RAB2A_HUMAN - dbPTM
RAB2A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAB2A_HUMAN
UniProt AC P61019
Protein Name Ras-related protein Rab-2A
Gene Name RAB2A
Organism Homo sapiens (Human).
Sequence Length 212
Subcellular Localization Endoplasmic reticulum-Golgi intermediate compartment membrane
Lipid-anchor . Melanosome . Endoplasmic reticulum membrane
Lipid-anchor . Golgi apparatus membrane
Lipid-anchor . Identified by mass spectrometry in melanosome fractions from stage I
Protein Description Required for protein transport from the endoplasmic reticulum to the Golgi complex..
Protein Sequence MAYAYLFKYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGVEFGARMITIDGKQIKLQIWDTAGQESFRSITRSYYRGAAGALLVYDITRRDTFNHLTTWLEDARQHSNSNMVIMLIGNKSDLESRREVKKEEGEAFAREHGLIFMETSAKTASNVEEAFINTAKEIYEKIQEGVFDINNEANGIKIGPQHAATNATHAGNQGGQQAGGGCC
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------MAYAYLFKY
------CCHHEEEEE
9.5419413330
3Phosphorylation-----MAYAYLFKYI
-----CCHHEEEEEE
8.4228152594
5Phosphorylation---MAYAYLFKYIII
---CCHHEEEEEEEE
10.4528442448
9PhosphorylationAYAYLFKYIIIGDTG
CHHEEEEEEEECCCC
7.0421945579
15PhosphorylationKYIIIGDTGVGKSCL
EEEEECCCCCCHHHE
28.6721945579
20PhosphorylationGDTGVGKSCLLLQFT
CCCCCCHHHEEEEEE
12.2220068231
27PhosphorylationSCLLLQFTDKRFQPV
HHEEEEEECCCCCCC
27.8720068231
29AcetylationLLLQFTDKRFQPVHD
EEEEEECCCCCCCCE
52.6425038526
38PhosphorylationFQPVHDLTIGVEFGA
CCCCCEEEEEEEECC
23.0322210691
53UbiquitinationRMITIDGKQIKLQIW
EEEEECCEEEEEEEE
45.1421906983
53MalonylationRMITIDGKQIKLQIW
EEEEECCEEEEEEEE
45.1426320211
56UbiquitinationTIDGKQIKLQIWDTA
EECCEEEEEEEEECC
31.6721906983
56AcetylationTIDGKQIKLQIWDTA
EECCEEEEEEEEECC
31.6725038526
56UbiquitinationTIDGKQIKLQIWDTA
EECCEEEEEEEEECC
31.6721890473
62PhosphorylationIKLQIWDTAGQESFR
EEEEEEECCCHHHHH
20.0728450419
67PhosphorylationWDTAGQESFRSITRS
EECCCHHHHHHHHHH
20.3325693802
70PhosphorylationAGQESFRSITRSYYR
CCHHHHHHHHHHHHC
26.7128450419
72PhosphorylationQESFRSITRSYYRGA
HHHHHHHHHHHHCCC
18.1428450419
86PhosphorylationAAGALLVYDITRRDT
CCCEEEEEECCCCHH
11.12-
89PhosphorylationALLVYDITRRDTFNH
EEEEEECCCCHHHHH
19.43-
93PhosphorylationYDITRRDTFNHLTTW
EECCCCHHHHHHHHH
25.2425693802
108PhosphorylationLEDARQHSNSNMVIM
HHHHHHHCCCCEEEE
33.3530108239
110PhosphorylationDARQHSNSNMVIMLI
HHHHHCCCCEEEEEE
29.3530108239
121O-linked_GlycosylationIMLIGNKSDLESRRE
EEEECCHHHHHHHHH
51.9725367160
121PhosphorylationIMLIGNKSDLESRRE
EEEECCHHHHHHHHH
51.9726437602
125PhosphorylationGNKSDLESRREVKKE
CCHHHHHHHHHHHHH
43.8926437602
130UbiquitinationLESRREVKKEEGEAF
HHHHHHHHHHHHHHH
50.1121906983
151UbiquitinationIFMETSAKTASNVEE
EEEECCCCCCCCHHH
44.37-
151AcetylationIFMETSAKTASNVEE
EEEECCCCCCCCHHH
44.3725953088
152PhosphorylationFMETSAKTASNVEEA
EEECCCCCCCCHHHH
34.7321406692
154PhosphorylationETSAKTASNVEEAFI
ECCCCCCCCHHHHHH
46.7921406692
163PhosphorylationVEEAFINTAKEIYEK
HHHHHHHHHHHHHHH
34.0021406692
165UbiquitinationEAFINTAKEIYEKIQ
HHHHHHHHHHHHHHH
42.4821906983
165UbiquitinationEAFINTAKEIYEKIQ
HHHHHHHHHHHHHHH
42.4821890473
165AcetylationEAFINTAKEIYEKIQ
HHHHHHHHHHHHHHH
42.4825038526
170UbiquitinationTAKEIYEKIQEGVFD
HHHHHHHHHHHCCCC
32.49-
211GeranylgeranylationGQQAGGGCC------
CCCCCCCCC------
2.551648736
211GeranylgeranylationGQQAGGGCC------
CCCCCCCCC------
2.551648736
212GeranylgeranylationQQAGGGCC-------
CCCCCCCC-------
7.651648736
212GeranylgeranylationQQAGGGCC-------
CCCCCCCC-------
7.651648736

