ARL2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ARL2_HUMAN
• UniProt AC: P36404
• Protein Name: ADP-ribosylation factor-like protein 2
• Gene Name: ARL2
• Organism: Homo sapiens (Human).
• Sequence Length: 184
• Subcellular Localization: Mitochondrion intermembrane space. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Cytoplasm. The complex formed with ARL2BP, ARL2 and SLC25A6 is expressed in mitochondria. The complex formed with ARL2BP, ARL2 and SLC25A4
• Protein Description: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. Regulates formation of new microtubules and centrosome integrity. Prevents the TBCD-induced microtubule destruction. Participates in association with TBCD, in the disassembly of the apical junction complexes. Antagonizes the effect of TBCD on epithelial cell detachment and tight and adherens junctions disassembly. Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. Component of a regulated secretory pathway involved in Ca(2+)-dependent release of acetylcholine. Required for normal progress through the cell cycle..
• Protein Sequence: MGLLTILKKMKQKERELRLLMLGLDNAGKTTILKKFNGEDIDTISPTLGFNIKTLEHRGFKLNIWDVGGQKSLRSYWRNYFESTDGLIWVVDSADRQRMQDCQRELQSLLVEERLAGATLLIFANKQDLPGALSSNAIREVLELDSIRSHHWCIQGCSAVTGENLLPGIDWLLDDISSRIFTAD

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	------MGLLTILKK ------CCHHHHHHH	29.42	-
8	Ubiquitination	MGLLTILKKMKQKER CCHHHHHHHHHHHHH	47.15	21906983
8	2-Hydroxyisobutyrylation	MGLLTILKKMKQKER CCHHHHHHHHHHHHH	47.15	-
35	Ubiquitination	GKTTILKKFNGEDID CCEEEEHHCCCCCCC	40.39	-
43	Phosphorylation	FNGEDIDTISPTLGF CCCCCCCCCCCCCCC	24.56	30266825
45	Phosphorylation	GEDIDTISPTLGFNI CCCCCCCCCCCCCEE	17.58	23401153
47	Phosphorylation	DIDTISPTLGFNIKT CCCCCCCCCCCEEEE	32.49	30266825
53	Ubiquitination	PTLGFNIKTLEHRGF CCCCCEEEECCCCCE	48.43	21906983
61	Acetylation	TLEHRGFKLNIWDVG ECCCCCEEEEEEECC	43.37	25953088
61	Ubiquitination	TLEHRGFKLNIWDVG ECCCCCEEEEEEECC	43.37	21906983
71	Ubiquitination	IWDVGGQKSLRSYWR EEECCCHHHHHHHHH	55.52	21890473
72	Phosphorylation	WDVGGQKSLRSYWRN EECCCHHHHHHHHHH	22.56	27422710
75	Phosphorylation	GGQKSLRSYWRNYFE CCHHHHHHHHHHHHC	34.05	20068231
76	Phosphorylation	GQKSLRSYWRNYFES CHHHHHHHHHHHHCC	11.27	20068231
80	Phosphorylation	LRSYWRNYFESTDGL HHHHHHHHHCCCCCE	10.51	20068231
83	Phosphorylation	YWRNYFESTDGLIWV HHHHHHCCCCCEEEE	23.15	20068231
84	Phosphorylation	WRNYFESTDGLIWVV HHHHHCCCCCEEEEE	27.21	20068231
126	Ubiquitination	TLLIFANKQDLPGAL EEEEEECCCCCCCCC	41.58	-
134	Phosphorylation	QDLPGALSSNAIREV CCCCCCCCHHHHHHH	22.47	28555341
135	Phosphorylation	DLPGALSSNAIREVL CCCCCCCHHHHHHHH	31.00	28555341

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

Oops, there are no upstream regulatory protein records of ARL2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ARL2_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 ARL2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PDE6D_HUMAN	PDE6D	physical	16189514
TBCD_HUMAN	TBCD	physical	12912990
PP2AA_HUMAN	PPP2CA	physical	12912990
PP2AB_HUMAN	PPP2CB	physical	12912990
2ABG_HUMAN	PPP2R2C	physical	12912990
2A5D_HUMAN	PPP2R5D	physical	12912990
AR2BP_HUMAN	ARL2BP	physical	11809823
TBCD_HUMAN	TBCD	physical	10831612
CYC_HUMAN	CYCS	physical	22939629
AR2BP_HUMAN	ARL2BP	physical	21988832
PDE6D_HUMAN	PDE6D	physical	25416956
U119A_HUMAN	UNC119	physical	25416956
AR2BP_HUMAN	ARL2BP	physical	25416956
TBL1R_HUMAN	TBL1XR1	physical	25416956
PDE6D_HUMAN	PDE6D	physical	21516116
AR2BP_BOVIN	ARL2BP	physical	10488091
AR2BP_HUMAN	ARL2BP	physical	10488091
ARL3_HUMAN	ARL3	physical	27173435
U119A_HUMAN	UNC119	physical	27173435

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

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, AND MASSSPECTROMETRY.
PubMed: 19690332

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, AND MASSSPECTROMETRY.
PubMed: 19413330

Ubiquitylation

"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry.";
Meierhofer D., Wang X., Huang L., Kaiser P.;
J. Proteome Res. 7:4566-4576(2008).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-71, AND MASSSPECTROMETRY.
PubMed: 18781797