSKRDEGSSPSLALNTYPSYLSQLDSWGDPKAAYRLEQPVGRPLSSCSYPPSVKEENVCCMYSAEKRAKSGPEAALYSHPLPESCLGEHEVPVPSYYRASPSYSALDKTPHCSGANDFEAPFEQRASLNPRAEHLESPQLGGKVSFPETPKSDSQTPSPNEIKTEQSLAGPKGSPSESEKERAKAADSSPDTSDNEAKEEIKAENTTGNWLTAKSGRKKRCPYTKHQTLELEKEFLFNMYLTRERRLEISKTINLTDRQVKIWFQNRRMKLKKMNRENRIRELTSNFNFT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MTCPRNVTPNSYAEP CCCCCCCCCCCCCCC	21.94	29255136
11	Phosphorylation	PRNVTPNSYAEPLAA CCCCCCCCCCCCCCC	27.24	29255136
11	O-linked_Glycosylation	PRNVTPNSYAEPLAA CCCCCCCCCCCCCCC	27.24	30379171
12	Phosphorylation	RNVTPNSYAEPLAAP CCCCCCCCCCCCCCC	22.94	27251275
25	Phosphorylation	APGGGERYSRSAGMY CCCCCCCCCCCCCCC	12.25	28555341
26	Phosphorylation	PGGGERYSRSAGMYM CCCCCCCCCCCCCCC	26.44	28555341
54	Phosphorylation	CGLAPSLSKRDEGSS CCCCCCCCCCCCCCC	29.95	28555341
55	Ubiquitination	GLAPSLSKRDEGSSP CCCCCCCCCCCCCCC	69.98	-
60	Phosphorylation	LSKRDEGSSPSLALN CCCCCCCCCCCHHHH	36.71	25159151
61	Phosphorylation	SKRDEGSSPSLALNT CCCCCCCCCCHHHHC	29.39	25159151
63	Phosphorylation	RDEGSSPSLALNTYP CCCCCCCCHHHHCCH	28.37	30576142
78	Phosphorylation	SYLSQLDSWGDPKAA HHHHHHHHCCCHHHH	41.36	-
83	Ubiquitination	LDSWGDPKAAYRLEQ HHHCCCHHHHHCCCC	50.84	-
86	Phosphorylation	WGDPKAAYRLEQPVG CCCHHHHHCCCCCCC	22.16	30576142
106	Sumoylation	CSYPPSVKEENVCCM CCCCCCCCCCCEEEE	64.74	28112733
114	Phosphorylation	EENVCCMYSAEKRAK CCCEEEEEEHHHHHH	7.27	29396449
115	Phosphorylation	ENVCCMYSAEKRAKS CCEEEEEEHHHHHHC	11.76	21815630
121	Ubiquitination	YSAEKRAKSGPEAAL EEHHHHHHCCCCHHH	61.04	-
122	Phosphorylation	SAEKRAKSGPEAALY EHHHHHHCCCCHHHH	59.60	25159151
129	Phosphorylation	SGPEAALYSHPLPES CCCCHHHHCCCCCHH	10.54	27642862
152	Phosphorylation	VPSYYRASPSYSALD CCCCCCCCCCCCCCC	12.84	25159151
154	Phosphorylation	SYYRASPSYSALDKT CCCCCCCCCCCCCCC	29.26	20873877
155	Phosphorylation	YYRASPSYSALDKTP CCCCCCCCCCCCCCC	11.01	27642862
156	Phosphorylation	YRASPSYSALDKTPH CCCCCCCCCCCCCCC	27.05	29396449
160	Acetylation	PSYSALDKTPHCSGA CCCCCCCCCCCCCCC	65.88	26051181
160	Ubiquitination	PSYSALDKTPHCSGA CCCCCCCCCCCCCCC	65.88	-
161	Phosphorylation	SYSALDKTPHCSGAN CCCCCCCCCCCCCCC	20.24	25159151
179	Phosphorylation	APFEQRASLNPRAEH CCHHHHHCCCCCHHH	30.76	28555341
189	Phosphorylation	PRAEHLESPQLGGKV CCHHHCCCCCCCCCC	25.06	30266825
195	Sumoylation	ESPQLGGKVSFPETP CCCCCCCCCCCCCCC	32.67	28112733
195	Acetylation	ESPQLGGKVSFPETP CCCCCCCCCCCCCCC	32.67	26051181
195	Sumoylation	ESPQLGGKVSFPETP CCCCCCCCCCCCCCC	32.67	-
197	Phosphorylation	PQLGGKVSFPETPKS CCCCCCCCCCCCCCC	38.27	30266825
201	Phosphorylation	GKVSFPETPKSDSQT CCCCCCCCCCCCCCC	35.93	30266825
203	Sumoylation	VSFPETPKSDSQTPS CCCCCCCCCCCCCCC	74.45	-
204	Phosphorylation	SFPETPKSDSQTPSP CCCCCCCCCCCCCCH	43.63	23663014
206	Phosphorylation	PETPKSDSQTPSPNE CCCCCCCCCCCCHHH	42.94	25159151
208	Phosphorylation	TPKSDSQTPSPNEIK CCCCCCCCCCHHHCC	29.68	23663014
210	Phosphorylation	KSDSQTPSPNEIKTE CCCCCCCCHHHCCCC	43.68	30278072
215	Sumoylation	TPSPNEIKTEQSLAG CCCHHHCCCCHHHCC	39.57	-
215	Ubiquitination	TPSPNEIKTEQSLAG CCCHHHCCCCHHHCC	39.57	-
215	Sumoylation	TPSPNEIKTEQSLAG CCCHHHCCCCHHHCC	39.57	-
216	Phosphorylation	PSPNEIKTEQSLAGP CCHHHCCCCHHHCCC	44.94	23663014
219	Phosphorylation	NEIKTEQSLAGPKGS HHCCCCHHHCCCCCC	17.60	23663014
226	Phosphorylation	SLAGPKGSPSESEKE HHCCCCCCCCHHHHH	31.23	30278072
228	Phosphorylation	AGPKGSPSESEKERA CCCCCCCCHHHHHHH	56.29	30278072
230	Phosphorylation	PKGSPSESEKERAKA CCCCCCHHHHHHHHH	59.30	26055452
240	Phosphorylation	ERAKAADSSPDTSDN HHHHHCCCCCCCCCH	38.76	23663014
241	Phosphorylation	RAKAADSSPDTSDNE HHHHCCCCCCCCCHH	27.61	23663014
244	Phosphorylation	AADSSPDTSDNEAKE HCCCCCCCCCHHHHH	41.17	23663014
245	Phosphorylation	ADSSPDTSDNEAKEE CCCCCCCCCHHHHHH	45.91	23663014
254	Sumoylation	NEAKEEIKAENTTGN HHHHHHHHHHHCCCC	53.58	-
254	Sumoylation	NEAKEEIKAENTTGN HHHHHHHHHHHCCCC	53.58	28112733
254	Ubiquitination	NEAKEEIKAENTTGN HHHHHHHHHHHCCCC	53.58	-
266	Ubiquitination	TGNWLTAKSGRKKRC CCCCEEECCCCCCCC	48.48	-
271	Ubiquitination	TAKSGRKKRCPYTKH EECCCCCCCCCCCCC	58.85	-
275	Phosphorylation	GRKKRCPYTKHQTLE CCCCCCCCCCCCCHH	31.85	12145285
277	Ubiquitination	KKRCPYTKHQTLELE CCCCCCCCCCCHHHH	28.07	-
280	Phosphorylation	CPYTKHQTLELEKEF CCCCCCCCHHHHHHH	23.17	-
292	Phosphorylation	KEFLFNMYLTRERRL HHHHHHHHHHHHHHH	13.16	12145285
302	Phosphorylation	RERRLEISKTINLTD HHHHHEECCEECCCH	17.86	24719451
308	Phosphorylation	ISKTINLTDRQVKIW ECCEECCCHHHHHHH	25.34	24719451
337	Phosphorylation	NRIRELTSNFNFT-- HHHHHHHHCCCCC--	52.64	18491316
342	Phosphorylation	LTSNFNFT------- HHHCCCCC-------	38.51	18491316

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 HXC10_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HXC10_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 HXC10_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CWC27_HUMAN	CWC27	physical	22939629
1433G_HUMAN	YWHAG	physical	21988832
NU205_HUMAN	NUP205	physical	21988832
SNX15_HUMAN	SNX15	physical	28514442
MTU1_HUMAN	TRMU	physical	28514442
MK14_HUMAN	MAPK14	physical	28514442
MK09_HUMAN	MAPK9	physical	28514442

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 HXC10_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-189, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, AND MASSSPECTROMETRY.	18691976 [Abstract]