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 RAB2A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAB2A_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 RAB2A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FA71C_HUMANFAM71Cphysical
16189514
GORS2_HUMANGORASP2physical
11739401
GOGA2_HUMANGOLGA2physical
11739401
ROA0_HUMANHNRNPA0physical
22939629
GO45_HUMANBLZF1physical
25416956
STALP_HUMANSTAMBPL1physical
25416956
NXP20_HUMANFAM114A1physical
25416956
FA71C_HUMANFAM71Cphysical
25416956
ABCB7_HUMANABCB7physical
26344197
ACADM_HUMANACADMphysical
26344197
APT_HUMANAPRTphysical
26344197
ARL8B_HUMANARL8Bphysical
26344197
AT1A1_HUMANATP1A1physical
26344197
BAP29_HUMANBCAP29physical
26344197
BAP31_HUMANBCAP31physical
26344197
CALX_HUMANCANXphysical
26344197
GMDS_HUMANGMDSphysical
26344197
HNRPU_HUMANHNRNPUphysical
26344197
PHB_HUMANPHBphysical
26344197
RB11A_HUMANRAB11Aphysical
26344197
RAB6A_HUMANRAB6Aphysical
26344197
RAB6B_HUMANRAB6Bphysical
26344197
RAC1_HUMANRAC1physical
26344197
SSRD_HUMANSSR4physical
26344197
SUCB2_HUMANSUCLG2physical
26344197
TES_HUMANTESphysical
26344197
ACTB_HUMANACTBphysical
26496610
ASSY_HUMANASS1physical
26496610
VATB2_HUMANATP6V1B2physical
26496610
CAV1_HUMANCAV1physical
26496610
COX6C_HUMANCOX6Cphysical
26496610
STOM_HUMANSTOMphysical
26496610
FLOT2_HUMANFLOT2physical
26496610
PHB_HUMANPHBphysical
26496610
SOAT1_HUMANSOAT1physical
26496610
VDAC1_HUMANVDAC1physical
26496610
RAB7A_HUMANRAB7Aphysical
26496610
VA0D1_HUMANATP6V0D1physical
26496610
AKA12_HUMANAKAP12physical
26496610
FLOT1_HUMANFLOT1physical
26496610
PHB2_HUMANPHB2physical
26496610
PUF60_HUMANPUF60physical
26496610
CHM2A_HUMANCHMP2Aphysical
26496610
VATH_HUMANATP6V1Hphysical
26496610
MIC19_HUMANCHCHD3physical
26496610
DOCK6_HUMANDOCK6physical
26496610
TM109_HUMANTMEM109physical
26496610
CAVN1_HUMANPTRFphysical
26496610
CCHL_HUMANHCCSphysical
27173435
COMT_HUMANCOMTphysical
27173435

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 RAB2A_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.
Prenylation
ReferencePubMed
"Isoprenoid modification of rab proteins terminating in CC or CXCmotifs.";
Khosravi-Far R., Lutz R.J., Cox A.D., Conroy L., Bourne J.R.,Sinensky M., Balch W.E., Buss J.E., Der C.J.;
Proc. Natl. Acad. Sci. U.S.A. 88:6264-6268(1991).
Cited for: ISOPRENYLATION AT CYS-211 AND CYS-212.

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