dbPTM

ARF6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ARF6_HUMAN
UniProt AC	P62330
Protein Name	ADP-ribosylation factor 6
Gene Name	ARF6 {ECO:0000312\|HGNC:HGNC:659}
Organism	Homo sapiens (Human).
Sequence Length	175
Subcellular Localization	Cytoplasm, cytosol . Cell membrane Lipid-anchor . Endosome membrane Lipid-anchor. Recycling endosome membrane Lipid-anchor . Cell projection, filopodium membrane Lipid-anchor. Cell projection, ruffle . Cleavage furrow . Midbody, Midbody ring . Golg
Protein Description	GTP-binding protein involved in protein trafficking that regulates endocytic recycling and cytoskeleton remodeling. [PubMed: 11266366]
Protein Sequence	MGKVLSKIFGNKEMRILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNVETVTYKNVKFNVWDVGGQDKIRPLWRHYYTGTQGLIFVVDCADRDRIDEARQELHRIINDREMRDAIILIFANKQDLPDAMKPHEIQEKLGLTRIRDRNWYVQPSCATSGDGLYEGLTWLTSNYKS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	N-myristoyl glycine	------MGKVLSKIF ------CCCHHHHHH	28.87	-
2	Myristoylation	------MGKVLSKIF ------CCCHHHHHH	28.87	7589240
3	Ubiquitination	-----MGKVLSKIFG -----CCCHHHHHHC	38.41	23000965
7	Ubiquitination	-MGKVLSKIFGNKEM -CCCHHHHHHCCHHH	37.58	23000965
12	Ubiquitination	LSKIFGNKEMRILML HHHHHCCHHHEEEEE	53.95	23000965
27	Phosphorylation	GLDAAGKTTILYKLK EECCCCCEEEEEEEE	20.39	20068231
28	Phosphorylation	LDAAGKTTILYKLKL ECCCCCEEEEEEEEC	16.69	20068231
31	Phosphorylation	AGKTTILYKLKLGQS CCCEEEEEEEECCCC	15.49	20068231
32	Acetylation	GKTTILYKLKLGQSV CCEEEEEEEECCCCE	35.38	22647651
32	Ubiquitination	GKTTILYKLKLGQSV CCEEEEEEEECCCCE	35.38	21963094
34	Ubiquitination	TTILYKLKLGQSVTT EEEEEEEECCCCEEE	46.55	32015554
38	Phosphorylation	YKLKLGQSVTTIPTV EEEECCCCEEECCCC	21.45	26657352
40	Phosphorylation	LKLGQSVTTIPTVGF EECCCCEEECCCCCE	25.01	28060719
41	Phosphorylation	KLGQSVTTIPTVGFN ECCCCEEECCCCCEE	23.85	27050516
44	O-linked_Glycosylation	QSVTTIPTVGFNVET CCEEECCCCCEEEEE	29.43	OGP
51	Phosphorylation	TVGFNVETVTYKNVK CCCEEEEEEEEECEE	17.54	20068231
53	Phosphorylation	GFNVETVTYKNVKFN CEEEEEEEEECEEEE	35.88	20068231
54	Phosphorylation	FNVETVTYKNVKFNV EEEEEEEEECEEEEE	9.02	20068231
55	Ubiquitination	NVETVTYKNVKFNVW EEEEEEEECEEEEEE	45.99	23000965
58	Ubiquitination	TVTYKNVKFNVWDVG EEEEECEEEEEEECC	40.38	23000965
58	Ubiquitination	TVTYKNVKFNVWDVG EEEEECEEEEEEECC	40.38	21890473
69	Ubiquitination	WDVGGQDKIRPLWRH EECCCCCCCCCCCHH	32.50	23000965
69	Ubiquitination	WDVGGQDKIRPLWRH EECCCCCCCCCCCHH	32.50	21890473
69	Sumoylation	WDVGGQDKIRPLWRH EECCCCCCCCCCCHH	32.50	-
77	Phosphorylation	IRPLWRHYYTGTQGL CCCCCHHCCCCCCEE	8.31	28152594
78	Phosphorylation	RPLWRHYYTGTQGLI CCCCHHCCCCCCEEE	7.80	28152594
79	Phosphorylation	PLWRHYYTGTQGLIF CCCHHCCCCCCEEEE	26.96	28152594
81	Phosphorylation	WRHYYTGTQGLIFVV CHHCCCCCCEEEEEE	16.21	28152594
131	Ubiquitination	QDLPDAMKPHEIQEK CCCCCCCCHHHHHHH	44.97	33845483
138	Ubiquitination	KPHEIQEKLGLTRIR CHHHHHHHHCCCCCC	31.32	23000965
150	Phosphorylation	RIRDRNWYVQPSCAT CCCCCCEEECCCCCC	7.86	24043423
154	Phosphorylation	RNWYVQPSCATSGDG CCEEECCCCCCCCCC	10.17	24043423
157	Phosphorylation	YVQPSCATSGDGLYE EECCCCCCCCCCHHH	37.25	24043423
158	Phosphorylation	VQPSCATSGDGLYEG ECCCCCCCCCCHHHC	19.16	24043423
163	Phosphorylation	ATSGDGLYEGLTWLT CCCCCCHHHCHHHHH	17.30	22817900
167	Phosphorylation	DGLYEGLTWLTSNYK CCHHHCHHHHHHCCC	29.32	24043423
170	Phosphorylation	YEGLTWLTSNYKS-- HHCHHHHHHCCCC--	13.39	24043423
171	Phosphorylation	EGLTWLTSNYKS--- HCHHHHHHCCCC---	35.67	24043423
173	Phosphorylation	LTWLTSNYKS----- HHHHHHCCCC-----	16.63	24043423
174	Ubiquitination	TWLTSNYKS------ HHHHHCCCC------	54.67	21963094

