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

Clathrin light chain A (Lca)

 CLCA_HUMAN              Reviewed;         248 AA.
P09496; A8K4W3; B4DIN1; F5H6N3; Q2XPN5; Q53XZ1;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
22-NOV-2017, entry version 175.
RecName: Full=Clathrin light chain A;
Short=Lca;
Name=CLTA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BRAIN AND NON-BRAIN).
PubMed=3267234;
Jackson A.P., Parham P.;
"Structure of human clathrin light chains. Conservation of light chain
polymorphism in three mammalian species.";
J. Biol. Chem. 263:16688-16695(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM NON-BRAIN).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS NON-BRAIN AND 4).
TISSUE=Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Lin L., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z.,
Liang M., Tang Z., Huang B., Li H., Yang S.;
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[6]
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM NON-BRAIN).
TISSUE=Lung;
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).
[8]
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).
[9]
INTERACTION WITH CALY.
PubMed=16595675; DOI=10.1074/jbc.M600265200;
Xiao J., Dai R., Negyessy L., Bergson C.;
"Calcyon, a novel partner of clathrin light chain, stimulates
clathrin-mediated endocytosis.";
J. Biol. Chem. 281:15182-15193(2006).
[10]
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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206 AND SER-236, 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).
[12]
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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105 AND SER-206, AND
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).
[14]
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).
[15]
INTERACTION WITH TACC3 AND CKAP5, FUNCTION, AND SUBCELLULAR LOCATION.
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).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, 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).
[18]
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).
[19]
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).
-!- FUNCTION: Clathrin is the major protein of the polyhedral coat of
coated pits and vesicles. 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:21297582).
{ECO:0000305|PubMed:15858577, ECO:0000305|PubMed:21297582}.
-!- SUBUNIT: Clathrin coats are formed from molecules containing 3
heavy chains and 3 light chains. Interacts with CALY; the
interaction stimulates clathrin self-assembly and clathrin-
mediated endocytosis. Interacts with CKAP5 and TACC3 forming the
TACC3/ch-TOG/clathrin complex located at spindle inter-
microtubules bridges; the complex implicates clathrin triskelions.
{ECO:0000269|PubMed:16595675, ECO:0000269|PubMed:21297582}.
-!- INTERACTION:
Q9NYX4:CALY; NbExp=4; IntAct=EBI-1171169, EBI-10904725;
Q9Y6A5:TACC3; NbExp=3; IntAct=EBI-1171169, EBI-2554984;
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral
membrane protein; Cytoplasmic side. Membrane, coated pit;
Peripheral membrane protein; Cytoplasmic side. Cytoplasm,
cytoskeleton, spindle {ECO:0000269|PubMed:21297582,
ECO:0000305|PubMed:15858577}. Note=Cytoplasmic face of coated pits
and vesicles. In complex with TACC3 and CKAP5 (forming the
TACC3/ch-TOG/clathrin complex) localized to inter-microtubule
bridges in mitotic spindles. {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=Brain;
IsoId=P09496-1; Sequence=Displayed;
Name=Non-brain;
IsoId=P09496-2; Sequence=VSP_001095;
Name=3;
IsoId=P09496-3; Sequence=VSP_024238;
Name=4;
IsoId=P09496-4; Sequence=VSP_043239;
Note=No experimental confirmation available.;
Name=5;
IsoId=P09496-5; Sequence=VSP_047168, VSP_001095;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
-!- SIMILARITY: Belongs to the clathrin light chain family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M20471; AAA51817.1; -; mRNA.
EMBL; M20472; AAA59505.1; -; mRNA.
EMBL; DQ270158; ABB76683.1; -; mRNA.
EMBL; BT007170; AAP35834.1; -; mRNA.
EMBL; AK291078; BAF83767.1; -; mRNA.
EMBL; AK295692; BAG58543.1; -; mRNA.
EMBL; AL158830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL161792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471071; EAW58312.1; -; Genomic_DNA.
EMBL; BC009201; AAH09201.1; -; mRNA.
EMBL; BC019287; AAH19287.1; -; mRNA.
CCDS; CCDS43802.1; -. [P09496-3]
CCDS; CCDS55306.1; -. [P09496-4]
CCDS; CCDS55307.1; -. [P09496-5]
CCDS; CCDS6600.1; -. [P09496-2]
CCDS; CCDS6601.1; -. [P09496-1]
PIR; A31775; A31775.
RefSeq; NP_001070145.1; NM_001076677.2. [P09496-3]
