ARL3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ARL3_HUMAN
• UniProt AC: P36405
• Protein Name: ADP-ribosylation factor-like protein 3
• Gene Name: ARL3
• Organism: Homo sapiens (Human).
• Sequence Length: 182
• Subcellular Localization: Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, spindle. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm. Cell projection, cilium. Detected predominantly in the
• 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). Required for normal cytokinesis and cilia signaling. Requires assistance from GTPase-activating proteins (GAPs) like RP2 and PDE6D, in order to cycle between inactive GDP-bound and active GTP-bound forms. Required for targeting proteins such as NPHP3 to the ciliary membrane by releasing myristoylated NPHP3 from UNC119B cargo adapter into the cilium. Does not act as an allosteric activator of the cholera toxin catalytic subunit..
• Protein Sequence: MGLLSILRKLKSAPDQEVRILLLGLDNAGKTTLLKQLASEDISHITPTQGFNIKSVQSQGFKLNVWDIGGQRKIRPYWKNYFENTDILIYVIDSADRKRFEETGQELAELLEEEKLSCVPVLIFANKQDLLTAAPASEIAEGLNLHTIRDRVWQIQSCSALTGEGVQDGMNWVCKNVNAKKK

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	------MGLLSILRK ------CCHHHHHHH	35.01	-
5	Phosphorylation	---MGLLSILRKLKS ---CCHHHHHHHHCC	25.31	25159151
9	Ubiquitination	GLLSILRKLKSAPDQ CHHHHHHHHCCCCCH	57.74	22817900
11	Ubiquitination	LSILRKLKSAPDQEV HHHHHHHCCCCCHHH	47.83	21906983
12	Phosphorylation	SILRKLKSAPDQEVR HHHHHHCCCCCHHHE	56.31	28348404
30	Ubiquitination	LGLDNAGKTTLLKQL EECCCCCHHHHHHHH	35.61	22817900
31	Phosphorylation	GLDNAGKTTLLKQLA ECCCCCHHHHHHHHH	23.04	20068231
32	Phosphorylation	LDNAGKTTLLKQLAS CCCCCHHHHHHHHHC	33.31	20068231
35	Ubiquitination	AGKTTLLKQLASEDI CCHHHHHHHHHCCCC	46.51	21906983
39	Phosphorylation	TLLKQLASEDISHIT HHHHHHHCCCCCCCC	44.38	21406692
43	Phosphorylation	QLASEDISHITPTQG HHHCCCCCCCCCCCC	22.59	21406692
46	Phosphorylation	SEDISHITPTQGFNI CCCCCCCCCCCCCCC	18.17	25159151
48	Phosphorylation	DISHITPTQGFNIKS CCCCCCCCCCCCCEE	32.45	27251275
54	Ubiquitination	PTQGFNIKSVQSQGF CCCCCCCEECCCCCE	45.75	21906983
55	Phosphorylation	TQGFNIKSVQSQGFK CCCCCCEECCCCCEE	22.92	28102081
58	Phosphorylation	FNIKSVQSQGFKLNV CCCEECCCCCEEEEE	30.07	28102081
62	Ubiquitination	SVQSQGFKLNVWDIG ECCCCCEEEEEEEEC	46.07	32015554
115	Ubiquitination	AELLEEEKLSCVPVL HHHHHHHCCCCCEEE	49.32	29967540
117	Phosphorylation	LLEEEKLSCVPVLIF HHHHHCCCCCEEEEE	24.92	21406692
118	S-nitrosocysteine	LEEEKLSCVPVLIFA HHHHCCCCCEEEEEE	6.09	-
118	S-nitrosylation	LEEEKLSCVPVLIFA HHHHCCCCCEEEEEE	6.09	19483679
127	Ubiquitination	PVLIFANKQDLLTAA EEEEEECHHHHHHHC	41.58	32015554
175	Ubiquitination	DGMNWVCKNVNAKKK CCHHHHHHCCCCCCC	55.07	32015554

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

Oops, there are no upstream regulatory protein records of ARL3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ARL3_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 ARL3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PDE6D_HUMAN	PDE6D	physical	16169070
LRIF1_HUMAN	LRIF1	physical	16169070
TLE1_HUMAN	TLE1	physical	16169070
P53_HUMAN	TP53	physical	16169070
UBR1_HUMAN	UBR1	physical	16169070
U119A_HUMAN	UNC119	physical	16169070
AR2BP_HUMAN	ARL2BP	physical	11303027
U119A_HUMAN	UNC119	physical	11303027
U119A_HUMAN	UNC119	physical	27173435
U119B_HUMAN	UNC119B	physical	27173435
ESF1_HUMAN	ESF1	physical	27173435
WRN_HUMAN	WRN	physical	27173435
XRP2_HUMAN	RP2	physical	16472755

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

"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 THR-32, AND MASSSPECTROMETRY.
PubMed: 19413330