Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00244
Entry Name
UniProt Accession
Theoretical PI
8.53
Molecular Weight
23025.22
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Ras-related protein Rab-35
Protein Synonyms/Alias
GTP-binding protein RAY; Ras-related protein Rab-1C;
Gene Name
RAB35
Gene Synonyms/Alias
RAB1C; RAY;
Created Date
15-JUL-1998
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
200
Canonical
NSKRKKRCC******
[1]
S-Geranylgeranylation
201
Canonical
SKRKKRCC*******
[1]
S-Geranylgeranylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Gavriljuk K, Itzen A, Goody RS, Gerwert K, Kötting C. Membrane extraction ofRab proteins by GDP dissociation inhibitor characterized using attenuated totalreflection infrared spectroscopy. Proc Natl Acad Sci U S A. 2013 Aug13;110(33):13380-5. doi: 10.1073/pnas.1307655110. Epub 2013 Jul 29.[PMID:23898197]
Functional 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 sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in the process of endocytosis and is an essential rate-limiting regulator of the fast recycling pathway back to the plasma membrane. During cytokinesis, required for the postfurrowing terminal steps, namely for intercellular bridge stability and abscission, possibly by controlling phosphatidylinositol 4,5-bis phosphate (PIP2) and SEPT2 localization at the intercellular bridge. May indirectly regulate neurite outgrowth.
Sequence Annotation
Nucleotide-binding: 15 22 GTP.
Nucleotide-binding: 63 67 GTP.
Nucleotide-binding: 120 123 GTP.
Motif: 37 45 Effector region.
Modified residue: 75 75 O-(2-cholinephosphoryl)serine; byLegionella AnkX.
Modified residue: 77 77 O-AMP-tyrosine; by Legionella DrrA.
Protein Length
201 AA.
Protein Sequence
(Canonical)
MARDYDHLFK LLIIGDSGVG KSSLLLRFAD NTFSGSYITT IGVDFKIRTV EINGEKVKLQ  60
IWDTAGQERF RTITSTYYRG THGVIVVYDV TSAESFVNVK RWLHEINQNC DDVCRILVGN  120
KNDDPERKVV ETEDAYKFAG QMGIQLFETS AKENVNVEEM FNCITELVLR AKKDNLAKQQ  180
QQQQNDVVKL TKNSKRKKRC C                                            201
FASTA
(Canonical)
>LipidDB-9606-00244|Q15286
MARDYDHLFKLLIIGDSGVGKSSLLLRFADNTFSGSYITTIGVDFKIRTVEINGEKVKLQ
IWDTAGQERFRTITSTYYRGTHGVIVVYDVTSAESFVNVKRWLHEINQNCDDVCRILVGN
KNDDPERKVVETEDAYKFAGQMGIQLFETSAKENVNVEEMFNCITELVLRAKKDNLAKQQ
QQQQNDVVKLTKNSKRKKRCC
Gene Ontology
GO:0031253; C:cell projection membrane; IDA:UniProtKB
GO:0045334; C:clathrin-coated endocytic vesicle; IDA:UniProtKB
GO:0005905; C:coated pit; IDA:UniProtKB
GO:0010008; C:endosome membrane; ISS:UniProtKB
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0045171; C:intercellular bridge; IDA:UniProtKB
GO:0005739; C:mitochondrion; IEA:Ensembl
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0019003; F:GDP binding; IDA:UniProtKB
GO:0005525; F:GTP binding; IDA:UniProtKB
GO:0003924; F:GTPase activity; IDA:UniProtKB
GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB
GO:0019882; P:antigen processing and presentation; IMP:UniProt
GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB
GO:0000910; P:cytokinesis; IMP:UniProtKB
GO:0016197; P:endosomal transport; IMP:UniProtKB
GO:0006184; P:GTP catabolic process; IDA:UniProtKB
GO:0031175; P:neuron projection development; ISS:UniProtKB
GO:0048227; P:plasma membrane to endosome transport; IMP:UniProtKB
GO:0008104; P:protein localization; IMP:UniProtKB
GO:0036010; P:protein localization to endosome; IMP:UniProtKB
GO:0015031; P:protein transport; IEA:UniProtKB-KW
GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro
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;