Q00610 · CLH1_HUMAN
- ProteinClathrin heavy chain 1
- GeneCLTC
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1675 (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. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network. 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: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).
Interaction with DNAJC6 mediates the recruitment of HSPA8 to the clathrin lattice and creates local destabilization of the lattice promoting uncoating (By similarity).
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).
Interaction with DNAJC6 mediates the recruitment of HSPA8 to the clathrin lattice and creates local destabilization of the lattice promoting uncoating (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 | |||
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Keywords
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameClathrin heavy 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 accessionQ00610
- 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. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. 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
Involvement in disease
Intellectual developmental disorder, autosomal dominant 56 (MRD56)
- Note
- DescriptionA form of intellectual disability, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period.
- See alsoMIM:617854
Natural variants in MRD56
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_080721 | 554-556 | missing | in MRD56; uncertain significance | |
VAR_080722 | 890 | P>L | in MRD56; dbSNP:rs1555606635 | |
VAR_080723 | 1047 | L>P | in MRD56; uncertain significance; dbSNP:rs1555607159 | |
VAR_080724 | 1108 | W>R | in MRD56; uncertain significance | |
VAR_080725 | 1199-1675 | missing | in MRD56 | |
VAR_080726 | 1207 | missing | in MRD56; uncertain significance | |
VAR_080727 | 1555-1675 | missing | in MRD56 | |
VAR_080728 | 1556-1675 | missing | in MRD56 |
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 65 | Disrupts spindle localization. | ||||
Sequence: P → N | ||||||
Mutagenesis | 67 | Disrupts spindle localization. | ||||
Sequence: S → G | ||||||
Mutagenesis | 87 | Disrupts spindle localization. | ||||
Sequence: T → A | ||||||
Mutagenesis | 89 | Disrupts spindle localization. | ||||
Sequence: Q → A | ||||||
Mutagenesis | 96 | Disrupts spindle localization. | ||||
Sequence: K → E | ||||||
Mutagenesis | 98 | Disrupts spindle localization. | ||||
Sequence: K → E | ||||||
Mutagenesis | 444 | Disrupts spindle localization; when associated with E-445, E-500 E-506 and E-507. | ||||
Sequence: R → E | ||||||
Mutagenesis | 445 | Disrupts spindle localization; when associated with E-444, E-500, E-506 and E-507. | ||||
Sequence: K → E | ||||||
Mutagenesis | 480-484 | Disrupts spindle localization and interaction with TACC3. | ||||
