ABC3H_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ABC3H_HUMAN
• UniProt AC: Q6NTF7
• Protein Name: DNA dC->dU-editing enzyme APOBEC-3H
• Gene Name: APOBEC3H
• Organism: Homo sapiens (Human).
• Sequence Length: 200
• Subcellular Localization: Nucleus. Cytoplasm. Cytoplasm, P-body. Haplotype 1 is distributed in both the nucleus and cytoplasm, whereas haplotype 2 is predominantly cytoplasmic.
• Protein Description: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. The A3H-var/haplotype 2 exhibits antiviral activity against vif-deficient HIV-1. 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 also against T-cell leukemia virus type 1 (HTLV-1) and may inhibit the mobility of LTR and non-LTR retrotransposons..
• Protein Sequence: MALLTAETFRLQFNNKRRLRRPYYPRKALLCYQLTPQNGSTPTRGYFENKKKCHAEICFINEIKSMGLDETQCYQVTCYLTWSPCSSCAWELVDFIKAHDHLNLGIFASRLYYHWCKPQQKGLRLLCGSQVPVEVMGFPKFADCWENFVDHEKPLSFNPYKMLEELDKNSRAIKRRLERIKIPGVRAQGRYMDILCDAEV

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
32	Phosphorylation	PRKALLCYQLTPQNG CCCEEEEEECCCCCC	13.41	29978859
35	Phosphorylation	ALLCYQLTPQNGSTP EEEEEECCCCCCCCC	13.80	29978859
40	Phosphorylation	QLTPQNGSTPTRGYF ECCCCCCCCCCCCCC	38.47	29978859
41	Phosphorylation	LTPQNGSTPTRGYFE CCCCCCCCCCCCCCC	30.03	29978859
43	Phosphorylation	PQNGSTPTRGYFENK CCCCCCCCCCCCCCC	36.49	29978859
46	Phosphorylation	GSTPTRGYFENKKKC CCCCCCCCCCCCCCC	12.39	29978859
156	Phosphorylation	VDHEKPLSFNPYKML CCCCCCCCCCHHHHH	31.35	29449344
160	Phosphorylation	KPLSFNPYKMLEELD CCCCCCHHHHHHHHH	15.33	29449344
170	Phosphorylation	LEELDKNSRAIKRRL HHHHHHCCHHHHHHH	28.91	29083192

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

Oops, there are no upstream regulatory protein records of ABC3H_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ABC3H_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 ABC3H_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of ABC3H_HUMAN !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.