Q13409 · DC1I2_HUMAN
- ProteinCytoplasmic dynein 1 intermediate chain 2
- GeneDYNC1I2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids638 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function (PubMed:31079899).
Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules (PubMed:31079899).
The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150-glued) DCTN1 (By similarity).
Involved in membrane-transport, such as Golgi apparatus, late endosomes and lysosomes (By similarity).
Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules (PubMed:31079899).
The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150-glued) DCTN1 (By similarity).
Involved in membrane-transport, such as Golgi apparatus, late endosomes and lysosomes (By similarity).
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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | centrosome | |
Cellular Component | cytoplasm | |
Cellular Component | cytoplasmic dynein complex | |
Cellular Component | cytosol | |
Cellular Component | dynein complex | |
Cellular Component | microtubule | |
Cellular Component | vesicle | |
Molecular Function | dynein heavy chain binding | |
Molecular Function | dynein light chain binding | |
Molecular Function | microtubule motor activity | |
Biological Process | microtubule-based movement | |
Biological Process | transport along microtubule |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCytoplasmic dynein 1 intermediate chain 2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ13409
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Detected in the cytoplasm of pachytene spermatocytes. Localizes to the manchette in elongating spermatids.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Neurodevelopmental disorder with microcephaly and structural brain anomalies (NEDMIBA)
- Note
- DescriptionAn autosomal recessive neurodevelopmental disorder characterized by global developmental delay, severe intellectual disability, microcephaly, dysmorphic facial features, and cerebral malformations including simplification of cerebral gyration, agenesis of the corpus callosum, and brainstem and white matter hypoplasia.
- See alsoMIM:618492
Natural variants in NEDMIBA
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_082947 | 247 | Y>C | in NEDMIBA; loss-of-function variant; does not rescue neurodevelopmental defects in zebrafish morphants | |
VAR_082948 | 290-638 | missing | in NEDMIBA; loss-of-function variant; does not rescue neurodevelopmental defects in zebrafish morphants | |
VAR_082949 | 516 | P>A | in NEDMIBA; likely benign; can rescue neurodevelopmental defects in zebrafish morphants; dbSNP:rs767705533 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_082947 | 247 | in NEDMIBA; loss-of-function variant; does not rescue neurodevelopmental defects in zebrafish morphants | |||
Sequence: Y → C | ||||||
Natural variant | VAR_082948 | 290-638 | in NEDMIBA; loss-of-function variant; does not rescue neurodevelopmental defects in zebrafish morphants | |||
Sequence: Missing | ||||||
Natural variant | VAR_082949 | 516 | in NEDMIBA; likely benign; can rescue neurodevelopmental defects in zebrafish morphants; dbSNP:rs767705533 | |||
Sequence: P → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 641 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
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_0000114655 | 2-638 | UniProt | Cytoplasmic dynein 1 intermediate chain 2 | |||
Sequence: SDKSELKAELERKKQRLAQIREEKKRKEEERKKKETDQKKEAVAPVQEESDLEKKRREAEALLQSMGLTPESPIVFSEYWVPPPMSPSSKSVSTPSEAGSQDSGDGAVGSRTLHWDTDPSVLQLHSDSDLGRGPIKLGMAKITQVDFPPREIVTYTKETQTPVMAQPKEDEEEDDDVVAPKPPIEPEEEKTLKKDEENDSKAPPHELTEEEKQQILHSEEFLSFFDHSTRIVERALSEQINIFFDYSGRDLEDKEGEIQAGAKLSLNRQFFDERWSKHRVVSCLDWSSQYPELLVASYNNNEDAPHEPDGVALVWNMKYKKTTPEYVFHCQSAVMSATFAKFHPNLVVGGTYSGQIVLWDNRSNKRTPVQRTPLSAAAHTHPVYCVNVVGTQNAHNLISISTDGKICSWSLDMLSHPQDSMELVHKQSKAVAVTSMSFPVGDVNNFVVGSEEGSVYTACRHGSKAGISEMFEGHQGPITGIHCHAAVGAVDFSHLFVTSSFDWTVKLWTTKNNKPLYSFEDNADYVYDVMWSPTHPALFACVDGMGRLDLWNLNNDTEVPTASISVEGNPALNRVRWTHSGREIAVGDSEGQIVIYDVGEQIAVPRNDEWARFGRTLAEINANRADAEEEAATRIPA | |||||||
Modified residue | 51 | UniProt | Diphosphoserine | ||||
Sequence: S | |||||||
Modified residue | 51 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 51 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 73 | UniProt | In isoform Q13409-2; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 73 | UniProt | In isoform Q13409-3; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 73 | UniProt | In isoform Q13409-6; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 81 | UniProt | In isoform Q13409-2; Phosphoserine | ||||
Sequence: W | |||||||
Modified residue | 81 | UniProt | In isoform Q13409-3; Phosphoserine | ||||
Sequence: W | |||||||
Modified residue | 81 | UniProt | In isoform Q13409-6; Phosphoserine | ||||
Sequence: W | |||||||
Modified residue | 84 | UniProt | In isoform Q13409-2; Phosphoserine | ||||
Sequence: P | |||||||
Modified residue | 84 | UniProt | In isoform Q13409-3; Phosphoserine | ||||
Sequence: P | |||||||
Modified residue | 84 | UniProt | In isoform Q13409-6; Phosphoserine | ||||
Sequence: P | |||||||
Modified residue | 90 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 92 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 94 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 95 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 95 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 97 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 97 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 101 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 101 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 104 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 104 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 162 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
The phosphorylation status of Ser-90 appears to be involved in dynactin-dependent target binding.
Pyrophosphorylation by 5-diphosphoinositol pentakisphosphate (5-IP7) promotes interaction with DCTN1. Serine pyrophosphorylation is achieved by Mg2+-dependent, but enzyme independent transfer of a beta-phosphate from a inositol pyrophosphate to a pre-phosphorylated serine residue.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Interaction
Subunit
Homodimer. 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 (PubMed:29420470, PubMed:36071160).
Interacts with DYNLT3 (By similarity).
Interacts with DYNLT1 (PubMed:27502274).
Interacts (dephosphorylated at Ser-90) with DCTN1 (By similarity).
Interacts with BICD2. Interacts with SPEF2 (By similarity).
Interacts with CFAP61 (By similarity).
Interacts with DYNLT3 (By similarity).
Interacts with DYNLT1 (PubMed:27502274).
Interacts (dephosphorylated at Ser-90) with DCTN1 (By similarity).
Interacts with BICD2. Interacts with SPEF2 (By similarity).
Interacts with CFAP61 (By similarity).
(Microbial infection) Interacts with human adenovirus 5 hexon protein; this interaction probably allows virus intracellular transport.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q13409 | DYNLRB1 Q9NP97 | 6 | EBI-742998, EBI-372128 | |
BINARY | Q13409 | DYNLT3 P51808 | 4 | EBI-742998, EBI-743027 | |
BINARY | Q13409-3 | DYNLT1 P63172 | 3 | EBI-12094038, EBI-1176455 | |
BINARY | Q13409-3 | DYNLT3 P51808 | 3 | EBI-12094038, EBI-743027 | |
BINARY | Q13409-3 | NECAB2 Q7Z6G3-2 | 3 | EBI-12094038, EBI-10172876 | |
BINARY | Q13409-3 | PPFIA1 Q13136 | 3 | EBI-12094038, EBI-745426 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-62 | Basic and acidic residues | ||||
Sequence: MSDKSELKAELERKKQRLAQIREEKKRKEEERKKKETDQKKEAVAPVQEESDLEKKRREAEA | ||||||
Region | 1-135 | Disordered | ||||
Sequence: MSDKSELKAELERKKQRLAQIREEKKRKEEERKKKETDQKKEAVAPVQEESDLEKKRREAEALLQSMGLTPESPIVFSEYWVPPPMSPSSKSVSTPSEAGSQDSGDGAVGSRTLHWDTDPSVLQLHSDSDLGRGP | ||||||
Compositional bias | 85-108 | Polar residues | ||||
Sequence: PMSPSSKSVSTPSEAGSQDSGDGA | ||||||
Region | 155-214 | Disordered | ||||
Sequence: TYTKETQTPVMAQPKEDEEEDDDVVAPKPPIEPEEEKTLKKDEENDSKAPPHELTEEEKQ | ||||||
Compositional bias | 180-214 | Basic and acidic residues | ||||
Sequence: APKPPIEPEEEKTLKKDEENDSKAPPHELTEEEKQ | ||||||
Repeat | 277-326 | WD 1 | ||||
Sequence: SKHRVVSCLDWSSQYPELLVASYNNNEDAPHEPDGVALVWNMKYKKTTPE | ||||||
Repeat | 330-370 | WD 2 | ||||
Sequence: HCQSAVMSATFAKFHPNLVVGGTYSGQIVLWDNRSNKRTPV | ||||||
Repeat | 379-420 | WD 3 | ||||
Sequence: AHTHPVYCVNVVGTQNAHNLISISTDGKICSWSLDMLSHPQD | ||||||
Repeat | 429-469 | WD 4 | ||||
Sequence: SKAVAVTSMSFPVGDVNNFVVGSEEGSVYTACRHGSKAGIS | ||||||
Repeat | 474-519 | WD 5 | ||||
Sequence: GHQGPITGIHCHAAVGAVDFSHLFVTSSFDWTVKLWTTKNNKPLYS | ||||||
Repeat | 522-562 | WD 6 | ||||
Sequence: DNADYVYDVMWSPTHPALFACVDGMGRLDLWNLNNDTEVPT | ||||||
Repeat | 568-607 | WD 7 | ||||
Sequence: EGNPALNRVRWTHSGREIAVGDSEGQIVIYDVGEQIAVPR |
Sequence similarities
Belongs to the dynein intermediate chain family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 6 isoforms produced by Alternative splicing.
Q13409-1
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.
- Name2A
- Length638
- Mass (Da)71,457
- Last updated2002-09-19 v3
- Checksum2F868EC9556C47F2
Q13409-2
- Name2B
- Differences from canonical
- 77-82: Missing
Q13409-3
- Name2C
Q13409-5
- Name2E
- Differences from canonical
- 602-602: Missing
Q13409-6
- Name2F
Q13409-7
- Name3
Computationally mapped potential isoform sequences
There are 12 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E7ETL8 | E7ETL8_HUMAN | DYNC1I2 | 184 | ||
E7EU01 | E7EU01_HUMAN | DYNC1I2 | 121 | ||
E7EUM4 | E7EUM4_HUMAN | DYNC1I2 | 137 | ||
E7EV09 | E7EV09_HUMAN | DYNC1I2 | 250 | ||
E7ERH4 | E7ERH4_HUMAN | DYNC1I2 | 151 | ||
E7ERR6 | E7ERR6_HUMAN | DYNC1I2 | 139 | ||
E7ESD3 | E7ESD3_HUMAN | DYNC1I2 | 187 | ||
E7ET01 | E7ET01_HUMAN | DYNC1I2 | 173 | ||
E7EQL5 | E7EQL5_HUMAN | DYNC1I2 | 305 | ||
E7EQU2 | E7EQU2_HUMAN | DYNC1I2 | 185 | ||
E9PGG1 | E9PGG1_HUMAN | DYNC1I2 | 110 | ||
E7EMU4 | E7EMU4_HUMAN | DYNC1I2 | 214 |
Sequence caution
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-62 | Basic and acidic residues | ||||
Sequence: MSDKSELKAELERKKQRLAQIREEKKRKEEERKKKETDQKKEAVAPVQEESDLEKKRREAEA | ||||||
Alternative sequence | VSP_054377 | 76-81 | in isoform 3 | |||
Sequence: VFSEYW → AEQPLRVVTADTCLFHYL | ||||||
Alternative sequence | VSP_001336 | 77-82 | in isoform 2B, isoform 2C and isoform 2F | |||
Sequence: Missing | ||||||
Compositional bias | 85-108 | Polar residues | ||||
Sequence: PMSPSSKSVSTPSEAGSQDSGDGA | ||||||
Alternative sequence | VSP_001337 | 113-132 | in isoform 2C, isoform 2F and isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 180-214 | Basic and acidic residues | ||||
Sequence: APKPPIEPEEEKTLKKDEENDSKAPPHELTEEEKQ | ||||||
Sequence conflict | 510 | in Ref. 1; AAP97254 | ||||
Sequence: T → S | ||||||
Sequence conflict | 525 | in Ref. 1; AAP97254 | ||||
Sequence: D → G | ||||||
Sequence conflict | 572 | in Ref. 8; AAI09376 | ||||
Sequence: A → G | ||||||
Alternative sequence | VSP_023011 | 602 | in isoform 2E and isoform 2F | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF134477 EMBL· GenBank· DDBJ | AAP97254.1 EMBL· GenBank· DDBJ | mRNA | ||
AF250307 EMBL· GenBank· DDBJ | AAK37426.1 EMBL· GenBank· DDBJ | mRNA | ||
AY037160 EMBL· GenBank· DDBJ | AAK67638.1 EMBL· GenBank· DDBJ | mRNA | ||
BT007130 EMBL· GenBank· DDBJ | AAP35794.1 EMBL· GenBank· DDBJ | mRNA | ||
AK055491 EMBL· GenBank· DDBJ | BAB70932.1 EMBL· GenBank· DDBJ | mRNA | ||
AK316119 EMBL· GenBank· DDBJ | BAH14490.1 EMBL· GenBank· DDBJ | mRNA | ||
AL137519 EMBL· GenBank· DDBJ | CAB70785.1 EMBL· GenBank· DDBJ | mRNA | ||
BX537412 EMBL· GenBank· DDBJ | CAD97654.1 EMBL· GenBank· DDBJ | mRNA | ||
AC064826 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC068039 EMBL· GenBank· DDBJ | AAY24133.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471058 EMBL· GenBank· DDBJ | EAX11202.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471058 EMBL· GenBank· DDBJ | EAX11204.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471058 EMBL· GenBank· DDBJ | EAX11206.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471058 EMBL· GenBank· DDBJ | EAX11207.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471058 EMBL· GenBank· DDBJ | EAX11208.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471058 EMBL· GenBank· DDBJ | EAX11209.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC091498 EMBL· GenBank· DDBJ | AAH91498.1 EMBL· GenBank· DDBJ | mRNA | ||
BC109375 EMBL· GenBank· DDBJ | AAI09376.1 EMBL· GenBank· DDBJ | mRNA | ||
BC015038 EMBL· GenBank· DDBJ | AAH15038.1 EMBL· GenBank· DDBJ | mRNA | ||
U39575 EMBL· GenBank· DDBJ | AAA89166.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. |