Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01411
Entry Name
UniProt Accession
Theoretical PI
5.09
Molecular Weight
24868.07
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Ras-related protein Rab-27A
Protein Synonyms/Alias
Rab-27; GTP-binding protein Ram;
Gene Name
RAB27A
Gene Synonyms/Alias
RAB27;
Created Date
01-OCT-1996
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
219
Canonical
EEKEKGACGC*****
[1]
S-Geranylgeranylation
221
Canonical
KEKGACGC*******
[1]
S-Geranylgeranylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Goody RS, Rak A, Alexandrov K. The structural and mechanistic basis forrecycling of Rab proteins between membrane compartments. Cell Mol Life Sci. 2005 Aug;62(15):1657-70. Review.[PMID:15924270]
Functional Description
Plays a role in cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse.
Sequence Annotation
Nucleotide-binding: 16 24 GTP.
Nucleotide-binding: 74 78 GTP.
Nucleotide-binding: 133 136 GTP.
Nucleotide-binding: 163 165 GTP.
Motif: 38 46 Effector region.
Modified residue: 2 2 N-acetylserine.
Modified residue: 221 221 Cysteine methyl ester.
Protein Length
221 AA.
Protein Sequence
(Canonical)
MSDGDYDYLI KFLALGDSGV GKTSVLYQYT DGKFNSKFIT TVGIDFREKR VVYRASGPDG  60
ATGRGQRIHL QLWDTAGQER FRSLTTAFFR DAMGFLLLFD LTNEQSFLNV RNWISQLQMH  120
AYCENPDIVL CGNKSDLEDQ RVVKEEEAIA LAEKYGIPYF ETSAANGTNI SQAIEMLLDL  180
IMKRMERCVD KSWIPEGVVR SNGHASTDQL SEEKEKGACG C                      221
FASTA
(Canonical)
>LipidDB-9606-01411|P51159
MSDGDYDYLIKFLALGDSGVGKTSVLYQYTDGKFNSKFITTVGIDFREKRVVYRASGPDG
ATGRGQRIHLQLWDTAGQERFRSLTTAFFRDAMGFLLLFDLTNEQSFLNVRNWISQLQMH
AYCENPDIVLCGNKSDLEDQRVVKEEEAIALAEKYGIPYFETSAANGTNISQAIEMLLDL
IMKRMERCVDKSWIPEGVVRSNGHASTDQLSEEKEKGACGC
Gene Ontology
GO:0016324; C:apical plasma membrane; IEA:Ensembl
GO:0030425; C:dendrite; IDA:UniProtKB
GO:0070382; C:exocytic vesicle; IDA:UniProtKB
GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB
GO:0005794; C:Golgi apparatus; IEA:Ensembl
GO:0005770; C:late endosome; IDA:UniProtKB
GO:0005764; C:lysosome; IDA:UniProtKB
GO:0042470; C:melanosome; IDA:UniProtKB
GO:0032585; C:multivesicular body membrane; IDA:UniProtKB
GO:0001750; C:photoreceptor outer segment; IEA:Ensembl
GO:0030667; C:secretory granule membrane; IEA:Ensembl
GO:0019003; F:GDP binding; IDA:UniProtKB
GO:0005525; F:GTP binding; ISS:UniProtKB
GO:0003924; F:GTPase activity; ISS:UniProtKB
GO:0019882; P:antigen processing and presentation; IMP:UniProt
GO:0007596; P:blood coagulation; IEA:Ensembl
GO:0044267; P:cellular protein metabolic process; TAS:Reactome
GO:0043316; P:cytotoxic T cell degranulation; IEA:Ensembl
GO:0006887; P:exocytosis; IDA:UniProtKB
GO:1990182; P:exosomal secretion; IMP:UniProtKB
GO:0030318; P:melanocyte differentiation; IEA:Ensembl
GO:0032402; P:melanosome transport; IEA:Ensembl
GO:0036257; P:multivesicular body organization; IMP:UniProtKB
GO:0071985; P:multivesicular body sorting pathway; IMP:UniProtKB
GO:0043320; P:natural killer cell degranulation; IEA:Ensembl
GO:0045921; P:positive regulation of exocytosis; IMP:UniProtKB
GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB
GO:0006605; P:protein targeting; IEA:Ensembl
GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro
GO:0048489; P:synaptic vesicle transport; TAS:ParkinsonsUK-UCL
Interpro
InterPro; IPR027417; P-loop_NTPase
InterPro; IPR005225; Small_GTP-bd_dom
InterPro; IPR001806; Small_GTPase
InterPro; IPR003579; Small_GTPase_Rab_type
Pfam
Pfam; PF00071; Ras;
SMART
SMART; SM00175; RAB;
PROSITE
PROSITE; PS51419; RAB;
PRINTS
PRINTS; PR00449; RASTRNSFRMNG;