Contact Molecules for Homologous Proteins
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PID	QueryLength	Homolgous Sequence in PDB	UniProt Query	TITLE
2691701	207	10	P51149(RAB7A_HUMAN)	RecName: Full=Ras-related protein Rab-7a ; EC=3.6.5.2 ;
QUERYSEQ	MTSRKKVLLKVIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTKEVMVDDRLVTMQIWDTAGQERFQSLGVAFYRGADCCVLVFDVTAPNTFKTLDSWRDEFLIQASPRDPENFPFVVLGNKIDLENRQVATKRAQAWCYSKNNIP YFETSAKEAINVEQAFQTIARNALKQETEVELYNEFPEPIKLDKNDRAKASAESCSC

  [n]:site number of query sequence.  [a]:amino acid of query sequence.  [s]:predicted secondary structure.
  [e]:predicted exposed/buried.  [acc]:predicted relative accesssibility(%).  [pdb]:PDB code of homologous structure.
  [contact_mols]:predicted binding molecules  [observed aa]:Observed amino acids among homologous sequences.  [feature table]:UniProt Feature Table
  [variant]:UniProt Human Variant.

n	a	s	e	acc	pdb	contact_mols	observed aa	feature table	variant
1	M	-	-	-	-		M	INIT_MET /note="Removed" INIT_MET /note="Removed" DISORDER predicted by DISOPRED
2	T	-	-	-	-		STANDLGPV	MOD_RES /note="N-acetylthreonine" MOD_RES /note="N-acetylthreonine" DISORDER predicted by DISOPRED
3	S	-	-	-	-		SPNGKTAEDIQFLY	DISORDER predicted by DISOPRED
4	R	-	-	-	-		RKQENGSTDHIYP
5	K	-	-	-	-		KRSQYENADFHLPT
6	K		e	66.0	1vg0_B		KEDSRNIQVPAH
7	V		e	50.0	1vg8_A		VLIAKPTDGHSYENRFMCQ
8	L	E	e	44.4	1vg8_A		LVEIAFRDMQKNSTY	MUTAGEN /note="L->A: Abolishes interaction with RILP and reduces its localization to late endosomal/lysosomal compartments." MUTAGEN /note="L->A: Abolishes interaction with RILP and reduces its localization to late endosomal/lysosomal compartments."
9	L	E	b	0.0	1vg8_A		FLIVMYARCHS
10	K	E	b	17.5	1vg8_A		KREHNQST	MUTAGEN /note="K->A: Abolishes interaction with RILP and localization to late endosomal/lysosomal compartments." MUTAGEN /note="K->A: Abolishes interaction with RILP and localization to late endosomal/lysosomal compartments."
11	V	E	b	0.0	1vg8_A		VILCFAMTY
12	I	E	b	0.0	1vg8_A		VLIATGMCS
13	I	E	b	1.2	1vg8_A		LVIMFTACS
14	L	E	b	0.0	1vg8_A		VLIAMCFNRT
15	G		b	0.0	1vg8_A		G	BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791"
16	D		e	20.4	1vg8_A	compound GDP GNP	DLAERNSPGHQYKM	BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791"
17	S	T	e	38.3	1vg8_A	hetero RAE1_RAT compound GDP GNP	SGPADQRVYLNTCEIKM	BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791"
18	G	T	e	40.5	1vg8_A	compound GDP GNP	GANSDECKQRTFHLMY	BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791"
19	V	S	b	0.0	1vg8_A	compound GDP GNP	VASTCHI	BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791"
20	G	S	b	14.3	1vg8_A	compound GDP GNP	GA	BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791"
21	K	H	b	5.2	1vg8_A	compound GDP GNP	KI	BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791"
