CCD58_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CCD58_HUMAN
• UniProt AC: Q4VC31
• Protein Name: Coiled-coil domain-containing protein 58
• Gene Name: CCDC58
• Organism: Homo sapiens (Human).
• Sequence Length: 144
• Protein Sequence: MAAPSGGVNCEEFAEFQELLKVMRTIDDRIVHELNTTVPTASFAGKIDASQTCKQLYESLMAAHASRDRVIKNCIAQTSAVVKNLREEREKNLDDLTLLKQLRKEQTKLKWMQSELNVEEVVNDRSWKVFNERCRIHFKPPKNE

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
46	Acetylation	PTASFAGKIDASQTC CCHHHCCCCCHHHHH	33.70	25953088
54	Acetylation	IDASQTCKQLYESLM CCHHHHHHHHHHHHH	46.88	25953088
72	Acetylation	ASRDRVIKNCIAQTS HCHHHHHHHHHHHHH	42.80	26051181
74	Glutathionylation	RDRVIKNCIAQTSAV HHHHHHHHHHHHHHH	2.01	22555962
128	Acetylation	VVNDRSWKVFNERCR HHCCCCHHHHHHCCC	37.89	26051181

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

Oops, there are no upstream regulatory protein records of CCD58_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CCD58_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 CCD58_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PCBP2_HUMAN	PCBP2	physical	26344197
PIPNA_HUMAN	PITPNA	physical	26344197
STABP_HUMAN	STAMBP	physical	26344197
CCD58_HUMAN	CCDC58	physical	27499296
TIM14_HUMAN	DNAJC19	physical	27499296
AFG32_HUMAN	AFG3L2	physical	27499296
FMT_HUMAN	MTFMT	physical	27499296
TIM16_HUMAN	PAM16	physical	27499296
CYC_HUMAN	CYCS	physical	27499296
ECH1_HUMAN	ECH1	physical	27499296

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

Acetylation

"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.
PubMed: 19413330

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-83 AND LYS-100, AND MASSSPECTROMETRY.
PubMed: 19608861