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 | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MAYAYLFKY ------CCHHEEEEE | 9.54 | 19413330 | |
3 | Phosphorylation | -----MAYAYLFKYI -----CCHHEEEEEE | 8.42 | 28152594 | |
5 | Phosphorylation | ---MAYAYLFKYIII ---CCHHEEEEEEEE | 10.45 | 28442448 | |
9 | Phosphorylation | AYAYLFKYIIIGDTG CHHEEEEEEEECCCC | 7.04 | 21945579 | |
15 | Phosphorylation | KYIIIGDTGVGKSCL EEEEECCCCCCHHHE | 28.67 | 21945579 | |
20 | Phosphorylation | GDTGVGKSCLLLQFT CCCCCCHHHEEEEEE | 12.22 | 20068231 | |
27 | Phosphorylation | SCLLLQFTDKRFQPV HHEEEEEECCCCCCC | 27.87 | 20068231 | |
29 | Acetylation | LLLQFTDKRFQPVHD EEEEEECCCCCCCCE | 52.64 | 25038526 | |
38 | Phosphorylation | FQPVHDLTIGVEFGA CCCCCEEEEEEEECC | 23.03 | 22210691 | |
53 | Ubiquitination | RMITIDGKQIKLQIW EEEEECCEEEEEEEE | 45.14 | 21906983 | |
53 | Malonylation | RMITIDGKQIKLQIW EEEEECCEEEEEEEE | 45.14 | 26320211 | |
56 | Ubiquitination | TIDGKQIKLQIWDTA EECCEEEEEEEEECC | 31.67 | 21906983 | |
56 | Acetylation | TIDGKQIKLQIWDTA EECCEEEEEEEEECC | 31.67 | 25038526 | |
56 | Ubiquitination | TIDGKQIKLQIWDTA EECCEEEEEEEEECC | 31.67 | 21890473 | |
62 | Phosphorylation | IKLQIWDTAGQESFR EEEEEEECCCHHHHH | 20.07 | 28450419 | |
67 | Phosphorylation | WDTAGQESFRSITRS EECCCHHHHHHHHHH | 20.33 | 25693802 | |
70 | Phosphorylation | AGQESFRSITRSYYR CCHHHHHHHHHHHHC | 26.71 | 28450419 | |
72 | Phosphorylation | QESFRSITRSYYRGA HHHHHHHHHHHHCCC | 18.14 | 28450419 | |
86 | Phosphorylation | AAGALLVYDITRRDT CCCEEEEEECCCCHH | 11.12 | - | |
89 | Phosphorylation | ALLVYDITRRDTFNH EEEEEECCCCHHHHH | 19.43 | - | |
93 | Phosphorylation | YDITRRDTFNHLTTW EECCCCHHHHHHHHH | 25.24 | 25693802 | |
108 | Phosphorylation | LEDARQHSNSNMVIM HHHHHHHCCCCEEEE | 33.35 | 30108239 | |
110 | Phosphorylation | DARQHSNSNMVIMLI HHHHHCCCCEEEEEE | 29.35 | 30108239 | |
121 | O-linked_Glycosylation | IMLIGNKSDLESRRE EEEECCHHHHHHHHH | 51.97 | 25367160 | |
121 | Phosphorylation | IMLIGNKSDLESRRE EEEECCHHHHHHHHH | 51.97 | 26437602 | |
125 | Phosphorylation | GNKSDLESRREVKKE CCHHHHHHHHHHHHH | 43.89 | 26437602 | |
130 | Ubiquitination | LESRREVKKEEGEAF HHHHHHHHHHHHHHH | 50.11 | 21906983 | |
151 | Ubiquitination | IFMETSAKTASNVEE EEEECCCCCCCCHHH | 44.37 | - | |
151 | Acetylation | IFMETSAKTASNVEE EEEECCCCCCCCHHH | 44.37 | 25953088 | |
152 | Phosphorylation | FMETSAKTASNVEEA EEECCCCCCCCHHHH | 34.73 | 21406692 | |
154 | Phosphorylation | ETSAKTASNVEEAFI ECCCCCCCCHHHHHH | 46.79 | 21406692 | |
163 | Phosphorylation | VEEAFINTAKEIYEK HHHHHHHHHHHHHHH | 34.00 | 21406692 | |
165 | Ubiquitination | EAFINTAKEIYEKIQ HHHHHHHHHHHHHHH | 42.48 | 21906983 | |
165 | Ubiquitination | EAFINTAKEIYEKIQ HHHHHHHHHHHHHHH | 42.48 | 21890473 | |
165 | Acetylation | EAFINTAKEIYEKIQ HHHHHHHHHHHHHHH | 42.48 | 25038526 | |
170 | Ubiquitination | TAKEIYEKIQEGVFD HHHHHHHHHHHCCCC | 32.49 | - | |
211 | Geranylgeranylation | GQQAGGGCC------ CCCCCCCCC------ | 2.55 | 1648736 | |
211 | Geranylgeranylation | GQQAGGGCC------ CCCCCCCCC------ | 2.55 | 1648736 | |
212 | Geranylgeranylation | QQAGGGCC------- CCCCCCCC------- | 7.65 | 1648736 | |
212 | Geranylgeranylation | QQAGGGCC------- CCCCCCCC------- | 7.65 | 1648736 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RAB2A_HUMAN !! |
* 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 !! |
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. |
loading...
Acetylation | |
Reference | PubMed |
"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 | |
Reference | PubMed |
"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. |