Sequence: LRANV → ERGQC | ||||||
Mutagenesis | 481 | Disrupts spindle localization; when associated with E-487, E-500, E-506 and E-507. | ||||
Sequence: R → E | ||||||
Mutagenesis | 487 | Disrupts spindle localization; when associated with E-481, E-500, E-506 and E-507. | ||||
Sequence: K → E | ||||||
Mutagenesis | 500 | Disrupts spindle localization; when associated with E-444, E-445, E-506 and E-507. | ||||
Sequence: K → E | ||||||
Mutagenesis | 500 | Disrupts spindle localization; when associated with E-481, E-487, E-506 and E-507. | ||||
Sequence: K → E | ||||||
Mutagenesis | 506 | Disrupts spindle localization; when associated with E-444, E-445, E-500 and E-507. | ||||
Sequence: K → E | ||||||
Mutagenesis | 506 | Disrupts spindle localization; when associated with E-481, E-487, E-500 and E-507. | ||||
Sequence: K → E | ||||||
Mutagenesis | 507 | Disrupts spindle localization; when associated with E-444, E-445, E-500 and E-506. | ||||
Sequence: K → E | ||||||
Mutagenesis | 507 | Disrupts spindle localization; when associated with E-481, E-487, E-500 and E-506. | ||||
Sequence: K → E | ||||||
Natural variant | VAR_080721 | 554-556 | in MRD56; uncertain significance | |||
Sequence: Missing | ||||||
Natural variant | VAR_080722 | 890 | in MRD56; dbSNP:rs1555606635 | |||
Sequence: P → L | ||||||
Natural variant | VAR_080723 | 1047 | in MRD56; uncertain significance; dbSNP:rs1555607159 | |||
Sequence: L → P | ||||||
Natural variant | VAR_080724 | 1108 | in MRD56; uncertain significance | |||
Sequence: W → R | ||||||
Natural variant | VAR_080725 | 1199-1675 | in MRD56 | |||
Sequence: Missing | ||||||
Natural variant | VAR_080726 | 1207 | in MRD56; uncertain significance | |||
Sequence: Missing | ||||||
Natural variant | VAR_080727 | 1555-1675 | in MRD56 | |||
Sequence: Missing | ||||||
Natural variant | VAR_080728 | 1556-1675 | in MRD56 | |||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,142 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-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000205778 | 2-1675 | UniProt | Clathrin heavy chain 1 | |||
Sequence: AQILPIRFQEHLQLQNLGINPANIGFSTLTMESDKFICIREKVGEQAQVVIIDMNDPSNPIRRPISADSAIMNPASKVIALKAGKTLQIFNIEMKSKMKAHTMTDDVTFWKWISLNTVALVTDNAVYHWSMEGESQPVKMFDRHSSLAGCQIINYRTDAKQKWLLLTGISAQQNRVVGAMQLYSVDRKVSQPIEGHAASFAQFKMEGNAEESTLFCFAVRGQAGGKLHIIEVGTPPTGNQPFPKKAVDVFFPPEAQNDFPVAMQISEKHDVVFLITKYGYIHLYDLETGTCIYMNRISGETIFVTAPHEATAGIIGVNRKGQVLSVCVEEENIIPYITNVLQNPDLALRMAVRNNLAGAEELFARKFNALFAQGNYSEAAKVAANAPKGILRTPDTIRRFQSVPAQPGQTSPLLQYFGILLDQGQLNKYESLELCRPVLQQGRKQLLEKWLKEDKLECSEELGDLVKSVDPTLALSVYLRANVPNKVIQCFAETGQVQKIVLYAKKVGYTPDWIFLLRNVMRISPDQGQQFAQMLVQDEEPLADITQIVDVFMEYNLIQQCTAFLLDALKNNRPSEGPLQTRLLEMNLMHAPQVADAILGNQMFTHYDRAHIAQLCEKAGLLQRALEHFTDLYDIKRAVVHTHLLNPEWLVNYFGSLSVEDSLECLRAMLSANIRQNLQICVQVASKYHEQLSTQSLIELFESFKSFEGLFYFLGSIVNFSQDPDVHFKYIQAACKTGQIKEVERICRESNCYDPERVKNFLKEAKLTDQLPLIIVCDRFDFVHDLVLYLYRNNLQKYIEIYVQKVNPSRLPVVIGGLLDVDCSEDVIKNLILVVRGQFSTDELVAEVEKRNRLKLLLPWLEARIHEGCEEPATHNALAKIYIDSNNNPERFLRENPYYDSRVVGKYCEKRDPHLACVAYERGQCDLELINVCNENSLFKSLSRYLVRRKDPELWGSVLLESNPYRRPLIDQVVQTALSETQDPEEVSVTVKAFMTADLPNELIELLEKIVLDNSVFSEHRNLQNLLILTAIKADRTRVMEYINRLDNYDAPDIANIAISNELFEEAFAIFRKFDVNTSAVQVLIEHIGNLDRAYEFAERCNEPAVWSQLAKAQLQKGMVKEAIDSYIKADDPSSYMEVVQAANTSGNWEELVKYLQMARKKARESYVETELIFALAKTNRLAELEEFINGPNNAHIQQVGDRCYDEKMYDAAKLLYNNVSNFGRLASTLVHLGEYQAAVDGARKANSTRTWKEVCFACVDGKEFRLAQMCGLHIVVHADELEELINYYQDRGYFEELITMLEAALGLERAHMGMFTELAILYSKFKPQKMREHLELFWSRVNIPKVLRAAEQAHLWAELVFLYDKYEEYDNAIITMMNHPTDAWKEGQFKDIITKVANVELYYRAIQFYLEFKPLLLNDLLMVLSPRLDHTRAVNYFSKVKQLPLVKPYLRSVQNHNNKSVNESLNNLFITEEDYQALRTSIDAYDNFDNISLAQRLEKHELIEFRRIAAYLFKGNNRWKQSVELCKKDSLYKDAMQYASESKDTELAEELLQWFLQEEKRECFGACLFTCYDLLRPDVVLETAWRHNIMDFAMPYFIQVMKEYLTKVDKLDASESLRKEEEQATETQPIVYGQPQLMLTAGPSVAVPPQAPFGYGYTAPPYGQPQPGFGYSM | |||||||
Modified residue | 67 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 67 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 105 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 105 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 146 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 184 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 235 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 238 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 394 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 394 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 397 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 412 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 430 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 634 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 634 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 737 | UniProt | N6-succinyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 751 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 856 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 899 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 899 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 900 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 1016 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1167 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1167 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1206 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 1206 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 1211 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 1222 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1229 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1229 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1237 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 1438 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 