dbPTM

ARF1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ARF1_HUMAN
UniProt AC	P84077
Protein Name	ADP-ribosylation factor 1
Gene Name	ARF1
Organism	Homo sapiens (Human).
Sequence Length	181
Subcellular Localization	Golgi apparatus . Cytoplasm, perinuclear region . Cell junction, synapse, synaptosome. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density. 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 among different compartments. Modulates vesicle budding and uncoating within the Golgi complex. Deactivation induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, suggesting a crucial role in protein trafficking. In its GTP-bound form, its triggers the association with coat proteins with the Golgi membrane. The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles. The GTP-bound form interacts with PICK1 to limit PICK1-mediated inhibition of Arp2/3 complex activity; the function is linked to AMPA receptor (AMPAR) trafficking, regulation of synaptic plasicity of excitatory synapses and spine shrinkage during long-term depression (LTD)..
Protein Sequence	MGNIFANLFKGLFGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLSNQLRNQK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	N-myristoyl glycine	------MGNIFANLF ------CCCHHHHHH	35.62	-
2	Myristoylation	------MGNIFANLF ------CCCHHHHHH	35.62	23535599
2	Acetylation	------MGNIFANLF ------CCCHHHHHH	35.62	19413330
22	Sulfoxidation	KKEMRILMVGLDAAG CCCEEEEEEEECCCC	1.77	30846556
35	Phosphorylation	AGKTTILYKLKLGEI CCCEEEEEEEECCCE	15.49	-
36	Acetylation	GKTTILYKLKLGEIV CCEEEEEEEECCCEE	35.38	22647619
36	Ubiquitination	GKTTILYKLKLGEIV CCEEEEEEEECCCEE	35.38	-
38	Ubiquitination	TTILYKLKLGEIVTT EEEEEEEECCCEEEE	50.74	21906983
58	Phosphorylation	FNVETVEYKNISFTV EEEEEEEEEEEEEEE	12.66	-
62	Phosphorylation	TVEYKNISFTVWDVG EEEEEEEEEEEEECC	25.02	22199227
64	Phosphorylation	EYKNISFTVWDVGGQ EEEEEEEEEEECCCC	17.56	20068231
73	Sumoylation	WDVGGQDKIRPLWRH EECCCCCCCHHHHHH	32.50	-
73	Ubiquitination	WDVGGQDKIRPLWRH EECCCCCCCHHHHHH	32.50	21906983
81	Phosphorylation	IRPLWRHYFQNTQGL CHHHHHHHHCCCCEE	9.78	29759185
85	Phosphorylation	WRHYFQNTQGLIFVV HHHHHCCCCEEEEEE	17.15	28152594
110	Sulfoxidation	AREELMRMLAEDELR HHHHHHHHHHHHHHH	2.31	30846556
117	Methylation	MLAEDELRDAVLLVF HHHHHHHHHHHHHHE	28.00	-
127	Ubiquitination	VLLVFANKQDLPNAM HHHHEECCCCCCCCC	41.58	21906983
134	Sulfoxidation	KQDLPNAMNAAEITD CCCCCCCCCHHHHHH	4.45	30846556
140	Phosphorylation	AMNAAEITDKLGLHS CCCHHHHHHHHCCHH	20.70	20860994
142	Acetylation	NAAEITDKLGLHSLR CHHHHHHHHCCHHCC	35.49	66698813
142	Ubiquitination	NAAEITDKLGLHSLR CHHHHHHHHCCHHCC	35.49	21906983
147	Phosphorylation	TDKLGLHSLRHRNWY HHHHCCHHCCCCCEE	31.94	23927012
167	Phosphorylation	ATSGDGLYEGLDWLS ECCCCCHHHHHHHHH	17.30	20736484

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	FBH1	Q8NFZ0	PMID:24658274

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
2	G	Myristoylation	19413330
Demyristoylated by S.flexneri cysteine protease IpaJ which cleaves the peptide bond between N-myristoylated Gly-2 and Asn-3.
3	N	Myristoylation	23535599
Demyristoylated by S.flexneri cysteine protease IpaJ which cleaves the peptide bond between N-myristoylated Gly-2 and Asn-3.

