ABC3C_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ABC3C_HUMAN
• UniProt AC: Q9NRW3
• Protein Name: DNA dC->dU-editing enzyme APOBEC-3C
• Gene Name: APOBEC3C
• Organism: Homo sapiens (Human).
• Sequence Length: 190
• Subcellular Localization: Nucleus. Cytoplasm.
• Protein Description: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single-or double-stranded RNA. Exhibits antiviral activity against simian immunodeficiency virus (SIV), hepatitis B virus (HBV), herpes simplex virus 1 (HHV-1) and Epstein-Barr virus (EBV) and may inhibit the mobility of LTR and non-LTR retrotransposons. May also play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation..
• Protein Sequence: MNPQIRNPMKAMYPGTFYFQFKNLWEANDRNETWLCFTVEGIKRRSVVSWKTGVFRNQVDSETHCHAERCFLSWFCDDILSPNTKYQVTWYTSWSPCPDCAGEVAEFLARHSNVNLTIFTARLYYFQYPCYQEGLRSLSQEGVAVEIMDYEDFKYCWENFVYNDNEPFKPWKGLKTNFRLLKRRLRESLQ

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
10	Ubiquitination	PQIRNPMKAMYPGTF CCCCCCHHHCCCCEE	31.12	21890473
46	Phosphorylation	VEGIKRRSVVSWKTG EECCCCCEEEEECCC	30.79	28555341
49	Phosphorylation	IKRRSVVSWKTGVFR CCCCEEEEECCCCCC	22.24	21857030
51	Ubiquitination	RRSVVSWKTGVFRNQ CCEEEEECCCCCCCC	28.09	21890473
51	Malonylation	RRSVVSWKTGVFRNQ CCEEEEECCCCCCCC	28.09	26320211
112	Phosphorylation	AEFLARHSNVNLTIF HHHHHHCCCCEEEEE	36.60	30108239
117	Phosphorylation	RHSNVNLTIFTARLY HCCCCEEEEEEEEEH	14.61	30108239
162	Phosphorylation	YCWENFVYNDNEPFK HHHHHCCCCCCCCCC	16.80	23917254
169	Ubiquitination	YNDNEPFKPWKGLKT CCCCCCCCCCCCHHH	61.76	29967540
175	Ubiquitination	FKPWKGLKTNFRLLK CCCCCCHHHHHHHHH	50.52	29967540
175	Malonylation	FKPWKGLKTNFRLLK CCCCCCHHHHHHHHH	50.52	26320211
175	Acetylation	FKPWKGLKTNFRLLK CCCCCCHHHHHHHHH	50.52	26822725

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
-	K	Ubiquitination	E3 ubiquitin ligase	vif	P69720	PMID:22199232

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ABC3C_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 ABC3C_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
VIF_HV1B1	vif	physical	18419775
VIF_HV1BR	vif	physical	18419775
VIF_HV1H2	vif	physical	18419775
TRAF3_HUMAN	TRAF3	physical	21988832
RBY1F_HUMAN	RBMY1F	physical	25416956

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.