RefSeq; NP_001171689.1; NM_001184760.1. [P09496-4]
RefSeq; NP_001171691.1; NM_001184762.1. [P09496-5]
RefSeq; NP_001824.1; NM_001833.3. [P09496-2]
RefSeq; NP_009027.1; NM_007096.3. [P09496-1]
UniGene; Hs.522114; -.
ProteinModelPortal; P09496; -.
SMR; P09496; -.
BioGrid; 107621; 80.
IntAct; P09496; 76.
MINT; MINT-1326541; -.
STRING; 9606.ENSP00000242285; -.
iPTMnet; P09496; -.
PhosphoSitePlus; P09496; -.
SwissPalm; P09496; -.
BioMuta; CLTA; -.
DMDM; 116501; -.
OGP; P09496; -.
EPD; P09496; -.
MaxQB; P09496; -.
PaxDb; P09496; -.
PeptideAtlas; P09496; -.
PRIDE; P09496; -.
TopDownProteomics; P09496-1; -. [P09496-1]
TopDownProteomics; P09496-2; -. [P09496-2]
DNASU; 1211; -.
Ensembl; ENST00000242285; ENSP00000242285; ENSG00000122705. [P09496-1]
Ensembl; ENST00000345519; ENSP00000242284; ENSG00000122705. [P09496-2]
Ensembl; ENST00000396603; ENSP00000379848; ENSG00000122705. [P09496-3]
Ensembl; ENST00000433436; ENSP00000401019; ENSG00000122705. [P09496-1]
Ensembl; ENST00000470744; ENSP00000419746; ENSG00000122705. [P09496-4]
Ensembl; ENST00000538225; ENSP00000442869; ENSG00000122705. [P09496-4]
Ensembl; ENST00000540080; ENSP00000437508; ENSG00000122705. [P09496-5]
GeneID; 1211; -.
KEGG; hsa:1211; -.
UCSC; uc003zzc.4; human. [P09496-1]
CTD; 1211; -.
DisGeNET; 1211; -.
EuPathDB; HostDB:ENSG00000122705.16; -.
GeneCards; CLTA; -.
HGNC; HGNC:2090; CLTA.
HPA; CAB002665; -.
HPA; HPA050918; -.
HPA; HPA054667; -.
MIM; 118960; gene.
neXtProt; NX_P09496; -.
OpenTargets; ENSG00000122705; -.
PharmGKB; PA26616; -.
eggNOG; KOG4031; Eukaryota.
eggNOG; ENOG4111J5K; LUCA.
GeneTree; ENSGT00390000010441; -.
HOGENOM; HOG000008147; -.
HOVERGEN; HBG003386; -.
InParanoid; P09496; -.
KO; K04644; -.
OMA; KTKTNNR; -.
OrthoDB; EOG091G0WEF; -.
PhylomeDB; P09496; -.
TreeFam; TF313162; -.
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.
ChiTaRS; CLTA; human.
GenomeRNAi; 1211; -.
PMAP-CutDB; P09496; -.
PRO; PR:P09496; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000122705; -.
CleanEx; HS_CLTA; -.
ExpressionAtlas; P09496; baseline and differential.
Genevisible; P09496; 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:0030125; C:clathrin vesicle coat; IBA:GO_Central.
GO; GO:0045334; C:clathrin-coated endocytic vesicle; NAS:ARUK-UCL.
GO; GO:0031410; C:cytoplasmic vesicle; ISS:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0036020; C:endolysosome membrane; TAS:Reactome.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
GO; GO:0030672; C:synaptic vesicle membrane; IEA:Ensembl.
GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
GO; GO:0032050; F:clathrin heavy chain binding; IPI:FlyBase.
GO; GO:0051020; F:GTPase binding; IEA:Ensembl.
GO; GO:0042277; F:peptide binding; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO; GO:0007049; P:cell cycle; 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; IBA:GO_Central.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
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.
InterPro; IPR000996; Clathrin_L-chain.
PANTHER; PTHR10639; PTHR10639; 1.
Pfam; PF01086; Clathrin_lg_ch; 1.
PROSITE; PS00224; CLATHRIN_LIGHT_CHN_1; 1.
PROSITE; PS00581; CLATHRIN_LIGHT_CHN_2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Calcium; Cell cycle; Cell division;
Coated pit; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Cytoskeleton; Membrane; Mitosis; Phosphoprotein; Reference proteome.
CHAIN 1 248 Clathrin light chain A.
/FTId=PRO_0000205767.
REGION 100 162 Involved in binding clathrin heavy chain.
MOD_RES 105 105 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 206 206 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 223 223 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q6IRU5}.
MOD_RES 236 236 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 242 242 N6-acetyllysine.
{ECO:0000250|UniProtKB:O08585}.
VAR_SEQ 73 124 Missing (in isoform 5). {ECO:0000305}.
/FTId=VSP_047168.
VAR_SEQ 162 180 RVADEAFYKQPFADVIGYV -> S (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043239.
VAR_SEQ 163 192 Missing (in isoform Non-brain and isoform
5). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:3267234,
ECO:0000303|Ref.2}.
/FTId=VSP_001095.
VAR_SEQ 181 192 Missing (in isoform 3).
{ECO:0000303|Ref.4}.
/FTId=VSP_024238.
CONFLICT 207 207 P -> Q (in Ref. 4; ABB76683).
{ECO:0000305}.
SEQUENCE 248 AA; 27077 MW; 8D8A3B49E6353D93 CRC64;
MAELDPFGAP AGAPGGPALG NGVAGAGEED PAAAFLAQQE SEIAGIENDE AFAILDGGAP
GPQPHGEPPG GPDAVDGVMN GEYYQESNGP TDSYAAISQV DRLQSEPESI RKWREEQMER
LEALDANSRK QEAEWKEKAI KELEEWYARQ DEQLQKTKAN NRVADEAFYK QPFADVIGYV
TNINHPCYSL EQAAEEAFVN DIDESSPGTE WERVARLCDF NPKSSKQAKD VSRMRSVLIS
LKQAPLVH


