RB27A_HUMAN - dbPTM
RB27A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RB27A_HUMAN
UniProt AC P51159
Protein Name Ras-related protein Rab-27A
Gene Name RAB27A
Organism Homo sapiens (Human).
Sequence Length 221
Subcellular Localization Membrane
Lipid-anchor . Melanosome . Late endosome . Lysosome . Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:12643545, PubMed:17081065). Localizes to endosomal exocytic vesicles (PubMed:17237785).
Protein Description Plays a role in cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse..
Protein Sequence MSDGDYDYLIKFLALGDSGVGKTSVLYQYTDGKFNSKFITTVGIDFREKRVVYRASGPDGATGRGQRIHLQLWDTAGQERFRSLTTAFFRDAMGFLLLFDLTNEQSFLNVRNWISQLQMHAYCENPDIVLCGNKSDLEDQRVVKEEEAIALAEKYGIPYFETSAANGTNISQAIEMLLDLIMKRMERCVDKSWIPEGVVRSNGHASTDQLSEEKEKGACGC
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
2Phosphorylation------MSDGDYDYL
------CCCCCHHHH		50.7530108239
2Acetylation------MSDGDYDYL
------CCCCCHHHH		50.7522223895
6Phosphorylation--MSDGDYDYLIKFL
--CCCCCHHHHHEEE		16.4126552605
8PhosphorylationMSDGDYDYLIKFLAL
CCCCCHHHHHEEEEE		12.2326552605
18PhosphorylationKFLALGDSGVGKTSV
EEEEECCCCCCCEEE		33.3120068231
27PhosphorylationVGKTSVLYQYTDGKF
CCCEEEEEEECCCCC		9.4123917254
33 (in isoform 2)Ubiquitination-44.1521890473
33 (in isoform 1)Ubiquitination-44.1521890473
33UbiquitinationLYQYTDGKFNSKFIT
EEEECCCCCCCEEEE		44.1521890473
64MethylationGPDGATGRGQRIHLQ
CCCCCCCCCCEEEEE		33.4416289449
75PhosphorylationIHLQLWDTAGQERFR
EEEEEECCCCHHHHH		22.5528857561
83PhosphorylationAGQERFRSLTTAFFR
CCHHHHHHHHHHHHH		27.6228450419
85PhosphorylationQERFRSLTTAFFRDA
HHHHHHHHHHHHHHH		19.8223186163
86PhosphorylationERFRSLTTAFFRDAM
HHHHHHHHHHHHHHH		27.1023186163
144UbiquitinationLEDQRVVKEEEAIAL
HCCHHHHCHHHHHHH		57.46-
155PhosphorylationAIALAEKYGIPYFET
HHHHHHHHCCCEEEC		16.2828851738
159PhosphorylationAEKYGIPYFETSAAN
HHHHCCCEEECCCCC		16.4828851738
162PhosphorylationYGIPYFETSAANGTN
HCCCEEECCCCCCCC		17.4828851738
163PhosphorylationGIPYFETSAANGTNI
CCCEEECCCCCCCCH		20.4128851738
168PhosphorylationETSAANGTNISQAIE
ECCCCCCCCHHHHHH		29.2325332170
171PhosphorylationAANGTNISQAIEMLL
CCCCCCHHHHHHHHH		18.6725332170
191UbiquitinationRMERCVDKSWIPEGV
HHHHHCCHHHCCCCC		27.56-
192PhosphorylationMERCVDKSWIPEGVV
HHHHCCHHHCCCCCC		26.2727251275
201PhosphorylationIPEGVVRSNGHASTD
CCCCCCCCCCCCCHH		35.2429255136
206PhosphorylationVRSNGHASTDQLSEE
CCCCCCCCHHHCCHH		27.1723401153
207PhosphorylationRSNGHASTDQLSEEK
CCCCCCCHHHCCHHH		28.6623401153
211PhosphorylationHASTDQLSEEKEKGA
CCCHHHCCHHHHHCC		37.7723927012
219GeranylgeranylationEEKEKGACGC-----
HHHHHCCCCC-----		8.56-
221MethylationKEKGACGC-------
HHHCCCCC-------		5.18-
221GeranylgeranylationKEKGACGC-------
HHHCCCCC-------		5.18-
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 RB27A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RB27A_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 RB27A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SYTL4_HUMANSYTL4physical
11865063
RPH3L_HUMANRPH3ALphysical
14593078
SYTL1_HUMANSYTL1physical
12590134
SYTL5_HUMANSYTL5physical
12590134
MYRIP_HUMANMYRIPphysical
12590134
SYTL2_HUMANSYTL2physical
12590134
SYTL3_HUMANSYTL3physical
12590134
SYTL4_HUMANSYTL4physical
12590134
EF1A1_HUMANEEF1A1physical
16169070
ZBT16_HUMANZBTB16physical
16169070
ERG28_HUMANC14orf1physical
16169070
CSN6_HUMANCOPS6physical
16169070
RBM48_HUMANRBM48physical
16169070
GDF9_HUMANGDF9physical
16169070
CE126_HUMANKIAA1377physical
16169070
LRIF1_HUMANLRIF1physical
16169070
SYTL4_HUMANSYTL4physical
12101244
MELPH_HUMANMLPHphysical
12062444
MYO5A_HUMANMYO5Aphysical
12062444
SYTL1_HUMANSYTL1physical
11980908
SYTL2_HUMANSYTL2physical
11980908
MELPH_HUMANMLPHphysical
11980908
SYTL1_HUMANSYTL1physical
11773082
MELPH_HUMANMLPHphysical
11773082
SYTL2_HUMANSYTL2physical
11773082
SYTL3_HUMANSYTL3physical
11773082
SYTL4_HUMANSYTL4physical
11773082
A4_HUMANAPPphysical
21832049
Drug and Disease Associations
Kegg Disease
H00101 Other phagocyte defects, including the following eight diseases: Chediak-Higashi syndrome; Griscelli
OMIM Disease
607624Griscelli syndrome 2 (GS2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RB27A_HUMAN

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Related Literatures of Post-Translational Modification

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