dbPTM

CC033_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CC033_HUMAN
UniProt AC	Q6P1S2
Protein Name	Protein C3orf33
Gene Name	C3orf33
Organism	Homo sapiens (Human).
Sequence Length	294
Subcellular Localization	Isoform 1: Membrane Single-pass membrane protein . Isoform 2: Secreted .
Protein Description	Isoform 2: Secreted protein may play a role in transcription regulation via the MAPK3/MAPK1 pathway through an unidentified receptor on the plasma membrane..
Protein Sequence	MAGQPAATGSPSADKDGMEPNVVARISQWADDHLRLVRNISTGMAIAGIMLLLRSIRLTSKFTSSSDIPVEFIRRNVKLRGRLRRITENGLEIEHIPITLPIIASLRKEPRGALLVKLAGVELAETGKAWLQKELKPSQLLWFQLLGKENSALFCYLLVSKGGYFSVNLNEEILRRGLGKTVLVKGLKYDSKIYWTVHRNLLKAELTALKKGEGIWKEDSEKESYLEKFKDSWREIWKKDSFLKTTGSDFSLKKESYYEKLKRTYEIWKDNMNNCSLILKFRELISRINFRRKG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAGQPAATG ------CCCCCCCCC	25.90	19413330
10	Phosphorylation	GQPAATGSPSADKDG CCCCCCCCCCCCCCC	16.01	24114839
12	Phosphorylation	PAATGSPSADKDGME CCCCCCCCCCCCCCC	51.28	24114839
41	Phosphorylation	LRLVRNISTGMAIAG HHHHHHHHHHHHHHH	23.58	24667141
42	Phosphorylation	RLVRNISTGMAIAGI HHHHHHHHHHHHHHH	27.46	23403867
65	Phosphorylation	LTSKFTSSSDIPVEF HHCCCCCCCCCCHHH	29.04	27135362
66	Phosphorylation	TSKFTSSSDIPVEFI HCCCCCCCCCCHHHH	39.05	27135362
87	Phosphorylation	RGRLRRITENGLEIE HHHHHHHHCCCEEEE	22.91	-
105	Phosphorylation	ITLPIIASLRKEPRG EEHHHHHHHCCCCCC	20.49	-
126	Phosphorylation	AGVELAETGKAWLQK HCCCHHHHCHHHHHH	38.07	-
151	Phosphorylation	QLLGKENSALFCYLL HHHCCCCCCHHHHHH	27.69	23663014
156	Phosphorylation	ENSALFCYLLVSKGG CCCCHHHHHHHCCCC	8.85	23663014
160	Phosphorylation	LFCYLLVSKGGYFSV HHHHHHHCCCCEEEE	26.08	23663014
164	Phosphorylation	LLVSKGGYFSVNLNE HHHCCCCEEEEECCH	11.01	-
166	Phosphorylation	VSKGGYFSVNLNEEI HCCCCEEEEECCHHH	11.12	-
185	Methylation	LGKTVLVKGLKYDSK CCCEEEECCCCCCCE	55.13	-
185	"N6,N6-dimethyllysine"	LGKTVLVKGLKYDSK CCCEEEECCCCCCCE	55.13	-
189	Phosphorylation	VLVKGLKYDSKIYWT EEECCCCCCCEEEEE	30.41	-
213	Phosphorylation	LTALKKGEGIWKEDS HHHHHCCCCCCCCCC	57.28	24719451
214	Phosphorylation	TALKKGEGIWKEDSE HHHHCCCCCCCCCCH	39.46	24719451
237	Ubiquitination	KDSWREIWKKDSFLK HHHHHHHHHHCCCCH	9.26	33845483
241	Phosphorylation	REIWKKDSFLKTTGS HHHHHHCCCCHHCCC	41.16	24719451
243	Phosphorylation	IWKKDSFLKTTGSDF HHHHCCCCHHCCCCC	5.80	24719451
248	Phosphorylation	SFLKTTGSDFSLKKE CCCHHCCCCCCCCHH	33.13	-
253	2-Hydroxyisobutyrylation	TGSDFSLKKESYYEK CCCCCCCCHHHHHHH	53.98	-
256	Phosphorylation	DFSLKKESYYEKLKR CCCCCHHHHHHHHHH	41.72	24719451
257	Phosphorylation	FSLKKESYYEKLKRT CCCCHHHHHHHHHHH	19.41	24719451
276	Phosphorylation	KDNMNNCSLILKFRE HHHCCCCHHHHHHHH	22.14	27732954
280	Acetylation	NNCSLILKFRELISR CCCHHHHHHHHHHHH	35.07	20167786
286	Phosphorylation	LKFRELISRINFRRK HHHHHHHHHHCCCCC	39.47	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 CC033_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CC033_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 CC033_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
A4_HUMAN	APP	physical	21832049

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 CC033_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]