RB39B_HUMAN - dbPTM
RB39B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RB39B_HUMAN
UniProt AC Q96DA2
Protein Name Ras-related protein Rab-39B
Gene Name RAB39B
Organism Homo sapiens (Human).
Sequence Length 213
Subcellular Localization Cell membrane
Lipid-anchor
Cytoplasmic side . Cytoplasmic vesicle membrane
Lipid-anchor
Cytoplasmic side . Golgi apparatus . Partial colocalization with markers that cycle from the cell surface to the trans-Golgi network.
Protein Description Small GTPases Rab involved in autophagy. [PubMed: 27103069 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 sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion]
Protein Sequence MEAIWLYQFRLIVIGDSTVGKSCLIRRFTEGRFAQVSDPTVGVDFFSRLVEIEPGKRIKLQIWDTAGQERFRSITRAYYRNSVGGLLLFDITNRRSFQNVHEWLEETKVHVQPYQIVFVLVGHKCDLDTQRQVTRHEAEKLAAAYGMKYIETSARDAINVEKAFTDLTRDIYELVKRGEITIQEGWEGVKSGFVPNVVHSSEEVVKSERRCLC
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
29PhosphorylationSCLIRRFTEGRFAQV
CHHHHHHCCCCEEEC
35.4024719451
56UbiquitinationLVEIEPGKRIKLQIW
HEEECCCCCEEEEEE
62.7632142685
65PhosphorylationIKLQIWDTAGQERFR
EEEEEECCCCHHHHH
20.0728857561
73PhosphorylationAGQERFRSITRAYYR
CCHHHHHHHHHHHHH
26.12-
92PhosphorylationGLLLFDITNRRSFQN
CEEEEECCCCCCCCC
25.2324260401
140UbiquitinationVTRHEAEKLAAAYGM
HHHHHHHHHHHHHCC
50.9323000965
140AcetylationVTRHEAEKLAAAYGM
HHHHHHHHHHHHHCC
50.9325953088
162UbiquitinationRDAINVEKAFTDLTR
HHHCCHHHHHHHHHH
44.5129967540
191PhosphorylationEGWEGVKSGFVPNVV
ECCHHHHCCCCCCCC
34.7523312004
200PhosphorylationFVPNVVHSSEEVVKS
CCCCCCCCCHHHHHH
28.0327732954
201PhosphorylationVPNVVHSSEEVVKSE
CCCCCCCCHHHHHHH
23.9327732954
206UbiquitinationHSSEEVVKSERRCLC
CCCHHHHHHHHCCCC
52.3432142685
207PhosphorylationSSEEVVKSERRCLC-
CCHHHHHHHHCCCC-
25.4023312004
211GeranylgeranylationVVKSERRCLC-----
HHHHHHCCCC-----
5.95-
213MethylationKSERRCLC-------
HHHHCCCC-------
6.32-
213GeranylgeranylationKSERRCLC-------
HHHHCCCC-------
6.32-

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 RB39B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RB39B_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 RB39B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GOGA2_HUMANGOLGA2physical
21516116
WHAMM_HUMANWHAMMphysical
28514442
CL16A_HUMANCLEC16Aphysical
28514442
TRIM4_HUMANTRIM4physical
28514442
CBL_HUMANCBLphysical
28514442
TRIP6_HUMANTRIP6physical
28514442
RB33B_HUMANRAB33Bphysical
28514442
RAD50_HUMANRAD50physical
28514442
HBS1L_HUMANHBS1Lphysical
28514442
CARM1_HUMANCARM1physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RB39B_HUMAN

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Related Literatures of Post-Translational Modification

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