RAB35_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RAB35_HUMAN
• UniProt AC: Q15286
• Protein Name: Ras-related protein Rab-35
• Gene Name: RAB35
• Organism: Homo sapiens (Human).
• Sequence Length: 201
• Subcellular Localization: Cell membrane ; Lipid-anchor ; Cytoplasmic side . Membrane, clathrin-coated pit . Cytoplasmic vesicle, clathrin-coated vesicle . Endosome . Melanosome . Present on sorting endosomes and recycling endosome tubules (PubMed:16950109). Tends to be enrich
• 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 sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in the process of endocytosis and is an essential rate-limiting regulator of the fast recycling pathway back to the plasma membrane. During cytokinesis, required for the postfurrowing terminal steps, namely for intercellular bridge stability and abscission, possibly by controlling phosphatidylinositol 4,5-bis phosphate (PIP2) and SEPT2 localization at the intercellular bridge. May indirectly regulate neurite outgrowth. Together with TBC1D13 may be involved in regulation of insulin-induced glucose transporter SLC2A4/GLUT4 translocation to the plasma membrane in adipocytes..
• Protein Sequence: MARDYDHLFKLLIIGDSGVGKSSLLLRFADNTFSGSYITTIGVDFKIRTVEINGEKVKLQIWDTAGQERFRTITSTYYRGTHGVIVVYDVTSAESFVNVKRWLHEINQNCDDVCRILVGNKNDDPERKVVETEDAYKFAGQMGIQLFETSAKENVNVEEMFNCITELVLRAKKDNLAKQQQQQQNDVVKLTKNSKRKKRCC

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	Acetylation	------MARDYDHLF ------CCCCHHHHE	17.04	-
5	Phosphorylation	---MARDYDHLFKLL ---CCCCHHHHEEEE	10.33	25627689
17	Phosphorylation	KLLIIGDSGVGKSSL EEEEECCCCCCCCHH	30.11	23911959
21	Ubiquitination	IGDSGVGKSSLLLRF ECCCCCCCCHHHHHC	34.17	-
22	Phosphorylation	GDSGVGKSSLLLRFA CCCCCCCCHHHHHCC	21.93	25072903
23	Phosphorylation	DSGVGKSSLLLRFAD CCCCCCCHHHHHCCC	26.90	25072903
34	Phosphorylation	RFADNTFSGSYITTI HCCCCCCCCCEEEEE	25.45	28796482
36	Phosphorylation	ADNTFSGSYITTIGV CCCCCCCCEEEEEEE	16.50	28796482
37	Phosphorylation	DNTFSGSYITTIGVD CCCCCCCEEEEEEEE	13.05	28796482
39	Phosphorylation	TFSGSYITTIGVDFK CCCCCEEEEEEEEEE	12.25	28796482
40	Phosphorylation	FSGSYITTIGVDFKI CCCCEEEEEEEEEEE	13.23	28796482
49	Phosphorylation	GVDFKIRTVEINGEK EEEEEEEEEEECCEE	26.43	22985185
56	Ubiquitination	TVEINGEKVKLQIWD EEEECCEEEEEEEEC	46.17	29967540
58	Ubiquitination	EINGEKVKLQIWDTA EECCEEEEEEEECCC	45.82	-
64	Phosphorylation	VKLQIWDTAGQERFR EEEEEECCCCHHHEE	20.07	28857561
72	Phosphorylation	AGQERFRTITSTYYR CCHHHEEEEEEEECC	26.37	23684312
74	Phosphorylation	QERFRTITSTYYRGT HHHEEEEEEEECCCC	17.88	30108239
75	Other	ERFRTITSTYYRGTH HHEEEEEEEECCCCC	15.57	21822290
75	O-(2-cholinephosphoryl)serine	ERFRTITSTYYRGTH HHEEEEEEEECCCCC	15.57	-
75	Phosphorylation	ERFRTITSTYYRGTH HHEEEEEEEECCCCC	15.57	30108239
76	Phosphorylation	RFRTITSTYYRGTHG HEEEEEEEECCCCCE	18.87	30108239
77	AMPylation	FRTITSTYYRGTHGV EEEEEEEECCCCCEE	7.31	21822290
77	Phosphorylation	FRTITSTYYRGTHGV EEEEEEEECCCCCEE	7.31	27732954
77	O-AMP-tyrosine	FRTITSTYYRGTHGV EEEEEEEECCCCCEE	7.31	-
78	Phosphorylation	RTITSTYYRGTHGVI EEEEEEECCCCCEEE	11.58	20068231
121	Ubiquitination	CRILVGNKNDDPERK HHHHCCCCCCCHHHC	56.69	21906983
128	Ubiquitination	KNDDPERKVVETEDA CCCCHHHCEEEHHHH	49.31	22817900
136	Phosphorylation	VVETEDAYKFAGQMG EEEHHHHHHHHHHHH	20.97	25159151
137	Ubiquitination	VETEDAYKFAGQMGI EEHHHHHHHHHHHHH	30.38	32015554
142	Sulfoxidation	AYKFAGQMGIQLFET HHHHHHHHHHHEEEC	5.09	28465586
172	Ubiquitination	TELVLRAKKDNLAKQ HHHHHHHHHHHHHHH	54.98	23000965
173	Ubiquitination	ELVLRAKKDNLAKQQ HHHHHHHHHHHHHHH	51.36	23000965
178	Ubiquitination	AKKDNLAKQQQQQQN HHHHHHHHHHHHHHH	52.37	23000965
189	Ubiquitination	QQQNDVVKLTKNSKR HHHHHHHHHHHCCCC	50.73	23000965
192	Ubiquitination	NDVVKLTKNSKRKKR HHHHHHHHCCCCCCC	70.43	23000965
195	Ubiquitination	VKLTKNSKRKKRCC- HHHHHCCCCCCCCC-	77.09	23000965
200	Geranylgeranylation	NSKRKKRCC------ CCCCCCCCC------	4.42	-
201	Geranylgeranylation	SKRKKRCC------- CCCCCCCC-------	7.89	-

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
72	T	Phosphorylation	Kinase	LRRK2	Q5S007	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RAB35_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 RAB35_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CBR3_HUMAN	CBR3	physical	16169070
TBPL1_HUMAN	TBPL1	physical	16169070
A16L1_HUMAN	ATG16L1	physical	18448665
A4_HUMAN	APP	physical	21832049
BICL2_MOUSE	Ccdc64b	physical	20360680
CACO2_HUMAN	CALCOCO2	physical	28848034

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

Acetylation

"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
PubMed: 19413330