Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Clathrin heavy chain 1 (Clathrin heavy chain on chromosome 17) (CLH-17)

 CLH1_HUMAN              Reviewed;        1675 AA.
Q00610; D3DU00; Q6N0A0; Q86TF2;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 5.
22-NOV-2017, entry version 185.
RecName: Full=Clathrin heavy chain 1;
AltName: Full=Clathrin heavy chain on chromosome 17;
Short=CLH-17;
Name=CLTC; Synonyms=CLH17, CLTCL2, KIAA0034;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow;
PubMed=7584026; DOI=10.1093/dnares/1.1.27;
Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y.,
Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.;
"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. 1:27-35(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Fetal kidney;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=PNS, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 560-864 (ISOFORMS 1/2).
TISSUE=Colon;
PubMed=1765375; DOI=10.1016/0888-7543(91)90115-U;
Dodge G.R., Kovalszky I., McBride O.W., Yi H.F., Chu M.-L., Saitta B.,
Stokes D.G., Iozzo R.V.;
"Human clathrin heavy chain (CLTC): partial molecular cloning,
expression, and mapping of the gene to human chromosome 17q11-qter.";
Genomics 11:174-178(1991).
[6]
PROTEIN SEQUENCE OF 2-8.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[7]
PROTEIN SEQUENCE OF 2-8; 64-78; 87-96; 164-205; 228-245; 270-278;
298-320; 355-382; 469-481; 507-519; 572-610; 626-638; 799-806;
831-852; 855-865; 882-903; 1011-1037; 1074-1101; 1123-1130; 1166-1179;
1183-1204; 1216-1245; 1312-1326; 1398-1406; 1435-1453; 1482-1498;
1502-1508; 1510-1516 AND 1610-1620, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Cervix carcinoma, Hepatoma, and Mammary carcinoma;
Bienvenut W.V., Calvo F., Matallanas D., Cooper W.N., Boldt K.,
von Kriegsheim A.F., Kolch W.;
Submitted (FEB-2008) to UniProtKB.
[8]
INTERACTION WITH HIP1.
PubMed=11532990; DOI=10.1093/hmg/10.17.1807;
Waelter S., Scherzinger E., Hasenbank R., Nordhoff E., Lurz R.,
Goehler H., Gauss C., Sathasivam K., Bates G.P., Lehrach H.,
Wanker E.E.;
"The huntingtin interacting protein HIP1 is a clathrin and alpha-
adaptin-binding protein involved in receptor-mediated endocytosis.";
Hum. Mol. Genet. 10:1807-1817(2001).
[9]
INTERACTION WITH ERBB2.
PubMed=16314522; DOI=10.1128/MCB.25.24.11005-11018.2005;
Giri D.K., Ali-Seyed M., Li L.Y., Lee D.F., Ling P., Bartholomeusz G.,
Wang S.C., Hung M.C.;
"Endosomal transport of ErbB-2: mechanism for nuclear entry of the
cell surface receptor.";
Mol. Cell. Biol. 25:11005-11018(2005).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15858577; DOI=10.1038/nature03502;
Royle S.J., Bright N.A., Lagnado L.;
"Clathrin is required for the function of the mitotic spindle.";
Nature 434:1152-1157(2005).
[11]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=16968737; DOI=10.1242/jcs.03192;
Royle S.J., Lagnado L.;
"Trimerisation is important for the function of clathrin at the
mitotic spindle.";
J. Cell Sci. 119:4071-4078(2006).
[12]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[13]
INTERACTION WITH FKBP6.
PubMed=18529014; DOI=10.1021/bi8001506;
Jarczowski F., Fischer G., Edlich F.;
"FKBP36 forms complexes with clathrin and Hsp72 in spermatocytes.";
Biochemistry 47:6946-6952(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1494, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-634 AND TYR-1477, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-856; LYS-1441 AND LYS-1501,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[19]
FUNCTION, AND INTERACTION WITH ATG16L1.