1441 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 1441 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 1462 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1477 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 1477 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 1487 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 1487 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 1494 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1494 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1501 | UniProt | N6-acetyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
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:21266579, PubMed:27022195).
Interacts with USP2 isoform 4 (PubMed:26756164).
Interacts with TMEM106B (via N-terminus) (PubMed:25066864).
Interacts with DNAJC6; this interaction produces a local change in heavy-chain contacts, creating a detectable global distortion of the clathrin coat and leads to the recruitment of HSPA8 (PubMed:29735704).
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:21266579, PubMed:27022195).
Interacts with USP2 isoform 4 (PubMed:26756164).
Interacts with TMEM106B (via N-terminus) (PubMed:25066864).
Interacts with DNAJC6; this interaction produces a local change in heavy-chain contacts, creating a detectable global distortion of the clathrin coat and leads to the recruitment of HSPA8 (PubMed:29735704).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q00610 | ARRB2 P32121 | 6 | EBI-354967, EBI-714559 | |
BINARY | Q00610 | CLTA P09496 | 4 | EBI-354967, EBI-1171169 | |
BINARY | Q00610 | DLGAP5 Q15398 | 4 | EBI-354967, EBI-748280 | |
BINARY | Q00610 | MYB P10242 | 4 | EBI-354967, EBI-298355 | |
BINARY | Q00610 | OCRL Q01968 | 10 | EBI-354967, EBI-6148898 | |
BINARY | Q00610 | PAAT Q9H8K7 | 5 | EBI-354967, EBI-714785 | |
XENO | Q00610 | Q306W6 | 4 | EBI-354967, EBI-38815211 | |
XENO | Q00610 | Q306W8 | 2 | EBI-354967, EBI-38259300 | |
BINARY | Q00610 | TNK2 Q07912 | 2 | EBI-354967, EBI-603457 | |
BINARY | Q00610 | TOM1L1 O75674 | 4 | EBI-354967, EBI-712991 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 2-479 | Globular terminal domain | ||||
Sequence: AQILPIRFQEHLQLQNLGINPANIGFSTLTMESDKFICIREKVGEQAQVVIIDMNDPSNPIRRPISADSAIMNPASKVIALKAGKTLQIFNIEMKSKMKAHTMTDDVTFWKWISLNTVALVTDNAVYHWSMEGESQPVKMFDRHSSLAGCQIINYRTDAKQKWLLLTGISAQQNRVVGAMQLYSVDRKVSQPIEGHAASFAQFKMEGNAEESTLFCFAVRGQAGGKLHIIEVGTPPTGNQPFPKKAVDVFFPPEAQNDFPVAMQISEKHDVVFLITKYGYIHLYDLETGTCIYMNRISGETIFVTAPHEATAGIIGVNRKGQVLSVCVEEENIIPYITNVLQNPDLALRMAVRNNLAGAEELFARKFNALFAQGNYSEAAKVAANAPKGILRTPDTIRRFQSVPAQPGQTSPLLQYFGILLDQGQLNKYESLELCRPVLQQGRKQLLEKWLKEDKLECSEELGDLVKSVDPTLALSVY | ||||||
Region | 24-67 | WD40-like repeat 1 | ||||
Sequence: NIGFSTLTMESDKFICIREKVGEQAQVVIIDMNDPSNPIRRPIS | ||||||
Region | 68-107 | WD40-like repeat 2 | ||||
