RAB34_HUMAN - dbPTM
RAB34_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAB34_HUMAN
UniProt AC Q9BZG1
Protein Name Ras-related protein Rab-34
Gene Name RAB34
Organism Homo sapiens (Human).
Sequence Length 259
Subcellular Localization Cytoplasm . Golgi apparatus . Cytoplasmic vesicle, phagosome . Cytoplasmic vesicle, phagosome membrane
Lipid-anchor
Cytoplasmic side . Cell projection, cilium . Recruited to phagosomes containing S.aureus or M.tuberculosis (PubMed:21255211).
Protein Description Protein transport. Involved in the redistribution of lysosomes to the peri-Golgi region (By similarity). Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. [PubMed: 21255211 Plays a role in the fusion of phagosomes with lysosomes]
Protein Sequence MNILAPVRRDRVLAELPQCLRKEAALHGHKDFHPRVTCACQEHRTGTVGFKISKVIVVGDLSVGKTCLINRFCKDTFDKNYKATIGVDFEMERFEVLGIPFSLQLWDTAGQERFKCIASTYYRGAQAIIIVFNLNDVASLEHTKQWLADALKENDPSSVLLFLVGSKKDLSTPAQYALMEKDALQVAQEMKAEYWAVSSLTGENVREFFFRVAALTFEANVLAELEKSGARRIGDVVRINSDDSNLYLTASKKKPTCCP
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
1Acetylation-------MNILAPVR
-------CCCCCCCC
6.7622223895
22UbiquitinationELPQCLRKEAALHGH
HHHHHHHHHHHHCCC
38.46-
30UbiquitinationEAALHGHKDFHPRVT
HHHHCCCCCCCCCCE
67.68-
51UbiquitinationRTGTVGFKISKVIVV
CCCCCCEEEEEEEEE
39.89-
62PhosphorylationVIVVGDLSVGKTCLI
EEEECCCCCCCCHHH
33.30-
74UbiquitinationCLINRFCKDTFDKNY
HHHCHHCHHCCCCCC
58.03-
76PhosphorylationINRFCKDTFDKNYKA
HCHHCHHCCCCCCCE
21.1629255136
79UbiquitinationFCKDTFDKNYKATIG
HCHHCCCCCCCEEEE
58.97-
81PhosphorylationKDTFDKNYKATIGVD
HHCCCCCCCEEEECE
14.0322817900
108PhosphorylationFSLQLWDTAGQERFK
EEEEEECCCCHHHHH
22.5528857561
146UbiquitinationSLEHTKQWLADALKE
CHHHHHHHHHHHHHH
8.6221890473
157PhosphorylationALKENDPSSVLLFLV
HHHHCCCCCEEEEEE
35.6220068231
157 (in isoform 2)Phosphorylation-35.6222210691
158PhosphorylationLKENDPSSVLLFLVG
HHHCCCCCEEEEEEC
23.3620068231
158 (in isoform 2)Phosphorylation-23.3622210691
164 (in isoform 2)Phosphorylation-6.7922210691
166PhosphorylationVLLFLVGSKKDLSTP
EEEEEECCCCCCCCH
29.1120068231
1672-HydroxyisobutyrylationLLFLVGSKKDLSTPA
EEEEECCCCCCCCHH
44.36-
168 (in isoform 1)Ubiquitination-66.6521890473
168UbiquitinationLFLVGSKKDLSTPAQ
EEEECCCCCCCCHHH
66.652189047
168 (in isoform 2)Phosphorylation-66.6522210691
181UbiquitinationAQYALMEKDALQVAQ
HHHHHHHHHHHHHHH
34.04-
227UbiquitinationNVLAELEKSGARRIG
HHHHHHHHCCCCEEC
67.81-
230UbiquitinationAELEKSGARRIGDVV
HHHHHCCCCEECCEE
12.5021890473
241PhosphorylationGDVVRINSDDSNLYL
CCEEEECCCCCCEEE
40.1823401153
244PhosphorylationVRINSDDSNLYLTAS
EEECCCCCCEEEEEC
33.4525159151
244 (in isoform 2)Ubiquitination-33.4521890473
247PhosphorylationNSDDSNLYLTASKKK
CCCCCCEEEEECCCC
13.2721945579
249PhosphorylationDDSNLYLTASKKKPT
CCCCEEEEECCCCCC
18.4821945579
251PhosphorylationSNLYLTASKKKPTCC
CCEEEEECCCCCCCC
39.5121945579
252UbiquitinationNLYLTASKKKPTCCP
CEEEEECCCCCCCCC
63.4521139048
2522-HydroxyisobutyrylationNLYLTASKKKPTCCP
CEEEEECCCCCCCCC
63.45-
252 (in isoform 1)Ubiquitination-63.4521890473
257GeranylgeranylationASKKKPTCCP-----
ECCCCCCCCC-----
4.39-
258GeranylgeranylationSKKKPTCCP------
CCCCCCCCC------
5.02-

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
247YPhosphorylationKinaseSRCP12931
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAB34_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 RAB34_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GDS1_HUMANRAP1GDS1physical
26186194
GDS1_HUMANRAP1GDS1physical
28514442
SNX11_HUMANSNX11physical
28514442

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RAB34_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND MASSSPECTROMETRY.

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