PubMed=20639872; DOI=10.1038/ncb2078;
Ravikumar B., Moreau K., Jahreiss L., Puri C., Rubinsztein D.C.;
"Plasma membrane contributes to the formation of pre-autophagosomal
structures.";
Nat. Cell Biol. 12:747-757(2010).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[22]
SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=21297582; DOI=10.1038/emboj.2011.15;
Booth D.G., Hood F.E., Prior I.A., Royle S.J.;
"A TACC3/ch-TOG/clathrin complex stabilises kinetochore fibres by
inter-microtubule bridging.";
EMBO J. 30:906-919(2011).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[25]
INTERACTION WITH TACC3, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
PRO-65; SER-67; THR-87; GLN-89; LYS-96; LYS-98 AND 480-LYS--VAL-484.
PubMed=23918938; DOI=10.1083/jcb.201211127;
Hood F.E., Williams S.J., Burgess S.G., Richards M.W., Roth D.,
Straube A., Pfuhl M., Bayliss R., Royle S.J.;
"Coordination of adjacent domains mediates TACC3-ch-TOG-clathrin
assembly and mitotic spindle binding.";
J. Cell Biol. 202:463-478(2013).
[26]
FUNCTION OF THE TACC3/CH-TOG/CLATHRIN COMPLEX.
PubMed=23532825; DOI=10.1242/jcs.124834;
Cheeseman L.P., Harry E.F., McAinsh A.D., Prior I.A., Royle S.J.;
"Specific removal of TACC3-ch-TOG-clathrin at metaphase deregulates
kinetochore fiber tension.";
J. Cell Sci. 126:2102-2113(2013).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; THR-394; SER-1229
AND SER-1494, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-394 AND SER-1494, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[29]
SUBCELLULAR LOCATION.
PubMed=25596274; DOI=10.1242/bio.201410843;
Gutierrez-Caballero C., Burgess S.G., Bayliss R., Royle S.J.;
"TACC3-ch-TOG track the growing tips of microtubules independently of
clathrin and Aurora-A phosphorylation.";
Biol. Open 4:170-179(2015).
[30]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[31]
X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 1-364 IN COMPLEX WITH
INHIBITORS, AND WD40-LIKE REPEATS.
PubMed=21816279; DOI=10.1016/j.cell.2011.06.025;
von Kleist L., Stahlschmidt W., Bulut H., Gromova K., Puchkov D.,
Robertson M.J., MacGregor K.A., Tomilin N., Pechstein A., Chau N.,
Chircop M., Sakoff J., von Kries J.P., Saenger W., Krausslich H.G.,
Shupliakov O., Robinson P.J., McCluskey A., Haucke V.;
"Role of the clathrin terminal domain in regulating coated pit
dynamics revealed by small molecule inhibition.";
Cell 146:471-484(2011).
[32]
INTERACTION WITH USP2.
PubMed=26756164; DOI=10.1371/journal.pone.0145155;
Pouly D., Chenaux S., Martin V., Babis M., Koch R., Nagoshi E.,
Katanaev V.L., Gachon F., Staub O.;
"USP2-45 is a circadian clock output effector regulating calcium
absorption at the post-translational level.";
PLoS ONE 11:E0145155-E0145155(2016).
-!- 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 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). {ECO:0000269|PubMed:15858577,
ECO:0000269|PubMed:16968737, ECO:0000269|PubMed:20639872,
ECO:0000269|PubMed:21297582, ECO:0000269|PubMed:23532825}.
-!- 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 USP2
isoform 4 (PubMed:26756164). {ECO:0000250|UniProtKB:P49951,
ECO:0000250|UniProtKB:Q68FD5, ECO:0000269|PubMed:11532990,
ECO:0000269|PubMed:16314522, ECO:0000269|PubMed:16968737,
ECO:0000269|PubMed:18529014, ECO:0000269|PubMed:20639872,
ECO:0000269|PubMed:21297582, ECO:0000269|PubMed:26756164}.
-!- INTERACTION:
O00291:HIP1; NbExp=2; IntAct=EBI-354967, EBI-473886;
P10242:MYB; NbExp=4; IntAct=EBI-354967, EBI-298355;
Q01968:OCRL; NbExp=5; IntAct=EBI-354967, EBI-6148898;
Q07912:TNK2; NbExp=2; IntAct=EBI-354967, EBI-603457;
O75674:TOM1L1; NbExp=4; IntAct=EBI-354967, EBI-712991;
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
{ECO:0000269|PubMed:17081065}; Peripheral membrane protein
{ECO:0000269|PubMed:17081065}; Cytoplasmic side
{ECO:0000269|PubMed:17081065}. Membrane, coated pit
{ECO:0000269|PubMed:17081065}; Peripheral membrane protein
{ECO:0000269|PubMed:17081065}; Cytoplasmic side
{ECO:0000269|PubMed:17081065}. Melanosome
{ECO:0000269|PubMed:17081065}. Cytoplasm, cytoskeleton, spindle
{ECO:0000269|PubMed:15858577, ECO:0000269|PubMed:16968737,
ECO:0000269|PubMed:23918938}. 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.
