ARF4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ARF4_HUMAN
• UniProt AC: P18085
• Protein Name: ADP-ribosylation factor 4
• Gene Name: ARF4
• Organism: Homo sapiens (Human).
• Sequence Length: 180
• Subcellular Localization: Golgi apparatus. Membrane ; Lipid-anchor .
• Protein Description: GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus..
• Protein Sequence: MGLTISSLFSRLFGKKQMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNICFTVWDVGGQDRIRPLWKHYFQNTQGLIFVVDSNDRERIQEVADELQKMLLVDELRDAVLLLFANKQDLPNAMAISEMTDKLGLQSLRNRTWYVQATCATQGTGLYEGLDWLSNELSKR

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
2	Myristoylation	------MGLTISSLF ------CCCCHHHHH	31.37	25255805
4	Phosphorylation	----MGLTISSLFSR ----CCCCHHHHHHH	17.06	24043423
6	Phosphorylation	--MGLTISSLFSRLF --CCCCHHHHHHHHH	18.76	24043423
7	Phosphorylation	-MGLTISSLFSRLFG -CCCCHHHHHHHHHC	29.59	24043423
10	Phosphorylation	LTISSLFSRLFGKKQ CCHHHHHHHHHCCCC	33.11	24043423
15	Ubiquitination	LFSRLFGKKQMRILM HHHHHHCCCCEEEEE	32.28	21906983
16	Ubiquitination	FSRLFGKKQMRILMV HHHHHCCCCEEEEEE	50.10	21890473
22	Sulfoxidation	KKQMRILMVGLDAAG CCCEEEEEEEECCCC	1.77	21406390
35	Phosphorylation	AGKTTILYKLKLGEI CCCEEEEEEEECCCE	15.49	-
36	Acetylation	GKTTILYKLKLGEIV CCEEEEEEEECCCEE	35.38	26051181
36	Ubiquitination	GKTTILYKLKLGEIV CCEEEEEEEECCCEE	35.38	21963094
38	Ubiquitination	TTILYKLKLGEIVTT EEEEEEEECCCEEEE	50.74	21906983
45	O-linked_Glycosylation	KLGEIVTTIPTIGFN ECCCEEEECCCCCCC	17.67	OGP
48	O-linked_Glycosylation	EIVTTIPTIGFNVET CEEEECCCCCCCCEE	29.86	OGP
58	Phosphorylation	FNVETVEYKNICFTV CCCEEEEEEEEEEEE	12.66	-
81	Phosphorylation	IRPLWKHYFQNTQGL CHHHHHHHHCCCCEE	11.79	28152594
85	Phosphorylation	WKHYFQNTQGLIFVV HHHHHCCCCEEEEEE	17.15	28152594
109	Ubiquitination	EVADELQKMLLVDEL HHHHHHHHHHHHHHH	44.11	21906983
127	Ubiquitination	VLLLFANKQDLPNAM HHHHHCCCCCCCCHH	41.58	21906983
134	Sulfoxidation	KQDLPNAMAISEMTD CCCCCCHHHHHHHCH	4.29	30846556
137	Phosphorylation	LPNAMAISEMTDKLG CCCHHHHHHHCHHHC	16.27	27251275
139	Sulfoxidation	NAMAISEMTDKLGLQ CHHHHHHHCHHHCHH	4.72	30846556
142	Ubiquitination	AISEMTDKLGLQSLR HHHHHCHHHCHHHHH	34.98	22817900
147	Phosphorylation	TDKLGLQSLRNRTWY CHHHCHHHHHCCEEE	34.05	19664994
152	Phosphorylation	LQSLRNRTWYVQATC HHHHHCCEEEEEEEE	25.38	-
167	Phosphorylation	ATQGTGLYEGLDWLS ECCCCCHHHHHHHHH	14.86	-

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

Oops, there are no upstream regulatory protein records of ARF4_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ARF4_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 ARF4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZN363_HUMAN	RCHY1	physical	21988832
SDCB2_HUMAN	SDCBP2	physical	25416956
ACADM_HUMAN	ACADM	physical	26344197
FUBP1_HUMAN	FUBP1	physical	26344197
FUBP3_HUMAN	FUBP3	physical	26344197
RACK1_HUMAN	GNB2L1	physical	26344197
IDHC_HUMAN	IDH1	physical	26344197
LEG1_HUMAN	LGALS1	physical	26344197
PCBP2_HUMAN	PCBP2	physical	26344197
SERC_HUMAN	PSAT1	physical	26344197
UBE2N_HUMAN	UBE2N	physical	26344197

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.

Related Literatures of Post-Translational Modification

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-36, AND MASS SPECTROMETRY.
PubMed: 19608861