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Reviewed, UniProtKB/Swiss-Prot P36404 (ARL2_HUMAN)

Last modified June 16, 2009. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    ADP-ribosylation factor-like protein 2
Gene names
Name: ARL2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length184 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. Component of a regulated secretory pathway involved in Ca2+-dependent release of acetylcholine. Regulates formation of new microtubules. Required for normal progress through the cell cycle. Ref.7

Subunit structure

Interacts with SCOC and ELMOD2. The GTP-bound form interacts with ARL2BP. Ref.5 Ref.6 Ref.8

Subcellular location

Centrosome. Ref.7

Sequence similarities

Belongs to the small GTPase superfamily. Arf family.

Ontologies

Keywords
   Biological processCell cycle
   Coding sequence diversityPolymorphism
   LigandGTP-binding
Nucleotide-binding
   PTMIsopeptide bond
Lipoprotein
Myristate
Ubl conjugation
   Technical term3D-structure
Gene Ontology (GO)
   Biological processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

tubulin complex assembly

Traceable author statement. Source: ProtInc

   Cellular componentcentrosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase inhibitor activity

Traceable author statement. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Potential
Chain2 – 184183ADP-ribosylation factor-like protein 2
PRO_0000207453

Regions

Nucleotide binding23 – 308GTP By similarity
Nucleotide binding66 – 705GTP By similarity
Nucleotide binding125 – 1284GTP By similarity

Sites

Binding site681GTP; via amide nitrogen By similarity

Amino acid modifications

Lipidation21N-myristoyl glycine Potential
Cross-link71Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9

Natural variations

Natural variant1411V → A: dbSNP rs664226. Ref.1 Ref.3
VAR_028056

Experimental info

Mutagenesis701Q → L: Cell cycle arrest, reduced ability to form microtubules, and centrosome fragmentation. Ref.7

Sequences

Sequence LengthMass (Da)Tools
P36404-1 [UniParc].

Last modified October 17, 2006. Version 4.
Checksum: 0823F005719C17F9

FASTA18420,878
        10         20         30         40         50         60 
MGLLTILKKM KQKERELRLL MLGLDNAGKT TILKKFNGED IDTISPTLGF NIKTLEHRGF 

        70         80         90        100        110        120 
KLNIWDVGGQ KSLRSYWRNY FESTDGLIWV VDSADRQRMQ DCQRELQSLL VEERLAGATL 

       130        140        150        160        170        180 
LIFANKQDLP GALSSNAIRE VLELDSIRSH HWCIQGCSAV TGENLLPGID WLLDDISSRI 


FTAD 

« Hide

References

« Hide 'large scale' references
[1]"Selective amplification of additional members of the ADP-ribosylation factor (ARF) family: cloning of additional human and Drosophila ARF-like genes."
Clark J., Moore L., Krasinskas A., Way J., Battey J.F., Tamkun J.W., Kahn R.A.
Proc. Natl. Acad. Sci. U.S.A. 90:8952-8956(1993) [PubMed: 8415637] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-141.
[2]Kahn R.A.
Submitted (NOV-1997) to UniProtKB
Cited for: SEQUENCE REVISION TO 11.
[3]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Puhl H.L. III, Ikeda S.R., Aronstam R.S.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-141.
Tissue: Brain.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[5]"The ARF-like 2 (ARL2)-binding protein, BART. Purification, cloning, and initial characterization."
Sharer J.D., Kahn R.A.
J. Biol. Chem. 274:27553-27561(1999) [PubMed: 10488091] [Abstract]
Cited for: INTERACTION WITH ARL2BP.
[6]"ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific and shared effectors: characterizing ARL1-binding proteins."
Van Valkenburgh H., Shern J.F., Sharer J.D., Zhu X., Kahn R.A.
J. Biol. Chem. 276:22826-22837(2001) [PubMed: 11303027] [Abstract]
Cited for: INTERACTION WITH SCOC.
[7]"Arl2 and Arl3 regulate different microtubule-dependent processes."
Zhou C., Cunningham L., Marcus A.I., Li Y., Kahn R.A.
Mol. Biol. Cell 17:2476-2487(2006) [PubMed: 16525022] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLN-70, SUBCELLULAR LOCATION.
[8]"ELMOD2 is an Arl2 GTPase-activating protein that also acts on Arfs."
Bowzard J.B., Cheng D., Peng J., Kahn R.A.
J. Biol. Chem. 282:17568-17580(2007) [PubMed: 17452337] [Abstract]
Cited for: INTERACTION WITH ELMOD2.
[9]"Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry."
Meierhofer D., Wang X., Huang L., Kaiser P.
J. Proteome Res. 7:4566-4576(2008) [PubMed: 18781797] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-71, MASS SPECTROMETRY.
[10]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

L13687 mRNA. Translation: AAC37606.1.
AF493888 mRNA. Translation: AAM12602.1.
BC002530 mRNA. Translation: AAH02530.1.
IPIIPI00003326.
PIRA48259.
RefSeqNP_001658.2.
UniGeneHs.502836

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
3DOEX-ray2.25A1-184[»]
3DOFX-ray3.30A1-184[»]
SMRP36404. Positions 1-179.
ModBaseSearch...

Protein-protein interaction databases

IntActP36404. 1 interaction.

PTM databases

PhosphoSiteP36404.

Proteomic databases

PRIDEP36404.

Genome annotation databases

EnsemblENSG00000213465. Homo sapiens. [Contig view]
GeneID402.
KEGGhsa:402.

Organism-specific databases

GeneCardsGC11P064539.
H-InvDBHIX0079275.
HIX0079396.
HGNCHGNC:693. ARL2.
MIM601175. gene.
PharmGKBPA24986.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP36404.
OMAP36404. TDGLVWV.

Gene expression databases

ArrayExpressP36404.
BgeeP36404.
CleanExHS_ARL2.
GermOnlineENSG00000110025. Homo sapiens.

Family and domain databases

InterProIPR006688. ARF.
IPR006689. ARF/SAR.
IPR005225. Small_GTP_bd.
[Graphical view]
PANTHERPTHR11711. ARF/SAR. 1 hit.
PfamPF00025. Arf. 1 hit.
[Graphical view]
PRINTSPR00328. SAR1GTPBP.
SMARTSM00177. ARF. 1 hit.
[Graphical view]
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51417. ARF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio1685.
SOURCESearch...

Entry information

Entry nameARL2_HUMAN
AccessionPrimary (citable) accession number: P36404
Secondary accession number(s): Q9BUK8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: October 17, 2006
Last modified: June 16, 2009
This is version 86 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents