RAB43_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RAB43_HUMAN
• UniProt AC: Q86YS6
• Protein Name: Ras-related protein Rab-43
• Gene Name: RAB43
• Organism: Homo sapiens (Human).
• Sequence Length: 212
• Subcellular Localization: Cytoplasmic vesicle, phagosome . Cytoplasmic vesicle, phagosome membrane ; Lipid-anchor ; Cytoplasmic side . Golgi apparatus . Golgi apparatus, trans-Golgi network membrane ; Lipid-anchor . Golgi apparatus, trans-Golgi network . Recruited to phagosom
• Protein Description: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. The low intrinsic GTPase activity of RAB43 is activated by USP6NL. Involved in retrograde transport from the endocytic pathway to the Golgi apparatus. Involved in the transport of Shiga toxin from early and recycling endosomes to the trans-Golgi network. Required for the structural integrity of the Golgi complex. Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis..
• Protein Sequence: MAGPGPGPGDPDEQYDFLFKLVLVGDASVGKTCVVQRFKTGAFSERQGSTIGVDFTMKTLEIQGKRVKLQIWDTAGQERFRTITQSYYRSANGAILAYDITKRSSFLSVPHWIEDVRKYAGSNIVQLLIGNKSDLSELREVSLAEAQSLAEHYDILCAIETSAKDSSNVEEAFLRVATELIMRHGGPLFSEKSPDHIQLNSKDIGEGWGCGC

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
15	Phosphorylation	PGDPDEQYDFLFKLV CCCHHHHHHHEEEEE	13.45	20068231
31	Ubiquitination	VGDASVGKTCVVQRF ECCCCCCCEEEEEEE	36.27	-
40	Phosphorylation	CVVQRFKTGAFSERQ EEEEEECCCCCCCCC	30.91	23898821
44	Phosphorylation	RFKTGAFSERQGSTI EECCCCCCCCCCCEE	31.19	28509920
49	Phosphorylation	AFSERQGSTIGVDFT CCCCCCCCEEEEEEE	14.44	23898821
50	Phosphorylation	FSERQGSTIGVDFTM CCCCCCCEEEEEEEE	28.68	23898821
56	Phosphorylation	STIGVDFTMKTLEIQ CEEEEEEEEEEEEEC	17.19	23898821
65	Ubiquitination	KTLEIQGKRVKLQIW EEEEECCEEEEEEEE	37.33	29967540
68	Ubiquitination	EIQGKRVKLQIWDTA EECCEEEEEEEECCC	38.41	-
74	Phosphorylation	VKLQIWDTAGQERFR EEEEEECCCCHHHHH	20.07	28857561
82	Phosphorylation	AGQERFRTITQSYYR CCHHHHHHHHHHHHH	26.18	29125462
84	Phosphorylation	QERFRTITQSYYRSA HHHHHHHHHHHHHCC	15.73	30108239
98	Phosphorylation	ANGAILAYDITKRSS CCCCEEEEECCCCCC	12.39	-
104	Phosphorylation	AYDITKRSSFLSVPH EEECCCCCCCCCCCH	27.31	-
105	Phosphorylation	YDITKRSSFLSVPHW EECCCCCCCCCCCHH	33.95	24719451
132	Ubiquitination	VQLLIGNKSDLSELR HHHHHCCCCCHHHHH	39.88	22817900
133	Phosphorylation	QLLIGNKSDLSELRE HHHHCCCCCHHHHHH	48.02	25332170
190	Phosphorylation	RHGGPLFSEKSPDHI HCCCCCCCCCCCCCE	52.37	26270265
192	Ubiquitination	GGPLFSEKSPDHIQL CCCCCCCCCCCCEEC	67.12	22817900
193	Phosphorylation	GPLFSEKSPDHIQLN CCCCCCCCCCCEECC	31.35	25159151
202	Ubiquitination	DHIQLNSKDIGEGWG CCEECCCCCCCCCCC	52.90	-
210	Geranylgeranylation	DIGEGWGCGC----- CCCCCCCCCC-----	3.97	-
212	Geranylgeranylation	GEGWGCGC------- CCCCCCCC-------	6.15	-
212	Methylation	GEGWGCGC------- CCCCCCCC-------	6.15	-

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
82	T	Phosphorylation	Kinase	LRRK2	Q5S007	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RAB43_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 RAB43_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049

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

"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-193, AND MASSSPECTROMETRY.
PubMed: 18669648