| Tag |
Content |
LipidDB ID |
LipidDB-9606-00520 |
Entry Name |
|
UniProt Accession |
|
Theoretical PI |
6.24 |
Molecular Weight |
23408.55 |
Genbank Protein ID |
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Genbank Nucleotide ID |
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Protein Name |
Ras-related protein Ral-B |
Protein Synonyms/Alias |
|
Gene Name |
RALB |
Gene Synonyms/Alias |
|
Created Date |
01-JUL-1989 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
203 | Canonical | KKSFKERCCLL**** | [2] | S-Geranylgeranylation | 204 | Canonical | KSFKERCCLL***** | [1] | S-Palmitoylation |
|
Organism |
Homo sapiens (Human) |
NCBI Taxa ID |
9606 |
Reference |
[1] Predicted from GPS-Lipid
[2] Falsetti SC, Wang DA, Peng H, Carrico D, Cox AD, Der CJ, Hamilton AD, SebtiSM. Geranylgeranyltransferase I inhibitors target RalB to inhibitanchorage-dependent growth and induce apoptosis and RalA to inhibitanchorage-independent growth. Mol Cell Biol. 2007 Nov;27(22):8003-14. Epub 2007Sep 17.[ PMID:17875936]
|
Functional Description |
Multifunctional GTPase involved in a variety of cellular processes including gene expression, cell migration, cell proliferation, oncogenic transformation and membrane trafficking. Accomplishes its multiple functions by interacting with distinct downstream effectors. Acts as a GTP sensor for GTP-dependent exocytosis of dense core vesicles. Required both to stabilize the assembly of the exocyst complex and to localize functional exocyst complexes to the leading edge of migrating cells. Plays a role in the late stages of cytokinesis and is required for the abscission of the bridge joining the sister cells emerging from mitosis. Required for suppression of apoptosis. |
Sequence Annotation |
Nucleotide-binding: 21 29 GTP.
Nucleotide-binding: 68 72 GTP.
Nucleotide-binding: 128 131 GTP.
Nucleotide-binding: 158 160 GTP.
Motif: 43 51 Effector region.
Modified residue: 203 203 Cysteine methyl ester.
|
Protein Length |
206 AA. |
Protein Sequence
(Canonical) |
MAANKSKGQS SLALHKVIMV GSGGVGKSAL TLQFMYDEFV EDYEPTKADS YRKKVVLDGE 60
EVQIDILDTA GQEDYAAIRD NYFRSGEGFL LVFSITEHES FTATAEFREQ ILRVKAEEDK 120
IPLLVVGNKS DLEERRQVPV EEARSKAEEW GVQYVETSAK TRANVDKVFF DLMREIRTKK 180
MSENKDKNGK KSSKNKKSFK ERCCLL 206
MAANKSKGQS SLALHKVIMV GSGGVGKSAL TLQFMYDEFV EDYEPTKADS YRKKVVLDGE 60
EVQIDILDTA GQEDYAAIRD NYFRSGEGFL LVFSITEHES FTATAEFREQ ILRVKAEEDK 120
IPLLVVGNKS DLEERRQVPV EEARSKAEEW GVQYVETSAK TRANVDKVFF DLMREIRTKK 180
MSENKDKNGK KSSKNKKSFK ERCCLL 206
|
FASTA
(Canonical) |
>LipidDB-9606-00520|P11234
MAANKSKGQSSLALHKVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGE
EVQIDILDTAGQEDYAAIRDNYFRSGEGFLLVFSITEHESFTATAEFREQILRVKAEEDK
IPLLVVGNKSDLEERRQVPVEEARSKAEEWGVQYVETSAKTRANVDKVFFDLMREIRTKK
MSENKDKNGKKSSKNKKSFKERCCLL
MAANKSKGQSSLALHKVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGE
EVQIDILDTAGQEDYAAIRDNYFRSGEGFLLVFSITEHESFTATAEFREQILRVKAEEDK
IPLLVVGNKSDLEERRQVPVEEARSKAEEWGVQYVETSAKTRANVDKVFFDLMREIRTKK
MSENKDKNGKKSSKNKKSFKERCCLL
|
Gene Ontology |
GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB GO:0030496; C:midbody; IDA:UniProtKB GO:0005886; C:plasma membrane; IDA:UniProtKB GO:0005525; F:GTP binding; IDA:UniProtKB GO:0003924; F:GTPase activity; IDA:UniProtKB GO:0006915; P:apoptotic process; IEA:UniProtKB-KW GO:0000910; P:cytokinesis; IDA:UniProtKB GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome GO:0007265; P:Ras protein signal transduction; TAS:Reactome GO:0001928; P:regulation of exocyst assembly; ISS:UniProtKB GO:0060178; P:regulation of exocyst localization; ISS:UniProtKB GO:0007165; P:signal transduction; TAS:ProtInc |
Interpro |
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Pfam |
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SMART |
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PROSITE |
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PRINTS |
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