{ECO:0000269|PubMed:25596274}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q00610-1; Sequence=Displayed;
Name=2;
IsoId=Q00610-2; Sequence=VSP_011570, VSP_011571;
Note=No experimental confirmation available.;
-!- 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.
-!- SIMILARITY: Belongs to the clathrin heavy chain family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA04801.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CLTCID360.html";
-!- WEB RESOURCE: Name=Wikipedia; Note=Clathrin entry;
URL="https://en.wikipedia.org/wiki/Clathrin";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; D21260; BAA04801.2; ALT_INIT; mRNA.
EMBL; BX640615; CAE45761.1; -; mRNA.
EMBL; CH471109; EAW94396.1; -; Genomic_DNA.
EMBL; CH471109; EAW94399.1; -; Genomic_DNA.
EMBL; BC051800; AAH51800.1; -; mRNA.
EMBL; BC054489; AAH54489.1; -; mRNA.
EMBL; X55878; CAA39363.1; -; mRNA.
CCDS; CCDS32696.1; -. [Q00610-1]
PIR; A40573; A40573.
RefSeq; NP_004850.1; NM_004859.3. [Q00610-1]
UniGene; Hs.491351; -.
PDB; 2XZG; X-ray; 1.70 A; A=1-364.
PDB; 4G55; X-ray; 1.69 A; A=1-364.
PDBsum; 2XZG; -.
PDBsum; 4G55; -.
ProteinModelPortal; Q00610; -.
SMR; Q00610; -.
BioGrid; 107623; 312.
CORUM; Q00610; -.
ELM; Q00610; -.
IntAct; Q00610; 198.
MINT; MINT-4998595; -.
STRING; 9606.ENSP00000269122; -.
BindingDB; Q00610; -.
ChEMBL; CHEMBL3108634; -.
iPTMnet; Q00610; -.
PhosphoSitePlus; Q00610; -.
SwissPalm; Q00610; -.
BioMuta; CLTC; -.
DMDM; 1705916; -.
EPD; Q00610; -.
MaxQB; Q00610; -.
PaxDb; Q00610; -.
PeptideAtlas; Q00610; -.
PRIDE; Q00610; -.
DNASU; 1213; -.
Ensembl; ENST00000269122; ENSP00000269122; ENSG00000141367. [Q00610-1]
Ensembl; ENST00000393043; ENSP00000376763; ENSG00000141367. [Q00610-2]
GeneID; 1213; -.
KEGG; hsa:1213; -.
UCSC; uc002ixp.4; human. [Q00610-1]
CTD; 1213; -.
DisGeNET; 1213; -.
EuPathDB; HostDB:ENSG00000141367.11; -.
GeneCards; CLTC; -.
H-InvDB; HIX0039315; -.
HGNC; HGNC:2092; CLTC.
HPA; CAB010389; -.
HPA; CAB011571; -.
HPA; CAB017155; -.
HPA; HPA059143; -.
MalaCards; CLTC; -.
MIM; 118955; gene.
neXtProt; NX_Q00610; -.
OpenTargets; ENSG00000141367; -.
Orphanet; 178342; Inflammatory myofibroblastic tumor.
Orphanet; 319308; Translocation renal cell carcinoma.
PharmGKB; PA26618; -.
eggNOG; KOG0985; Eukaryota.
eggNOG; ENOG410XPH1; LUCA.
GeneTree; ENSGT00400000022107; -.
HOGENOM; HOG000188877; -.
HOVERGEN; HBG005344; -.
InParanoid; Q00610; -.
KO; K04646; -.
PhylomeDB; Q00610; -.
TreeFam; TF300059; -.
Reactome; R-HSA-168275; Entry of Influenza Virion into Host Cell via Endocytosis.
Reactome; R-HSA-177504; Retrograde neurotrophin signalling.
Reactome; R-HSA-190873; Gap junction degradation.
Reactome; R-HSA-196025; Formation of annular gap junctions.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
Reactome; R-HSA-437239; Recycling pathway of L1.
Reactome; R-HSA-5099900; WNT5A-dependent internalization of FZD4.
Reactome; R-HSA-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
Reactome; R-HSA-8866427; VLDLR internalisation and degradation.
Reactome; R-HSA-8964038; LDL clearance.
SignaLink; Q00610; -.
SIGNOR; Q00610; -.
ChiTaRS; CLTC; human.
EvolutionaryTrace; Q00610; -.
GeneWiki; CLTC; -.
GenomeRNAi; 1213; -.
PRO; PR:Q00610; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000141367; -.
CleanEx; HS_CLTC; -.
ExpressionAtlas; Q00610; baseline and differential.
Genevisible; Q00610; HS.
GO; GO:0030118; C:clathrin coat; IMP:CAFA.
GO; GO:0030132; C:clathrin coat of coated pit; IEA:InterPro.
GO; GO:0030130; C:clathrin coat of trans-Golgi network vesicle; IEA:InterPro.
GO; GO:0071439; C:clathrin complex; IDA:FlyBase.
GO; GO:0045334; C:clathrin-coated endocytic vesicle; NAS:ARUK-UCL.
GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0036020; C:endolysosome membrane; TAS:Reactome.
GO; GO:0005768; C:endosome; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:1903561; C:extracellular vesicle; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005764; C:lysosome; IDA:HPA.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:1990498; C:mitotic spindle microtubule; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0005819; C:spindle; IDA:UniProtKB.
GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
GO; GO:0032051; F:clathrin light chain binding; IPI:FlyBase.
GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IPI:ARUK-UCL.
GO; GO:0019901; F:protein kinase binding; ISS:ParkinsonsUK-UCL.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0005198; F:structural molecule activity; NAS:UniProtKB.
GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:UniProtKB.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0048268; P:clathrin coat assembly; IMP:CAFA.
GO; GO:0072583; P:clathrin-dependent endocytosis; IMP:ARUK-UCL.
GO; GO:0006886; P:intracellular protein transport; NAS:UniProtKB.
GO; GO:0034383; P:low-density lipoprotein particle clearance; TAS:Reactome.
GO; GO:0032802; P:low-density lipoprotein particle receptor catabolic process; TAS:Reactome.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0007018; P:microtubule-based movement; TAS:Reactome.
GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
GO; GO:1900126; P:negative regulation of hyaluronan biosynthetic process; IDA:UniProtKB.
GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IMP:UniProtKB.
GO; GO:0001649; P:osteoblast differentiation; IDA:UniProtKB.
GO; GO:0031623; P:receptor internalization; IMP:BHF-UCL.
GO; GO:0006898; P:receptor-mediated endocytosis; IMP:UniProtKB.
GO; GO:0060236; P:regulation of mitotic spindle organization; IMP:UniProtKB.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
GO; GO:0045056; P:transcytosis; IMP:ARUK-UCL.
GO; GO:0033572; P:transferrin transport; IMP:BHF-UCL.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
Gene3D; 1.25.40.10; -; 4.
Gene3D; 1.25.40.30; -; 1.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
InterPro; IPR012331; Clathrin_H-chain_linker.
InterPro; IPR015348; Clathrin_H-chain_linker_core.
InterPro; IPR022365; Clathrin_H-chain_propeller_rpt.
InterPro; IPR016341; Clathrin_heavy_chain.
InterPro; IPR011990; TPR-like_helical_dom_sf.
Pfam; PF00637; Clathrin; 7.
Pfam; PF09268; Clathrin-link; 1.
Pfam; PF01394; Clathrin_propel; 5.
PIRSF; PIRSF002290; Clathrin_H_chain; 1.
SMART; SM00299; CLH; 7.
SUPFAM; SSF48371; SSF48371; 6.
PROSITE; PS50236; CHCR; 7.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Autophagy;
Cell cycle; Cell division; Coated pit; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Cytoskeleton; Direct protein sequencing;
Membrane; Mitosis; Phosphoprotein; Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:12665801,
ECO:0000269|Ref.7}.
