RAB5C_HUMAN - dbPTM
RAB5C_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAB5C_HUMAN
UniProt AC P51148
Protein Name Ras-related protein Rab-5C
Gene Name RAB5C
Organism Homo sapiens (Human).
Sequence Length 216
Subcellular Localization Cell membrane
Lipid-anchor
Cytoplasmic side. Early endosome membrane
Lipid-anchor. Melanosome . Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Protein Description Protein transport. Probably involved in vesicular traffic (By similarity)..
Protein Sequence MAGRGGAARPNGPAAGNKICQFKLVLLGESAVGKSSLVLRFVKGQFHEYQESTIGAAFLTQTVCLDDTTVKFEIWDTAGQERYHSLAPMYYRGAQAAIVVYDITNTDTFARAKNWVKELQRQASPNIVIALAGNKADLASKRAVEFQEAQAYADDNSLLFMETSAKTAMNVNEIFMAIAKKLPKNEPQNATGAPGRNRGVDLQENNPASRSQCCSN
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 Orthologous
Protein Cluster
2Acetylation------MAGRGGAAR
------CCCCCCCCC
19.18-
4Methylation----MAGRGGAARPN
----CCCCCCCCCCC
30.73115367883
9MethylationAGRGGAARPNGPAAG
CCCCCCCCCCCCCCC
25.36115385817
18UbiquitinationNGPAAGNKICQFKLV
CCCCCCCCCCEEEEE
43.89-
18AcetylationNGPAAGNKICQFKLV
CCCCCCCCCCEEEEE
43.8926822725
23AcetylationGNKICQFKLVLLGES
CCCCCEEEEEEECCC
16.29129523
30PhosphorylationKLVLLGESAVGKSSL
EEEEECCCCCCCCHH
26.8423911959
34UbiquitinationLGESAVGKSSLVLRF
ECCCCCCCCHHHHHH
30.21-
36PhosphorylationESAVGKSSLVLRFVK
CCCCCCCHHHHHHHC
26.4424719451
83PhosphorylationDTAGQERYHSLAPMY
CCCCCCCCHHCCCCH
8.6025106551
85PhosphorylationAGQERYHSLAPMYYR
CCCCCCHHCCCCHHC
19.7928857561
89SulfoxidationRYHSLAPMYYRGAQA
CCHHCCCCHHCCCCE
3.6928183972
116PhosphorylationFARAKNWVKELQRQA
HHHHHHHHHHHHHHC
4.8927642862
117UbiquitinationARAKNWVKELQRQAS
HHHHHHHHHHHHHCC
44.3021906983
118PhosphorylationRAKNWVKELQRQASP
HHHHHHHHHHHHCCC
40.2827251275
123PhosphorylationVKELQRQASPNIVIA
HHHHHHHCCCCEEEE
29.1927642862
124PhosphorylationKELQRQASPNIVIAL
HHHHHHCCCCEEEEE
15.3325159151
135UbiquitinationVIALAGNKADLASKR
EEEECCCHHHHHHHH
42.2221906983
140PhosphorylationGNKADLASKRAVEFQ
CCHHHHHHHHHHHHH
29.9417137347
141UbiquitinationNKADLASKRAVEFQE
CHHHHHHHHHHHHHH
38.48-
141AcetylationNKADLASKRAVEFQE
CHHHHHHHHHHHHHH
38.4825953088
152PhosphorylationEFQEAQAYADDNSLL
HHHHHHHHCCCCCEE
9.8521406692
157PhosphorylationQAYADDNSLLFMETS
HHHCCCCCEEEEECC
33.1821406692
161SulfoxidationDDNSLLFMETSAKTA
CCCCEEEEECCCCCC
5.7630846556
163PhosphorylationNSLLFMETSAKTAMN
CCEEEEECCCCCCCC
23.3821406692
164PhosphorylationSLLFMETSAKTAMNV
CEEEEECCCCCCCCH
17.9221406692
167PhosphorylationFMETSAKTAMNVNEI
EEECCCCCCCCHHHH
30.7522210691
173PhosphorylationKTAMNVNEIFMAIAK
CCCCCHHHHHHHHHH
33.0627251275
180UbiquitinationEIFMAIAKKLPKNEP
HHHHHHHHHCCCCCC
49.0521906983
180AcetylationEIFMAIAKKLPKNEP
HHHHHHHHHCCCCCC
49.0525953088
184AcetylationAIAKKLPKNEPQNAT
HHHHHCCCCCCCCCC
81.8423236377
191PhosphorylationKNEPQNATGAPGRNR
CCCCCCCCCCCCCCC
41.2324173317
191O-linked_GlycosylationKNEPQNATGAPGRNR
CCCCCCCCCCCCCCC
41.23OGP
209O-linked_GlycosylationLQENNPASRSQCCSN
CCCCCCCCHHHHCCC
33.4523301498
209PhosphorylationLQENNPASRSQCCSN
CCCCCCCCHHHHCCC
33.4521712546
213GeranylgeranylationNPASRSQCCSN----
CCCCHHHHCCC----
2.64-
214GeranylgeranylationPASRSQCCSN-----
CCCHHHHCCC-----
3.20-

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
85SPhosphorylationKinaseLRRK2Q5S007
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
85SPhosphorylation

