dbPTM

RAB12_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RAB12_HUMAN
UniProt AC	Q6IQ22
Protein Name	Ras-related protein Rab-12
Gene Name	RAB12
Organism	Homo sapiens (Human).
Sequence Length	244
Subcellular Localization	Recycling endosome membrane Lipid-anchor Cytoplasmic side . Lysosome membrane Lipid-anchor Cytoplasmic side . Golgi apparatus membrane . Cytoplasmic vesicle, autophagosome .
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. That Rab may play a role in protein transport from recycling endosomes to lysosomes regulating, for instance, the degradation of the transferrin receptor. Involved in autophagy (By similarity)..
Protein Sequence	MDPGAALQRRAGGGGGLGAGSPALSGGQGRRRKQPPRPADFKLQVIIIGSRGVGKTSLMERFTDDTFCEACKSTVGVDFKIKTVELRGKKIRLQIWDTAGQERFNSITSAYYRSAKGIILVYDITKKETFDDLPKWMKMIDKYASEDAELLLVGNKLDCETDREITRQQGEKFAQQITGMRFCEASAKDNFNVDEIFLKLVDDILKKMPLDILRNELSNSILSLQPEPEIPPELPPPRPHVRCC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDPGAALQ -------CCHHHHHC	14.66	22223895
10	Methylation	PGAALQRRAGGGGGL HHHHHCCCCCCCCCC	25.32	115489883
21	Phosphorylation	GGGLGAGSPALSGGQ CCCCCCCCCCCCCCC	13.38	19664994
25	Phosphorylation	GAGSPALSGGQGRRR CCCCCCCCCCCCCCC	42.88	23927012
83	Phosphorylation	GVDFKIKTVELRGKK CCCEEEEEEEECCEE	23.76	23403867
98	Phosphorylation	IRLQIWDTAGQERFN EEEEEECCCCHHHHH	20.07	28857561
106	Phosphorylation	AGQERFNSITSAYYR CCHHHHHHHHHHHHH	25.24	26824392
108	Phosphorylation	QERFNSITSAYYRSA HHHHHHHHHHHHHHC	13.71	23927012
109	Phosphorylation	ERFNSITSAYYRSAK HHHHHHHHHHHHHCC	16.77	23927012
140	Ubiquitination	LPKWMKMIDKYASED HHHHHHHHHHHCCCC	3.26	21890473
156	Ubiquitination	ELLLVGNKLDCETDR EEEEECCCCCCCCHH	39.51	29967540
172	Ubiquitination	ITRQQGEKFAQQITG HHHHHHHHHHHHHHC	53.47	23000965
218	Phosphorylation	DILRNELSNSILSLQ HHHHHHHHHCHHHCC	23.50	28348404
220	Phosphorylation	LRNELSNSILSLQPE HHHHHHHCHHHCCCC	22.87	26657352
223	Phosphorylation	ELSNSILSLQPEPEI HHHHCHHHCCCCCCC	24.24	28348404
243	Geranylgeranylation	PPRPHVRCC------ CCCCCCCCC------	2.92	-
244	Geranylgeranylation	PRPHVRCC------- CCCCCCCC-------	4.35	-

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
106	S	Phosphorylation	Kinase	LRRK2	Q5S007	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
106	S	Phosphorylation		23186163
Phosphorylation of Ser-106 in the switch II region by LRRK2 prevents the association of RAB regulatory proteins, including CHM, CHML and RAB GDP dissociation inhibitors GDI1 and GDI2.

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 RAB12_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BICL2_MOUSE	Ccdc64b	physical	20360680
BICL1_MOUSE	Ccdc64	physical	20360680
OPTN_HUMAN	OPTN	physical	23357852

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 RAB12_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-21, AND MASSSPECTROMETRY.	19413330 [Abstract]
"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-21 AND SER-25, AND MASSSPECTROMETRY.	18669648 [Abstract]