UniProt Accession

 RALA_HUMAN; P11233; A4D1W3 

Genbank Protein ID

 X15014; M29893; AF493910; AC004837; CH236951; CH471073; BC039858 

Genbank Nucleotide ID

 CAA33118.1; AAA36542.1; AAM12624.1; EAL23994.1; EAW94123.1; AAH39858.1 

Protein Name

 Ras-related protein Ral-A 

Protein Synonyms/Alias

  

Gene Name

 RALA 

Gene Synonyms/Alias

 RAL 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
7	*MAANKPKGQNSLAL	ubiquitination	[1, 2]
134	NKSDLEDKRQVSVEE	ubiquitination	[3]
143	QVSVEEAKNRAEQWN	ubiquitination	[2, 3]
159	NYVETSAKTRANVDK	ubiquitination	[3, 4, 5, 6]

Reference

 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 

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. Plays a role in the early stages of cytokinesis and is required to tether the exocyst to the cytokinetic furrow. The RALA-exocyst complex regulates integrin- dependent membrane raft exocytosis and growth signaling. Key regulator of LPAR1 signaling and competes with ADRBK1 for binding to LPAR1 thus affecting the signaling properties of the receptor. Required for anchorage-independent proliferation of transformed cells. 

Sequence Annotation

 NP_BIND 24 29 GTP.
 NP_BIND 40 46 GTP.
 NP_BIND 127 130 GTP.
 MOTIF 43 51 Effector region (By similarity).
 MOD_RES 203 203 Cysteine methyl ester.
 LIPID 203 203 S-geranylgeranyl cysteine.  

Keyword

 3D-structure; Cell cycle; Cell division; Cell membrane; Complete proteome; Exocytosis; GTP-binding; Host-virus interaction; Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 206 AA 

Protein Sequence

Gene Ontology

 GO:0009986; C:cell surface; IDA:UniProtKB.
 GO:0032154; C:cleavage furrow; IDA:UniProtKB.
 GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
 GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0031755; F:Edg-2 lysophosphatidic acid receptor binding; IDA:UniProtKB.
 GO:0005525; F:GTP binding; TAS:ProtInc.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0031532; P:actin cytoskeleton reorganization; IDA:BHF-UCL.
 GO:0016044; P:cellular membrane organization; TAS:Reactome.
 GO:0006935; P:chemotaxis; TAS:ProtInc.
 GO:0000910; P:cytokinesis; IDA:UniProtKB.
 GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
 GO:0051665; P:membrane raft localization; IDA:UniProtKB.
 GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
 GO:0051491; P:positive regulation of filopodium assembly; IDA:BHF-UCL.
 GO:0007265; P:Ras protein signal transduction; TAS:Reactome.
 GO:0017157; P:regulation of exocytosis; IDA:UniProtKB.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 

Interpro

 IPR027417; P-loop_NTPase.
 IPR005225; Small_GTP-bd_dom.
 IPR001806; Small_GTPase.
 IPR020849; Small_GTPase_Ras. 

Pfam

 PF00071; Ras 

SMART

 SM00173; RAS 

PROSITE

 PS51421; RAS 

PRINTS

 PR00449; RASTRNSFRMNG.