dbPTM

CA226_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CA226_HUMAN
UniProt AC	A1L170
Protein Name	Uncharacterized protein C1orf226
Gene Name	C1orf226
Organism	Homo sapiens (Human).
Sequence Length	272
Subcellular Localization
Protein Description
Protein Sequence	MFENLNTALTPKLQASRSFPHLSKPVAPGSAPLGSGEPGGPGLWVGSSQHLKNLGKAMGAKVNDFLRRKEPSSLGSVGVTEINKTAGAQLASGTDAAPEAWLEDERSVLQETFPRLDPPPPITRKRTPRALKTTQDMLISSQPVLSSLEYGTEPSPGQAQDSAPTAQPDVPADASQPEATMEREERGKVLPNGEVSLSVPDLIHKDSQDESKLKMTECRRASSPSLIERNGFKLSLSPISLAESWEDGSPPPQARTSSLDNEGPHPDLLSFE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MFENLNTALTPKLQ -CCCCHHHCCCHHHH	26.64	21406692
10	Phosphorylation	ENLNTALTPKLQASR CCHHHCCCHHHHHCC	18.86	21406692
16	Phosphorylation	LTPKLQASRSFPHLS CCHHHHHCCCCCCCC	18.59	25849741
18	Phosphorylation	PKLQASRSFPHLSKP HHHHHCCCCCCCCCC	40.40	25159151
23	Phosphorylation	SRSFPHLSKPVAPGS CCCCCCCCCCCCCCC	31.70	28152594
30	Phosphorylation	SKPVAPGSAPLGSGE CCCCCCCCCCCCCCC	26.17	25159151
35	Phosphorylation	PGSAPLGSGEPGGPG CCCCCCCCCCCCCCC	47.90	25159151
47	Phosphorylation	GPGLWVGSSQHLKNL CCCCCCCCHHHHHHH	19.73	25849741
48	Phosphorylation	PGLWVGSSQHLKNLG CCCCCCCHHHHHHHH	18.72	25159151
56	Ubiquitination	QHLKNLGKAMGAKVN HHHHHHHHHHCHHHH	38.06	29967540
61	Phosphorylation	LGKAMGAKVNDFLRR HHHHHCHHHHHHHHC	35.52	32142685
66	Phosphorylation	GAKVNDFLRRKEPSS CHHHHHHHHCCCCCC	6.04	24719451
72	Phosphorylation	FLRRKEPSSLGSVGV HHHCCCCCCCCCCCC	39.01	28985074
73	Phosphorylation	LRRKEPSSLGSVGVT HHCCCCCCCCCCCCE	47.68	25849741
76	Phosphorylation	KEPSSLGSVGVTEIN CCCCCCCCCCCEEEC	22.46	22985185
90	Phosphorylation	NKTAGAQLASGTDAA CCCCCCHHCCCCCCC	3.98	27251275
91	Phosphorylation	KTAGAQLASGTDAAP CCCCCHHCCCCCCCC	8.20	24719451
99	Ubiquitination	SGTDAAPEAWLEDER CCCCCCCHHHHHHHH	47.99	29967540
107	Phosphorylation	AWLEDERSVLQETFP HHHHHHHHHHHHHCC	25.73	24719451
112	Phosphorylation	ERSVLQETFPRLDPP HHHHHHHHCCCCCCC	26.44	24719451
115	Phosphorylation	VLQETFPRLDPPPPI HHHHHCCCCCCCCCC	47.75	27251275
146	Phosphorylation	ISSQPVLSSLEYGTE HHCCCCHHHCCCCCC	32.86	28348404
147	Phosphorylation	SSQPVLSSLEYGTEP HCCCCHHHCCCCCCC	22.51	28348404
150	Phosphorylation	PVLSSLEYGTEPSPG CCHHHCCCCCCCCCC	34.34	24719451
152	Phosphorylation	LSSLEYGTEPSPGQA HHHCCCCCCCCCCCC	43.77	28348404
155	Phosphorylation	LEYGTEPSPGQAQDS CCCCCCCCCCCCCCC	35.12	24719451
162	Phosphorylation	SPGQAQDSAPTAQPD CCCCCCCCCCCCCCC	24.86	28348404
196	Phosphorylation	VLPNGEVSLSVPDLI CCCCCEEEEEHHHHH	15.60	30266825
198	Phosphorylation	PNGEVSLSVPDLIHK CCCEEEEEHHHHHCC	24.89	30266825
207	Phosphorylation	PDLIHKDSQDESKLK HHHHCCCCCCHHHHC	44.31	25159151
211	Phosphorylation	HKDSQDESKLKMTEC CCCCCCHHHHCHHHH	52.13	25627689
214	Acetylation	SQDESKLKMTECRRA CCCHHHHCHHHHHHC	47.73	19827385
222	Phosphorylation	MTECRRASSPSLIER HHHHHHCCCCHHHHH	40.76	23927012
223	Phosphorylation	TECRRASSPSLIERN HHHHHCCCCHHHHHC	19.95	19664994
225	Phosphorylation	CRRASSPSLIERNGF HHHCCCCHHHHHCCE	43.88	30266825
235	Phosphorylation	ERNGFKLSLSPISLA HHCCEEEEECCCCHH	27.65	28387310
237	Phosphorylation	NGFKLSLSPISLAES CCEEEEECCCCHHHH	19.46	28387310
240	Phosphorylation	KLSLSPISLAESWED EEEECCCCHHHHCCC	25.55	28176443
241	Phosphorylation	LSLSPISLAESWEDG EEECCCCHHHHCCCC	6.75	24719451
244	Phosphorylation	SPISLAESWEDGSPP CCCCHHHHCCCCCCC	30.11	25849741
249	Phosphorylation	AESWEDGSPPPQART HHHCCCCCCCCCCCC	46.70	25159151
250	Phosphorylation	ESWEDGSPPPQARTS HHCCCCCCCCCCCCC	50.55	27251275
256	Phosphorylation	SPPPQARTSSLDNEG CCCCCCCCCCCCCCC	26.19	30278072
257	Phosphorylation	PPPQARTSSLDNEGP CCCCCCCCCCCCCCC	24.29	30278072
258	Phosphorylation	PPQARTSSLDNEGPH CCCCCCCCCCCCCCC	38.85	28355574
265	Phosphorylation	SLDNEGPHPDLLSFE CCCCCCCCCCCCCCC	39.09	24719451
266	Phosphorylation	LDNEGPHPDLLSFE- CCCCCCCCCCCCCC-	36.76	24719451
270	Phosphorylation	GPHPDLLSFE----- CCCCCCCCCC-----	34.33	25159151
278	Phosphorylation	FE------------- CC-------------		24719451
280	Phosphorylation	--------------- ---------------		27251275
287	Phosphorylation	---------------------- ----------------------		24719451
292	Phosphorylation	--------------------------- ---------------------------		24719451
301	Phosphorylation	------------------------------------ ------------------------------------		27251275
313	Phosphorylation	------------------------------------------------ ------------------------------------------------		24719451

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 CA226_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CA226_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 CA226_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of CA226_HUMAN !!

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 CA226_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-222; SER-223; SER-249AND SER-258, AND MASS SPECTROMETRY.	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-223, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223; SER-249 ANDSER-258, AND MASS SPECTROMETRY.	18220336 [Abstract]