ABC3B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ABC3B_HUMAN
• UniProt AC: Q9UH17
• Protein Name: DNA dC->dU-editing enzyme APOBEC-3B
• Gene Name: APOBEC3B
• Organism: Homo sapiens (Human).
• Sequence Length: 382
• Subcellular Localization: Nucleus .
• 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) and human T-cell leukemia virus type 1 (HTLV-1) and may inhibit the mobility of LTR and non-LTR retrotransposons..
• Protein Sequence: MNPQIRNPMERMYRDTFYDNFENEPILYGRSYTWLCYEVKIKRGRSNLLWDTGVFRGQVYFKPQYHAEMCFLSWFCGNQLPAYKCFQITWFVSWTPCPDCVAKLAEFLSEHPNVTLTISAARLYYYWERDYRRALCRLSQAGARVTIMDYEEFAYCWENFVYNEGQQFMPWYKFDENYAFLHRTLKEILRYLMDPDTFTFNFNNDPLVLRRRQTYLCYEVERLDNGTWVLMDQHMGFLCNEAKNLLCGFYGRHAELRFLDLVPSLQLDPAQIYRVTWFISWSPCFSWGCAGEVRAFLQENTHVRLRIFAARIYDYDPLYKEALQMLRDAGAQVSIMTYDEFEYCWDTFVYRQGCPFQPWDGLEEHSQALSGRLRAILQNQGN

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
13	Phosphorylation	RNPMERMYRDTFYDN CCHHHHHHCHHCHHC	16.14	25219547
46	Phosphorylation	VKIKRGRSNLLWDTG EEECCCCCCEEEECC	34.35	20068231
137	Methylation	DYRRALCRLSQAGAR HHHHHHHHHHHCCCE	37.92	-
139	Phosphorylation	RRALCRLSQAGARVT HHHHHHHHHCCCEEE	9.91	29457462
178	Phosphorylation	WYKFDENYAFLHRTL CEECCCCHHHHHHHH	9.18	-
191	Phosphorylation	TLKEILRYLMDPDTF HHHHHHHHHCCCCCE	11.70	-
234 (in isoform 2)	Phosphorylation	-	17.67	22210691
243	Ubiquitination	GFLCNEAKNLLCGFY HHHCHHHHHHHCCHH	41.78	-
295	Ubiquitination	GCAGEVRAFLQENTH CCHHHHHHHHHCCCC	18.06	23000965
313	Phosphorylation	RIFAARIYDYDPLYK EEEEEEECCCCHHHH	11.69	-
315	Phosphorylation	FAARIYDYDPLYKEA EEEEECCCCHHHHHH	11.50	-
319	Phosphorylation	IYDYDPLYKEALQML ECCCCHHHHHHHHHH	16.51	-
320	Ubiquitination	YDYDPLYKEALQMLR CCCCHHHHHHHHHHH	44.16	23000965
320 (in isoform 1)	Ubiquitination	-	44.16	21906983
334	Phosphorylation	RDAGAQVSIMTYDEF HHCCCCEEEEEHHHC	8.44	-

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

Oops, there are no upstream regulatory protein records of ABC3B_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ABC3B_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 ABC3B_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of ABC3B_HUMAN !!

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.