Related products :

Catalog number Product name Quantity
LF-MA10063 anti-Clathrin light chain (4B12-1E3), Mouse monoclonal to Clathrin light chain, Isotype IgG2b, Host Mouse 100 ug
20-272-191036 Clathrin light chain - Mouse monoclonal [3F133] to Clathrin light chain; Lca Monoclonal 0.25 ml
20-272-190460 Clathrin light chain - Mouse monoclonal [CON.1] to Clathrin light chain; Lca Monoclonal 0.1 ml
20-272-191581 Clathrin light chain. prediluted - Mouse monoclonal [SPM174] to Clathrin light chain. prediluted; Lca Monoclonal 7 ml
20-272-191037 Clathrin light chain - BSA and Azide free - Mouse monoclonal [3F133] to Clathrin light chain - BSA and Azide free; Lca Monoclonal 0.05 ml
10-288-22180F Clathrin light chain B - Lcb 0.05 mg
GTX82294 Clathrin light chain B 50 µg
GTX101938 Clathrin light chain B 100 µg
GTX101938 Clathrin light chain B 100 µg
10-288-22180F Clathrin light chain B - Lcb 0.1 mg
GTX14408 Clathrin light chain A (CLTA_CLTB) 250 µl
GTX14408 Clathrin light chain A (CLTA_CLTB) 250 µl
BMMS-1291-R1 Clathrin, Light Chain 1mL
BMMS-1291-B Clathrin, Light Chain 1mL
BMMS-1291-MX Clathrin, Light Chain MTO
BMMS-1291-B1 Clathrin, Light Chain 0.5mL
BMMS-1291-B1 Clathrin, Light Chain 0.5mL
BMMS-1291-B0 Clathrin, Light Chain 0.1mL
GTX11332 Clathrin light chain A (CLTA_CLTB) 100 µl
5134 Protein,Clathrin light chain B 0.1 mg
BMMS-1291-B0 Clathrin, Light Chain 0.1mL
BMMS-1291-B Clathrin, Light Chain 1mL
GTX14409 Clathrin light chain A (CLTA_CLTB) 50 µl
GTX17949 Clathrin light chain A (CLTA_CLTB) 7 ml
GTX14409 Clathrin light chain A (CLTA_CLTB) 50 µl


 

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