Sequence: ADSAIMNPASKVIALKAGKTLQIFNIEMKSKMKAHTMTDD | ||||||
Region | 108-149 | WD40-like repeat 3 | ||||
Sequence: VTFWKWISLNTVALVTDNAVYHWSMEGESQPVKMFDRHSSLA | ||||||
Region | 150-195 | WD40-like repeat 4 | ||||
Sequence: GCQIINYRTDAKQKWLLLTGISAQQNRVVGAMQLYSVDRKVSQPIE | ||||||
Region | 196-257 | WD40-like repeat 5 | ||||
Sequence: GHAASFAQFKMEGNAEESTLFCFAVRGQAGGKLHIIEVGTPPTGNQPFPKKAVDVFFPPEAQ | ||||||
Region | 258-301 | WD40-like repeat 6 | ||||
Sequence: NDFPVAMQISEKHDVVFLITKYGYIHLYDLETGTCIYMNRISGE | ||||||
Region | 302-330 | WD40-like repeat 7 | ||||
Sequence: TIFVTAPHEATAGIIGVNRKGQVLSVCVE | ||||||
Region | 449-465 | Binding site for the uncoating ATPase, involved in lattice disassembly | ||||
Sequence: EKWLKEDKLECSEELGD | ||||||
Region | 457-507 | Involved in spindle localization and interaction with TACC3 | ||||
Sequence: LECSEELGDLVKSVDPTLALSVYLRANVPNKVIQCFAETGQVQKIVLYAKK | ||||||
Region | 480-523 | Flexible linker | ||||
Sequence: LRANVPNKVIQCFAETGQVQKIVLYAKKVGYTPDWIFLLRNVMR | ||||||
Region | 524-634 | Distal segment | ||||
Sequence: ISPDQGQQFAQMLVQDEEPLADITQIVDVFMEYNLIQQCTAFLLDALKNNRPSEGPLQTRLLEMNLMHAPQVADAILGNQMFTHYDRAHIAQLCEKAGLLQRALEHFTDLY | ||||||
Region | 524-1675 | Heavy chain arm | ||||
Sequence: ISPDQGQQFAQMLVQDEEPLADITQIVDVFMEYNLIQQCTAFLLDALKNNRPSEGPLQTRLLEMNLMHAPQVADAILGNQMFTHYDRAHIAQLCEKAGLLQRALEHFTDLYDIKRAVVHTHLLNPEWLVNYFGSLSVEDSLECLRAMLSANIRQNLQICVQVASKYHEQLSTQSLIELFESFKSFEGLFYFLGSIVNFSQDPDVHFKYIQAACKTGQIKEVERICRESNCYDPERVKNFLKEAKLTDQLPLIIVCDRFDFVHDLVLYLYRNNLQKYIEIYVQKVNPSRLPVVIGGLLDVDCSEDVIKNLILVVRGQFSTDELVAEVEKRNRLKLLLPWLEARIHEGCEEPATHNALAKIYIDSNNNPERFLRENPYYDSRVVGKYCEKRDPHLACVAYERGQCDLELINVCNENSLFKSLSRYLVRRKDPELWGSVLLESNPYRRPLIDQVVQTALSETQDPEEVSVTVKAFMTADLPNELIELLEKIVLDNSVFSEHRNLQNLLILTAIKADRTRVMEYINRLDNYDAPDIANIAISNELFEEAFAIFRKFDVNTSAVQVLIEHIGNLDRAYEFAERCNEPAVWSQLAKAQLQKGMVKEAIDSYIKADDPSSYMEVVQAANTSGNWEELVKYLQMARKKARESYVETELIFALAKTNRLAELEEFINGPNNAHIQQVGDRCYDEKMYDAAKLLYNNVSNFGRLASTLVHLGEYQAAVDGARKANSTRTWKEVCFACVDGKEFRLAQMCGLHIVVHADELEELINYYQDRGYFEELITMLEAALGLERAHMGMFTELAILYSKFKPQKMREHLELFWSRVNIPKVLRAAEQAHLWAELVFLYDKYEEYDNAIITMMNHPTDAWKEGQFKDIITKVANVELYYRAIQFYLEFKPLLLNDLLMVLSPRLDHTRAVNYFSKVKQLPLVKPYLRSVQNHNNKSVNESLNNLFITEEDYQALRTSIDAYDNFDNISLAQRLEKHELIEFRRIAAYLFKGNNRWKQSVELCKKDSLYKDAMQYASESKDTELAEELLQWFLQEEKRECFGACLFTCYDLLRPDVVLETAWRHNIMDFAMPYFIQVMKEYLTKVDKLDASESLRKEEEQATETQPIVYGQPQLMLTAGPSVAVPPQAPFGYGYTAPPYGQPQPGFGYSM | ||||||
Repeat | 537-683 | CHCR 1 | ||||
Sequence: VQDEEPLADITQIVDVFMEYNLIQQCTAFLLDALKNNRPSEGPLQTRLLEMNLMHAPQVADAILGNQMFTHYDRAHIAQLCEKAGLLQRALEHFTDLYDIKRAVVHTHLLNPEWLVNYFGSLSVEDSLECLRAMLSANIRQNLQICV | ||||||
Region | 639-1675 | Proximal segment | ||||
