P38696 · ARP1_YEAST
- ProteinCentractin
- GeneARP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids384 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Core component of the dynactin complex which assists cytoplasmic dynein by increasing its processivity and by regulation of its cargo binding (By similarity).
The dynactin complex is required for the spindle translocation late in anaphase and is involved in a cell wall synthesis checkpoint. ARP1 forms the backbone filament of the dynactin rod structure and serves as the scaffold for the remaining subunits. Required for proper orientation of the mitotic spindle
The dynactin complex is required for the spindle translocation late in anaphase and is involved in a cell wall synthesis checkpoint. ARP1 forms the backbone filament of the dynactin rod structure and serves as the scaffold for the remaining subunits. Required for proper orientation of the mitotic spindle
Miscellaneous
Present with 1580 molecules/cell in log phase SD medium.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | actin cytoskeleton | |
Cellular Component | cytoplasm | |
Cellular Component | dynactin complex | |
Cellular Component | dynein complex | |
Cellular Component | membrane | |
Cellular Component | microtubule | |
Molecular Function | structural constituent of cytoskeleton | |
Biological Process | actin filament-based movement | |
Biological Process | establishment of mitotic spindle orientation | |
Biological Process | mitotic spindle orientation checkpoint signaling | |
Biological Process | nuclear migration |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCentractin
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP38696
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Membrane-associated.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 2 | Temperature-sensitive; when associated with A-6. | ||||
Sequence: D → A | ||||||
Mutagenesis | 6 | Temperature-sensitive; when associated with A-2. | ||||
Sequence: D → A | ||||||
Mutagenesis | 46 | Strongly reduces interaction with JNM1. Reduces nuclear migration in mitosis; when associated with 48-A-A-49. | ||||
Sequence: K → A | ||||||
Mutagenesis | 48-49 | Strongly reduces interaction with JNM1. Reduces nuclear migration in mitosis; when associated with A-46. | ||||
Sequence: DK → AA | ||||||
Mutagenesis | 73 | Reduces spindle formation; when associated with A-75. | ||||
Sequence: K → A | ||||||
Mutagenesis | 75 | Reduces spindle formation; when associated with A-73. | ||||
Sequence: R → A | ||||||
Mutagenesis | 79-80 | Reduces nuclear migration in mitosis. | ||||
Sequence: KH → AA | ||||||
Mutagenesis | 84-85 | Reduces spindle formation. Strongly reduces interaction with JNM1. Reduces nuclear migration in mitosis; when associated with A-87. | ||||
Sequence: ED → AA | ||||||
Mutagenesis | 87 | Reduces spindle formation. Reduces nuclear migration in mitosis; when associated with 84-A-A-85. | ||||
Sequence: D → A | ||||||
Mutagenesis | 108-109 | Reduces nuclear migration in mitosis. | ||||
Sequence: EH → AA | ||||||
Mutagenesis | 133 | Lethal. Strongly reduces interaction with JNM1; when associated with A-136. | ||||
Sequence: E → A | ||||||
Mutagenesis | 136 | Lethal. Strongly reduces interaction with JNM1; when associated with A-133. | ||||
Sequence: D → A | ||||||
Mutagenesis | 162 | Reduces spindle formation. Reduces nuclear migration in mitosis; when associated with A-165. | ||||
Sequence: D → A | ||||||
Mutagenesis | 165 | Reduces spindle formation. Reduces nuclear migration in mitosis; when associated with A-162. | ||||
Sequence: E → A | ||||||
Mutagenesis | 185 | Temperature-sensitive. Strongly reduces interaction with JNM1; when associated with A-187. | ||||
Sequence: R → A | ||||||
Mutagenesis | 187 | Temperature-sensitive. Strongly reduces interaction with JNM1; when associated with A-185. | ||||
Sequence: D → A | ||||||
Mutagenesis | 214-216 | Lethal. Reduces spindle formation. Reduces nuclear migration in mitosis. Alters complex assembly; when associated with A-219. | ||||
Sequence: ERE → AAA | ||||||
Mutagenesis | 219 | Lethal; when associated with 214-A--A-216. | ||||
Sequence: R → A | ||||||
Mutagenesis | 222-224 | Lethal. Reduces spindle formation. Reduces nuclear migration in mitosis. | ||||
Sequence: KEK → AAA | ||||||
Mutagenesis | 233-235 | Reduces spindle formation. | ||||
Sequence: KKE → AAA | ||||||
Mutagenesis | 233-238 | Temperature-sensitive. Strongly reduces interaction with JNM1. | ||||
Sequence: KKEEEK → AAAAAA | ||||||
Mutagenesis | 236-238 | Reduces spindle formation. | ||||
Sequence: EEK → AAA | ||||||
