dbPTM

CL045_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CL045_HUMAN
UniProt AC	Q8N5I9
Protein Name	Uncharacterized protein C12orf45
Gene Name	C12orf45
Organism	Homo sapiens (Human).
Sequence Length	185
Subcellular Localization
Protein Description
Protein Sequence	MEVHGKPKASPSCSSPTRDSSGVPVSKELLTAGSDGRGGIWDRLLINSQPKSRKTSTLQTVRIERSPLLDQVQTFLPQMARANEKLRKEMAAAPPGRFNIENIDGPHSKVIQMDVALFEMNQSDSKEVDSSEESSQDSSENSSESEDEDDSIPSEVTIDNIKLPNSEGGKGKIEVLDSPASKKKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Acetylation	--MEVHGKPKASPSC --CCCCCCCCCCCCC	28.59	23749302
10	Phosphorylation	VHGKPKASPSCSSPT CCCCCCCCCCCCCCC	24.38	23927012
12	Phosphorylation	GKPKASPSCSSPTRD CCCCCCCCCCCCCCC	24.92	23927012
14	Phosphorylation	PKASPSCSSPTRDSS CCCCCCCCCCCCCCC	43.63	23401153
15	Phosphorylation	KASPSCSSPTRDSSG CCCCCCCCCCCCCCC	34.32	23401153
17	Phosphorylation	SPSCSSPTRDSSGVP CCCCCCCCCCCCCCC	49.40	29255136
20	Phosphorylation	CSSPTRDSSGVPVSK CCCCCCCCCCCCCCH	26.21	23927012
21	Phosphorylation	SSPTRDSSGVPVSKE CCCCCCCCCCCCCHH	48.36	23927012
26	Phosphorylation	DSSGVPVSKELLTAG CCCCCCCCHHHHCCC	17.84	23927012
27	Ubiquitination	SSGVPVSKELLTAGS CCCCCCCHHHHCCCC	53.25	29967540
31	Phosphorylation	PVSKELLTAGSDGRG CCCHHHHCCCCCCCC	41.41	25627689
34	Phosphorylation	KELLTAGSDGRGGIW HHHHCCCCCCCCCCH	34.13	21815630
37	Methylation	LTAGSDGRGGIWDRL HCCCCCCCCCCHHHH	45.19	-
48	Phosphorylation	WDRLLINSQPKSRKT HHHHHCCCCCCCCCC	40.65	25159151
51	Ubiquitination	LLINSQPKSRKTSTL HHCCCCCCCCCCCCC	56.08	24816145
54	Ubiquitination	NSQPKSRKTSTLQTV CCCCCCCCCCCCEEE	54.65	24816145
55	Phosphorylation	SQPKSRKTSTLQTVR CCCCCCCCCCCEEEE	26.32	23312004
56	Phosphorylation	QPKSRKTSTLQTVRI CCCCCCCCCCEEEEE	30.10	28857561
57	Phosphorylation	PKSRKTSTLQTVRIE CCCCCCCCCEEEEEE	28.28	23312004
60	Phosphorylation	RKTSTLQTVRIERSP CCCCCCEEEEEECCH	18.18	23312004
66	Phosphorylation	QTVRIERSPLLDQVQ EEEEEECCHHHHHHH	13.70	25159151
79	Sulfoxidation	VQTFLPQMARANEKL HHHHHHHHHHHHHHH	2.29	21406390
88	Ubiquitination	RANEKLRKEMAAAPP HHHHHHHHHHHCCCC	63.38	29967540
123	Phosphorylation	ALFEMNQSDSKEVDS EEEECCCCCCCCCCC	38.56	28348404
125	Phosphorylation	FEMNQSDSKEVDSSE EECCCCCCCCCCCCH	35.64	28102081
134	Phosphorylation	EVDSSEESSQDSSEN CCCCCHHHCCCCCCC	29.28	-
135	Phosphorylation	VDSSEESSQDSSENS CCCCHHHCCCCCCCC	41.09	-
162	Ubiquitination	EVTIDNIKLPNSEGG EEEEEEEECCCCCCC	65.23	-
172	Ubiquitination	NSEGGKGKIEVLDSP CCCCCCCCEEECCCC	38.90	-
178	Phosphorylation	GKIEVLDSPASKKKK CCEEECCCCHHHCCC	20.43	19664994
181	Phosphorylation	EVLDSPASKKKK--- EECCCCHHHCCC---	48.68	30266825

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 CL045_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CL045_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 CL045_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
TBC23_HUMAN	TBC1D23	physical	21988832
PR38A_HUMAN	PRPF38A	physical	27173435

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 CL045_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-178, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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-178, AND MASSSPECTROMETRY.	19413330 [Abstract]
"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-34; SER-48; SER-66 ANDSER-178, AND MASS SPECTROMETRY.	18669648 [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-66, AND MASSSPECTROMETRY.	18220336 [Abstract]