Contact Molecules for Homologous Proteins


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PID QueryLength Homolgous Sequence in PDB UniProt Query TITLE
3652451 207 40 P51149(RAB7A_HUMAN) RecName: Full=Ras-related protein Rab-7a ; EC=3.6.5.2 ;
QUERYSEQ
MTSRKKVLLKVIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTKEVMVDDRLVTMQIWDTAGQERFQSLGVAFYRGADCCVLVFDVTAPNTFKTLDSWRDEFLIQASPRDPENFPFVVLGNKIDLENRQVATKRAQAWCYSKNNIP
YFETSAKEAINVEQAFQTIARNALKQETEVELYNEFPEPIKLDKNDRAKASAESCSC
[BLAST file for PDB] (plain) (bar) (multiple alignment) [BLAST for UniProt: (plain) (bar) (multiple alignment) (PSSM file) ]
  [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
1M----
M
INIT_MET /note="Removed" INIT_MET /note="Removed" DISORDER predicted by DISOPRED
2T----
STANDLGPV
MOD_RES /note="N-acetylthreonine" MOD_RES /note="N-acetylthreonine" DISORDER predicted by DISOPRED
3S e142.2 1yhn_A hetero RILP_HUMAN
SPNGKTAEDIQFLY
DISORDER predicted by DISOPRED
4R e 41.9 1yhn_A
RKQENGSTDHIYP
5K e 62.3 1yhn_A hetero WDR91_HUMAN
KRSQYENADFHLPT
6K e 66.0 1vg0_B hetero WDR91_HUMAN
KEDSRNIQVPAH
7V e 54.0 1vg8_D
VLIAKPTDGHSYENRFMCQ
8LEe 46.1 1vg8_D hetero RILP_HUMAN G0SGS3_CHATD WDR91_HUMAN PDZD8_HUMAN
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."
9LEb 0.0 1vg8_D
FLIVMYARCHS
10KEb 16.5 1vg8_D hetero RILP_HUMAN G0SGS3_CHATD PDZD8_HUMAN WDR91_HUMAN
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."
11VEb 0.0 1vg8_D
VILCFAMTY
12IEb 0.0 1vg8_D
VLIATGMCS
13IEb 1.2 1vg8_D
LVIMFTACS
14LEb 0.0 1vg8_D
VLIAMCFNRT
15G b 0.0 1vg8_D
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"
16D e 20.4 1vg8_D hetero PDZD8_HUMAN compound GTP GNP GDP 2UK 2UH 2UJ precipitant
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"
17STe 36.7 1vg8_D hetero RAE1_RAT compound GTP GNP GDP 2UK 2UH 2UJ precipitant
SGPADRQVYLNTCEIKM
BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791"
18GTe 41.7 1vg8_D compound GTP GNP GDP 2UK 2UH 2UJ precipitant
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"
19VSb 0.0 1vg8_D compound GTP GNP GDP 2UK 2UH 2UJ precipitant
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"
20GSb 14.3 1vg8_D compound GTP GNP GDP 2UK 2UH 2UJ precipitant
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"
21KHb 5.7 1vg8_D compound GTP GNP GDP 2UK 2UH 2UJ metal MG precipitant
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"
22THe 26.6 1vg8_D compound GTP GNP GDP 2UK 2UH 2UJ metal MG precipitant
