CLTC

Protein-coding gene in the species Homo sapiens
CLTC
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2XZG, 4G55

Identifiers
AliasesCLTC, CHC, CHC17, CLH-17, CLTCL2, Hc, clathrin heavy chain, MRD56
External IDsOMIM: 118955; MGI: 2388633; HomoloGene: 3572; GeneCards: CLTC; OMA:CLTC - orthologs
Gene location (Human)
Chromosome 17 (human)
Chr.Chromosome 17 (human)[1]
Chromosome 17 (human)
Genomic location for CLTC
Genomic location for CLTC
Band17q23.1Start59,619,689 bp[1]
End59,696,956 bp[1]
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[2]
Chromosome 11 (mouse)
Genomic location for CLTC
Genomic location for CLTC
Band11|11 CStart86,585,177 bp[2]
End86,648,391 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • pons

  • lateral nuclear group of thalamus

  • Brodmann area 46

  • middle temporal gyrus

  • mucosa of sigmoid colon

  • orbitofrontal cortex

  • postcentral gyrus

  • corpus epididymis

  • trabecular bone

  • Pars compacta
Top expressed in
  • stroma of bone marrow

  • habenula

  • pontine nuclei

  • medial geniculate nucleus

  • medial dorsal nucleus

  • medial vestibular nucleus

  • dorsomedial hypothalamic nucleus

  • lateral geniculate nucleus

  • deep cerebellar nuclei

  • ventral tegmental area
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • protein binding
  • double-stranded RNA binding
  • protein kinase binding
  • structural molecule activity
  • RNA binding
  • clathrin light chain binding
  • disordered domain specific binding
  • low-density lipoprotein particle receptor binding
  • ubiquitin-specific protease binding
Cellular component
  • extracellular vesicle
  • cytosol
  • clathrin-coated endocytic vesicle membrane
  • clathrin coat of coated pit
  • trans-Golgi network membrane
  • clathrin coat of trans-Golgi network vesicle
  • focal adhesion
  • melanosome
  • plasma membrane
  • endolysosome membrane
  • clathrin-coated pit
  • extracellular exosome
  • cytoplasmic vesicle membrane
  • cytoplasmic vesicle
  • clathrin-coated vesicle
  • extracellular matrix
  • membrane
  • mitotic spindle microtubule
  • cytoplasm
  • lysosome
  • endosome
  • spindle
  • cytoskeleton
  • clathrin coat
  • clathrin complex
  • protein-containing complex
  • intracellular membrane-bounded organelle
  • clathrin-coated endocytic vesicle
  • mitotic spindle
  • intracellular anatomical structure
Biological process
  • antigen processing and presentation of exogenous peptide antigen via MHC class II
  • transferrin transport
  • receptor internalization
  • negative regulation of protein localization to plasma membrane
  • retrograde transport, endosome to Golgi
  • osteoblast differentiation
  • vesicle-mediated transport
  • negative regulation of hyaluronan biosynthetic process
  • intracellular protein transport
  • Wnt signaling pathway, planar cell polarity pathway
  • regulation of mitotic spindle organization
  • autophagy
  • microtubule-based movement
  • cell cycle
  • cell division
  • membrane organization
  • mitotic cell cycle
  • receptor-mediated endocytosis
  • low-density lipoprotein particle receptor catabolic process
  • low-density lipoprotein particle clearance
  • clathrin coat assembly
  • clathrin-dependent endocytosis
  • amyloid-beta clearance by transcytosis
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

1213

67300

Ensembl

ENSG00000141367

ENSMUSG00000047126

UniProt

Q00610

Q68FD5

RefSeq (mRNA)

NM_001288653
NM_004859

NM_001003908
NM_001356393

RefSeq (protein)

NP_001275582
NP_004850

NP_001003908
NP_001343322

Location (UCSC)Chr 17: 59.62 – 59.7 MbChr 11: 86.59 – 86.65 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Clathrin heavy chain 1 is a protein that in humans is encoded by the CLTC gene.[5][6]

Clathrin is a major protein component of the cytoplasmic face of intracellular organelles, called coated vesicles and coated pits. These specialized organelles are involved in the intracellular trafficking of receptors and endocytosis of a variety of macromolecules. The basic subunit of the clathrin coat is composed of three heavy chains and three light chains.[7]

