dbPTM

RAB13_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RAB13_HUMAN
UniProt AC	P51153
Protein Name	Ras-related protein Rab-13
Gene Name	RAB13
Organism	Homo sapiens (Human).
Sequence Length	203
Subcellular Localization	Cell membrane Lipid-anchor Cytoplasmic side . Cytoplasmic vesicle membrane Lipid-anchor Cytoplasmic side . Cell junction, tight junction . Golgi apparatus, trans-Golgi network membrane . Recycling endosome membrane . Cell projection, lamellipodium
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 endocytic recycling and regulates the transport to the plasma membrane of transmembrane proteins like the tight junction protein OCLN/occludin. Thereby, it regulates the assembly and the activity of tight junctions. Moreover, it may also regulate tight junction assembly by activating the PKA signaling pathway and by reorganizing the actin cytoskeleton through the activation of the downstream effectors PRKACA and MICALL2 respectively. Through its role in tight junction assembly, may play a role in the establishment of Sertoli cell barrier. Plays also a role in angiogenesis through regulation of endothelial cells chemotaxis. Also involved in neurite outgrowth. Has also been proposed to play a role in post-Golgi membrane trafficking from the TGN to the recycling endosome. Finally, it has been involved in insulin-induced transport to the plasma membrane of the glucose transporter GLUT4 and therefore may play a role in glucose homeostasis..
Protein Sequence	MAKAYDHLFKLLLIGDSGVGKTCLIIRFAEDNFNNTYISTIGIDFKIRTVDIEGKKIKLQVWDTAGQERFKTITTAYYRGAMGIILVYDITDEKSFENIQNWMKSIKENASAGVERLLLGNKCDMEAKRKVQKEQADKLAREHGIRFFETSAKSSMNVDEAFSSLARDILLKSGGRRSGNGNKPPSTDLKTCDKKNTNKCSLG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Acetylation	-----MAKAYDHLFK -----CHHHHHHHHH	46.29	22424773
3	Ubiquitination	-----MAKAYDHLFK -----CHHHHHHHHH	46.29	-
3	Malonylation	-----MAKAYDHLFK -----CHHHHHHHHH	46.29	26320211
5	Phosphorylation	---MAKAYDHLFKLL ---CHHHHHHHHHHH	11.82	21945579
17	Phosphorylation	KLLLIGDSGVGKTCL HHHHHCCCCCCCEEE	30.11	23911959
36	Phosphorylation	AEDNFNNTYISTIGI EECCCCCEEEEEEEE	24.28	29978859
37	Phosphorylation	EDNFNNTYISTIGID ECCCCCEEEEEEEEE	8.59	25106551
39	Phosphorylation	NFNNTYISTIGIDFK CCCCEEEEEEEEEEE	11.98	29978859
40	Phosphorylation	FNNTYISTIGIDFKI CCCEEEEEEEEEEEE	17.42	29978859
49	Phosphorylation	GIDFKIRTVDIEGKK EEEEEEEEEECCCCE	26.46	22985185
56	Malonylation	TVDIEGKKIKLQVWD EEECCCCEEEEEEEE	56.80	26320211
58	Ubiquitination	DIEGKKIKLQVWDTA ECCCCEEEEEEEECC	41.57	-
58	Malonylation	DIEGKKIKLQVWDTA ECCCCEEEEEEEECC	41.57	26320211
58	Acetylation	DIEGKKIKLQVWDTA ECCCCEEEEEEEECC	41.57	23954790
64	Phosphorylation	IKLQVWDTAGQERFK EEEEEEECCCHHHHH	19.58	25850435
71	Ubiquitination	TAGQERFKTITTAYY CCCHHHHHHHHHHHH	45.28	21890473
72	Phosphorylation	AGQERFKTITTAYYR CCHHHHHHHHHHHHC	22.35	28857561
74	Phosphorylation	QERFKTITTAYYRGA HHHHHHHHHHHHCCC	15.59	28060719
75	Phosphorylation	ERFKTITTAYYRGAM HHHHHHHHHHHCCCC	14.60	24961811
77	Phosphorylation	FKTITTAYYRGAMGI HHHHHHHHHCCCCEE	7.51	-
88	Phosphorylation	AMGIILVYDITDEKS CCEEEEEEECCCHHH	9.74	20049867
95	Phosphorylation	YDITDEKSFENIQNW EECCCHHHHHHHHHH	35.43	30622161
104	Ubiquitination	ENIQNWMKSIKENAS HHHHHHHHHHHHHHC	40.41	21890473
105	Phosphorylation	NIQNWMKSIKENASA HHHHHHHHHHHHHCH	23.84	28857561
107	Acetylation	QNWMKSIKENASAGV HHHHHHHHHHHCHHH	52.59	27452117
107	Ubiquitination	QNWMKSIKENASAGV HHHHHHHHHHHCHHH	52.59	21890473
111	Phosphorylation	KSIKENASAGVERLL HHHHHHHCHHHHHHH	36.82	28857561
122	Ubiquitination	ERLLLGNKCDMEAKR HHHHHCCCCCHHHHH	29.79	-
130	Ubiquitination	CDMEAKRKVQKEQAD CCHHHHHHHHHHHHH	48.59	-
133	Ubiquitination	EAKRKVQKEQADKLA HHHHHHHHHHHHHHH	55.57	-
138	Ubiquitination	VQKEQADKLAREHGI HHHHHHHHHHHHHCC	47.24	-
146	Methylation	LAREHGIRFFETSAK HHHHHCCEEEECCCC	34.49	-
153	Ubiquitination	RFFETSAKSSMNVDE EEEECCCCCCCCHHH	42.71	-
154	Phosphorylation	FFETSAKSSMNVDEA EEECCCCCCCCHHHH	34.24	30622161
155	Phosphorylation	FETSAKSSMNVDEAF EECCCCCCCCHHHHH	17.42	30622161
163	Phosphorylation	MNVDEAFSSLARDIL CCHHHHHHHHHHHHH	31.33	26471730
164	Phosphorylation	NVDEAFSSLARDILL CHHHHHHHHHHHHHH	21.42	26471730
172	Ubiquitination	LARDILLKSGGRRSG HHHHHHHHCCCCCCC	43.54	-
173	Phosphorylation	ARDILLKSGGRRSGN HHHHHHHCCCCCCCC	46.58	22496350
178	Phosphorylation	LKSGGRRSGNGNKPP HHCCCCCCCCCCCCC	34.94	30266825
186	Phosphorylation	GNGNKPPSTDLKTCD CCCCCCCCCCCCCCC	42.98	23927012
187	Phosphorylation	NGNKPPSTDLKTCDK CCCCCCCCCCCCCCC	51.64	25159151
195	Ubiquitination	DLKTCDKKNTNKCSL CCCCCCCCCCCCCCC	56.61	-
200	Methylation	DKKNTNKCSLG---- CCCCCCCCCCC----	4.38	-
200	Geranylgeranylation	DKKNTNKCSLG---- CCCCCCCCCCC----	4.38	8375503
200	Geranylgeranylation	DKKNTNKCSLG---- CCCCCCCCCCC----	4.38	8375503

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
Oops, there are no upstream regulatory protein records of RAB13_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RAB13_HUMAN !!

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 RAB13_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
PDE6D_HUMAN	PDE6D	physical	9712853
BICL2_MOUSE	Ccdc64b	physical	20360680

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 RAB13_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-178, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND MASSSPECTROMETRY.	18691976 [Abstract]