O14576 · DC1I1_HUMAN
- ProteinCytoplasmic dynein 1 intermediate chain 1
- GeneDYNC1I1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids645 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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 | cytoplasm | |
Cellular Component | cytoplasmic dynein complex | |
Cellular Component | cytoplasmic ribonucleoprotein granule | |
Cellular Component | cytosol | |
Cellular Component | kinetochore | |
Cellular Component | microtubule | |
Cellular Component | nucleus | |
Cellular Component | perinuclear region of cytoplasm | |
Cellular Component | recycling endosome | |
Cellular Component | spindle pole | |
Cellular Component | vesicle | |
Molecular Function | cytoskeletal motor activity | |
Molecular Function | dynein heavy chain binding | |
Molecular Function | dynein light chain binding | |
Molecular Function | microtubule binding | |
Molecular Function | microtubule motor activity | |
Molecular Function | spectrin binding | |
Biological Process | transport along microtubule | |
Biological Process | vesicle transport along microtubule |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCytoplasmic dynein 1 intermediate chain 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO14576
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 148 | Disrupts interaction with DYNLT1. | ||||
Sequence: L → G | ||||||
Mutagenesis | 149 | No effect on interaction with DYNLT1. | ||||
Sequence: G → E | ||||||
Mutagenesis | 150 | Disrupts interaction with DYNLT1. | ||||
Sequence: V → G | ||||||
Mutagenesis | 150 | No effect on interaction with DYNLT1. | ||||
Sequence: V → W | ||||||
Mutagenesis | 152 | No effect on interaction with DYNLT1. | ||||
Sequence: K → A or Y | ||||||
Mutagenesis | 153 | Decreases interaction with DYNLT1. | ||||
Sequence: V → G | ||||||
Mutagenesis | 155 | No effect on interaction with DYNLT1. | ||||
Sequence: Q → H, R, T, or Y | ||||||
Mutagenesis | 156 | Decreases interaction with DYNLT1. | ||||
Sequence: V → G | ||||||
Mutagenesis | 157 | No effect on interaction with DYNLT1. | ||||
Sequence: D → R | ||||||
Mutagenesis | 158 | Disrupts interaction with DYNLT1. | ||||
Sequence: F → G | ||||||
Natural variant | VAR_064709 | 373 | found in a renal cell carcinoma case; somatic mutation | |||
Sequence: H → L | ||||||
Natural variant | VAR_048905 | 582 | in dbSNP:rs35077523 | |||
Sequence: N → T |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 675 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylserine | ||||
Sequence: S | |||||||
Chain | PRO_0000114652 | 2-645 | UniProt | Cytoplasmic dynein 1 intermediate chain 1 | |||
Sequence: SDKSDLKAELERKKQRLAQIREEKKRKEEERKKKEADMQQKKEPVQDDSDLDRKRRETEALLQSIGISPEPPLVQPLHFLTWDTCYFHYLVPTPMSPSSKSVSTPSEAGSQDSGDLGPLTRTLQWDTDPSVLQLQSDSELGRRLHKLGVSKVTQVDFLPREVVSYSKETQTPLATHQSEEDEEDEEMVESKVGQDSELENQDKKQEVKEAPPRELTEEEKQQILHSEEFLIFFDRTIRVIERALAEDSDIFFDYSGRELEEKDGDVQAGANLSFNRQFYDEHWSKHRVVTCMDWSLQYPELMVASYNNNEDAPHEPDGVALVWNMKFKKTTPEYVFHCQSSVMSVCFARFHPNLVVGGTYSGQIVLWDNRSHRRTPVQRTPLSAAAHTHPVYCVNVVGTQNAHNLITVSTDGKMCSWSLDMLSTPQESMELVYNKSKPVAVTGMAFPTGDVNNFVVGSEEGTVYTACRHGSKAGIGEVFEGHQGPVTGINCHMAVGPIDFSHLFVTSSFDWTVKLWTTKHNKPLYSFEDNADYVYDVMWSPVHPALFACVDGMGRLDLWNLNNDTEVPTASVAIEGASALNRVRWAQAGKEVAVGDSEGRIWVYDVGELAVPHNDEWTRFARTLVEIRANRADSEEEGTVELSA | |||||||
Modified residue | 50 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 100 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 105 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 107 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 111 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 114 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 170 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 176 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 176 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 179 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 179 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 197 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 635 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 635 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs); the composition seems to vary in respect to the IC, LIC and LC composition. The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits. The ICs and LICs bind directly to the HC dimer and the LCs assemble on the IC dimer. Interacts with DYNC1H1. Interacts with DYNLT1 and DYNLT3. Interacts with DCTN1 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O14576 | BICD2 Q8TD16 | 2 | EBI-366267, EBI-2372628 | |
BINARY | O14576 | DYNLL2 Q96FJ2 | 3 | EBI-366267, EBI-742371 | |
BINARY | O14576 | DYNLRB1 Q9NP97 | 3 | EBI-366267, EBI-372128 | |
BINARY | O14576 | FAM83D Q9H4H8 | 3 | EBI-366267, EBI-2556127 | |
XENO | O14576 | Nde1 Q9CZA6 | 2 | EBI-366267, EBI-309934 | |
BINARY | O14576-2 | APP P05067 | 3 | EBI-25840445, EBI-77613 | |
BINARY | O14576-2 | DCTN1 Q14203-5 | 3 | EBI-25840445, EBI-25840379 | |
BINARY | O14576-2 | MAP1LC3B Q9GZQ8 | 3 | EBI-25840445, EBI-373144 | |
BINARY | O14576-2 | PNP P00491 | 3 | EBI-25840445, EBI-712238 | |
BINARY | O14576-2 | S100B P04271 | 3 | EBI-25840445, EBI-458391 | |
BINARY | O14576-2 | SQSTM1 Q13501 | 3 | EBI-25840445, EBI-307104 | |
BINARY | O14576-2 | SYK P43405-2 | 3 | EBI-25840445, EBI-25892332 | |
BINARY | O14576-2 | UTP14A Q9BVJ6 | 3 | EBI-25840445, EBI-473284 | |
BINARY | O14576-2 | VPS29 Q9UBQ0-2 | 3 | EBI-25840445, EBI-11141397 | |
BINARY | O14576-5 | APP P05067 | 3 | EBI-25936079, EBI-77613 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-58 | Disordered | ||||
Sequence: MSDKSDLKAELERKKQRLAQIREEKKRKEEERKKKEADMQQKKEPVQDDSDLDRKRRE | ||||||
Region | 2-123 | Interaction with DCTN1 | ||||
Sequence: SDKSDLKAELERKKQRLAQIREEKKRKEEERKKKEADMQQKKEPVQDDSDLDRKRRETEALLQSIGISPEPPLVQPLHFLTWDTCYFHYLVPTPMSPSSKSVSTPSEAGSQDSGDLGPLTRT | ||||||
Region | 95-125 | Disordered | ||||
Sequence: PMSPSSKSVSTPSEAGSQDSGDLGPLTRTLQ | ||||||
Region | 147-163 | Interaction with DYNLT1 | ||||
Sequence: KLGVSKVTQVDFLPREV | ||||||
Region | 169-221 | Disordered | ||||
Sequence: ETQTPLATHQSEEDEEDEEMVESKVGQDSELENQDKKQEVKEAPPRELTEEEK | ||||||
Compositional bias | 192-221 | Basic and acidic residues | ||||
Sequence: KVGQDSELENQDKKQEVKEAPPRELTEEEK | ||||||
Repeat | 285-334 | WD 1 | ||||
Sequence: SKHRVVTCMDWSLQYPELMVASYNNNEDAPHEPDGVALVWNMKFKKTTPE | ||||||
Repeat | 338-378 | WD 2 | ||||
Sequence: HCQSSVMSVCFARFHPNLVVGGTYSGQIVLWDNRSHRRTPV | ||||||
Repeat | 387-428 | WD 3 | ||||
Sequence: AHTHPVYCVNVVGTQNAHNLITVSTDGKMCSWSLDMLSTPQE | ||||||
Repeat | 437-477 | WD 4 | ||||
Sequence: SKPVAVTGMAFPTGDVNNFVVGSEEGTVYTACRHGSKAGIG | ||||||
Repeat | 482-527 | WD 5 | ||||
Sequence: GHQGPVTGINCHMAVGPIDFSHLFVTSSFDWTVKLWTTKHNKPLYS | ||||||
Repeat | 530-570 | WD 6 | ||||
Sequence: DNADYVYDVMWSPVHPALFACVDGMGRLDLWNLNNDTEVPT | ||||||
Repeat | 576-615 | WD 7 | ||||
Sequence: EGASALNRVRWAQAGKEVAVGDSEGRIWVYDVGELAVPHN |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative splicing.
O14576-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length645
- Mass (Da)72,955
- Last updated1999-05-01 v2
- Checksum55A6FF971E632DA0
O14576-2
- Name2
- Differences from canonical
- 74-90: Missing
O14576-3
- Name3
O14576-4
- Name4
O14576-5
- Name5
- Differences from canonical
- 123-142: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
C9J3E7 | C9J3E7_HUMAN | DYNC1I1 | 116 | ||
A0A0A0MTG2 | A0A0A0MTG2_HUMAN | DYNC1I1 | 544 | ||
E5RJ75 | E5RJ75_HUMAN | DYNC1I1 | 128 | ||
E5RFE1 | E5RFE1_HUMAN | DYNC1I1 | 85 |
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_001332 | 74-90 | in isoform 2, isoform 3 and isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_001333 | 123-142 | in isoform 3, isoform 4 and isoform 5 | |||
Sequence: Missing | ||||||
Compositional bias | 192-221 | Basic and acidic residues | ||||
Sequence: KVGQDSELENQDKKQEVKEAPPRELTEEEK | ||||||
Sequence conflict | 254 | in Ref. 3; BAG59855 | ||||
Sequence: D → G | ||||||
Sequence conflict | 517 | in Ref. 6; AAH22540 | ||||
Sequence: W → C | ||||||
Alternative sequence | VSP_054766 | 610-645 | in isoform 4 | |||
Sequence: LAVPHNDEWTRFARTLVEIRANRADSEEEGTVELSA → GLAMLPGWSQNSWTQAILLCWPPKVLGLQT |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF063228 EMBL· GenBank· DDBJ | AAC33443.1 EMBL· GenBank· DDBJ | mRNA | ||
AF123074 EMBL· GenBank· DDBJ | AAD26852.1 EMBL· GenBank· DDBJ | mRNA | ||
AK091339 EMBL· GenBank· DDBJ | BAC03639.1 EMBL· GenBank· DDBJ | mRNA | ||
AK297427 EMBL· GenBank· DDBJ | BAG59855.1 EMBL· GenBank· DDBJ | mRNA | ||
AC022261 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC091779 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC002452 EMBL· GenBank· DDBJ | AAB67047.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC002540 EMBL· GenBank· DDBJ | AAB70113.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471091 EMBL· GenBank· DDBJ | EAW76753.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC022540 EMBL· GenBank· DDBJ | AAH22540.1 EMBL· GenBank· DDBJ | mRNA |