dbPTM

RAB7A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RAB7A_HUMAN
UniProt AC	P51149
Protein Name	Ras-related protein Rab-7a
Gene Name	RAB7A
Organism	Homo sapiens (Human).
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 M.tuberculosis. 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. [PubMed: 11179213]
Protein Sequence	MTSRKKVLLKVIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTKEVMVDDRLVTMQIWDTAGQERFQSLGVAFYRGADCCVLVFDVTAPNTFKTLDSWRDEFLIQASPRDPENFPFVVLGNKIDLENRQVATKRAQAWCYSKNNIPYFETSAKEAINVEQAFQTIARNALKQETEVELYNEFPEPIKLDKNDRAKASAESCSC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MTSRKKVLL ------CCCHHHEEE	36.92	25944712
17	Phosphorylation	KVIILGDSGVGKTSL EEEECCCCCCCHHHH	33.31	21406692
21	Ubiquitination	LGDSGVGKTSLMNQY CCCCCCCHHHHHHHH	32.31	-
28	Nitration	KTSLMNQYVNKKFSN HHHHHHHHHHHHHCH	10.86	-
28	Phosphorylation	KTSLMNQYVNKKFSN HHHHHHHHHHHHHCH	10.86	-
31	Ubiquitination	LMNQYVNKKFSNQYK HHHHHHHHHHCHHHC	45.19	-
31	2-Hydroxyisobutyrylation	LMNQYVNKKFSNQYK HHHHHHHHHHCHHHC	45.19	-
31	Malonylation	LMNQYVNKKFSNQYK HHHHHHHHHHCHHHC	45.19	26320211
31	Acetylation	LMNQYVNKKFSNQYK HHHHHHHHHHCHHHC	45.19	25953088
32	Ubiquitination	MNQYVNKKFSNQYKA HHHHHHHHHCHHHCC	49.15	21906983
32	Acetylation	MNQYVNKKFSNQYKA HHHHHHHHHCHHHCC	49.15	25953088
34	Phosphorylation	QYVNKKFSNQYKATI HHHHHHHCHHHCCEE	31.72	25849741
37	Phosphorylation	NKKFSNQYKATIGAD HHHHCHHHCCEECCC	13.57	-
38	Ubiquitination	KKFSNQYKATIGADF HHHCHHHCCEECCCC	29.32	21906983
40	Phosphorylation	FSNQYKATIGADFLT HCHHHCCEECCCCCC	18.78	27050516
47	Phosphorylation	TIGADFLTKEVMVDD EECCCCCCCEEEECC	25.75	20860994
48	Acetylation	IGADFLTKEVMVDDR ECCCCCCCEEEECCE	50.92	26051181
48	Ubiquitination	IGADFLTKEVMVDDR ECCCCCCCEEEECCE	50.92	21890473
55	Methylation	KEVMVDDRLVTMQIW CEEEECCEEEEEEEE	26.96	115489977
58	Phosphorylation	MVDDRLVTMQIWDTA EECCEEEEEEEECCC	14.14	21406692
64	Phosphorylation	VTMQIWDTAGQERFQ EEEEEECCCCHHHHH	20.07	21406692
72	Phosphorylation	AGQERFQSLGVAFYR CCHHHHHHHCCCHHC	25.12	29255136
78	Phosphorylation	QSLGVAFYRGADCCV HHHCCCHHCCCCEEE	9.82	23403867
97	Ubiquitination	VTAPNTFKTLDSWRD ECCCCCCCCCHHHCC	46.25	-
98	Phosphorylation	TAPNTFKTLDSWRDE CCCCCCCCCHHHCCE	31.44	28102081
101	Phosphorylation	NTFKTLDSWRDEFLI CCCCCCHHHCCEEEE	27.42	22817900
111	Phosphorylation	DEFLIQASPRDPENF CEEEEECCCCCCCCC	12.23	29255136
126	Ubiquitination	PFVVLGNKIDLENRQ CEEEECCEEECCCCH	35.48	21906983
132	Methylation	NKIDLENRQVATKRA CEEECCCCHHHHHHH	23.99	115489985
137	Ubiquitination	ENRQVATKRAQAWCY CCCHHHHHHHHHHHH	35.68	21906983
144	Phosphorylation	KRAQAWCYSKNNIPY HHHHHHHHHCCCCCC	16.39	28152594
145	Phosphorylation	RAQAWCYSKNNIPYF HHHHHHHHCCCCCCC	26.27	28152594
146	Acetylation	AQAWCYSKNNIPYFE HHHHHHHCCCCCCCC	27.78	26051181
146	Ubiquitination	AQAWCYSKNNIPYFE HHHHHHHCCCCCCCC	27.78	-
151	Phosphorylation	YSKNNIPYFETSAKE HHCCCCCCCCCCHHH	15.39	28152594
154	Phosphorylation	NNIPYFETSAKEAIN CCCCCCCCCHHHHCC	24.88	28152594
155	Phosphorylation	NIPYFETSAKEAINV CCCCCCCCHHHHCCH	30.10	28152594
157	Ubiquitination	PYFETSAKEAINVEQ CCCCCCHHHHCCHHH	47.66	-
168	Phosphorylation	NVEQAFQTIARNALK CHHHHHHHHHHHHHH	15.34	29255136
175	Ubiquitination	TIARNALKQETEVEL HHHHHHHHHCCEEEH	43.61	21906983
178	Phosphorylation	RNALKQETEVELYNE HHHHHHCCEEEHHHC	42.72	21945579
183	Phosphorylation	QETEVELYNEFPEPI HCCEEEHHHCCCCCC	10.11	21945579
191	Ubiquitination	NEFPEPIKLDKNDRA HCCCCCCCCCCCHHH	62.44	21906983
194	Ubiquitination	PEPIKLDKNDRAKAS CCCCCCCCCHHHHHH	71.79	-
201	Phosphorylation	KNDRAKASAESCSC- CCHHHHHHHHHCCC-	31.68	-
204	Phosphorylation	RAKASAESCSC---- HHHHHHHHCCC----	15.85	-
205	Geranylgeranylation	AKASAESCSC----- HHHHHHHCCC-----	3.47	-
206	Phosphorylation	KASAESCSC------ HHHHHHCCC------	31.94	-
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, ...)

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 RAB7A_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RAB7A_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 RAB7A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RAE1_HUMAN	CHM	physical	12576024
RILP_HUMAN	RILP	physical	11179213
RAE1_HUMAN	CHM	physical	9563513
RAB17_HUMAN	RAB17	physical	10329441
RAB4A_HUMAN	RAB4A	physical	10329441
RAB4B_HUMAN	RAB4B	physical	10329441
RAB5A_HUMAN	RAB5A	physical	10329441
RAB5B_HUMAN	RAB5B	physical	10329441
RAB6A_HUMAN	RAB6A	physical	10329441
RB22A_HUMAN	RAB22A	physical	10329441
PSA7_HUMAN	PSMA7	physical	14998988
RN115_HUMAN	RNF115	physical	12972561
RB11A_HUMAN	RAB11A	physical	22939629
RAB8A_HUMAN	RAB8A	physical	22939629
RB11B_HUMAN	RAB11B	physical	22939629
KR109_HUMAN	KRTAP10-9	physical	25416956
KR103_HUMAN	KRTAP10-3	physical	25416956
SNX3_HUMAN	SNX3	physical	24344282
VP26A_HUMAN	VPS26A	physical	24344282
VPS35_HUMAN	VPS35	physical	24344282
VPS29_HUMAN	VPS29	physical	24344282
VPS11_HUMAN	VPS11	physical	25445562
VPS16_HUMAN	VPS16	physical	25445562
VPS18_HUMAN	VPS18	physical	25445562
VPS39_HUMAN	VPS39	physical	25445562
VPS41_HUMAN	VPS41	physical	25445562
RILP_HUMAN	RILP	physical	25445562
ANXA2_HUMAN	ANXA2	physical	26344197
ARL8B_HUMAN	ARL8B	physical	26344197
ATPO_HUMAN	ATP5O	physical	26344197
HNRPK_HUMAN	HNRNPK	physical	26344197
ENPL_HUMAN	HSP90B1	physical	26344197
GRP75_HUMAN	HSPA9	physical	26344197
MECR_HUMAN	MECR	physical	26344197
RAB2A_HUMAN	RAB2A	physical	26344197
RAB5A_HUMAN	RAB5A	physical	26344197
RAB5B_HUMAN	RAB5B	physical	26344197
RAB5C_HUMAN	RAB5C	physical	26344197
RAB8A_HUMAN	RAB8A	physical	26344197
RAB8B_HUMAN	RAB8B	physical	26344197
RHEB_HUMAN	RHEB	physical	26344197
ABCD1_HUMAN	ABCD1	physical	26496610
RHOG_HUMAN	RHOG	physical	26496610
AT2A2_HUMAN	ATP2A2	physical	26496610
AT2B1_HUMAN	ATP2B1	physical	26496610
VATB2_HUMAN	ATP6V1B2	physical	26496610
VPP1_HUMAN	ATP6V0A1	physical	26496610
VAS1_HUMAN	ATP6AP1	physical	26496610
CAV1_HUMAN	CAV1	physical	26496610
COF1_HUMAN	CFL1	physical	26496610
AP2M1_HUMAN	AP2M1	physical	26496610
CBPM_HUMAN	CPM	physical	26496610
CPT1A_HUMAN	CPT1A	physical	26496610
STOM_HUMAN	STOM	physical	26496610
FLOT2_HUMAN	FLOT2	physical	26496610
GBB2_HUMAN	GNB2	physical	26496610
PLAK_HUMAN	JUP	physical	26496610
KTN1_HUMAN	KTN1	physical	26496610
NDUA7_HUMAN	NDUFA7	physical	26496610
NDUA8_HUMAN	NDUFA8	physical	26496610
NDUB4_HUMAN	NDUFB4	physical	26496610
NDUB7_HUMAN	NDUFB7	physical	26496610
NDUB8_HUMAN	NDUFB8	physical	26496610
NDUS1_HUMAN	NDUFS1	physical	26496610
NDUS6_HUMAN	NDUFS6	physical	26496610
NDUV2_HUMAN	NDUFV2	physical	26496610
PYC_HUMAN	PC	physical	26496610
CHM1A_HUMAN	CHMP1A	physical	26496610
PHB_HUMAN	PHB	physical	26496610
ABCD3_HUMAN	ABCD3	physical	26496610
RPN2_HUMAN	RPN2	physical	26496610
SOAT1_HUMAN	SOAT1	physical	26496610
SSFA2_HUMAN	SSFA2	physical	26496610
TFR1_HUMAN	TFRC	physical	26496610
VDAC1_HUMAN	VDAC1	physical	26496610
VDAC2_HUMAN	VDAC2	physical	26496610
RAI3_HUMAN	GPRC5A	physical	26496610
VA0D1_HUMAN	ATP6V0D1	physical	26496610
XPR1_HUMAN	XPR1	physical	26496610
ABCG2_HUMAN	ABCG2	physical	26496610
VATG1_HUMAN	ATP6V1G1	physical	26496610
MLEC_HUMAN	MLEC	physical	26496610
PIEZ1_HUMAN	PIEZO1	physical	26496610
IST1_HUMAN	IST1	physical	26496610
LPPRC_HUMAN	LRPPRC	physical	26496610
FLOT1_HUMAN	FLOT1	physical	26496610
ERLN1_HUMAN	ERLIN1	physical	26496610
CKAP4_HUMAN	CKAP4	physical	26496610
MIC60_HUMAN	IMMT	physical	26496610
ERLN2_HUMAN	ERLIN2	physical	26496610
PHB2_HUMAN	PHB2	physical	26496610
CHM2B_HUMAN	CHMP2B	physical	26496610
MYOF_HUMAN	MYOF	physical	26496610
QCR8_HUMAN	UQCRQ	physical	26496610
CHM2A_HUMAN	CHMP2A	physical	26496610
STML2_HUMAN	STOML2	physical	26496610
TRPM7_HUMAN	TRPM7	physical	26496610
MIC19_HUMAN	CHCHD3	physical	26496610
MUC13_HUMAN	MUC13	physical	26496610
KDIS_HUMAN	KIDINS220	physical	26496610
MBOA7_HUMAN	MBOAT7	physical	26496610
TMM43_HUMAN	TMEM43	physical	26496610
CYBR1_HUMAN	CYBRD1	physical	26496610
YIPF5_HUMAN	YIPF5	physical	26496610
RILP_HUMAN	RILP	physical	26496610
TMUB1_HUMAN	TMUB1	physical	26496610
MIC25_HUMAN	CHCHD6	physical	26496610
CC115_HUMAN	CCDC115	physical	26496610
MCU_HUMAN	MCU	physical	26496610
CAVN3_HUMAN	PRKCDBP	physical	26496610
CHM4B_HUMAN	CHMP4B	physical	26496610
STT3B_HUMAN	STT3B	physical	26496610
CAVN1_HUMAN	PTRF	physical	26496610
CF120_HUMAN	C6orf120	physical	26496610
RILP_HUMAN	RILP	physical	26911690

Drug and Disease Associations

Kegg Disease
H00264	Charcot-Marie-Tooth disease (CMT); Hereditary motor and sensory neuropathy; Peroneal muscular atroph
OMIM Disease
600882	Charcot-Marie-Tooth disease 2B (CMT2B)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RAB7A_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, AND MASSSPECTROMETRY.	19690332 [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-72, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-183, AND MASSSPECTROMETRY.	17389395 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-183, AND MASSSPECTROMETRY.	15592455 [Abstract]