RAB7A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RAB7A_MOUSE
• UniProt AC: P51150
• Protein Name: Ras-related protein Rab-7a
• Gene Name: Rab7a
• Organism: Mus musculus (Mouse).
• Sequence Length: 207
• Subcellular Localization: Cytoplasmic vesicle, phagosome membrane ; Peripheral membrane protein ; Cytoplasmic side . Late endosome membrane ; Peripheral membrane protein ; Cytoplasmic side . Lysosome membrane ; Peripheral membrane protein ; Cytoplasmic side . Melanosome membrane
• Protein Description: Key regulator in endo-lysosomal trafficking. Governs early-to-late endosomal maturation, microtubule minus-end as well as plus-end directed endosomal migration and positioning, and endosome-lysosome transport through different protein-protein interaction cascades. Plays a central role, not only in endosomal traffic, but also in many other cellular and physiological events, such as growth-factor-mediated cell signaling, nutrient-transportor mediated nutrient uptake, neurotrophin transport in the axons of neurons and lipid metabolism. Also involved in regulation of some specialized endosomal membrane trafficking, such as maturation of melanosomes, pathogen-induced phagosomes (or vacuoles) and autophagosomes. Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and Mycobacteria. Plays a role in the fusion of phagosomes with lysosomes. Plays important roles in microbial pathogen infection and survival, as well as in participating in the life cycle of viruses. Microbial pathogens possess survival strategies governed by RAB7A, sometimes by employing RAB7A function (e.g. Salmonella) and sometimes by excluding RAB7A function (e.g. Mycobacterium). In concert with RAC1, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. Controls the endosomal trafficking and neurite outgrowth signaling of NTRK1/TRKA. Regulates the endocytic trafficking of the EGF-EGFR complex by regulating its lysosomal degradation (By similarity). Involved in the ADRB2-stimulated lipolysis through lipophagy, a cytosolic lipase-independent autophagic pathway. [PubMed: 23708524 Required for the exosomal release of SDCBP, CD63 and syndecan (By similarity]
• Protein Sequence: MTSRKKVLLKVIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTKEVMVDDRLVTMQIWDTAGQERFQSLGVAFYRGADCCVLVFDVTAPNTFKTLDSWRDEFLIQASPRDPENFPFVVLGNKIDLENRQVATKRAQAWCYSKNNIPYFETSAKEAINVEQAFQTIARNALKQETEVELYNEFPEPIKLDKNDRAKASAESCSC

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	------MTSRKKVLL ------CCCHHHEEE	36.92	-
17	Phosphorylation	KVIILGDSGVGKTSL EEEECCCCCCCHHHH	33.31	22817900
31	Acetylation	LMNQYVNKKFSNQYK HHHHHHHHHHCHHHC	45.19	22826441
32	Malonylation	MNQYVNKKFSNQYKA HHHHHHHHHCHHHCC	49.15	26320211
34	Phosphorylation	QYVNKKFSNQYKATI HHHHHHHCHHHCCEE	31.72	25338131
37	Phosphorylation	NKKFSNQYKATIGAD HHHHCHHHCCEECCC	13.57	29514104
38	Ubiquitination	KKFSNQYKATIGADF HHHCHHHCCEECCCC	29.32	22790023
40	Phosphorylation	FSNQYKATIGADFLT HCHHHCCEECCCCCC	18.78	25338131
72	Phosphorylation	AGQERFQSLGVAFYR CCHHHHHHHCCCHHC	25.12	27087446
78	Phosphorylation	QSLGVAFYRGADCCV HHHCCCHHCCCCEEE	9.82	28833060
83	S-palmitoylation	AFYRGADCCVLVFDV CHHCCCCEEEEEEEE	1.39	28680068
84	Glutathionylation	FYRGADCCVLVFDVT HHCCCCEEEEEEEEC	2.46	24333276
111	Phosphorylation	DEFLIQASPRDPENF CEEEEECCCCCCCCC	12.23	28066266
126	Ubiquitination	PFVVLGNKIDLENRQ CEEEECCEEECCCCH	35.48	22790023
143	S-palmitoylation	TKRAQAWCYSKNNIP HHHHHHHHHHCCCCC	2.85	28526873
143	Glutathionylation	TKRAQAWCYSKNNIP HHHHHHHHHHCCCCC	2.85	24333276
144	Phosphorylation	KRAQAWCYSKNNIPY HHHHHHHHHCCCCCC	16.39	25195567
168	Phosphorylation	NVEQAFQTIARNALK CHHHHHHHHHHHHHH	15.34	29514104
178	Phosphorylation	RNALKQETEVELYNE HHHHHHCCEEEHHHC	42.72	25159016
183	Phosphorylation	QETEVELYNEFPEPI HCCEEEHHHCCCCCC	10.11	25159016
191	Ubiquitination	NEFPEPIKLDKNDRA HCCCCCCCCCCCHHH	62.44	22790023
194	Ubiquitination	PEPIKLDKNDRAKAS CCCCCCCCCHHHHHH	71.79	22790023
205	Geranylgeranylation	AKASAESCSC----- HHHHHHHCCC-----	3.47	-
207	Geranylgeranylation	ASAESCSC------- HHHHHCCC-------	8.30	-
207	Methylation	ASAESCSC------- HHHHHCCC-------	8.30	-

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

Oops, there are no upstream regulatory protein records of RAB7A_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RAB7A_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RAB7A_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RN115_MOUSE	Rnf115	physical	12972561
RAE1_HUMAN	CHM	physical	26496610
SDCG8_HUMAN	SDCCAG8	physical	26496610
TPX2_HUMAN	TPX2	physical	26496610
PDS5A_HUMAN	PDS5A	physical	26496610
AAMDC_HUMAN	AAMDC	physical	26496610
S38AA_HUMAN	SLC38A10	physical	26496610

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, AND MASSSPECTROMETRY.
PubMed: 19144319