Sequence: AVVHTHLLNPEWLVNYFGSLSVEDSLECLRAMLSANIRQNLQICVQVASKYHEQLSTQSLIELFESFKSFEGLFYFLGSIVNFSQDPDVHFKYIQAACKTGQIKEVERICRESNCYDPERVKNFLKEAKLTDQLPLIIVCDRFDFVHDLVLYLYRNNLQKYIEIYVQKVNPSRLPVVIGGLLDVDCSEDVIKNLILVVRGQFSTDELVAEVEKRNRLKLLLPWLEARIHEGCEEPATHNALAKIYIDSNNNPERFLRENPYYDSRVVGKYCEKRDPHLACVAYERGQCDLELINVCNENSLFKSLSRYLVRRKDPELWGSVLLESNPYRRPLIDQVVQTALSETQDPEEVSVTVKAFMTADLPNELIELLEKIVLDNSVFSEHRNLQNLLILTAIKADRTRVMEYINRLDNYDAPDIANIAISNELFEEAFAIFRKFDVNTSAVQVLIEHIGNLDRAYEFAERCNEPAVWSQLAKAQLQKGMVKEAIDSYIKADDPSSYMEVVQAANTSGNWEELVKYLQMARKKARESYVETELIFALAKTNRLAELEEFINGPNNAHIQQVGDRCYDEKMYDAAKLLYNNVSNFGRLASTLVHLGEYQAAVDGARKANSTRTWKEVCFACVDGKEFRLAQMCGLHIVVHADELEELINYYQDRGYFEELITMLEAALGLERAHMGMFTELAILYSKFKPQKMREHLELFWSRVNIPKVLRAAEQAHLWAELVFLYDKYEEYDNAIITMMNHPTDAWKEGQFKDIITKVANVELYYRAIQFYLEFKPLLLNDLLMVLSPRLDHTRAVNYFSKVKQLPLVKPYLRSVQNHNNKSVNESLNNLFITEEDYQALRTSIDAYDNFDNISLAQRLEKHELIEFRRIAAYLFKGNNRWKQSVELCKKDSLYKDAMQYASESKDTELAEELLQWFLQEEKRECFGACLFTCYDLLRPDVVLETAWRHNIMDFAMPYFIQVMKEYLTKVDKLDASESLRKEEEQATETQPIVYGQPQLMLTAGPSVAVPPQAPFGYGYTAPPYGQPQPGFGYSM | ||||||
Repeat | 686-828 | CHCR 2 | ||||
Sequence: ASKYHEQLSTQSLIELFESFKSFEGLFYFLGSIVNFSQDPDVHFKYIQAACKTGQIKEVERICRESNCYDPERVKNFLKEAKLTDQLPLIIVCDRFDFVHDLVLYLYRNNLQKYIEIYVQKVNPSRLPVVIGGLLDVDCSEDV | ||||||
Repeat | 833-972 | CHCR 3 | ||||
Sequence: ILVVRGQFSTDELVAEVEKRNRLKLLLPWLEARIHEGCEEPATHNALAKIYIDSNNNPERFLRENPYYDSRVVGKYCEKRDPHLACVAYERGQCDLELINVCNENSLFKSLSRYLVRRKDPELWGSVLLESNPYRRPLID | ||||||
Repeat | 979-1124 | CHCR 4 | ||||
Sequence: LSETQDPEEVSVTVKAFMTADLPNELIELLEKIVLDNSVFSEHRNLQNLLILTAIKADRTRVMEYINRLDNYDAPDIANIAISNELFEEAFAIFRKFDVNTSAVQVLIEHIGNLDRAYEFAERCNEPAVWSQLAKAQLQKGMVKEA | ||||||
Repeat | 1128-1269 | CHCR 5 | ||||
Sequence: YIKADDPSSYMEVVQAANTSGNWEELVKYLQMARKKARESYVETELIFALAKTNRLAELEEFINGPNNAHIQQVGDRCYDEKMYDAAKLLYNNVSNFGRLASTLVHLGEYQAAVDGARKANSTRTWKEVCFACVDGKEFRLA | ||||||
Region | 1213-1522 | Involved in binding clathrin light chain | ||||
Sequence: AAKLLYNNVSNFGRLASTLVHLGEYQAAVDGARKANSTRTWKEVCFACVDGKEFRLAQMCGLHIVVHADELEELINYYQDRGYFEELITMLEAALGLERAHMGMFTELAILYSKFKPQKMREHLELFWSRVNIPKVLRAAEQAHLWAELVFLYDKYEEYDNAIITMMNHPTDAWKEGQFKDIITKVANVELYYRAIQFYLEFKPLLLNDLLMVLSPRLDHTRAVNYFSKVKQLPLVKPYLRSVQNHNNKSVNESLNNLFITEEDYQALRTSIDAYDNFDNISLAQRLEKHELIEFRRIAAYLFKGNNRWK | ||||||
Repeat | 1274-1420 | CHCR 6 | ||||
Sequence: LHIVVHADELEELINYYQDRGYFEELITMLEAALGLERAHMGMFTELAILYSKFKPQKMREHLELFWSRVNIPKVLRAAEQAHLWAELVFLYDKYEEYDNAIITMMNHPTDAWKEGQFKDIITKVANVELYYRAIQFYLEFKPLLLN | ||||||
Repeat | 1423-1566 | CHCR 7 | ||||
Sequence: LMVLSPRLDHTRAVNYFSKVKQLPLVKPYLRSVQNHNNKSVNESLNNLFITEEDYQALRTSIDAYDNFDNISLAQRLEKHELIEFRRIAAYLFKGNNRWKQSVELCKKDSLYKDAMQYASESKDTELAEELLQWFLQEEKRECF | ||||||
Region | 1550-1675 | Trimerization | ||||
Sequence: AEELLQWFLQEEKRECFGACLFTCYDLLRPDVVLETAWRHNIMDFAMPYFIQVMKEYLTKVDKLDASESLRKEEEQATETQPIVYGQPQLMLTAGPSVAVPPQAPFGYGYTAPPYGQPQPGFGYSM |
Domain
The N-terminal seven-bladed beta-propeller is formed by WD40-like repeats, and projects inward from the polyhedral outer clathrin coat. It constitutes a major protein-protein interaction node.
