A1CF_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: A1CF_HUMAN
• UniProt AC: Q9NQ94
• Protein Name: APOBEC1 complementation factor
• Gene Name: A1CF
• Organism: Homo sapiens (Human).
• Sequence Length: 594
• Subcellular Localization: Nucleus . Endoplasmic reticulum. Cytoplasm . Predominantly nuclear where it localizes to heterochromatin. Also cytoplasmic where it is found at the outer surface of the endoplasmic reticulum (By similarity). Shuttles between the nucleus and cytoplasm
• Protein Description: Essential component of the apolipoprotein B mRNA editing enzyme complex which is responsible for the postranscriptional editing of a CAA codon for Gln to a UAA codon for stop in APOB mRNA. Binds to APOB mRNA and is probably responsible for docking the catalytic subunit, APOBEC1, to the mRNA to allow it to deaminate its target cytosine. The complex also protects the edited APOB mRNA from nonsense-mediated decay..
• Protein Sequence: MESNHKSGDGLSGTQKEAALRALVQRTGYSLVQENGQRKYGGPPPGWDAAPPERGCEIFIGKLPRDLFEDELIPLCEKIGKIYEMRMMMDFNGNNRGYAFVTFSNKVEAKNAIKQLNNYEIRNGRLLGVCASVDNCRLFVGGIPKTKKREEILSEMKKVTEGVVDVIVYPSAADKTKNRGFAFVEYESHRAAAMARRKLLPGRIQLWGHGIAVDWAEPEVEVDEDTMSSVKILYVRNLMLSTSEEMIEKEFNNIKPGAVERVKKIRDYAFVHFSNREDAVEAMKALNGKVLDGSPIEVTLAKPVDKDSYVRYTRGTGGRGTMLQGEYTYSLGQVYDPTTTYLGAPVFYAPQTYAAIPSLHFPATKGHLSNRAIIRAPSVREIYMNVPVGAAGVRGLGGRGYLAYTGLGRGYQVKGDKREDKLYDILPGMELTPMNPVTLKPQGIKLAPQILEEICQKNNWGQPVYQLHSAIGQDQRQLFLYKITIPALASQNPAIHPFTPPKLSAFVDEAKTYAAEYTLQTLGIPTDGGDGTMATAAAAATAFPGYAVPNATAPVSAAQLKQAVTLGQDLAAYTTYEVYPTFAVTARGDGYGTF

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
7	Phosphorylation	-MESNHKSGDGLSGT -CCCCCCCCCCCCHH	34.27	22798277
12	Phosphorylation	HKSGDGLSGTQKEAA CCCCCCCCHHHHHHH	45.37	22985185
14	Phosphorylation	SGDGLSGTQKEAALR CCCCCCHHHHHHHHH	32.85	24275569
40	Phosphorylation	QENGQRKYGGPPPGW HHCCCCCCCCCCCCC	29.51	-
119	Phosphorylation	AIKQLNNYEIRNGRL HHHHHHCCEECCCEE	16.20	29978859
186	Phosphorylation	RGFAFVEYESHRAAA CCEEEEEEHHHHHHH	19.89	-
313	Phosphorylation	KDSYVRYTRGTGGRG CCCEEEEECCCCCCC	16.44	46157579
401	Phosphorylation	RGLGGRGYLAYTGLG CCCCCCCCEEECCCC	6.18	22817900
404	Phosphorylation	GGRGYLAYTGLGRGY CCCCCEEECCCCCCE	9.95	22817900
411	Phosphorylation	YTGLGRGYQVKGDKR ECCCCCCEEEECCCC	14.58	2029481
423	Phosphorylation	DKREDKLYDILPGME CCCCCCCCCCCCCCC	13.48	20563455
499	Phosphorylation	NPAIHPFTPPKLSAF CCCCCCCCCCCHHHH	43.03	10781591
504	Phosphorylation	PFTPPKLSAFVDEAK CCCCCCHHHHHHHHH	26.28	46157573
512	Phosphorylation	AFVDEAKTYAAEYTL HHHHHHHHHHHHEEH	25.99	46157585
546	Phosphorylation	AATAFPGYAVPNATA HHHHCCCCCCCCCCC	12.50	46157597
552	Phosphorylation	GYAVPNATAPVSAAQ CCCCCCCCCCCCHHH	37.83	46157591

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

Oops, there are no upstream regulatory protein records of A1CF_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of A1CF_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 A1CF_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FUBP2_HUMAN	KHSRP	physical	10781591
HNRPQ_HUMAN	SYNCRIP	physical	11134005
ABEC1_HUMAN	APOBEC1	physical	11134005
ABEC1_HUMAN	APOBEC1	physical	10669759
PSMG2_HUMAN	PSMG2	physical	28514442
PSMG3_HUMAN	PSMG3	physical	28514442

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.