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	FBXO8	Q9NRD0	PMID:18094045

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ARF6_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of ARF6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LPPRC_HUMAN	LRPPRC	physical	17353931
IQGA1_HUMAN	IQGAP1	physical	17353931
DYHC1_HUMAN	DYNC1H1	physical	17353931
ECM29_HUMAN	KIAA0368	physical	17353931
SYYC_HUMAN	YARS	physical	17353931
EPIPL_HUMAN	EPPK1	physical	17353931
DHYS_HUMAN	DHPS	physical	17353931
PABP4_HUMAN	PABPC4	physical	17353931
PUR2_HUMAN	GART	physical	17353931
IF6_HUMAN	EIF6	physical	17353931
EXOC5_HUMAN	EXOC5	physical	14662749
PI51C_HUMAN	PIP5K1C	physical	12847086
ACM3_HUMAN	CHRM3	physical	12799371
ARFP2_HUMAN	ARFIP2	physical	9312003
RFIP5_HUMAN	RAB11FIP5	physical	16148947
UBP6_HUMAN	USP6	physical	15509780
RFIP3_HUMAN	RAB11FIP3	physical	16148947
RFIP4_HUMAN	RAB11FIP4	physical	16148947
A4_HUMAN	APP	physical	21832049
GNAQ_HUMAN	GNAQ	physical	16650966
TBCE_HUMAN	TBCE	physical	26344197
ADAP1_HUMAN	ADAP1	physical	15923660
KI13B_HUMAN	KIF13B	physical	15923660
CLH1_HUMAN	CLTC	physical	16413285
AP180_HUMAN	SNAP91	physical	16413285
AP2A1_HUMAN	AP2A1	physical	16413285
PI51C_HUMAN	PIP5K1C	physical	16413285
AP1G1_HUMAN	AP1G1	physical	16413285
ACAP1_HUMAN	ACAP1	physical	16527809
RHG10_HUMAN	ARHGAP10	physical	16527809
ASAP1_HUMAN	ASAP1	physical	16527809

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.

Regulatory Network of ARF6_HUMAN

Related Literatures of Post-Translational Modification

Myristoylation
Reference	PubMed
"Myristoylation is required for the intracellular localization andendocytic function of ARF6."; D'Souza-Schorey C., Stahl P.D.; Exp. Cell Res. 221:153-159(1995). Cited for: MYRISTOYLATION AT GLY-2, FUNCTION, SUBCELLULAR LOCATION, ANDMUTAGENESIS OF GLY-2.	7589240 [Abstract]