Interactions

CLTC has been shown to interact with PICALM[8] and HGS.[9]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000141367 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000047126 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Dodge GR, Kovalszky I, McBride OW, Yi HF, Chu ML, Saitta B, Stokes DG, Iozzo RV (Feb 1992). "Human clathrin heavy chain (CLTC): partial molecular cloning, expression, and mapping of the gene to human chromosome 17q11-qter". Genomics. 11 (1): 174–8. doi:10.1016/0888-7543(91)90115-U. PMID 1765375.
  6. ^ Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S (Dec 1995). "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1". DNA Res. 1 (1): 27–35. doi:10.1093/dnares/1.1.27. PMID 7584026.
  7. ^ "Entrez Gene: CLTC clathrin, heavy chain (Hc)".
  8. ^ Tebar, F; Bohlander S K; Sorkin A (Aug 1999). "Clathrin assembly lymphoid myeloid leukemia (CALM) protein: localization in endocytic-coated pits, interactions with clathrin, and the impact of overexpression on clathrin-mediated traffic". Mol. Biol. Cell. 10 (8): 2687–702. doi:10.1091/mbc.10.8.2687. ISSN 1059-1524. PMC 25500. PMID 10436022.
  9. ^ Raiborg, C; Bache K G; Mehlum A; Stang E; Stenmark H (Sep 2001). "Hrs recruits clathrin to early endosomes". EMBO J. 20 (17): 5008–21. doi:10.1093/emboj/20.17.5008. ISSN 0261-4189. PMC 125612. PMID 11532964.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


Further reading

  • Murphy JE, Keen JH (1992). "Recognition sites for clathrin-associated proteins AP-2 and AP-3 on clathrin triskelia". J. Biol. Chem. 267 (15): 10850–5. doi:10.1016/S0021-9258(19)50096-5. PMID 1587861.
  • Corvera S (1990). "Insulin stimulates the assembly of cytosolic clathrin onto adipocyte plasma membranes". J. Biol. Chem. 265 (5): 2413–6. doi:10.1016/S0021-9258(19)39811-4. PMID 2154445.
  • Scarmato P, Kirchhausen T (1990). "Analysis of clathrin light chain-heavy chain interactions using truncated mutants of rat liver light chain LCB3". J. Biol. Chem. 265 (7): 3661–8. doi:10.1016/S0021-9258(19)39644-9. PMID 2406259.
  • Hanspal M, Luna E, Branton D (1984). "The association of clathrin fragments with coated vesicle membranes". J. Biol. Chem. 259 (17): 11075–82. doi:10.1016/S0021-9258(18)90624-1. PMID 6147350.
  • Nomura N, Miyajima N, Sazuka T, et al. (1995). "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1 (supplement)". DNA Res. 1 (1): 47–56. doi:10.1093/dnares/1.1.47. PMID 7584028.
  • Fausser JL, Ungewickell E, Ruch JV, Lesot H (1994). "Interaction of vinculin with the clathrin heavy chain". J. Biochem. 114 (4): 498–503. doi:10.1093/oxfordjournals.jbchem.a124206. PMID 8276759.
  • Kedra D, Peyrard M, Fransson I, et al. (1997). "Characterization of a second human clathrin heavy chain polypeptide gene (CLH-22) from chromosome 22q11". Hum. Mol. Genet. 5 (5): 625–31. doi:10.1093/hmg/5.5.625. PMID 8733129.
  • Goodman OB, Krupnick JG, Gurevich VV, et al. (1997). "Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain". J. Biol. Chem. 272 (23): 15017–22. doi:10.1074/jbc.272.23.15017. PMID 9169477.
  • Ramjaun AR, Micheva KD, Bouchelet I, McPherson PS (1997). "Identification and characterization of a nerve terminal-enriched amphiphysin isoform". J. Biol. Chem. 272 (26): 16700–6. doi:10.1074/jbc.272.26.16700. PMID 9195986.
  • McMahon HT, Wigge P, Smith C (1997). "Clathrin interacts specifically with amphiphysin and is displaced by dynamin". FEBS Lett. 413 (2): 319–22. doi:10.1016/S0014-5793(97)00928-9. PMID 9280305. S2CID 42520828.
  • Foti M, Mangasarian A, Piguet V, et al. (1998). "Nef-mediated clathrin-coated pit formation". J. Cell Biol. 139 (1): 37–47. doi:10.1083/jcb.139.1.37. PMC 2139808. PMID 9314527.
  • Dell'Angelica EC, Klumperman J, Stoorvogel W, Bonifacino JS (1998). "Association of the AP-3 adaptor complex with clathrin". Science. 280 (5362): 431–4. Bibcode:1998Sci...280..431D. doi:10.1126/science.280.5362.431. PMID 9545220.
  • Ramjaun AR, McPherson PS (1998). "Multiple amphiphysin II splice variants display differential clathrin binding: identification of two distinct clathrin-binding sites". J. Neurochem. 70 (6): 2369–76. doi:10.1046/j.1471-4159.1998.70062369.x. PMID 9603201. S2CID 21910795.
  • ter Haar E, Musacchio A, Harrison SC, Kirchhausen T (1998). "Atomic structure of clathrin: a beta propeller terminal domain joins an alpha zigzag linker". Cell. 95 (4): 563–73. doi:10.1016/S0092-8674(00)81623-2. PMC 4428171. PMID 9827808.
  • Laporte SA, Oakley RH, Zhang J, et al. (1999). "The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis". Proc. Natl. Acad. Sci. U.S.A. 96 (7): 3712–7. Bibcode:1999PNAS...96.3712L. doi:10.1073/pnas.96.7.3712. PMC 22359. PMID 10097102.
  • Turner CE, Brown MC, Perrotta JA, et al. (1999). "Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal remodeling". J. Cell Biol. 145 (4): 851–63. doi:10.1083/jcb.145.4.851. PMC 2133183. PMID 10330411.
  • Hussain NK, Yamabhai M, Ramjaun AR, et al. (1999). "Splice variants of intersectin are components of the endocytic machinery in neurons and nonneuronal cells". J. Biol. Chem. 274 (22): 15671–7. doi:10.1074/jbc.274.22.15671. PMID 10336464.
  • Ybe JA, Brodsky FM, Hofmann K, et al. (1999). "Clathrin self-assembly is mediated by a tandemly repeated superhelix". Nature. 399 (6734): 371–5. Bibcode:1999Natur.399..371Y. doi:10.1038/20708. PMID 10360576. S2CID 4406014.

External links

  • v
  • t
  • e
  • 1b89: CLATHRIN HEAVY CHAIN PROXIMAL LEG SEGMENT (BOVINE)
    1b89: CLATHRIN HEAVY CHAIN PROXIMAL LEG SEGMENT (BOVINE)
  • 1bpo: CLATHRIN HEAVY-CHAIN TERMINAL DOMAIN AND LINKER
    1bpo: CLATHRIN HEAVY-CHAIN TERMINAL DOMAIN AND LINKER
  • 1c9i: PEPTIDE-IN-GROOVE INTERACTIONS LINK TARGET PROTEINS TO THE B-PROPELLER OF CLATHRIN
    1c9i: PEPTIDE-IN-GROOVE INTERACTIONS LINK TARGET PROTEINS TO THE B-PROPELLER OF CLATHRIN
  • 1c9l: PEPTIDE-IN-GROOVE INTERACTIONS LINK TARGET PROTEINS TO THE B-PROPELLER OF CLATHRIN
    1c9l: PEPTIDE-IN-GROOVE INTERACTIONS LINK TARGET PROTEINS TO THE B-PROPELLER OF CLATHRIN
  • 1utc: CLATHRIN TERMINAL DOMAIN COMPLEXED WITH TLPWDLWTT
    1utc: CLATHRIN TERMINAL DOMAIN COMPLEXED WITH TLPWDLWTT
  • v
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  • e
Synaptic vesicle
SNARE
Q-SNARE
R-SNARE
Synaptotagmin
Other
COPI
COPII
RME/Clathrin
Caveolae
Other/ungrouped
Vesicle formation
Adaptor protein complex 1:
Adaptor protein complex 2:
Adaptor protein complex 3:
Adaptor protein complex 4:
BLOC-1:
BLOC-2:
BLOC-3:
Coats:
Small GTPase
Other
See also vesicular transport protein disorders


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