UniProt Accession

 ARL2_HUMAN; P36404; G3V184; Q9BUK8 

Genbank Protein ID

 L13687; AF493888; CN338497; AP000436; CH471076; BC002530 

Genbank Nucleotide ID

 AAC37606.1; AAM12602.1; EAW74333.1; AAH02530.1 

Protein Name

 ADP-ribosylation factor-like protein 2 

Protein Synonyms/Alias

  

Gene Name

 ARL2 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
8	MGLLTILKKMKQKER	ubiquitination	[1]
53	PTLGFNIKTLEHRGF	ubiquitination	[1]
61	TLEHRGFKLNIWDVG	ubiquitination	[1, 2]
71	IWDVGGQKSLRSYWR	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 9]
126	TLLIFANKQDLPGAL	ubiquitination	[6]

Reference

 [1] 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]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry.
 Meierhofer D, Wang X, Huang L, Kaiser P.
 J Proteome Res. 2008 Oct;7(10):4566-76. [PMID: 18781797]
 [4] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
 [5] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [6] 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]
 [7] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [8] 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]
 [9] 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] 

Functional Description

 Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. Regulates formation of new microtubules and centrosome integrity. Prevents the TBCD-induced microtubule destruction. Participates in association with TBCD, in the disassembly of the apical junction complexes. Antagonizes the effect of TBCD on epithelial cell detachment and tight and adherens junctions disassembly. Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. Component of a regulated secretory pathway involved in Ca(2+)-dependent release of acetylcholine. Required for normal progress through the cell cycle. 

Sequence Annotation

 NP_BIND 23 30 GTP (By similarity).
 NP_BIND 66 70 GTP (By similarity).
 NP_BIND 125 128 GTP (By similarity).
 BINDING 68 68 GTP; via amide nitrogen (By similarity).
 MOD_RES 45 45 Phosphoserine.
 LIPID 2 2 N-myristoyl glycine (Potential).
 CROSSLNK 71 71 Glycyl lysine isopeptide (Lys-Gly)  

Keyword

 3D-structure; Alternative splicing; Cell cycle; Complete proteome; Cytoplasm; Cytoskeleton; GTP-binding; Isopeptide bond; Lipoprotein; Mitochondrion; Myristate; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 184 AA 

Protein Sequence

Gene Ontology

 GO:0005813; C:centrosome; IDA:UniProtKB.
 GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
 GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0019003; F:GDP binding; IEA:Compara.
 GO:0005525; F:GTP binding; IMP:UniProtKB.
 GO:0003924; F:GTPase activity; IMP:UniProtKB.
 GO:0005095; F:GTPase inhibitor activity; TAS:ProtInc.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0051297; P:centrosome organization; IMP:UniProtKB.
 GO:0051457; P:maintenance of protein location in nucleus; IDA:UniProtKB.
 GO:0034260; P:negative regulation of GTPase activity; IDA:UniProtKB.
 GO:0010811; P:positive regulation of cell-substrate adhesion; ISS:UniProtKB.
 GO:0031116; P:positive regulation of microtubule polymerization; IDA:UniProtKB.
 GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
 GO:0070830; P:tight junction assembly; ISS:UniProtKB.
 GO:0007021; P:tubulin complex assembly; TAS:ProtInc. 

Interpro

 IPR027417; P-loop_NTPase.
 IPR005225; Small_GTP-bd_dom.
 IPR024156; Small_GTPase_ARF.
 IPR006689; Small_GTPase_ARF/SAR. 

Pfam

 PF00025; Arf 

SMART

 SM00177; ARF 

PROSITE

 PS51417; ARF 

PRINTS

 PR00328; SAR1GTPBP.