CC124_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CC124_HUMAN
• UniProt AC: Q96CT7
• Protein Name: Coiled-coil domain-containing protein 124
• Gene Name: CCDC124
• Organism: Homo sapiens (Human).
• Sequence Length: 223
• Subcellular Localization: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Midbody . Colocalizes with gamma-tubulin at interphase, prophase, metaphase, and anaphase. Relocates from centrosome to midbody at telophase.
• Protein Description: Required for proper progression of late cytokinetic stages..
• Protein Sequence: MPKKFQGENTKSAAARARRAEAKAAADAKKQKELEDAYWKDDDKHVMRKEQRKEEKEKRRLDQLERKKETQRLLEEEDSKLKGGKAPRVATSSKVTRAQIEDTLRRDHQLREAPDTAEKAKSHLEVPLEENVNRRVLEEGSVEARTIEDAIAVLSVAEEAADRHPERRMRAAFTAFEEAQLPRLKQENPNMRLSQLKQLLKKEWLRSPDNPMNQRAVPFNAPK

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
11	Acetylation	KFQGENTKSAAARAR CCCCCCHHHHHHHHH	50.07	25953088
11	Ubiquitination	KFQGENTKSAAARAR CCCCCCHHHHHHHHH	50.07	-
32	Ubiquitination	AADAKKQKELEDAYW HHHHHHHHHHHHHHC	73.48	-
38	Phosphorylation	QKELEDAYWKDDDKH HHHHHHHHCCCCCHH	25.88	25159151
80	Acetylation	LLEEEDSKLKGGKAP HHHHHHHHCCCCCCC	67.55	23954790
85	Acetylation	DSKLKGGKAPRVATS HHHCCCCCCCCEECC	64.98	34677431
91	Phosphorylation	GKAPRVATSSKVTRA CCCCCEECCCCCCHH	30.58	20068231
92	Phosphorylation	KAPRVATSSKVTRAQ CCCCEECCCCCCHHH	20.58	20068231
93	Phosphorylation	APRVATSSKVTRAQI CCCEECCCCCCHHHH	27.13	20068231
94	Ubiquitination	PRVATSSKVTRAQIE CCEECCCCCCHHHHH	47.60	-
96	Phosphorylation	VATSSKVTRAQIEDT EECCCCCCHHHHHHH	24.83	20068231
103	Phosphorylation	TRAQIEDTLRRDHQL CHHHHHHHHHHHHHH	14.90	17287340
105	Methylation	AQIEDTLRRDHQLRE HHHHHHHHHHHHHHH	44.03	-
111	Methylation	LRRDHQLREAPDTAE HHHHHHHHHCCCHHH	31.31	-
116	Phosphorylation	QLREAPDTAEKAKSH HHHHCCCHHHHHHHH	35.34	21815630
122	Phosphorylation	DTAEKAKSHLEVPLE CHHHHHHHHCCCCCH	37.86	20873877
141	Phosphorylation	RRVLEEGSVEARTIE HHHHHCCCEEEEEHH	21.77	29255136
155	Phosphorylation	EDAIAVLSVAEEAAD HHHHHHHHHHHHHHH	16.81	-
163	Methylation	VAEEAADRHPERRMR HHHHHHHHCHHHHHH	42.40	-
185	Ubiquitination	EAQLPRLKQENPNMR HHHHHHHHCCCCCCC	57.77	-
194	Phosphorylation	ENPNMRLSQLKQLLK CCCCCCHHHHHHHHH	24.09	28450419
197	Ubiquitination	NMRLSQLKQLLKKEW CCCHHHHHHHHHHHH	31.12	-
207	Phosphorylation	LKKEWLRSPDNPMNQ HHHHHHCCCCCCCCC	34.14	21815630

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

Oops, there are no upstream regulatory protein records of CC124_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CC124_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 CC124_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
APEX1_HUMAN	APEX1	physical	22863883
RED1_HUMAN	ADARB1	physical	24778252
PRKRA_HUMAN	PRKRA	physical	24778252

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

"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 SER-92 AND THR-103, AND MASSSPECTROMETRY.
PubMed: 17287340