CR021_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CR021_HUMAN
• UniProt AC: Q32NC0
• Protein Name: UPF0711 protein C18orf21
• Gene Name: C18orf21
• Organism: Homo sapiens (Human).
• Sequence Length: 220
• Protein Sequence: MRQKHYLEAAARGLHDSCPGQARYLLWAYTSSHDDKSTFEETCPYCFQLLVLDNSRVRLKPKARLTPKIQKLLNREARNYTLSFKEAKMVKKFKDSKSVLLITCKTCNRTVKHHGKSRSFVSTLKSNPATPTSKLSLKTPERRTANPNHDMSGSKGKSPASVFRTPTSGQSVSTCSSKNTSKTKKHFSQLKMLLSQNESQKIPKVDFRNFLSSLKGGLLK

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
6	Phosphorylation	--MRQKHYLEAAARG --CCCHHHHHHHHCC	17.17	20068231
83	Phosphorylation	EARNYTLSFKEAKMV HHHHCCCCHHHHHHH	26.86	24719451
106	Phosphorylation	VLLITCKTCNRTVKH EEEEEECCCCCCCCC	19.70	20068231
110	Phosphorylation	TCKTCNRTVKHHGKS EECCCCCCCCCCCCC	21.66	20068231
117	Phosphorylation	TVKHHGKSRSFVSTL CCCCCCCCCCHHHHH	37.44	20068231
119	Phosphorylation	KHHGKSRSFVSTLKS CCCCCCCCHHHHHHC	36.77	26434776
122	Phosphorylation	GKSRSFVSTLKSNPA CCCCCHHHHHHCCCC	26.47	29214152
123	Phosphorylation	KSRSFVSTLKSNPAT CCCCHHHHHHCCCCC	32.67	29978859
125	Ubiquitination	RSFVSTLKSNPATPT CCHHHHHHCCCCCCC	48.56	-
126	Phosphorylation	SFVSTLKSNPATPTS CHHHHHHCCCCCCCC	51.67	16964243
130	Phosphorylation	TLKSNPATPTSKLSL HHHCCCCCCCCCCCC	28.49	16964243
132	Phosphorylation	KSNPATPTSKLSLKT HCCCCCCCCCCCCCC	33.85	18669648
133	Phosphorylation	SNPATPTSKLSLKTP CCCCCCCCCCCCCCC	32.57	20068231
134	Ubiquitination	NPATPTSKLSLKTPE CCCCCCCCCCCCCCC	44.57	-
136	Phosphorylation	ATPTSKLSLKTPERR CCCCCCCCCCCCCCC	31.40	23186163
139	Phosphorylation	TSKLSLKTPERRTAN CCCCCCCCCCCCCCC	35.36	23898821
152	Phosphorylation	ANPNHDMSGSKGKSP CCCCCCCCCCCCCCC	46.07	20068231
154	Phosphorylation	PNHDMSGSKGKSPAS CCCCCCCCCCCCCCH	30.81	29978859
158	Phosphorylation	MSGSKGKSPASVFRT CCCCCCCCCCHHEEC	34.07	25159151
161	Phosphorylation	SKGKSPASVFRTPTS CCCCCCCHHEECCCC	25.77	22199227
165	Phosphorylation	SPASVFRTPTSGQSV CCCHHEECCCCCCCC	21.32	19691289
167	Phosphorylation	ASVFRTPTSGQSVST CHHEECCCCCCCCCC	44.89	19691289
168	Phosphorylation	SVFRTPTSGQSVSTC HHEECCCCCCCCCCC	35.72	19691289
171	Phosphorylation	RTPTSGQSVSTCSSK ECCCCCCCCCCCCCC	22.89	19691289
173	Phosphorylation	PTSGQSVSTCSSKNT CCCCCCCCCCCCCCC	29.01	22199227
174	Phosphorylation	TSGQSVSTCSSKNTS CCCCCCCCCCCCCCH	17.79	22199227
178	Ubiquitination	SVSTCSSKNTSKTKK CCCCCCCCCCHHHHH	48.20	-
185	Ubiquitination	KNTSKTKKHFSQLKM CCCHHHHHHHHHHHH	55.93	-
195	Phosphorylation	SQLKMLLSQNESQKI HHHHHHHHCCCCCCC	27.31	25159151
199	Phosphorylation	MLLSQNESQKIPKVD HHHHCCCCCCCCCCC	44.30	23532336
212	Phosphorylation	VDFRNFLSSLKGGLL CCHHHHHHHHCCCCC	29.50	20068231
213	Phosphorylation	DFRNFLSSLKGGLLK CHHHHHHHHCCCCCC	35.93	20068231
215	Ubiquitination	RNFLSSLKGGLLK-- HHHHHHHCCCCCC--	53.53	-
215	Methylation	RNFLSSLKGGLLK-- HHHHHHHCCCCCC--	53.53	-

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

Oops, there are no upstream regulatory protein records of CR021_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CR021_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 CR021_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
RPP25_HUMAN	RPP25	physical	28514442
RPP30_HUMAN	RPP30	physical	28514442
RPP40_HUMAN	RPP40	physical	28514442
RPP14_HUMAN	RPP14	physical	28514442
NEPRO_HUMAN	C3orf17	physical	28514442
RP25L_HUMAN	RPP25L	physical	28514442
POP5_HUMAN	POP5	physical	28514442
RPP38_HUMAN	RPP38	physical	28514442
POP7_HUMAN	POP7	physical	28514442
POP1_HUMAN	POP1	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.

Related Literatures of Post-Translational Modification

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-126; THR-130 ANDTHR-139, AND MASS SPECTROMETRY.
PubMed: 18669648

"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-158, AND MASSSPECTROMETRY.
PubMed: 18691976

"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158 AND SER-161, ANDMASS SPECTROMETRY.
PubMed: 19007248

"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117 AND SER-122, ANDMASS SPECTROMETRY.
PubMed: 17924679

"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126 AND THR-130, ANDMASS SPECTROMETRY.
PubMed: 16964243