dbPTM

CWC15_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CWC15_HUMAN
UniProt AC	Q9P013
Protein Name	Spliceosome-associated protein CWC15 homolog
Gene Name	CWC15
Organism	Homo sapiens (Human).
Sequence Length	229
Subcellular Localization	Nucleus .
Protein Description	Involved in pre-mRNA splicing as component of the spliceosome. [PubMed: 28502770]
Protein Sequence	MTTAARPTFEPARGGRGKGEGDLSQLSKQYSSRDLPSHTKIKYRQTTQDAPEEVRNRDFRRELEERERAAAREKNRDRPTREHTTSSSVSKKPRLDQIPAANLDADDPLTDEEDEDFEEESDDDDTAALLAELEKIKKERAEEQARKEQEQKAEEERIRMENILSGNPLLNLTGPSQPQANFKVKRRWDDDVVFKNCAKGVDDQKKDKRFVNDTLRSEFHKKFMEKYIK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MTTAARPTF ------CCCCCCCCC	25.74	27486199
2	Acetylation	------MTTAARPTF ------CCCCCCCCC	25.74	19413330
3	Phosphorylation	-----MTTAARPTFE -----CCCCCCCCCC	19.61	28450419
6	Methylation	--MTTAARPTFEPAR --CCCCCCCCCCCCC	28.47	115368741
8	Phosphorylation	MTTAARPTFEPARGG CCCCCCCCCCCCCCC	34.77	21406692
13	Methylation	RPTFEPARGGRGKGE CCCCCCCCCCCCCCC	59.83	58857949
16	Methylation	FEPARGGRGKGEGDL CCCCCCCCCCCCCCH	46.61	115368749
18	Acetylation	PARGGRGKGEGDLSQ CCCCCCCCCCCCHHH	53.05	23749302
18	Ubiquitination	PARGGRGKGEGDLSQ CCCCCCCCCCCCHHH	53.05	24816145
24	Phosphorylation	GKGEGDLSQLSKQYS CCCCCCHHHHHHHHH	33.54	21406692
27	Phosphorylation	EGDLSQLSKQYSSRD CCCHHHHHHHHHCCC	15.29	26074081
28	Ubiquitination	GDLSQLSKQYSSRDL CCHHHHHHHHHCCCC	62.94	32015554
28	Acetylation	GDLSQLSKQYSSRDL CCHHHHHHHHHCCCC	62.94	25953088
30	Phosphorylation	LSQLSKQYSSRDLPS HHHHHHHHHCCCCCC	16.61	26074081
31	Phosphorylation	SQLSKQYSSRDLPSH HHHHHHHHCCCCCCC	19.19	25159151
32	Phosphorylation	QLSKQYSSRDLPSHT HHHHHHHCCCCCCCC	25.53	25159151
37	Phosphorylation	YSSRDLPSHTKIKYR HHCCCCCCCCCEEEE	51.60	27251275
40	Acetylation	RDLPSHTKIKYRQTT CCCCCCCCEEEEECC	31.60	25953088
43	Phosphorylation	PSHTKIKYRQTTQDA CCCCCEEEEECCCCC	16.07	23186163
46	Phosphorylation	TKIKYRQTTQDAPEE CCEEEEECCCCCCHH	19.89	23312004
47	Phosphorylation	KIKYRQTTQDAPEEV CEEEEECCCCCCHHH	19.00	27134283
92	Ubiquitination	TSSSVSKKPRLDQIP CCCCCCCCCCHHHCC	28.06	24816145
110	Phosphorylation	LDADDPLTDEEDEDF CCCCCCCCCCCCCCC	46.91	30175587
121	Phosphorylation	DEDFEEESDDDDTAA CCCCCHHCCCHHHHH	50.01	30175587
126	Phosphorylation	EESDDDDTAALLAEL HHCCCHHHHHHHHHH	22.33	20363803
160	Sulfoxidation	AEEERIRMENILSGN HHHHHHHHHHHHCCC	4.26	21406390
173	Phosphorylation	GNPLLNLTGPSQPQA CCCCCCCCCCCCCCC	46.07	28450419
176	Phosphorylation	LLNLTGPSQPQANFK CCCCCCCCCCCCCCE	56.70	28450419
183	Methylation	SQPQANFKVKRRWDD CCCCCCCEECCCCCC	46.80	115971253
185	Methylation	PQANFKVKRRWDDDV CCCCCEECCCCCCCC	36.51	115971261
195	Acetylation	WDDDVVFKNCAKGVD CCCCCEECCCCCCCC	39.24	26051181
214	Phosphorylation	DKRFVNDTLRSEFHK CHHHHHHHHHHHHHH	20.90	17192257
226	Acetylation	FHKKFMEKYIK---- HHHHHHHHHHC----	40.25	25953088

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 CWC15_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CWC15_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 CWC15_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PRP19_HUMAN	PRPF19	physical	20176811
CDC5L_HUMAN	CDC5L	physical	20176811
HSP7C_HUMAN	HSPA8	physical	20176811
CTBL1_HUMAN	CTNNBL1	physical	20176811
PLRG1_HUMAN	PLRG1	physical	20176811
SPF27_HUMAN	BCAS2	physical	20176811
A4_HUMAN	APP	physical	21832049
SF3B4_HUMAN	SF3B4	physical	22939629
SF3B5_HUMAN	SF3B5	physical	22939629
SPF45_HUMAN	RBM17	physical	22365833
CTBL1_HUMAN	CTNNBL1	physical	22365833
SGCE_HUMAN	SGCE	physical	21988832
SIR1_HUMAN	SIRT1	physical	26186194
CTBL1_HUMAN	CTNNBL1	physical	26186194
SIR5_HUMAN	SIRT5	physical	26186194
CTBL1_HUMAN	CTNNBL1	physical	28514442
SIR5_HUMAN	SIRT5	physical	28514442
SIR1_HUMAN	SIRT1	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 CWC15_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 THR-110 AND SER-121, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"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 THR-110 AND SER-121, ANDMASS SPECTROMETRY.	17081983 [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 THR-214, AND MASSSPECTROMETRY.	18691976 [Abstract]