22	T	H	e	26.0	1vg8_A	compound GDP GNP metal MG	TSGKL	MUTAGEN /note="T->N: Abolishes localization on late endosomes, lysosomes and phagosomes and reduces phagosomal fusions. Abolishes association of RILP with the phagosomes. No loss of interaction with CLN5. No loss of interaction with PRPH. Reduced interaction with VPS13A. Inhibits SARS-CoV-2 infection." ECO:0000269|PubMed:22431521, ECO:0000269|PubMed:23179371, ECO:0000269|PubMed:30709847, ECO:0000269|PubMed:34159616" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" MUTAGEN /note="T->N: Abolishes localization on late endosomes, lysosomes and phagosomes and reduces phagosomal fusions. Abolishes association of RILP with the phagosomes. No loss of interaction with CLN5. No loss of interaction with PRPH. Reduced interaction with VPS13A. Inhibits SARS-CoV-2 infection." ECO:0000269|PubMed:22431521, ECO:0000269|PubMed:23179371, ECO:0000269|PubMed:30709847, ECO:0000269|PubMed:34159616" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791"
23	S	H	e	26.6	1vg8_A	compound GDP GNP	SATCNQEFKRV
24	L	H	b	1.1	1vg8_A		LIFMVT
25	M	H	b	4.8	1vg8_A		LVITAMCFRW
26	N	H	e	21.8	1vg8_A		NILVHKESQRYFMTADGC
27	Q	H	b	12.2	1vg8_A		RQSAVKLTCEINFHMY
28	Y	H	b	3.0	1vg8_A		FLYIHADRSTVW
29	V	H	b	19.3	1vg8_A		TLVAICSMGKRQDFHN
30	N	H	e	47.9	1vg8_A		TDGKEQSNRHYLACFM
31	K	S	e	72.6	1vg8_A		GNKDRESTLQAHV
32	K		e	50.9	1vg8_A		ERKQTSAHDIGNPVCLMY		K->E:(17.0 %):LB/B - dbSNP:rs1154975
33	F		e	33.0	1vg8_A	compound GDP GNP	FYVIADGLTEKPRSW
34	S		e	50.8	1vg8_A	compound GNP GDP	SPVEADINQTGLKRCFHMY	BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791"
35	N	S	e	68.5	1vg8_A	compound GNP GDP	EDKSTGPNIALMQVHFRY	BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791"
36	Q	S	e	80.1	1vg8_A		EDQKVGNSTAHRILPFMY	BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791"
37	Y		e	63.5	1vg8_A	compound GNP	YHTSEFVILPQCMAKRW	BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" MOTIF /note="Effector region" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" MOTIF /note="Effector region"
38	K		e	83.5	1vg8_A		EKDIVAQTLSGPRHNFMY	BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" MOTIF /note="Effector region" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" MOTIF /note="Effector region"
39	A		e	23.2	1vg8_A	compound GNP	PASGLTQCEHKMNRIVWY	BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" MOTIF /note="Effector region" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" MOTIF /note="Effector region"
40	T		e	21.4	1vg8_A	compound GNP metal MG	TGSNEPIVAKLQW	BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" MOTIF /note="Effector region" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" MOTIF /note="Effector region"
41	I		e	64.3	1vg8_A		IVLTAENQSDFGHKY	MOTIF /note="Effector region" MOTIF /note="Effector region"
42	G	S	b	17.9	1vg8_A	hetero RAE1_RAT	GFTEAPSLQRDHIKVY	MOTIF /note="Effector region" MOTIF /note="Effector region"