Mutagenesis | 251 | Lethal and dominant cold-sensitive. Reduces nuclear migration in mitosis; when associated with A-254. | ||||
Sequence: K → A | ||||||
Mutagenesis | 254 | Lethal and dominant cold-sensitive. Reduces nuclear migration in mitosis; when associated with A-251. | ||||
Sequence: D → A | ||||||
Mutagenesis | 263-264 | Reduces spindle formation. | ||||
Sequence: DR → AA | ||||||
Mutagenesis | 266 | Lethal. Reduces spindle formation. Reduces nuclear migration in mitosis; when associated with A-269. | ||||
Sequence: R → A | ||||||
Mutagenesis | 269 | Lethal. Reduces spindle formation. Reduces nuclear migration in mitosis; when associated with A-266. | ||||
Sequence: E → A | ||||||
Mutagenesis | 294 | Reduces nuclear migration in mitosis; when associated with A-296 and A-298. | ||||
Sequence: K → A | ||||||
Mutagenesis | 296 | Reduces nuclear migration in mitosis; when associated with A-294 and A-298. | ||||
Sequence: D → A | ||||||
Mutagenesis | 298 | Reduces nuclear migration in mitosis; when associated with A-294 and A-296. | ||||
Sequence: D → A | ||||||
Mutagenesis | 321-322 | Lethal. Strongly reduces interaction with JNM1. | ||||
Sequence: DR → AA | ||||||
Mutagenesis | 326 | Temperature-sensitive. Reduces nuclear migration in mitosis. Strongly reduces interaction with JNM1; when associated with A-328. | ||||
Sequence: D → A | ||||||
Mutagenesis | 328 | Temperature-sensitive. Reduces nuclear migration in mitosis. Strongly reduces interaction with JNM1; when associated with A-326. | ||||
Sequence: E → A | ||||||
Mutagenesis | 336 | Strongly reduces interaction with JNM1; when associated with A-338. | ||||
Sequence: K → A | ||||||
Mutagenesis | 338 | Strongly reduces interaction with JNM1; when associated with A-336. | ||||
Sequence: K → A | ||||||
Mutagenesis | 344-346 | Temperature-sensitive. Reduces nuclear migration in mitosis. Strongly reduces interaction with JNM1. | ||||
Sequence: ERK → AAA | ||||||
Mutagenesis | 368-369 | Reduces nuclear migration in mitosis; when associated with A-371. | ||||
Sequence: KK → AA | ||||||
Mutagenesis | 369 | Lethal. Strongly reduces interaction with JNM1; when associated with A-371. | ||||
Sequence: K → A | ||||||
Mutagenesis | 371 | Lethal. Strongly reduces interaction with JNM1; when associated with A-369. | ||||
Sequence: D → A | ||||||
Mutagenesis | 371 | Reduces nuclear migration in mitosis; when associated with 368-A-A-369. | ||||
Sequence: D → AA | ||||||
Mutagenesis | 374-375 | Temperature-sensitive. Reduces nuclear migration in mitosis. Strongly reduces interaction with JNM1; when associated with A-378. | ||||
Sequence: ED → AA | ||||||
Mutagenesis | 378 | Temperature-sensitive. Reduces nuclear migration in mitosis. Strongly reduces interaction with JNM1; when associated with 374-A-A-375. | ||||
Sequence: R → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 5 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000089066 | 1-384 | Centractin | |||
Sequence: MDQLSDSYALYNQPVVIDNGSGIIKAGFSGEERPKALEYCLVGNTKYDKVMLEGLQGDTFIGNNAQKLRGLLKLRYPIKHGVVEDWDSMELIWSYVLNEVLQLQNIGEHPLLITEAPMNPLKNREQMAQVLFETFDVSALYVSNPAVLSLYASGRTTGCVVDCGEGYCSTVPIYDGFALPASMMRMDIGGADITEQLQFQLRKSAGVSLFSSSEREIVRTMKEKVCYLAKNIKKEEEKYLQGTQDLISTFKLPDGRCIEVGNDRYRAPEILFSPQIIGLGYDGLSDMCMQSIWKVDLDLRKPLLSSIILSGGTTTLKGFGDRMLWDLEALTKGTSKIKIIAPSERKYTTWIGGSILTGLSTFQRLWTKKSDWLEDSTRVYSNLM |
Proteomic databases
Interaction
Subunit
Self-associates to form an actin-like filament of 8-10 monomers. Component of the dynactin complex composed of at least ARP1, JNM1, NIP100 and ARP10. Dynactin comprises a short rod of the ARP1 filament attached to ARP10 at its pointed-end and probably associated with the capping protein at its barbed-end. The rod is implicated in dynein cargo binding. A sidearm formed by NIP100 projects from the ARP1 filament and is implicated in motor binding (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P38696 | ARP10 Q04549 | 5 | EBI-2920, EBI-2977 | |
BINARY | P38696 | JNM1 P36224 | 7 | EBI-2920, EBI-9415 | |
BINARY | P38696 | NIP100 P33420 | 4 | EBI-2920, EBI-12049 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Length384
- Mass (Da)42,995
- Last updated1995-02-01 v1
- Checksum98EEA90DC9497B81
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 3 | in Ref. 5; AAT93103 | ||||
Sequence: Q → P |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X79811 EMBL· GenBank· DDBJ | CAA56206.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U10398 EMBL· GenBank· DDBJ | AAB68412.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY693084 EMBL· GenBank· DDBJ | AAT93103.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006934 EMBL· GenBank· DDBJ | DAA06822.1 EMBL· GenBank· DDBJ | Genomic DNA |