Sequence similarities
Belongs to the clathrin heavy chain family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q00610-1
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
- Length1,675
- Mass (Da)191,615
- Last updated2007-01-23 v5
- Checksum6C4F2D54950079E2
Q00610-2
- Name2
- Differences from canonical
- 1636-1639: QPQL → NLSL
- 1640-1675: Missing
Computationally mapped potential isoform sequences
There are 20 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
J3KRF5 | J3KRF5_HUMAN | CLTC | 1629 | ||
J3KS13 | J3KS13_HUMAN | CLTC | 612 | ||
J3KTN1 | J3KTN1_HUMAN | CLTC | 324 | ||
A0AAQ5BHT1 | A0AAQ5BHT1_HUMAN | CLTC | 426 | ||
A0AAQ5BHT6 | A0AAQ5BHT6_HUMAN | CLTC | 1638 | ||
A0AAQ5BHU5 | A0AAQ5BHU5_HUMAN | CLTC | 1668 | ||
A0AAQ5BHN4 | A0AAQ5BHN4_HUMAN | CLTC | 1618 | ||
A0AAQ5BHN6 | A0AAQ5BHN6_HUMAN | CLTC | 1644 | ||
A0AAQ5BHN7 | A0AAQ5BHN7_HUMAN | CLTC | 1412 | ||
K7EJJ5 | K7EJJ5_HUMAN | CLTC | 1682 | ||
A0A8V8TRE8 | A0A8V8TRE8_HUMAN | CLTC | 1617 | ||
A0A8V8TRF0 | A0A8V8TRF0_HUMAN | CLTC | 1676 | ||
A0A8V8TQK1 | A0A8V8TQK1_HUMAN | CLTC | 1651 | ||
A0A8V8TQK3 | A0A8V8TQK3_HUMAN | CLTC | 1579 | ||
A0A8V8TQK7 | A0A8V8TQK7_HUMAN | CLTC | 1656 | ||
A0A8V8TR47 | A0A8V8TR47_HUMAN | CLTC | 1679 | ||
A0A8V8TQ14 | A0A8V8TQ14_HUMAN | CLTC | 1680 | ||
A0A8V8TQ18 | A0A8V8TQ18_HUMAN | CLTC | 1721 | ||
J3QL20 | J3QL20_HUMAN | CLTC | 97 | ||
A0A087WVQ6 | A0A087WVQ6_HUMAN | CLTC | 1679 |
Sequence caution
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 560 | in Ref. 5; CAA39363 | ||||
Sequence: Q → R | ||||||
Sequence conflict | 817 | in Ref. 5; CAA39363 | ||||
Sequence: G → V | ||||||
Sequence conflict | 923 | in Ref. 2; CAE45761 | ||||
Sequence: R → H | ||||||
Sequence conflict | 1563 | in Ref. 2; CAE45761 | ||||
Sequence: R → G | ||||||
Alternative sequence | VSP_011570 | 1636-1639 | in isoform 2 | |||
Sequence: QPQL → NLSL | ||||||
Alternative sequence | VSP_011571 | 1640-1675 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 1652 | in Ref. 2; CAE45761 | ||||
Sequence: Q → R |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D21260 EMBL· GenBank· DDBJ | BAA04801.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BX640615 EMBL· GenBank· DDBJ | CAE45761.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471109 EMBL· GenBank· DDBJ | EAW94396.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471109 EMBL· GenBank· DDBJ | EAW94399.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC051800 EMBL· GenBank· DDBJ | AAH51800.1 EMBL· GenBank· DDBJ | mRNA | ||
BC054489 EMBL· GenBank· DDBJ | AAH54489.1 EMBL· GenBank· DDBJ | mRNA | ||
X55878 EMBL· GenBank· DDBJ | CAA39363.1 EMBL· GenBank· DDBJ | mRNA |