43	A	E	e	23.2	1vg8_A	hetero RAE1_RAT	VEAIRDFGLQCNSPKT	MOTIF /note="Effector region" MOTIF /note="Effector region"
44	D	E	e	68.5	1vg8_A	hetero RAE1_RAT	DNETARSHIKLYCGV	MOTIF /note="Effector region" MOTIF /note="Effector region"
45	F	E	e	36.4	1vg8_A	hetero RAE1_RAT	FYVILSTMQRACDEGHKNP	MOTIF /note="Effector region" MOTIF /note="Effector region"
46	L	E	e	32.6	1vg8_A		YLVKGAFHIRDENSQTCMP
47	T	E	e	51.3	1vg8_A		TSRVAEIKNLPYDMCFHQW
48	K	E	e	23.6	1vg8_A		KREQALTPSVGHIYDFNW
49	E	E	e	76.4	1vg8_A		ETQSHKDNVAIRLPFGMY
50	V	E	b	16.7	1vg8_A		VILMFCYAESTDGNW
51	M	E	e	57.0	1vg8_A		TEVLMQSHINYADFPRCGK
52	V	S	b	4.7	1vg8_A		VILTPAGKMRYCEFNQSW
53	D	S	e	67.3	1vg8_A		DENGKRSTPQAFHL
54	D	S	e	96.9	1vg8_A		GDNESKHACFILQRTVY
55	R		e	44.7	1vg8_A		KREQTGADNSHIVLMP
56	L	E	e	63.5	1vg8_A		TLKPERSVQDGIANCFHMY
57	V	E	b	2.0	1vg8_A		VIYLCFAMHTEKPS
58	T	E	e	30.5	1vg8_A		KTLSRNPEHVADGIMQCFY
59	M	E	b	0.0	1vg8_A		LFIVAMTCEY
60	Q	E	b	14.8	1vg8_A		QEDHNGKRLAMSTFIV
61	I	E	b	0.0	1vg8_A		ILVFMACT
62	W	E	b	11.6	1vg8_A	hetero RAE1_RAT	WLFIYVQRMTCH
63	D	E	b	6.2	1vg8_A	hetero RAE1_RAT metal MG	DEAGN	BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791"
64	T	E	b	4.5	1vg8_A	compound GNP	TIVELSAFCGMNPY	BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791"
65	A		b	0.9	1vg8_A	hetero RAE1_RAT compound GNP	AGPSCENRDFHKQTVW	BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791"
66	G	S	b	16.7	1vg8_A	compound GNP	GSDEAKPQ	BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791"
67	Q	S	e	23.5	1vg8_A	hetero RAE1_RAT	QHSLDGKPTAEINCMRW	MUTAGEN /note="Q->L: Does not abolish localization on late endosomes, lysosomes and phagosomes and does not reduce phagosomal fusions. No loss of interaction with CLN5 and VPS13A. Increases interaction with PRPH. Inhibits SARS-CoV- 2 infection." ECO:0000269|PubMed:22431521, ECO:0000269|PubMed:23179371, ECO:0000269|PubMed:30709847, ECO:0000269|PubMed:34159616" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" MUTAGEN /note="Q->L: Does not abolish localization on late endosomes, lysosomes and phagosomes and does not reduce phagosomal fusions. No loss of interaction with CLN5 and VPS13A. Increases interaction with PRPH. Inhibits SARS-CoV- 2 infection." ECO:0000269|PubMed:22431521, ECO:0000269|PubMed:23179371, ECO:0000269|PubMed:30709847, ECO:0000269|PubMed:34159616" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791"
68	E	G	e	81.9	1vg8_A		EDPAQRSGHKNCFILTVY
69	R	G	e	74.3	1vg8_A	hetero RAE1_RAT	REKDASHQFGILTYCNPVW
70	F	G	e	25.4	1vg8_A	hetero RAE1_RAT	FYLVAIGCHKDEMNQW
71	Q	S	e	31.6	1vg8_A	hetero RAE1_RAT metal K precipitant	REQSDKGNTHLAPCVY
72	S		e	34.4	1vg8_A	hetero RAE1_RAT	SARTEGKNQPCDIVFHLW	MOD_RES /note="Phosphoserine" ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" MOD_RES /note="Phosphoserine" ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
73	L	S	e	100.6	1vg8_A		LMIVTCFAEGHKNPQRSWY
74	G		e	61.9	1vg8_A	hetero RAE1_RAT	RGTWAPNDILSQVCEFHK
75	V		e	24.7	1vg8_A	hetero RAE1_RAT	PDSRIEAKVTLQHNCFGMY