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"
23SHe 27.3 1vg8_D compound GTP GNP GDP 2UK 2UH 2UJ
SATCNQEFKRV
24LHb 1.1 1vg8_D
LIFMVT
25MHb 5.3 1vg8_D
LVITAMCFRW
26NHe 21.8 1vg8_D
NILVHKESQRYFMTADGC
27QHb 11.2 1vg8_D precipitant
RQSAVKLTCEINFHMY
28YHb 2.2 1vg8_D
FLYIHADRSTVW
29VHb 18.7 1vg8_D
TLVAICSMGKRQDFHN
30NHe 46.7 1vg8_D hetero G0SGS3_CHATD
TDGKEQSNRHYLACFM
31KSe 67.9 1vg8_D metal YT3
GNKDRESTLQAHV
32K e 56.1 1vg8_D hetero G0SGS3_CHATD
ERKQTSAHDIGNPVCLMY
K->E:(17.0 %):LB/B - dbSNP:rs1154975
33F e 34.4 1vg8_D hetero G0SGS3_CHATD compound GTP GNP GDP 2UK 2UH 2UJ
FYVIADGLTEKPRSW
34S e 50.0 1vg8_D compound GTP GNP GDP 2UK 2UJ
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"
35NSe 77.0 1vg8_D hetero G0SGS3_CHATD compound GTP GNP 2UK GDP 2UH 2UJ
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"
36QSe 79.1 1vg8_D compound GTP 2UJ
EDQKVGNSTAHRIPFLMY
BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791" BINDING /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565" ECO:0000269|PubMed:20028791"
37Y e 59.6 1vg8_D hetero G0SGS3_CHATD G0SD94_CHATD compound GTP GNP 2UK 2UJ
YHTSEVFILPQCMAKRW
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"
38K e 61.8 1vg8_D hetero RILP_HUMAN PDZD8_HUMAN compound GNP 2UK GTP precipitant
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"
39A b 11.6 1vg8_D compound GTP GNP 2UK 2UJ
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"
40T e 21.4 1vg8_D hetero G0SD94_CHATD compound GTP GNP 2UK 2UJ 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"
41I e 57.3 1vg8_D hetero RILP_HUMAN G0SGS3_CHATD PDZD8_HUMAN G0SD94_CHATD OSBL1_MOUSE RUBIC_HUMAN
IVLTAENQSDFGHKY
MOTIF /note="Effector region" MOTIF /note="Effector region"
42GSb 17.9 1vg8_D hetero RAE1_RAT PDZD8_HUMAN OSBL1_MOUSE RUBIC_HUMAN
GFTEAPSLQRDHIKNVY
MOTIF /note="Effector region" MOTIF /note="Effector region"
43AEe 22.3 1vg8_D hetero RAE1_RAT RILP_HUMAN PDZD8_HUMAN OSBL1_MOUSE RUBIC_HUMAN
VEAIRDFGLQCNSPKT
MOTIF /note="Effector region" MOTIF /note="Effector region"
44DEe 68.5 1vg8_D hetero RAE1_RAT RILP_HUMAN PDZD8_HUMAN OSBL1_MOUSE RUBIC_HUMAN
DNETARSHIKLYCGV
MOTIF /note="Effector region" MOTIF /note="Effector region"
45FEe 37.3 1vg8_D hetero RAE1_RAT RILP_HUMAN G0SGS3_CHATD PDZD8_HUMAN WDR91_HUMAN
FYVILSTMQRACDEGHKNP
MOTIF /note="Effector region" MOTIF /note="Effector region"
46LEe 32.6 1vg8_D
YLVKGAFHIRDENSQTCMP