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 ARF1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GGA3_HUMAN	GGA3	physical	10747089
ACM3_HUMAN	CHRM3	physical	12799371
NOA1_HUMAN	NOA1	physical	16169070
WBP11_HUMAN	WBP11	physical	16169070
EF1G_HUMAN	EEF1G	physical	16169070
COPB_HUMAN	COPB1	physical	10921873
COPE_HUMAN	COPE	physical	10921873
ARFP1_HUMAN	ARFIP1	physical	9038142
ARFP2_HUMAN	ARFIP2	physical	9038142
GGA3_HUMAN	GGA3	physical	11301005
ARF1_HUMAN	ARF1	physical	7990966
AP4M1_HUMAN	AP4M1	physical	11707398
AP4E1_HUMAN	AP4E1	physical	11707398
PLD1_HUMAN	PLD1	physical	9688545
ERD21_HUMAN	KDELR1	physical	11703931
GEA1_YEAST	GEA1	physical	14690595
NEF_HV1H2	nef	physical	15202998
COPB_HUMAN	COPB1	physical	15202998
ARF3_HUMAN	ARF3	physical	22939629
T106A_HUMAN	TMEM106A	physical	21988832
ACADM_HUMAN	ACADM	physical	26344197
AHSA1_HUMAN	AHSA1	physical	26344197
ARF4_HUMAN	ARF4	physical	26344197
ARF5_HUMAN	ARF5	physical	26344197
ARFG1_HUMAN	ARFGAP1	physical	26344197
ARFG2_HUMAN	ARFGAP2	physical	26344197
ARFG3_HUMAN	ARFGAP3	physical	26344197
TCPG_HUMAN	CCT3	physical	26344197
TCPZ_HUMAN	CCT6A	physical	26344197
EI2BA_HUMAN	EIF2B1	physical	26344197
ETFA_HUMAN	ETFA	physical	26344197
GALE_HUMAN	GALE	physical	26344197
GLRX5_HUMAN	GLRX5	physical	26344197
LDHA_HUMAN	LDHA	physical	26344197
LDH6A_HUMAN	LDHAL6A	physical	26344197
LDH6B_HUMAN	LDHAL6B	physical	26344197
LDHB_HUMAN	LDHB	physical	26344197
LDHC_HUMAN	LDHC	physical	26344197
PUR6_HUMAN	PAICS	physical	26344197
PLD1_HUMAN	PLD1	physical	26344197
KAPCB_HUMAN	PRKACB	physical	26344197
RB11A_HUMAN	RAB11A	physical	26344197
RB11B_HUMAN	RAB11B	physical	26344197
RAB1A_HUMAN	RAB1A	physical	26344197
RAB1B_HUMAN	RAB1B	physical	26344197
RAB2A_HUMAN	RAB2A	physical	26344197
RAB5A_HUMAN	RAB5A	physical	26344197
RAB6A_HUMAN	RAB6A	physical	26344197
RAB6B_HUMAN	RAB6B	physical	26344197
SAR1A_HUMAN	SAR1A	physical	26344197
EFTU_HUMAN	TUFM	physical	26344197
SNUT2_HUMAN	USP39	physical	26344197
APRIO_HUMAN	PRNP	physical	25896910
PRIO_HUMAN	PRNP	physical	25896910
ASAP1_HUMAN	ASAP1	physical	16332543
AGAP1_HUMAN	AGAP1	physical	16332543
ARFG1_HUMAN	ARFGAP1	physical	16332543
PAXI_HUMAN	PXN	physical	16332543
COPB_HUMAN	COPB1	physical	16332543

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 ARF1_HUMAN

Related Literatures of Post-Translational Modification

Myristoylation
Reference	PubMed
"Strategy for comprehensive identification of human N-myristoylatedproteins using an insect cell-free protein synthesis system."; Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,Tsunasawa S., Utsumi T.; Proteomics 10:1780-1793(2010). Cited for: MYRISTOYLATION AT GLY-2.	20213681 [Abstract]
Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, AND MASSSPECTROMETRY.	18669648 [Abstract]

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