CHAIN 2 1675 Clathrin heavy chain 1.
/FTId=PRO_0000205778.
REPEAT 537 683 CHCR 1. {ECO:0000255|PROSITE-
ProRule:PRU01006,
ECO:0000269|PubMed:21816279}.
REPEAT 686 828 CHCR 2. {ECO:0000255|PROSITE-
ProRule:PRU01006,
ECO:0000269|PubMed:21816279}.
REPEAT 833 972 CHCR 3. {ECO:0000255|PROSITE-
ProRule:PRU01006,
ECO:0000269|PubMed:21816279}.
REPEAT 979 1124 CHCR 4. {ECO:0000255|PROSITE-
ProRule:PRU01006,
ECO:0000269|PubMed:21816279}.
REPEAT 1128 1269 CHCR 5. {ECO:0000255|PROSITE-
ProRule:PRU01006,
ECO:0000269|PubMed:21816279}.
REPEAT 1274 1420 CHCR 6. {ECO:0000255|PROSITE-
ProRule:PRU01006,
ECO:0000269|PubMed:21816279}.
REPEAT 1423 1566 CHCR 7. {ECO:0000255|PROSITE-
ProRule:PRU01006,
ECO:0000269|PubMed:21816279}.
REGION 2 479 Globular terminal domain.
REGION 24 67 WD40-like repeat 1.
REGION 68 107 WD40-like repeat 2.
REGION 108 149 WD40-like repeat 3.
REGION 150 195 WD40-like repeat 4.
REGION 196 257 WD40-like repeat 5.
REGION 258 301 WD40-like repeat 6.
REGION 302 330 WD40-like repeat 7.
REGION 449 465 Binding site for the uncoating ATPase,
involved in lattice disassembly.
{ECO:0000255}.
REGION 457 507 Involved in spindle localization and
interaction with TACC3.
{ECO:0000269|PubMed:23918938}.
REGION 480 523 Flexible linker.
REGION 524 1675 Heavy chain arm.
REGION 524 634 Distal segment.
REGION 639 1675 Proximal segment.
REGION 1213 1522 Involved in binding clathrin light chain.
{ECO:0000250}.
REGION 1550 1675 Trimerization. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712,
ECO:0000269|Ref.7}.
MOD_RES 67 67 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 105 105 Phosphothreonine.
{ECO:0000250|UniProtKB:Q68FD5}.
MOD_RES 184 184 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q68FD5}.
MOD_RES 394 394 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 634 634 Phosphotyrosine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 737 737 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q68FD5}.
MOD_RES 856 856 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 899 899 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q68FD5}.
MOD_RES 1167 1167 Phosphoserine.
{ECO:0000250|UniProtKB:Q68FD5}.
MOD_RES 1206 1206 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q68FD5}.
MOD_RES 1229 1229 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1441 1441 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1441 1441 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q68FD5}.
MOD_RES 1477 1477 Phosphotyrosine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1487 1487 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q68FD5}.
MOD_RES 1494 1494 Phosphoserine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1501 1501 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 1636 1639 QPQL -> NLSL (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_011570.
VAR_SEQ 1640 1675 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_011571.
MUTAGEN 65 65 P->N: Disrupts spindle localization.
{ECO:0000269|PubMed:23918938}.
MUTAGEN 67 67 S->G: Disrupts spindle localization.
{ECO:0000269|PubMed:23918938}.
MUTAGEN 87 87 T->A: Disrupts spindle localization.
{ECO:0000269|PubMed:23918938}.
MUTAGEN 89 89 Q->A: Disrupts spindle localization.
{ECO:0000269|PubMed:23918938}.
MUTAGEN 96 96 K->E: Disrupts spindle localization.
{ECO:0000269|PubMed:23918938}.
MUTAGEN 98 98 K->E: Disrupts spindle localization.
{ECO:0000269|PubMed:23918938}.
MUTAGEN 444 444 R->E: Disrupts spindle localization; when
associated with E-445, E-500 E-506 and E-
507. {ECO:0000269|PubMed:23918938}.
MUTAGEN 445 445 K->E: Disrupts spindle localization; when
associated with E-444, E-500, E-506 and
E-507. {ECO:0000269|PubMed:23918938}.
MUTAGEN 480 484 LRANV->ERGQC: Disrupts spindle
localization and interaction with TACC3.
{ECO:0000269|PubMed:23918938}.
MUTAGEN 481 481 R->E: Disrupts spindle localization; when
associated with E-487, E-500, E-506 and
E-507. {ECO:0000269|PubMed:23918938}.
MUTAGEN 487 487 K->E: Disrupts spindle localization; when
associated with E-481, E-500, E-506 and
E-507. {ECO:0000269|PubMed:23918938}.
MUTAGEN 500 500 K->E: Disrupts spindle localization; when
associated with E-444, E-445, E-506 and
E-507. {ECO:0000269|PubMed:23918938}.
MUTAGEN 500 500 K->E: Disrupts spindle localization; when
associated with E-481, E-487, E-506 and
E-507. {ECO:0000269|PubMed:23918938}.
MUTAGEN 506 506 K->E: Disrupts spindle localization; when
associated with E-444, E-445, E-500 and
E-507. {ECO:0000269|PubMed:23918938}.
MUTAGEN 506 506 K->E: Disrupts spindle localization; when
associated with E-481, E-487, E-500 and
E-507. {ECO:0000269|PubMed:23918938}.
MUTAGEN 507 507 K->E: Disrupts spindle localization; when
associated with E-444, E-445, E-500 and
E-506. {ECO:0000269|PubMed:23918938}.
MUTAGEN 507 507 K->E: Disrupts spindle localization; when
associated with E-481, E-487, E-500 and
E-506. {ECO:0000269|PubMed:23918938}.
CONFLICT 560 560 Q -> R (in Ref. 5; CAA39363).
{ECO:0000305}.
CONFLICT 817 817 G -> V (in Ref. 5; CAA39363).
{ECO:0000305}.
CONFLICT 923 923 R -> H (in Ref. 2; CAE45761).
{ECO:0000305}.
CONFLICT 1563 1563 R -> G (in Ref. 2; CAE45761).
{ECO:0000305}.
CONFLICT 1652 1652 Q -> R (in Ref. 2; CAE45761).
{ECO:0000305}.
STRAND 6 14 {ECO:0000244|PDB:4G55}.
HELIX 15 18 {ECO:0000244|PDB:4G55}.
HELIX 22 24 {ECO:0000244|PDB:4G55}.
TURN 27 29 {ECO:0000244|PDB:4G55}.
STRAND 30 34 {ECO:0000244|PDB:4G55}.
STRAND 37 44 {ECO:0000244|PDB:4G55}.
STRAND 47 54 {ECO:0000244|PDB:4G55}.
STRAND 62 65 {ECO:0000244|PDB:4G55}.
STRAND 69 73 {ECO:0000244|PDB:4G55}.
STRAND 75 84 {ECO:0000244|PDB:4G55}.
STRAND 87 92 {ECO:0000244|PDB:4G55}.
TURN 93 96 {ECO:0000244|PDB:4G55}.
STRAND 97 103 {ECO:0000244|PDB:4G55}.
STRAND 108 113 {ECO:0000244|PDB:4G55}.
STRAND 115 133 {ECO:0000244|PDB:4G55}.
STRAND 139 143 {ECO:0000244|PDB:4G55}.
HELIX 146 148 {ECO:0000244|PDB:4G55}.
STRAND 152 158 {ECO:0000244|PDB:4G55}.
STRAND 164 173 {ECO:0000244|PDB:4G55}.
STRAND 176 185 {ECO:0000244|PDB:4G55}.
TURN 186 189 {ECO:0000244|PDB:4G55}.
STRAND 190 194 {ECO:0000244|PDB:4G55}.
STRAND 197 204 {ECO:0000244|PDB:4G55}.
STRAND 213 222 {ECO:0000244|PDB:4G55}.
STRAND 225 232 {ECO:0000244|PDB:4G55}.
STRAND 246 250 {ECO:0000244|PDB:4G55}.
STRAND 261 267 {ECO:0000244|PDB:4G55}.
TURN 268 271 {ECO:0000244|PDB:4G55}.
STRAND 272 277 {ECO:0000244|PDB:4G55}.
STRAND 280 286 {ECO:0000244|PDB:4G55}.
TURN 287 289 {ECO:0000244|PDB:4G55}.