47TEe 42.2 1vg8_D hetero RILP_HUMAN G0SGS3_CHATD
TSRVAEIKNLPYDMCFHQW
48KEe 20.3 1vg8_D
KRQAELTPSVGHIYDFNW
49EEe 53.3 1vg8_D hetero G0SGS3_CHATD
ETQSHKDNVAIRLPFGMY
50VEb 16.7 1vg8_D
VILMFCYAESTDGNW
51MEe 52.7 1vg8_D
TEVMQSHILNYADFPRCGK
52VSb 4.0 1vg8_D
VILTPYAGKMRCEFNQSW
53DSe 67.3 1vg8_D
DENGKRSTPQAFHL
54DSe 93.2 1vg8_D
GDNESKHACFILQRTVY
55R e 49.0 1vg8_D
KREQTGADNSHIVLMP
56LEe 59.0 1vg8_D
TLKPSERVQDGIANCFHMY
57VEb 1.3 1vg8_D
VILYCFAMHTEKPS
58TEe 21.4 1vg8_D hetero RILP_HUMAN G0SGS3_CHATD WDR91_HUMAN
KTLSRNPEHVADGIMQCFY
59MEb 0.0 1vg8_D hetero G0SGS3_CHATD
LFIVAMTCEY
60QEb 14.3 1vg8_D hetero RILP_HUMAN G0SGS3_CHATD WDR91_HUMAN PDZD8_HUMAN
QEDHNGKRLAMSTFIV
61IEb 0.0 1vg8_D
ILVFMACT
62WEb 11.2 1vg8_D hetero RAE1_RAT RILP_HUMAN G0SGS3_CHATD PDZD8_HUMAN WDR91_HUMAN RUBIC_HUMAN
WLFIYVQRMTCH
63DEb 6.8 1vg8_D hetero RAE1_RAT compound GTP 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"
64TEb 3.9 1vg8_D compound GNP GTP 2UK metal MG
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"
65A b 0.9 1vg8_D hetero RAE1_RAT compound GTP GNP 2UJ 2UK
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"
66GSb 15.5 1vg8_D hetero PDZD8_HUMAN compound GTP GNP 2UK 2UJ
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"
67QSe 20.9 1vg8_D hetero RAE1_RAT G0SD94_CHATD OSBL1_MOUSE compound GTP
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"
68EGe 81.4 1vg8_D hetero G0SD94_CHATD PDZD8_HUMAN compound GTP metal YT3
EDPAQRSGHKNCFILTVY
69RGe 73.9 1vg8_D hetero RAE1_RAT G0SD94_CHATD OSBL1_MOUSE PDZD8_HUMAN
REKDASHQFGILTYCNPVW
70FGe 27.3 1vg8_D hetero RAE1_RAT RILP_HUMAN PDZD8_HUMAN OSBL1_MOUSE
FYLVAIGCHKDEMNQW
71QSe 37.8 1vg8_D hetero RAE1_RAT OSBL1_HUMAN PDZD8_HUMAN metal K precipitant
REQSDKGNTHLAPCVY
72S e 33.6 1vg8_D hetero RAE1_RAT RILP_HUMAN RUBIC_HUMAN PDZD8_HUMAN
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"
73LSe 99.4 1vg8_D hetero RILP_HUMAN G0SGS3_CHATD PDZD8_HUMAN OSBL1_MOUSE RUBIC_HUMAN
LMIVTCFAEGHKNPQRSWY
74G e 60.7 1vg8_D hetero RAE1_RAT RUBIC_HUMAN PDZD8_HUMAN
RGTWAPNDILSQVCEFHK
75V e 24.0 1vg8_D hetero RAE1_RAT PDZD8_HUMAN WDR91_HUMAN RUBIC_HUMAN
PDSRIEAKVTLQHNCFGMY
76AGe 48.2 1vg8_D hetero RAE1_RAT RILP_HUMAN G0SGS3_CHATD WDR91_HUMAN RUBIC_HUMAN PDZD8_HUMAN
ASLHQREKMITVGCDFNPW
77FGb 14.4 1vg8_D hetero RAE1_RAT RILP_HUMAN G0SGS3_CHATD PDZD8_HUMAN WDR91_HUMAN OSBL1_MOUSE RUBIC_HUMAN
YFSRCGILAVWDEHNQ
78YGb 5.7 1vg8_D hetero PDZD8_HUMAN
YIMFLSCATGWDHV
79RTe 58.1 1vg8_D hetero RAE1_RAT RILP_HUMAN G0SGS3_CHATD WDR91_HUMAN RUBIC_HUMAN PDZD8_HUMAN
RKEPSIQTAGNHVLMY
80GTe 69.0 1vg8_D hetero RILP_HUMAN G0SGS3_CHATD WDR91_HUMAN PDZD8_HUMAN
GDNQSWTAKRVEHLCFIMY
81A b 4.5 1vg8_D hetero WDR91_HUMAN PDZD8_HUMAN
ATGSVCIFLPQR
82D b 7.4 1vg8_D hetero RILP_HUMAN G0SGS3_CHATD WDR91_HUMAN PDZD8_HUMAN
DNHQEVSALMIKRTY
83CEb 0.0 1vg8_D
GAVCILRFHMTY
84CEb 0.0 1vg8_D
VFAIYCLHGT
85VEb 0.0 1vg8_D
LIVMCFGAT
86LEb 0.0 1vg8_D
LIVFYCMAGHN
87VEb 0.7 1vg8_D
VCMILATFGSY
88FEb 0.0 1vg8_D
YFVIHLQ
89DEb 8.0 1vg8_D
DSANEGIV
90VTb 0.0 1vg8_D
IVLSAGCMNPTY
91TTb 19.5 1vg8_D
TDSANVEHICGQKLM
92A e 25.0 1vg8_D
SDNRAKETCQVGHILM
93PHe 22.5 1vg8_D
RPEKQTAGLSHMVYCDFIN
94NHe 75.2 1vg8_D hetero OSBL1_MOUSE
EDSKQANGRITVHLPW
95THb 10.4 1vg8_D
STRADNEGHKMP
96FHb 6.7 1vg8_D hetero OSBL1_MOUSE
FLYIRVESTACKMQ
97KHe 67.0 1vg8_D hetero OSBL1_MOUSE
EDQKNLSARTHIGMPVY
98TTe 26.0 1vg8_D hetero OSBL1_MOUSE PDZD8_HUMAN precipitant
NSEAKRHDLVPTGIQYCFM
99LHb 0.0 1vg8_D
VLIAMCSTDFHK
100DHe 35.2 1vg8_D metal CL
KEDSQAPRTNGHILYMV
101SHe 63.3 1vg8_D hetero OSBL1_HUMAN RUBIC_HUMAN PDZD8_HUMAN precipitant
KSNERTAQIDHLGPFMVY
102WHb 8.0 1vg8_D hetero OSBL1_HUMAN PDZD8_HUMAN precipitant
WLAFYIEKSVCGMQ
103RHb 7.1 1vg8_D hetero OSBL1_HUMAN
RLIKYHVEAMSFPQTWDGN
104DHe 46.3 1vg8_D hetero OSBL1_HUMAN RUBIC_HUMAN
EDKQPNSRATGIHLVFMY
105EHe 31.2 1vg8_D hetero OSBL1_HUMAN RUBIC_HUMAN PDZD8_HUMAN metal YT3 precipitant
EQDKNTLRAPSCGHIMV
106FHb 0.0 1vg8_D hetero PDZD8_HUMAN
LIFVAYEMWHKSTCDGNPQR
107LHb 15.7 1vg8_D hetero OSBL1_HUMAN
LIRVKQADEHFSCMNTYGPW
108IHe 67.3 1vg8_D hetero RAE1_RAT OSBL1_HUMAN RUBIC_HUMAN
LRIKASVQDETNPGHYCFM
109QHe 30.1 1vg8_D hetero RUBIC_HUMAN PDZD8_HUMAN
HQKELRYNSTVIMADFGPCW
110AHb 8.9 1vg8_D
ALVRSTCDFGIKENHPQYW
111S e 68.8 1vg8_D hetero RAE1_RAT OSBL1_HUMAN WDR91_HUMAN RUBIC_HUMAN
RSAGKDNTELHCPVFIQYM
112P b 17.8 1vg8_D hetero OSBL1_HUMAN
PVASGETHKLDINQRCFYMW
113RSe 48.2 1vg8_D hetero OSBL1_HUMAN WDR91_HUMAN RAE1_RAT
RKELSAGHDNPQYFITVCM
114DSe 43.2 1vg8_D
DGENLVASTQRCHIPFKYM
115PGe 38.0 1vg8_D hetero OSBL1_HUMAN
PLAKSGTNCDEIHQRVMFWY
116EGe 51.8 1vg8_D hetero OSBL1_HUMAN metal YT3
EDKSAQPRTVGHLNIYCFM
117NGe 59.4 1vg8_D
NGDSEKRTAHPLQCIVY
118FSb 3.3 1vg8_D precipitant
VILAFTMYCSEGQ
119P b 14.0 1vg8_D
PVIATKLNQSCEGHMR
120FEb 1.4 1vg8_D precipitant
IVLFMKARTYCGNSW
121VEb 0.0 1vg8_D
VILMATCFGY
122VEb 0.7 1vg8_D
LVIMAG
123LEb 1.1 1vg8_D
VLIACFTM
124GEb 0.0 1vg8_D
GARIQFPSV
125NEb 2.4 1vg8_D compound GTP GNP GDP 2UK 2UH 2UJ
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"
126K e 28.8 1vg8_D compound GTP GNP GDP 2UK 2UH 2UJ
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"
127ITe 27.5 1vg8_D
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"
128DTe 23.5 1vg8_D compound GTP GNP GDP 2UK 2UH 2UJ
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"
129LSe 44.4 1vg8_D compound GTP GNP GDP
LMIVKARCDEFHPQST
L->F:(1.0 %):LP/P Charcot-Marie-Tooth disease, axonal, 2B (CMT2B) dbSNP:rs1219090 [MIM:600882]
130ESe 96.0 1vg8_D
ERDSAKPQTGHLNVCIMY
131N e 83.0 1vg8_D
DNSEHKGTAQRFILMPVY
132R e 34.4 1vg8_D
REKDQSGYAHLNTVIMP
133Q e 63.8 1vg8_D
QREKVADLPSMNTCGHI
134VSb 0.0 1vg8_D
VIAELQTDGKFNPRS
135A e 49.1 1vg8_D
SVDTPAGIKLQECFNRY
136THe 42.9 1vg8_D
TSDEKIPVALFRYMNQGHW
137KHe 84.9 1vg8_D
EKDSAQNRTHIPYFGLV
138RHe 38.3 1vg8_D hetero OSBL1_MOUSE
ERQKDTAILMNVFGHPSWY
139AHb 0.0 1vg8_D
AGEILVDQSTMHKNPRY
140QHe 39.3 1vg8_D
QEKGRALDNHSCFIMPTVY
141AHe 54.5 1vg8_D hetero OSBL1_MOUSE
AEKQLSGDRINVHTFMPY
142WHb 11.6 1vg8_D hetero OSBL1_MOUSE
LWFYAEKVMQSGIRTCDHNP
143CHb 0.0 1vg8_D
ACLFSVGRIKPTDEMNQY
144YHe 67.8 1vg8_D
AKLERYDHNSVFGIQTMPC
145SHe 58.6 1vg8_D
SEDKRAQGTNVHLMP
146KTb 17.9 1vg8_D
KEIRLQDHMSAGNVPTYFW
147NTe 52.1 1vg8_D precipitant
GNLKEFRHDYAMQSTWCIPV
148NSe 61.8 1vg8_D
GNARSDEKFIQTCHLV
149I b 7.0 1vg8_D precipitant
ILCVAMFTRSYKNP
150P e 34.1 1vg8_D precipitant
PKSALGQTCEFHIMRDVYN
151YEb 13.0 1vg8_D
FYLCHIVWAM
152FEb 17.2 1vg8_D
FILYMVCHTWEGKPQS
153EEb 17.1 1vg8_D
EDSAFQRGHKMNPTVY
154TEb 0.0 1vg8_D
TCIVALSEGMNQ
155SBb 0.0 1vg8_D compound GTP GNP GDP 2UK 2UH 2UJ
SCNAHILQT
156ATb 0.9 1vg8_D compound GTP GNP GDP 2UK 2UH 2UJ
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"
157KTe 41.0 1vg8_D compound GTP GNP GDP 2UK 2UH 2UJ
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]
158ETe 57.8 1vg8_D
TEDSLNQAYKCFHIMV
159ATe 48.2 1vg8_D metal CL precipitant
NGSRAQDKHMCEFL
160IBe 39.2 1vg8_D metal CL precipitant
IETQLYDFHSKVMARWCNP
161NSe 35.8 1vg8_D metal CL precipitant
NGSHRTCDEKLQ
N->T:(2.0 %):LP/P Charcot-Marie-Tooth disease, axonal, 2B (CMT2B) dbSNP:rs1219090 [MIM:600882]
162VHb 2.0 1vg8_D metal CL precipitant
VILFTAEKMY
V->M:(1.0 %):LP/P Charcot-Marie-Tooth disease, axonal, 2B (CMT2B) dbSNP:rs1219090 [MIM:600882]
163EHe 31.2 1vg8_D metal CL precipitant
EDKNQIRTYLVAFGHPS
164QHe 44.9 1vg8_D
EDKQALNRSITCGHMP
165AHb 0.0 1vg8_D
AVLPISMTCDFGK
166FHb 0.5 1vg8_D
FLAIKMPTVY
167QHe 57.1 1vg8_D
EQLDRTYHIKNMSFVA
168THe 20.1 1vg8_D
ETADKSWLRYCGHMNQVFI
169IHb 0.0 1vg8_D
LIAVMTCF
170AHb 0.9 1vg8_D
AVILTSCEFGMQR
171RHe 35.6 1vg8_D
RKEQASCHLDMNT
172NHe 24.2 1vg8_D
EKADNQSVHLTIRCF
173AHb 0.0 1vg8_D
IAVLSHKMCFGTY
174LHb 10.7 1vg8_D
LIRKVFMPESYACNQT
175KHe 75.9 1vg8_D
KQRENTASGLIMPYDFHV
176QHb 19.4 1vg8_D
QRKNELDSTAHMPYGV
177EHb 14.1 1vg8_D
ERKQSDPHNMFGILVYAT
178THe 33.8 1vg8_D hetero RILP_HUMAN
TSGKRAEMNPDQCILVH
179EHe 29.1 1vg8_D
ESKQRLDAGTHPIMNVY
180VHe 38.7 1vg8_D hetero RILP_HUMAN
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
181EHe 41.2 1vg8_D hetero RILP_HUMAN
EQDAHKSLNPRTVMFGI
DISORDER predicted by DISOPRED
182LHe 42.7 1vg8_D hetero RILP_HUMAN
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
183YHe 29.6 1vg8_D hetero RILP_HUMAN
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
184NHe 76.4 1vg8_D
NGSADREQPTHIKMVCFL
DISORDER predicted by DISOPRED
185EHe 61.3 1vg8_D hetero RILP_HUMAN
EQKDGLNSAIVHRPTMY
DISORDER predicted by DISOPRED
186FSe 67.9 1vg8_D hetero RAE1_RAT
FLSADGIRKNTVQEMPY
DISORDER predicted by DISOPRED
187P e 59.7 1vg8_D
PGSDTKIMNAQVELR
DISORDER predicted by DISOPRED
188E e 56.3 1vg8_D
EDQSKLNPAGRTIVH
DISORDER predicted by DISOPRED
189P e 98.4 1vg8_D hetero RAE1_RAT
PSGTDEAHQRIKNVL
DISORDER predicted by DISOPRED
190I e123.4 1vg8_D hetero RAE1_RAT
IVLGSMPTADEKQRN
DISORDER predicted by DISOPRED
191K 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
192L e123.0 1vg0_B hetero RAE1_RAT
LIVKPSMFREQDT
DISORDER predicted by DISOPRED
193D----
DSNEGTKRVIAPYHQ
DISORDER predicted by DISOPRED
194K----
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
195N----
NGSHTKQAEPRDLIV
DISORDER predicted by DISOPRED
196D----
DNPQSTAERGLKHW
DISORDER predicted by DISOPRED
197R----
RKQESGPITLVAYDMN
DISORDER predicted by DISOPRED
198A----
ASKPGQHETVILMRN
DISORDER predicted by DISOPRED
199K----
KQRSANTEGLPDFMV
DISORDER predicted by DISOPRED
200A----
SAGTKPRNQDCEHLV
DISORDER predicted by DISOPRED
201S----
SAQTNEGKPMDLRWYCV
DISORDER predicted by DISOPRED
202A----
AGSKVEFCLPQTDIN
DISORDER predicted by DISOPRED
203E----
SGEQKADNRCFYMPTVIL
DISORDER predicted by DISOPRED
204S----
SGCKNATEHRQVP
DISORDER predicted by DISOPRED
205C----
CSAIKGTV
LIPID /note="S-geranylgeranyl cysteine" LIPID /note="S-geranylgeranyl cysteine" DISORDER predicted by DISOPRED
206S----
SGAHCENQTVYIKP
DISORDER predicted by DISOPRED
207C----
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