29125462

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 RAB5C_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SUN2_HUMANSUN2physical
17353931
EEA1_HUMANEEA1physical
12493736
RBNS5_HUMANRBSNphysical
12493736
A4_HUMANAPPphysical
21832049
DP13B_HUMANAPPL2physical
25416956
ARF1_HUMANARF1physical
26344197
ARL8A_HUMANARL8Aphysical
26344197
ETFA_HUMANETFAphysical
26344197
LDHA_HUMANLDHAphysical
26344197
LDH6A_HUMANLDHAL6Aphysical
26344197
LDH6B_HUMANLDHAL6Bphysical
26344197
LDHB_HUMANLDHBphysical
26344197
PRS7_HUMANPSMC2physical
26344197
RAB1A_HUMANRAB1Aphysical
26344197
RAB1B_HUMANRAB1Bphysical
26344197
RAB2A_HUMANRAB2Aphysical
26344197
RAB8A_HUMANRAB8Aphysical
26344197
RAB8B_HUMANRAB8Bphysical
26344197
RPN1_HUMANRPN1physical
26344197
QCR2_HUMANUQCRC2physical
26344197
VATA_HUMANATP6V1Aphysical
26496610
VATB2_HUMANATP6V1B2physical
26496610
VPP1_HUMANATP6V0A1physical
26496610
CAV1_HUMANCAV1physical
26496610
CLCN7_HUMANCLCN7physical
26496610
COX5B_HUMANCOX5Bphysical
26496610
CX6B1_HUMANCOX6B1physical
26496610
FLOT2_HUMANFLOT2physical
26496610
H33_HUMANH3F3Aphysical
26496610
MPRI_HUMANIGF2Rphysical
26496610
NDUA7_HUMANNDUFA7physical
26496610
NDUB7_HUMANNDUFB7physical
26496610
NDUS1_HUMANNDUFS1physical
26496610
NDUS5_HUMANNDUFS5physical
26496610
CHM1A_HUMANCHMP1Aphysical
26496610
PHB_HUMANPHBphysical
26496610
PPIA_HUMANPPIAphysical
26496610
RAD51_HUMANRAD51physical
26496610
SMCA4_HUMANSMARCA4physical
26496610
SMRC1_HUMANSMARCC1physical
26496610
SOAT1_HUMANSOAT1physical
26496610
SSXT_HUMANSS18physical
26496610
TFR1_HUMANTFRCphysical
26496610
TTC3_HUMANTTC3physical
26496610
VDAC1_HUMANVDAC1physical
26496610
VDAC2_HUMANVDAC2physical
26496610
STX7_HUMANSTX7physical
26496610
RAI3_HUMANGPRC5Aphysical
26496610
VA0D1_HUMANATP6V0D1physical
26496610
XPR1_HUMANXPR1physical
26496610
CSN2_HUMANCOPS2physical
26496610
GOSR1_HUMANGOSR1physical
26496610
EPN4_HUMANCLINT1physical
26496610
CAPON_HUMANNOS1APphysical
26496610
PIEZ1_HUMANPIEZO1physical
26496610
IST1_HUMANIST1physical
26496610
C2CD5_HUMANC2CD5physical
26496610
FLOT1_HUMANFLOT1physical
26496610
CKAP4_HUMANCKAP4physical
26496610
TMEDA_HUMANTMED10physical
26496610
MIC60_HUMANIMMTphysical
26496610
RASF8_HUMANRASSF8physical
26496610
PHB2_HUMANPHB2physical
26496610
KDM2A_HUMANKDM2Aphysical
26496610
WDFY3_HUMANWDFY3physical
26496610
FAF2_HUMANFAF2physical
26496610
SCFD1_HUMANSCFD1physical
26496610
HAUS5_HUMANHAUS5physical
26496610
BICRL_HUMANGLTSCR1Lphysical
26496610
SUN2_HUMANSUN2physical
26496610
GRAN_HUMANGCAphysical
26496610
LTMD1_HUMANLETMD1physical
26496610
CHM2B_HUMANCHMP2Bphysical
26496610
MYOF_HUMANMYOFphysical
26496610
AT2C1_HUMANATP2C1physical
26496610
CHM2A_HUMANCHMP2Aphysical
26496610
SGSM3_HUMANSGSM3physical
26496610
ABT1_HUMANABT1physical
26496610
STML2_HUMANSTOML2physical
26496610
NDUBB_HUMANNDUFB11physical
26496610
MIC19_HUMANCHCHD3physical
26496610
OCAD1_HUMANOCIAD1physical
26496610
RMD3_HUMANRMDN3physical
26496610
IMPCT_HUMANIMPACTphysical
26496610
TTC17_HUMANTTC17physical
26496610
MUC13_HUMANMUC13physical
26496610
BBX_HUMANBBXphysical
26496610
KDIS_HUMANKIDINS220physical
26496610
SUGP1_HUMANSUGP1physical
26496610
RT14_HUMANMRPS14physical
26496610
S35E1_HUMANSLC35E1physical
26496610
YIPF5_HUMANYIPF5physical
26496610
ZCRB1_HUMANZCRB1physical
26496610
G45IP_HUMANGADD45GIP1physical
26496610
ACBD5_HUMANACBD5physical
26496610
S38A5_HUMANSLC38A5physical
26496610
CAVN3_HUMANPRKCDBPphysical
26496610
LLR1_HUMANLRR1physical
26496610
RM55_HUMANMRPL55physical
26496610
CHM4B_HUMANCHMP4Bphysical
26496610
MITD1_HUMANMITD1physical
26496610
CAVN1_HUMANPTRFphysical
26496610
RAB43_HUMANRAB43physical
26496610
RAE1_HUMANCHMphysical
28514442
GDIA_HUMANGDI1physical
28514442
GNAT3_HUMANGNAT3physical
28514442
RAE2_HUMANCHMLphysical
28514442
GDIB_HUMANGDI2physical
28514442

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 RAB5C_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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