STRAND 292 297 {ECO:0000244|PDB:4G55}.
STRAND 303 309 {ECO:0000244|PDB:4G55}.
HELIX 310 312 {ECO:0000244|PDB:4G55}.
STRAND 314 319 {ECO:0000244|PDB:4G55}.
STRAND 323 329 {ECO:0000244|PDB:4G55}.
TURN 331 333 {ECO:0000244|PDB:4G55}.
HELIX 334 340 {ECO:0000244|PDB:4G55}.
HELIX 345 354 {ECO:0000244|PDB:4G55}.
SEQUENCE 1675 AA; 191615 MW; 6C4F2D54950079E2 CRC64;
MAQILPIRFQ EHLQLQNLGI NPANIGFSTL TMESDKFICI REKVGEQAQV VIIDMNDPSN
PIRRPISADS AIMNPASKVI ALKAGKTLQI FNIEMKSKMK AHTMTDDVTF WKWISLNTVA
LVTDNAVYHW SMEGESQPVK MFDRHSSLAG CQIINYRTDA KQKWLLLTGI SAQQNRVVGA
MQLYSVDRKV SQPIEGHAAS FAQFKMEGNA EESTLFCFAV RGQAGGKLHI IEVGTPPTGN
QPFPKKAVDV FFPPEAQNDF PVAMQISEKH DVVFLITKYG YIHLYDLETG TCIYMNRISG
ETIFVTAPHE ATAGIIGVNR KGQVLSVCVE EENIIPYITN VLQNPDLALR MAVRNNLAGA
EELFARKFNA LFAQGNYSEA AKVAANAPKG ILRTPDTIRR FQSVPAQPGQ TSPLLQYFGI
LLDQGQLNKY ESLELCRPVL QQGRKQLLEK WLKEDKLECS EELGDLVKSV DPTLALSVYL
RANVPNKVIQ CFAETGQVQK IVLYAKKVGY TPDWIFLLRN VMRISPDQGQ QFAQMLVQDE
EPLADITQIV DVFMEYNLIQ QCTAFLLDAL KNNRPSEGPL QTRLLEMNLM HAPQVADAIL
GNQMFTHYDR AHIAQLCEKA GLLQRALEHF TDLYDIKRAV VHTHLLNPEW LVNYFGSLSV
EDSLECLRAM LSANIRQNLQ ICVQVASKYH EQLSTQSLIE LFESFKSFEG LFYFLGSIVN
FSQDPDVHFK YIQAACKTGQ IKEVERICRE SNCYDPERVK NFLKEAKLTD QLPLIIVCDR
FDFVHDLVLY LYRNNLQKYI EIYVQKVNPS RLPVVIGGLL DVDCSEDVIK NLILVVRGQF
STDELVAEVE KRNRLKLLLP WLEARIHEGC EEPATHNALA KIYIDSNNNP ERFLRENPYY
DSRVVGKYCE KRDPHLACVA YERGQCDLEL INVCNENSLF KSLSRYLVRR KDPELWGSVL
LESNPYRRPL IDQVVQTALS ETQDPEEVSV TVKAFMTADL PNELIELLEK IVLDNSVFSE
HRNLQNLLIL TAIKADRTRV MEYINRLDNY DAPDIANIAI SNELFEEAFA IFRKFDVNTS
AVQVLIEHIG NLDRAYEFAE RCNEPAVWSQ LAKAQLQKGM VKEAIDSYIK ADDPSSYMEV
VQAANTSGNW EELVKYLQMA RKKARESYVE TELIFALAKT NRLAELEEFI NGPNNAHIQQ
VGDRCYDEKM YDAAKLLYNN VSNFGRLAST LVHLGEYQAA VDGARKANST RTWKEVCFAC
VDGKEFRLAQ MCGLHIVVHA DELEELINYY QDRGYFEELI TMLEAALGLE RAHMGMFTEL
AILYSKFKPQ KMREHLELFW SRVNIPKVLR AAEQAHLWAE LVFLYDKYEE YDNAIITMMN
HPTDAWKEGQ FKDIITKVAN VELYYRAIQF YLEFKPLLLN DLLMVLSPRL DHTRAVNYFS
KVKQLPLVKP YLRSVQNHNN KSVNESLNNL FITEEDYQAL RTSIDAYDNF DNISLAQRLE
KHELIEFRRI AAYLFKGNNR WKQSVELCKK DSLYKDAMQY ASESKDTELA EELLQWFLQE
EKRECFGACL FTCYDLLRPD VVLETAWRHN IMDFAMPYFI QVMKEYLTKV DKLDASESLR
KEEEQATETQ PIVYGQPQLM LTAGPSVAVP PQAPFGYGYT APPYGQPQPG FGYSM


Related products :

Catalog number Product name Quantity
EIAAB07885 Clathrin heavy chain 2,Clathrin heavy chain on chromosome 22,CLH22,CLH-22,CLTCL,CLTCL1,CLTD,Homo sapiens,Human
EIAAB07883 Clathrin heavy chain 1,Clathrin heavy chain on chromosome 17,CLH17,CLH-17,CLTC,CLTCL2,Homo sapiens,Human,KIAA0034
