RAB17_HUMAN - dbPTM
RAB17_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAB17_HUMAN
UniProt AC Q9H0T7
Protein Name Ras-related protein Rab-17
Gene Name RAB17
Organism Homo sapiens (Human).
Sequence Length 212
Subcellular Localization Recycling endosome membrane
Lipid-anchor
Cytoplasmic side . Melanosome . Cell projection, dendrite . May also localize at the basolateral and apical plasma membrane. In neurons, localizes to the cell body and dendritic shaft and spine.
Protein Description The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in transcytosis, the directed movement of endocytosed material through the cell and its exocytosis from the plasma membrane at the opposite side. Mainly observed in epithelial cells, transcytosis mediates for instance, the transcellular transport of immunoglobulins from the basolateral surface to the apical surface. Most probably controls membrane trafficking through apical recycling endosomes in a post-endocytic step of transcytosis. Required for melanosome transport and release from melanocytes, it also regulates dendrite and dendritic spine development (By similarity). May also play a role in cell migration..
Protein Sequence MAQAHRTPQPRAAPSQPRVFKLVLLGSGSVGKSSLALRYVKNDFKSILPTVGCAFFTKVVDVGATSLKLEIWDTAGQEKYHSVCHLYFRGANAALLVYDITRKDSFLKAQQWLKDLEEELHPGEVLVMLVGNKTDLSQEREVTFQEGKEFADSQKLLFMETSAKLNHQVSEVFNTVAQELLQRSDEEGQALRGDAAVALNKGPARQAKCCAH
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
7Phosphorylation-MAQAHRTPQPRAAP
-CCCCCCCCCCCCCC
19.1925159151
27PhosphorylationFKLVLLGSGSVGKSS
EEEEEECCCCCCCHH
28.0625072903
29PhosphorylationLVLLGSGSVGKSSLA
EEEECCCCCCCHHHH
29.4125072903
105PhosphorylationYDITRKDSFLKAQQW
EECCCHHHHHHHHHH
35.2024719451
108UbiquitinationTRKDSFLKAQQWLKD
CCHHHHHHHHHHHHH
41.98-
133UbiquitinationLVMLVGNKTDLSQER
EEEEECCCCCCCCCE
37.17-
148UbiquitinationEVTFQEGKEFADSQK
EEEHHHCHHHHHHHE
49.24-
155UbiquitinationKEFADSQKLLFMETS
HHHHHHHEEEEEHHH
51.62-
184PhosphorylationAQELLQRSDEEGQAL
HHHHHHCCCHHCCCC
36.0930576142
201UbiquitinationDAAVALNKGPARQAK
HHCCCCCCCHHHCCC
68.10-
209GeranylgeranylationGPARQAKCCAH----
CHHHCCCCCCC----
2.51-
210GeranylgeranylationPARQAKCCAH-----
HHHCCCCCCC-----
3.68-

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 RAB17_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAB17_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 RAB17_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHMP6_HUMANCHMP6physical
17353931
CK049_HUMANC11orf49physical
25416956
FAM9B_HUMANFAM9Bphysical
25416956
RAE2_HUMANCHMLphysical
26186194
RAE1_HUMANCHMphysical
26186194
MOCS1_HUMANMOCS1physical
26186194
GEMI6_HUMANGEMIN6physical
26186194
GTPB1_HUMANGTPBP1physical
26186194
PGTB2_HUMANRABGGTBphysical
26186194
RAE1_HUMANCHMphysical
28514442
RAE2_HUMANCHMLphysical
28514442
MOCS1_HUMANMOCS1physical
28514442
BOLA1_HUMANBOLA1physical
28514442
GTPB1_HUMANGTPBP1physical
28514442
GEMI6_HUMANGEMIN6physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RAB17_HUMAN

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Related Literatures of Post-Translational Modification

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