CCD43_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CCD43_HUMAN
• UniProt AC: Q96MW1
• Protein Name: Coiled-coil domain-containing protein 43
• Gene Name: CCDC43
• Organism: Homo sapiens (Human).
• Sequence Length: 224
• Protein Sequence: MAAPSEVAAIAPGEGDGGGGGFGSWLDGRLEALGVDRAVYGAYILGILQEEEEEEKLDALQGILSAFLEEDSLLNICKEIVERWSETQNVVTKVKKEDEVQAIATLIEKQAQIVVKPRMVSEEEKQRKAALLAQYADVTDEEDEADEKDDSGATTMNIGSDKLLFRNTNVEDVLNARKLERDSLRDESQRKKEQDKLQRERDKLAKQERKEKEKKRTQRGERKR

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
93	Ubiquitination	ETQNVVTKVKKEDEV HHHCHHHCCCHHHHH	40.21	29967540
95	Sumoylation	QNVVTKVKKEDEVQA HCHHHCCCHHHHHHH	52.59	25114211
105	Phosphorylation	DEVQAIATLIEKQAQ HHHHHHHHHHHHHHH	23.35	28060719
109	Ubiquitination	AIATLIEKQAQIVVK HHHHHHHHHHHHHCC	43.89	29967540
116	Acetylation	KQAQIVVKPRMVSEE HHHHHHCCCCCCCHH	18.93	25953088
116	Ubiquitination	KQAQIVVKPRMVSEE HHHHHHCCCCCCCHH	18.93	32015554
121	Phosphorylation	VVKPRMVSEEEKQRK HCCCCCCCHHHHHHH	29.92	30624053
128	Ubiquitination	SEEEKQRKAALLAQY CHHHHHHHHHHHHHH	35.20	29967540
135	Phosphorylation	KAALLAQYADVTDEE HHHHHHHHCCCCCCC	10.12	30266825
139 (in isoform 2)	Phosphorylation	-	37.94	28348404
139	Phosphorylation	LAQYADVTDEEDEAD HHHHCCCCCCCCCCC	37.94	19664994
144	Phosphorylation	DVTDEEDEADEKDDS CCCCCCCCCCCCCCC	62.39	-
144 (in isoform 2)	Phosphorylation	-	62.39	-
151	Phosphorylation	EADEKDDSGATTMNI CCCCCCCCCCCEEEE	40.22	30266825
154	Phosphorylation	EKDDSGATTMNIGSD CCCCCCCCEEEECCC	30.06	30266825
155	Phosphorylation	KDDSGATTMNIGSDK CCCCCCCEEEECCCE	14.00	30266825
160	Phosphorylation	ATTMNIGSDKLLFRN CCEEEECCCEEEECC	27.98	23927012
162	Ubiquitination	TMNIGSDKLLFRNTN EEEECCCEEEECCCC	49.11	23000965
168	Phosphorylation	DKLLFRNTNVEDVLN CEEEECCCCHHHHHH	36.06	28555341
183	Phosphorylation	ARKLERDSLRDESQR HHHHHHHHHCCHHHH	31.37	29214152
188	Phosphorylation	RDSLRDESQRKKEQD HHHHCCHHHHHHHHH	39.30	23401153
192	Ubiquitination	RDESQRKKEQDKLQR CCHHHHHHHHHHHHH	63.90	24816145
203	Ubiquitination	KLQRERDKLAKQERK HHHHHHHHHHHHHHH	57.47	24816145
217	Phosphorylation	KEKEKKRTQRGERKR HHHHHHHHHHHHCCC	31.34	-

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

Oops, there are no upstream regulatory protein records of CCD43_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CCD43_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 CCD43_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GOPC_HUMAN	GOPC	physical	26186194
SCML1_HUMAN	SCML1	physical	26186194
PNKP_HUMAN	PNKP	physical	26186194
SCML1_HUMAN	SCML1	physical	28514442
PNKP_HUMAN	PNKP	physical	28514442
GOPC_HUMAN	GOPC	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

"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 THR-139, 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 THR-139, AND MASSSPECTROMETRY.
PubMed: 19413330

"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-139, AND MASSSPECTROMETRY.
PubMed: 17287340