Reviewed,
UniProtKB/Swiss-Prot P40616 (ARL1_HUMAN)
Last modified
November 25, 2008.
Version 83.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: ADP-ribosylation factor-like protein 1 | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 181 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Does not act as an allosteric activator of the cholera toxin catalytic subunit By similarity. |
| Subunit structure | Interacts with SCOC. |
| Sequence similarities | Belongs to the small GTPase superfamily. Arf family. |
Ontologies
Keywords | |
|---|---|
| Ligand | GTP-binding Nucleotide-binding |
| PTM | Lipoprotein Myristate |
| Technical term | 3D-structure |
Gene Ontology (GO) | |
| Biological process | small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro |
| Cellular component | Golgi apparatus Inferred from direct assay. Source: LIFEdb |
| Molecular function | GTP binding Inferred from electronic annotation. Source: InterPro GTPase activityTraceable author statement. Source: ProtInc enzyme activator activityTraceable author statement. Source: ProtInc protein bindingInferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| CDK5RAP3 | Q96JB5 | 1 | EBI-1052746,EBI-718818 | |
| RIOK3 | O14730 | 1 | EBI-1052746,EBI-1047061 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Potential | ||||||||||||||||||||||||||||||||||
| Chain | 2 – 181 | 180 | ADP-ribosylation factor-like protein 1 | PRO_0000207450 | |||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||
| Nucleotide binding | 24 – 31 | 8 | GTP By similarity | ||||||||||||||||||||||||||||||||||
| Nucleotide binding | 67 – 71 | 5 | GTP By similarity | ||||||||||||||||||||||||||||||||||
| Nucleotide binding | 126 – 129 | 4 | GTP By similarity | ||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||
| Lipidation | 2 | 1 | N-myristoyl glycine Potential | ||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||
| Beta strand | 18 – 23 | 6 | |||||||||||||||||||||||||||||||||||
| Helix | 30 – 39 | 10 | |||||||||||||||||||||||||||||||||||
| Beta strand | 49 – 58 | 10 | |||||||||||||||||||||||||||||||||||
| Beta strand | 61 – 68 | 8 | |||||||||||||||||||||||||||||||||||
| Helix | 72 – 81 | 10 | |||||||||||||||||||||||||||||||||||
| Beta strand | 86 – 93 | 8 | |||||||||||||||||||||||||||||||||||
| Helix | 100 – 111 | 12 | |||||||||||||||||||||||||||||||||||
| Helix | 114 – 116 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 120 – 126 | 7 | |||||||||||||||||||||||||||||||||||
| Helix | 136 – 143 | 8 | |||||||||||||||||||||||||||||||||||
| Helix | 145 – 147 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 153 – 157 | 5 | |||||||||||||||||||||||||||||||||||
| Turn | 160 – 162 | 3 | |||||||||||||||||||||||||||||||||||
| Helix | 166 – 178 | 13 | |||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | Rosenwald A.G., Kahn R.A. Submitted (JAN-1995) to UniProtKB Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Umbilical vein endothelial cell. |
| [2] | "Different ARF domains are required for the activation of cholera toxin and phospholipase D." Zhang G.-F., Patton W.A., Lee F.-J.S., Liyange M., Han J.-S., Rhee S.G., Moss J., Vaughan M. J. Biol. Chem. 270:21-24(1995) [PubMed: 7814376] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [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]. 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: Urinary bladder. |
| [5] | "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. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| L28997 mRNA. Translation: AAC37567.1. AF493887 mRNA. Translation: AAM12601.1. BC007000 mRNA. Translation: AAH07000.1. | |||||||||||||
| RefSeq | NP_001168.1. | ||||||||||||
| UniGene | Hs.372616 | ||||||||||||
3D structure databases | |||||||||||||
| |||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | P40616. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | P40616. | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSG00000120805. Homo sapiens. [Contig view] | ||||||||||||
| GeneID | 400. | ||||||||||||
| KEGG | hsa:400. | ||||||||||||
Organism-specific databases | |||||||||||||
| H-InvDB | HIX0010921. | ||||||||||||
| HGNC | HGNC:692. ARL1. | ||||||||||||
| MIM | 603425. gene. | ||||||||||||
| PharmGKB | PA24985. | ||||||||||||
| GenAtlas | Search... | ||||||||||||
| GeneCards | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | P40616. | ||||||||||||
| HOVERGEN | P40616. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | P40616. | ||||||||||||
| CleanEx | HS_ARL1. | ||||||||||||
| GermOnline | ENSG00000120805. Homo sapiens. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR006688. ARF. IPR006689. ARF/SAR. IPR001806. Ras_trnsfrmng. IPR005225. Small_GTP_bd. [Graphical view] | ||||||||||||
| PANTHER | PTHR11711. ARF/SAR. 1 hit. | ||||||||||||
| Pfam | PF00025. Arf. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00449. RASTRNSFRMNG. PR00328. SAR1GTPBP. | ||||||||||||
| SMART | SM00177. ARF. 1 hit. [Graphical view] | ||||||||||||
| TIGRFAMs | TIGR00231. small_GTP. 1 hit. | ||||||||||||
| PROSITE | PS01019. ARF. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other Resources | |||||||||||||
| NextBio | 1677. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | ARL1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P40616 Secondary accession number(s): P80417 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 12 Human chromosome 12: entries, gene names and cross-references to MIM |
| 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 |

Clusters with


