P09496 · CLCA_HUMAN
- ProteinClathrin light chain A
- GeneCLTA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids248 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Acts as a component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge (PubMed:15858577, PubMed:21297582).
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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Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameClathrin light chain A
- Short namesLca
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP09496
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cytoplasmic vesicle membrane ; Peripheral membrane protein
Membrane, coated pit ; Peripheral membrane protein
Note: Cytoplasmic face of coated pits and vesicles. In complex with TACC3 and CKAP5 (forming the TACC3/ch-TOG/clathrin complex) localized to inter-microtubule bridges in mitotic spindles.
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 265 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000205767 | 1-248 | UniProt | Clathrin light chain A | |||
Sequence: MAELDPFGAPAGAPGGPALGNGVAGAGEEDPAAAFLAQQESEIAGIENDEAFAILDGGAPGPQPHGEPPGGPDAVDGVMNGEYYQESNGPTDSYAAISQVDRLQSEPESIRKWREEQMERLEALDANSRKQEAEWKEKAIKELEEWYARQDEQLQKTKANNRVADEAFYKQPFADVIGYVTNINHPCYSLEQAAEEAFVNDIDESSPGTEWERVARLCDFNPKSSKQAKDVSRMRSVLISLKQAPLVH | |||||||
Modified residue | 105 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 105 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 205 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 206 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 206 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 209 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 223 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 236 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 236 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 242 | UniProt | N6-acetyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Interaction
Subunit
Clathrin coats are formed from molecules containing 3 heavy chains and 3 light chains. Interacts with CALY; the interaction stimulates clathrin self-assembly and clathrin-mediated endocytosis. Interacts with CKAP5 and TACC3 forming the TACC3/ch-TOG/clathrin complex located at spindle inter-microtubules bridges; the complex implicates clathrin triskelions.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P09496 | CALY Q9NYX4 | 4 | EBI-1171169, EBI-10904725 | |
BINARY | P09496 | CLTC Q00610 | 4 | EBI-1171169, EBI-354967 | |
BINARY | P09496 | TACC3 Q9Y6A5 | 3 | EBI-1171169, EBI-2554984 | |
BINARY | P09496-2 | CASP6 P55212 | 3 | EBI-4401010, EBI-718729 | |
BINARY | P09496-2 | CLSTN1 O94985-2 | 3 | EBI-4401010, EBI-16041593 | |
BINARY | P09496-2 | COQ8A Q8NI60 | 3 | EBI-4401010, EBI-745535 | |
BINARY | P09496-2 | HIP1 O00291 | 3 | EBI-4401010, EBI-473886 | |
BINARY | P09496-2 | LAMP2 P13473-2 | 3 | EBI-4401010, EBI-21591415 | |
BINARY | P09496-2 | PRPF40A O75400-2 | 3 | EBI-4401010, EBI-5280197 | |
BINARY | P09496-2 | SH3GLB1 Q9Y371 | 3 | EBI-4401010, EBI-2623095 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-92 | Disordered | ||||
Sequence: MAELDPFGAPAGAPGGPALGNGVAGAGEEDPAAAFLAQQESEIAGIENDEAFAILDGGAPGPQPHGEPPGGPDAVDGVMNGEYYQESNGPTD | ||||||
Region | 100-162 | Involved in binding clathrin heavy chain | ||||
Sequence: VDRLQSEPESIRKWREEQMERLEALDANSRKQEAEWKEKAIKELEEWYARQDEQLQKTKANNR |
Sequence similarities
Belongs to the clathrin light chain family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative splicing.
P09496-1
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.
- NameBrain
- Length248
- Mass (Da)27,077
- Last updated1989-07-01 v1
- Checksum8D8A3B49E6353D93
P09496-2
- NameNon-brain
- Differences from canonical
- 163-192: Missing
P09496-3
- Name3
- Differences from canonical
- 181-192: Missing
P09496-4
- Name4
- Differences from canonical
- 162-180: RVADEAFYKQPFADVIGYV → S
P09496-5
- Name5
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_047168 | 73-124 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_043239 | 162-180 | in isoform 4 | |||
Sequence: RVADEAFYKQPFADVIGYV → S | ||||||
Alternative sequence | VSP_001095 | 163-192 | in isoform Non-brain and isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_024238 | 181-192 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 207 | in Ref. 4; ABB76683 | ||||
Sequence: P → Q |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M20471 EMBL· GenBank· DDBJ | AAA51817.1 EMBL· GenBank· DDBJ | mRNA | ||
M20472 EMBL· GenBank· DDBJ | AAA59505.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ270158 EMBL· GenBank· DDBJ | ABB76683.1 EMBL· GenBank· DDBJ | mRNA | ||
BT007170 EMBL· GenBank· DDBJ | AAP35834.1 EMBL· GenBank· DDBJ | mRNA | ||
AK291078 EMBL· GenBank· DDBJ | BAF83767.1 EMBL· GenBank· DDBJ | mRNA | ||
AK295692 EMBL· GenBank· DDBJ | BAG58543.1 EMBL· GenBank· DDBJ | mRNA | ||
AL158830 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL161792 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471071 EMBL· GenBank· DDBJ | EAW58312.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC009201 EMBL· GenBank· DDBJ | AAH09201.1 EMBL· GenBank· DDBJ | mRNA | ||
BC019287 EMBL· GenBank· DDBJ | AAH19287.1 EMBL· GenBank· DDBJ | mRNA |