76	A	G	e	53.6	1vg8_A	hetero RAE1_RAT	ASLHQREKMITVGCDFNPW
77	F	G	b	14.4	1vg8_A	hetero RAE1_RAT	YFSRCGILAVWDEHNQ
78	Y	G	b	3.5	1vg8_A		YIMLSFCATGWDHV
79	R	T	e	56.5	1vg8_A	hetero RAE1_RAT	RKEPSIQTAGNHVLMY
80	G	T	e	67.9	1vg8_A		GDNQSWTAKRVEHLCFIMY
81	A		b	4.5	1vg8_A		ATGSVCIPFLQR
82	D	S	b	7.4	1vg8_A		DNHQEVSALMIKRTY
83	C	E	b	0.0	1vg8_A		GAVCILRFHMTY
84	C	E	b	0.0	1vg8_A		VFAICLYHGT
85	V	E	b	0.0	1vg8_A		LIVMCFGAT
86	L	E	b	0.0	1vg8_A		LIVFYCMAGHN
87	V	E	b	0.0	1vg8_A		VCMILATFGSY
88	F	E	b	0.0	1vg8_A		YFVIHLQ
89	D	E	b	8.0	1vg8_A		DSANEGIV
90	V	T	b	0.0	1vg8_A		IVLSAGCMNPTY
91	T	T	b	11.0	1vg8_A		TDSANVEHICGQKLM
92	A		e	25.0	1vg8_A		SDNRAKETCQVGHILM
93	P	H	e	20.9	1vg8_A		RPEKQTAGLSHMVYCDFIN
94	N	H	e	76.4	1vg8_A		EDSKQANGRITVHLPW
95	T	H	b	9.7	1vg8_A		STRADNEGHKMP
96	F	H	b	7.7	1vg8_A		FLYIRVESTACKMQ
97	K	H	e	56.6	1vg8_A		EDQKNLSARTHIGMPVY
98	T	T	e	26.0	1vg8_A	precipitant	NSEAKRHDLVPTGIQYCFM
99	L	H	b	0.0	1vg8_A		VLIAMSCTDFHK
100	D	H	e	35.2	1vg8_A		KEDSQAPRTNGHILYMV
101	S	H	e	65.6	1vg8_A	precipitant	KSNERTAQIDHLGPFMYV
102	W	H	b	7.6	1vg8_A	precipitant	WLAFYIEKSVCGMQ
103	R	H	b	7.9	1vg8_A		RLIKYHVEAMSFPQTWDGN
104	D	H	e	48.1	1vg8_A		EDKQPNSRATGIHLVFMY
105	E	H	e	23.1	1vg8_A	precipitant	EQDKNTLRAPSCGHIMV
106	F	H	b	0.0	1vg8_A		LIFVAYEMWHKSTCDGNPQR
107	L	H	b	17.4	1vg8_A		LIRVKQADEHFSCMNTYGPW
108	I	H	e	69.0	1vg8_A	hetero RAE1_RAT	LRIKASVQDETNPGHYCFM
109	Q	H	e	32.1	1vg8_A		HQKELRYNSTVIMADFGPCW
110	A	H	b	8.0	1vg8_A		ALVRSTCDFGIKENHPQYW
111	S		e	67.2	1vg8_A	hetero RAE1_RAT	RSAGKDNTELHCPVFIQYM
112	P		b	17.8	1vg8_A		PVASGETHKLDINQRCFYMW
113	R	S	e	38.3	1vg8_A	hetero RAE1_RAT	RKELSAGHDNPQYFITVCM
114	D	S	e	54.9	1vg8_A		DEGNLVASTQRCHIPFKYM
115	P	G	e	39.5	1vg8_A		PLAKSGTNCDEIHQRVMYFW
116	E	G	e	56.3	1vg8_A		EDKSAQPRTVGHLNIYCFM
117	N	G	e	58.2	1vg8_A		NGDSEKRTAHPLQCIVY
118	F	S	b	2.4	1vg8_A		VILAFTMYCSEGQ
119	P		b	12.4	1vg8_A		PVIATKLNQSCEGHMR
120	F	E	b	1.0	1vg8_A		IVLFMKARTYCGNSW
121	V	E	b	0.0	1vg8_A		VILMATCFGY
122	V	E	b	0.0	1vg8_A		LVIMAG
123	L	E	b	1.1	1vg8_A		VLIACFTM
124	G	E	b	0.0	1vg8_A		GARIQFPSV
125	N	E	b	3.6	1vg8_A	compound GDP GNP	NTCLDHS	BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791"
126	K		e	28.3	1vg8_A	compound GDP GNP	KQRHNY	BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791"
127	I	T	e	20.5	1vg8_A		CSIAVLQTKMRDFGNY	BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791"
128	D	T	e	33.3	1vg8_A	compound GDP GNP	DASEHQT	BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791"
129	L	S	e	37.1	1vg8_A	compound GDP GNP	LMIVKARCDEFHPQST		L->F:(1.0 %):LP/P Charcot-Marie-Tooth disease, axonal, 2B (CMT2B) dbSNP:rs1219090 [MIM:600882]
130	E	S	e	99.5	1vg8_A		ERDSAKPQTGHLNVCIMY
131	N		e	54.5	1vg8_A		DNSEHKGTAQRFILMPVY
132	R		e	37.9	1vg8_A		REKDQSGYAHLNTVIMP
133	Q		e	61.7	1vg8_A		QREKVADLPSMNTCGHI
134	V	S	b	0.0	1vg8_A		VIAELQGTDKFNPRS
135	A		e	48.2	1vg8_A		SVDTPAGIKLQECFNRY
136	T	H	e	43.5	1vg8_A		TSDEKIPVALFQRYMNGHW
137	K	H	e	85.8	1vg8_A		EKDSAQNRTHIPYFGLV
138	R	H	e	37.2	1vg8_A		ERQKDTAILMNVFGHPSWY
139	A	H	b	0.0	1vg8_A		AGEILVDQSTMHKNPRY
140	Q	H	e	39.8	1vg8_A		QEKGRALDNHSCFIMPTVY
141	A	H	e	51.8	1vg8_A		AEKQLSGDRINVHTFMPY
142	W	H	b	13.1	1vg8_A		LWFYAEKVMQISGRTCDHNP
143	C	H	b	0.7	1vg8_A		ACLFSVGRIKPTDEMNQY
144	Y	H	e	70.9	1vg8_A		AKLERYDHNSVFGIQTMPC
145	S	H	e	59.4	1vg8_A		SEDKRAQGTNVHLMP
146	K	T	b	18.4	1vg8_A		KEIRLQDHMSAGNVPTYFW
147	N	T	e	53.3	1vg8_A		GNLKEFRHDYAMQSTWCIPV
148	N	S	e	61.8	1vg8_A		GNARSDEKFIQTCHLV
149	I		b	7.0	1vg8_A		ILCVAMFTRSYKNP
150	P		e	31.0	1vg8_A		PKSALGQTCEFHIMRDVYN
151	Y	E	b	12.6	1vg8_A		FYLCHIVWAM
152	F	E	b	11.5	1vg8_A		FILYMVCHTWEGKPQS
153	E	E	b	16.1	1vg8_A		EDSAFQRGHKMNPTVY
154	T		b	0.0	1vg8_A		TCIVALSEGMNQ
155	S	B	b	0.0	1vg8_A	compound GDP GNP	SCNAHILQT
156	A	T	b	0.9	1vg8_A	compound GDP GNP	ASVCPGKLT	BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791"
157	K	T	e	37.3	1vg8_A	compound GDP GNP	KLARTMSEFIQV	BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791"	K->N:(0.0 %):LP/P Charcot-Marie-Tooth disease, axonal, 2B (CMT2B) dbSNP:rs1219090 [MIM:600882]
158	E	T	e	57.3	1vg8_A		TEDSLNQAYKCFHIMV
159	A	T	e	49.1	1vg8_A		NGSRAQDKHMCEFL
160	I	B	e	38.6	1vg8_A		IETQLYDFHSKVMARWCNP
161	N	S	e	30.9	1vg8_A		NGSHRTCDEKLQ		N->T:(2.0 %):LP/P Charcot-Marie-Tooth disease, axonal, 2B (CMT2B) dbSNP:rs1219090 [MIM:600882]
162	V	H	b	2.7	1vg8_A		VILFTAEKMY		V->M:(1.0 %):LP/P Charcot-Marie-Tooth disease, axonal, 2B (CMT2B) dbSNP:rs1219090 [MIM:600882]
163	E	H	e	39.7	1vg8_A		EDKNQIRTYLVAFGHPS
164	Q	H	e	54.6	1vg8_A		EDQKALNRSITCGHMP
165	A	H	b	0.9	1vg8_A		AVLPISMTCDFGK
166	F	H	b	1.0	1vg8_A		FLAIKMPTVY
167	Q	H	e	56.1	1vg8_A		EQLDRTYHIKNMSFVA
168	T	H	b	19.5	1vg8_A		ETADKSWLRYCGHMNQVFI
169	I	H	b	0.0	1vg8_A		LIAVMTCF
170	A	H	b	1.8	1vg8_A		AVILTSCEFGMQR
171	R	H	e	35.2	1vg8_A		RKEQASCHLDMNT
172	N	H	e	21.8	1vg8_A		EKADNQSVHLTIRCF
173	A	H	b	0.0	1vg8_A		IAVLSHKMCFGTY
174	L	H	b	10.7	1vg8_A		LIRKVFMPESYACNQT
175	K	H	e	66.0	1vg8_A		KQRENTASGLIMPYDFHV
176	Q	H	b	13.8	1vg8_A		QRKNELDSTAHMPYGV
177	E	H	b	11.1	1vg8_A		ERKQSDPHNMFGILVYAT
178	T	H	e	37.0	1vg8_A		TSGKRAEMNPDQCILVH
179	E	H	e	37.7	1vg8_A		ESKQRLDAGTHPIMNVY
180	V	H	e	27.3	1vg8_A		VLIQGTDEKNPRSACFMW	MUTAGEN /note="V->A: Abolishes interaction with RILP and localization to late endosomal/lysosomal compartments." MUTAGEN /note="V->A: Abolishes interaction with RILP and localization to late endosomal/lysosomal compartments." DISORDER predicted by DISOPRED
181	E	H	e	57.8	1vg8_A		EQDAHKSLNPRTVMFGI	DISORDER predicted by DISOPRED
182	L	H	e	48.9	1vg8_A		LIAVEFKTGQRDNSYHMP	MUTAGEN /note="L->A: Does not abolish interaction with RILP and localization to late endosomal/lysosomal compartments. Does not abolish interaction with RILP and localization to late endosomal/lysosomal compartments; when associated with A- 183." MUTAGEN /note="L->A: Does not abolish interaction with RILP and localization to late endosomal/lysosomal compartments. Does not abolish interaction with RILP and localization to late endosomal/lysosomal compartments; when associated with A- 183." DISORDER predicted by DISOPRED
183	Y	H	e	37.0	1vg8_A		FYHGLSEVAIKPRWTDNQM	MUTAGEN /note="Y->A: Does not abolish interaction with RILP and localization to late endosomal/lysosomal compartments. Does not abolish interaction with RILP and localization to late endosomal/lysosomal compartments; when associated with A- 182." MUTAGEN /note="Y->A: Does not abolish interaction with RILP and localization to late endosomal/lysosomal compartments. Does not abolish interaction with RILP and localization to late endosomal/lysosomal compartments; when associated with A- 182." DISORDER predicted by DISOPRED
184	N	H	e	74.5	1vg8_A		NGSADREQPTHIKMVCFL	DISORDER predicted by DISOPRED
185	E	H	e	71.9	1vg8_A		EQKDGLNSAIVHRPTMY	DISORDER predicted by DISOPRED
186	F	S	e	64.1	1vg8_A	hetero RAE1_RAT	FLSADGIRKNTVQEMPY	DISORDER predicted by DISOPRED
187	P		e	58.9	1vg8_A		PGSDTKIMNAQVELR	DISORDER predicted by DISOPRED
188	E		e	74.4	1vg8_A		EDQSKLNPAGRTIVH	DISORDER predicted by DISOPRED
189	P		e	99.2	1vg8_A	hetero RAE1_RAT	PSGTDEAHQRIKNVL	DISORDER predicted by DISOPRED
190	I		e	129.8	1vg8_A	hetero RAE1_RAT	IVLGSMPTADEKQRN	DISORDER predicted by DISOPRED
191	K		e	77.8	1vg0_B	hetero RAE1_RAT	KRSDEQAGLNTHIVP	CROSSLNK /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" CROSSLNK /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" DISORDER predicted by DISOPRED
192	L		e	123.0	1vg0_B	hetero RAE1_RAT	LIVKPSMFREQDT	DISORDER predicted by DISOPRED
193	D	-	-	-	-		DSNEGTKRVIAPYHQ	DISORDER predicted by DISOPRED
194	K	-	-	-	-		KSLNTIPRAEFGQCDVYH	CROSSLNK /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" CROSSLNK /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" DISORDER predicted by DISOPRED
195	N	-	-	-	-		NGSHTKQAEPRDLIV	DISORDER predicted by DISOPRED
196	D	-	-	-	-		DNPQSTAERGLKHW	DISORDER predicted by DISOPRED
197	R	-	-	-	-		RKQESGPITLVAYDMN	DISORDER predicted by DISOPRED
198	A	-	-	-	-		ASKPGQHETVILMRN	DISORDER predicted by DISOPRED
199	K	-	-	-	-		KQRSANTEGLPDFMV	DISORDER predicted by DISOPRED
200	A	-	-	-	-		SAGTKPRNQDCEHLV	DISORDER predicted by DISOPRED
201	S	-	-	-	-		SAQTNEGKPMDLRWYCV	DISORDER predicted by DISOPRED
202	A	-	-	-	-		AGSKVEFCLPQTDIN	DISORDER predicted by DISOPRED
203	E	-	-	-	-		SGEQKADNRCFYMPTVIL	DISORDER predicted by DISOPRED
204	S	-	-	-	-		SGCKNATEHRQVP	DISORDER predicted by DISOPRED
205	C	-	-	-	-		CSAIKGTV	LIPID /note="S-geranylgeranyl cysteine" LIPID /note="S-geranylgeranyl cysteine" DISORDER predicted by DISOPRED
206	S	-	-	-	-		SGAHCENQTVYIKP	DISORDER predicted by DISOPRED
207	C	-	-	-	-		C	MOD_RES /note="Cysteine methyl ester" LIPID /note="S-geranylgeranyl cysteine" MOD_RES /note="Cysteine methyl ester" LIPID /note="S-geranylgeranyl cysteine" DISORDER predicted by DISOPRED