CC137_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CC137_HUMAN
• UniProt AC: Q6PK04
• Protein Name: Coiled-coil domain-containing protein 137
• Gene Name: CCDC137
• Organism: Homo sapiens (Human).
• Sequence Length: 289
• Subcellular Localization: Chromosome .
• Protein Sequence: MAGAGRGAAVSRVQAGPGSPRRARGRQQVQPLGKQRPAPWPGLRSKEKKKVNCKPKNQDEQEIPFRLREIMRSRQEMKNPISNKKRKKAAQVTFRKTLEKEAKGEEPDIAVPKFKQRKGESDGAYIHRMQQEAQHVLFLSKNQAIRQPEVQAAPKEKSEQKKAKKAFQKRRLDKVRRKKEEKAADRLEQELLRDTVKFGEVVLQPPELTARPQRSVSKDQPGRRSQMLRMLLSPGGVSQPLTASLARQRIVEEERERAVQAYRALKQRQQQLHGERPHLTSRKKPEPQL

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	Methylation	--MAGAGRGAAVSRV --CCCCCCCCCCCCC	30.92	115368227
12	Methylation	GRGAAVSRVQAGPGS CCCCCCCCCCCCCCC	20.26	115483207
13	Ubiquitination	RGAAVSRVQAGPGSP CCCCCCCCCCCCCCC	3.40	23000965
19	Phosphorylation	RVQAGPGSPRRARGR CCCCCCCCCCCCCCC	20.54	29255136
48	Acetylation	PGLRSKEKKKVNCKP CCCCCCCCCCCCCCC	62.73	90589
56	Ubiquitination	KKVNCKPKNQDEQEI CCCCCCCCCCCCCCC	53.38	33845483
82	Phosphorylation	QEMKNPISNKKRKKA HHHHCCCCHHHHHHH	43.80	-
100	Sumoylation	TFRKTLEKEAKGEEP HHHHHHHHHHCCCCC	67.11	-
100	Sumoylation	TFRKTLEKEAKGEEP HHHHHHHHHHCCCCC	67.11	-
113	Ubiquitination	EPDIAVPKFKQRKGE CCCCCCCHHHCCCCC	59.60	24816145
118	Ubiquitination	VPKFKQRKGESDGAY CCHHHCCCCCCCCCH	65.62	-
125	Phosphorylation	KGESDGAYIHRMQQE CCCCCCCHHHHHHHH	11.64	-
129	Ubiquitination	DGAYIHRMQQEAQHV CCCHHHHHHHHHHHH	2.74	24816145
141	Acetylation	QHVLFLSKNQAIRQP HHHHHCCCCHHHCCH	56.05	26051181
141	Ubiquitination	QHVLFLSKNQAIRQP HHHHHCCCCHHHCCH	56.05	23000965
156	Ubiquitination	EVQAAPKEKSEQKKA HHHCCCHHHHHHHHH	61.83	24816145
157	Ubiquitination	VQAAPKEKSEQKKAK HHCCCHHHHHHHHHH	66.47	23000965
195	Phosphorylation	EQELLRDTVKFGEVV HHHHHHHHCHHCCEE	21.11	28555341
197	Acetylation	ELLRDTVKFGEVVLQ HHHHHHCHHCCEECC	50.14	11921397
223	Dimethylation	VSKDQPGRRSQMLRM CCCCCCCHHHHHHHH	41.58	-
223	Methylation	VSKDQPGRRSQMLRM CCCCCCCHHHHHHHH	41.58	115372663
224	Methylation	SKDQPGRRSQMLRML CCCCCCHHHHHHHHH	36.84	6567619
224	Dimethylation	SKDQPGRRSQMLRML CCCCCCHHHHHHHHH	36.84	-
230	Sulfoxidation	RRSQMLRMLLSPGGV HHHHHHHHHHCCCCC	3.77	21406390
233	Phosphorylation	QMLRMLLSPGGVSQP HHHHHHHCCCCCCHH	19.96	26055452
238	Phosphorylation	LLSPGGVSQPLTASL HHCCCCCCHHHHHHH	29.38	24732914
242	Phosphorylation	GGVSQPLTASLARQR CCCCHHHHHHHHHHH	22.38	24732914
244	Phosphorylation	VSQPLTASLARQRIV CCHHHHHHHHHHHHH	19.82	24732914
284	Ubiquitination	PHLTSRKKPEPQL-- CCCCCCCCCCCCC--	54.20	24816145

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

Oops, there are no upstream regulatory protein records of CC137_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CC137_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 CC137_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of CC137_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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233, AND MASSSPECTROMETRY.
PubMed: 19690332

"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASSSPECTROMETRY.
PubMed: 19413330

"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-233, AND MASSSPECTROMETRY.
PubMed: 18669648

"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-233, AND MASSSPECTROMETRY.
PubMed: 18220336

"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-19, AND MASSSPECTROMETRY.
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-233, AND MASSSPECTROMETRY.
PubMed: 17924679

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASSSPECTROMETRY.
PubMed: 17081983