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Protein

Clathrin heavy chain 1

Gene

CLTC

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network. Acts as 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:16968737, PubMed:21297582). The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension (PubMed:23532825). Plays a role in early autophagosome formation (PubMed:20639872).5 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • clathrin light chain binding Source: FlyBase
  • disordered domain specific binding Source: CAFA
  • double-stranded RNA binding Source: MGI
  • low-density lipoprotein particle receptor binding Source: ARUK-UCL
  • protein kinase binding Source: ParkinsonsUK-UCL
  • RNA binding Source: UniProtKB
  • structural molecule activity Source: UniProtKB
  • ubiquitin-specific protease binding Source: UniProtKB

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processAutophagy, Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-168275 Entry of Influenza Virion into Host Cell via Endocytosis
R-HSA-177504 Retrograde neurotrophin signalling
R-HSA-190873 Gap junction degradation
R-HSA-196025 Formation of annular gap junctions
R-HSA-2132295 MHC class II antigen presentation
R-HSA-3928665 EPH-ephrin mediated repulsion of cells
R-HSA-432720 Lysosome Vesicle Biogenesis
R-HSA-432722 Golgi Associated Vesicle Biogenesis
R-HSA-437239 Recycling pathway of L1
R-HSA-5099900 WNT5A-dependent internalization of FZD4
R-HSA-5140745 WNT5A-dependent internalization of FZD2, FZD5 and ROR2
R-HSA-8856825 Cargo recognition for clathrin-mediated endocytosis
R-HSA-8856828 Clathrin-mediated endocytosis
R-HSA-8866427 VLDLR internalisation and degradation
R-HSA-8964038 LDL clearance

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
Q00610

SIGNOR Signaling Network Open Resource

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SIGNORi
Q00610

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
Q00610 Curated

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Clathrin heavy chain 12 Publications
Alternative name(s):
Clathrin heavy chain on chromosome 17
Short name:
CLH-17
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CLTC2 PublicationsImported
Synonyms:CLH17, CLTCL2, KIAA0034
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 17

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000141367.11

Human Gene Nomenclature Database

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HGNCi
HGNC:2092 CLTC

Online Mendelian Inheritance in Man (OMIM)

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MIMi
118955 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q00610

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Coated pit, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Mental retardation, autosomal dominant 56 (MRD56)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of mental retardation, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period.
See also OMIM:617854
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_080721554 – 556Missing in MRD56; unknown pathological significance. 1 Publication3
Natural variantiVAR_080722890P → L in MRD56. 1 Publication1
Natural variantiVAR_0807231047L → P in MRD56; unknown pathological significance. 1 Publication1
Natural variantiVAR_0807241108W → R in MRD56; unknown pathological significance. 1 Publication1
Natural variantiVAR_0807251199 – 1675Missing in MRD56. 1 PublicationAdd BLAST477
Natural variantiVAR_0807261207Missing in MRD56; unknown pathological significance. 1 Publication1
Natural variantiVAR_0807271555 – 1675Missing in MRD56. 1 PublicationAdd BLAST121
Natural variantiVAR_0807281556 – 1675Missing in MRD56. 1 PublicationAdd BLAST120

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi65P → N: Disrupts spindle localization. 1 Publication1
Mutagenesisi67S → G: Disrupts spindle localization. 1 Publication1
Mutagenesisi87T → A: Disrupts spindle localization. 1 Publication1
Mutagenesisi89Q → A: Disrupts spindle localization. 1 Publication1
Mutagenesisi96K → E: Disrupts spindle localization. 1 Publication1
Mutagenesisi98K → E: Disrupts spindle localization. 1 Publication1
Mutagenesisi444R → E: Disrupts spindle localization; when associated with E-445, E-500 E-506 and E-507. 1 Publication1
Mutagenesisi445K → E: Disrupts spindle localization; when associated with E-444, E-500, E-506 and E-507. 1 Publication1
Mutagenesisi480 – 484LRANV → ERGQC: Disrupts spindle localization and interaction with TACC3. 1 Publication5
Mutagenesisi481R → E: Disrupts spindle localization; when associated with E-487, E-500, E-506 and E-507. 1 Publication1
Mutagenesisi487K → E: Disrupts spindle localization; when associated with E-481, E-500, E-506 and E-507. 1 Publication1
Mutagenesisi500K → E: Disrupts spindle localization; when associated with E-444, E-445, E-506 and E-507. 1 Publication1
Mutagenesisi500K → E: Disrupts spindle localization; when associated with E-481, E-487, E-506 and E-507. 1 Publication1
Mutagenesisi506K → E: Disrupts spindle localization; when associated with E-444, E-445, E-500 and E-507. 1 Publication1
Mutagenesisi506K → E: Disrupts spindle localization; when associated with E-481, E-487, E-500 and E-507. 1 Publication1
Mutagenesisi507K → E: Disrupts spindle localization; when associated with E-444, E-445, E-500 and E-506. 1 Publication1
Mutagenesisi507K → E: Disrupts spindle localization; when associated with E-481, E-487, E-500 and E-506. 1 Publication1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNET

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DisGeNETi
1213

MalaCards human disease database

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MalaCardsi
CLTC
MIMi617854 phenotype

Open Targets

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OpenTargetsi
ENSG00000141367

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
178469 Autosomal dominant non-syndromic intellectual disability
178342 Inflammatory myofibroblastic tumor
319308 MiT family translocation renal cell carcinoma
442835 Undetermined early-onset epileptic encephalopathy

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA26618

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3108634

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
CLTC

Domain mapping of disease mutations (DMDM)

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DMDMi
1705916

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources2 Publications
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002057782 – 1675Clathrin heavy chain 1Add BLAST1674

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei67PhosphoserineCombined sources1
Modified residuei105PhosphothreonineBy similarity1
Modified residuei184PhosphotyrosineBy similarity1
Modified residuei394PhosphothreonineCombined sources1
Modified residuei634PhosphotyrosineCombined sources1
Modified residuei737N6-succinyllysineBy similarity1
Modified residuei856N6-acetyllysineCombined sources1
Modified residuei899PhosphotyrosineBy similarity1
Modified residuei1167PhosphoserineBy similarity1
Modified residuei1206PhosphotyrosineBy similarity1
Modified residuei1229PhosphoserineCombined sources1
Modified residuei1441N6-acetyllysine; alternateCombined sources1
Modified residuei1441N6-succinyllysine; alternateBy similarity1
Modified residuei1477PhosphotyrosineCombined sources1
Modified residuei1487PhosphotyrosineBy similarity1
Modified residuei1494PhosphoserineCombined sources1
Modified residuei1501N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q00610

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q00610

MaxQB - The MaxQuant DataBase

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MaxQBi
Q00610

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q00610

PeptideAtlas

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PeptideAtlasi
Q00610

PRoteomics IDEntifications database

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PRIDEi
Q00610

ProteomicsDB human proteome resource

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ProteomicsDBi
57862
57863 [Q00610-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q00610

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q00610

SwissPalm database of S-palmitoylation events

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SwissPalmi
Q00610

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000141367 Expressed in 240 organ(s), highest expression level in dorsolateral prefrontal cortex

CleanEx database of gene expression profiles

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CleanExi
HS_CLTC

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q00610 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q00610 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB010389
CAB011571
CAB017155
HPA059143

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Clathrin triskelions, composed of 3 heavy chains and 3 light chains, are the basic subunits of the clathrin coat (PubMed:16968737). In the presence of light chains, hub assembly is influenced by both the pH and the concentration of calcium. Interacts with HIP1 (PubMed:11532990). Interacts with DENND1A, DENND1B and DENND1C (By similarity). May interact with OCRL (By similarity). Interacts with ERBB2 (PubMed:16314522). Interacts with FKBP6 (PubMed:18529014). Interacts with CKAP5 and TACC3 forming the TACC3/ch-TOG/clathrin complex located at spindle inter-microtubules bridges; the complex implicates clathrin triskelions; TACC3 and CLTC are proposed to form a composite microtubule interaction surface (PubMed:21297582). Interacts with ATG16L1 (via N-terminus) (PubMed:20639872). Interacts with RFTN1; the interaction occurs in response to pathogens (PubMed:27022195, PubMed:21266579). Interacts with USP2 isoform 4 (PubMed:26756164).By similarity9 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
107623, 333 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q00610

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
Q00610

Protein interaction database and analysis system

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IntActi
Q00610, 200 interactors

Molecular INTeraction database

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MINTi
Q00610

STRING: functional protein association networks

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STRINGi
9606.ENSP00000269122

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q00610

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11675
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XZGX-ray1.70A1-364[»]
4G55X-ray1.69A1-364[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q00610

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q00610

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q00610

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati537 – 683CHCR 1PROSITE-ProRule annotation1 PublicationAdd BLAST147
Repeati686 – 828CHCR 2PROSITE-ProRule annotation1 PublicationAdd BLAST143
Repeati833 – 972CHCR 3PROSITE-ProRule annotation1 PublicationAdd BLAST140
Repeati979 – 1124CHCR 4PROSITE-ProRule annotation1 PublicationAdd BLAST146
Repeati1128 – 1269CHCR 5PROSITE-ProRule annotation1 PublicationAdd BLAST142
Repeati1274 – 1420CHCR 6PROSITE-ProRule annotation1 PublicationAdd BLAST147
Repeati1423 – 1566CHCR 7PROSITE-ProRule annotation1 PublicationAdd BLAST144

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni2 – 479Globular terminal domainAdd BLAST478
Regioni24 – 67WD40-like repeat 1Add BLAST44
Regioni68 – 107WD40-like repeat 2Add BLAST40
Regioni108 – 149WD40-like repeat 3Add BLAST42
Regioni150 – 195WD40-like repeat 4Add BLAST46
Regioni196 – 257WD40-like repeat 5Add BLAST62
Regioni258 – 301WD40-like repeat 6Add BLAST44