AS10 690 Antibody: Clathrin heavy-chain, Immunogen: KLH-conjugated peptide derived from available plant clathrin heavy chain sequences including Arabidopsis thaliana Q0WNJ6, Host: rabbit, polyclonal 100
11-526-C100 Mouse Monoclonal to Clathrin heavy chain Antigen Clathrin heavy chain Isotype IgM Antigen Clathrin heavy chain Isotype IgM 0.1 mg
11-526-C025 Mouse Monoclonal to Clathrin heavy chain Antigen Clathrin heavy chain Isotype IgM Antigen Clathrin heavy chain Isotype IgM 0.025 mg
1F-268-T025 Mouse Monoclonal to Clathrin heavy chain Antigen Clathrin heavy chain Species Reactivity Human, Porcine, Mouse, Rat, Bovine, Other not determined Negative Species Clone MEM_108 Isotype IgG1 Appl 25 tests
1F-268-T100 Mouse Monoclonal to Clathrin heavy chain Antigen Clathrin heavy chain Species Reactivity Human, Porcine, Mouse, Rat, Bovine, Other not determined Negative Species Clone MEM_108 Isotype IgG1 Appl 100 tests
20-272-191035 Clathrin heavy chain - Mouse monoclonal [3F132] to Clathrin heavy chain; CLH-17 Monoclonal 0.05 ml
20-272-191034 Clathrin heavy chain - Mouse monoclonal [3F132] to Clathrin heavy chain; CLH-17 Monoclonal 0.25 ml
20-272-191030 Clathrin heavy chain - Mouse monoclonal [2Q2166] to Clathrin heavy chain; CLH-17 Monoclonal 0.05 mg
A020077 Rabbit Anti-Clathrin heavy chain per Clathrin HC Ab 200Ul
20-272-190292 Clathrin heavy chain - Mouse monoclonal [STo 3H9] to Clathrin heavy chain; CLH-17 Monoclonal 0.25 mg
20-272-190459 Clathrin heavy chain - Mouse monoclonal [TD.1] to Clathrin heavy chain; CLH-17 Monoclonal 0.1 ml
SCH-MCA2883 MOUSE ANTI CLATHRIN HEAVY CHAIN, Product Type Monoclonal Antibody, Specificity CLATHRIN, Target Species Mouse, Host Mouse, Format Purified, Isotypes IgM, Applications E, IF, IP, WB, Clone BF_0 0.1 mg
MCA2883 MOUSE ANTI CLATHRIN HEAVY CHAIN, Product Type Monoclonal Antibody, Specificity CLATHRIN, Target Species Mouse, Host Mouse, Format Purified, Isotypes IgM, Applications E, IF, IP, WB, Clone BF_0 0.1 mg
R-165-100 Clathrin heavy chain 0.1 ml
GTX14399 Clathrin heavy chain 25 µg
GTX26316 Clathrin heavy chain 200 µl
BM295 Clathrin heavy chain 0.1 mg
GTX10822 Clathrin heavy chain 0.25 mg
GTX14406 Clathrin heavy chain 250 µl
GTX14407 Clathrin heavy chain 50 µl
GTX11331 Clathrin heavy chain 100 µl
GTX14401 Clathrin heavy chain 50 µg
NB300-613 Clathrin heavy chain 0.1 ml


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur