CLCB_HUMAN
ID CLCB_HUMAN Reviewed; 229 AA.
AC P09497; Q53Y37; Q6FHW1;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Clathrin light chain B;
DE Short=Lcb;
GN Name=CLTB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX PubMed=3267234; DOI=10.1016/s0021-9258(18)37445-3;
RA Jackson A.P., Parham P.;
RT "Structure of human clathrin light chains. Conservation of light chain
RT polymorphism in three mammalian species.";
RL J. Biol. Chem. 263:16688-16695(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM NON-BRAIN).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM NON-BRAIN).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM NON-BRAIN).
RC TISSUE=Lung, and Retinal pigment epithelium;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH HIP1 AND HIP1R.
RX PubMed=11889126; DOI=10.1074/jbc.m112310200;
RA Legendre-Guillemin V., Metzler M., Charbonneau M., Gan L., Chopra V.,
RA Philie J., Hayden M.R., McPherson P.S.;
RT "HIP1 and HIP12 display differential binding to F-actin, AP2, and clathrin.
RT Identification of a novel interaction with clathrin light chain.";
RL J. Biol. Chem. 277:19897-19904(2002).
RN [7]
RP INTERACTION WITH HIP1R.
RX PubMed=15533940; DOI=10.1074/jbc.m408454200;
RA Chen C.-Y., Brodsky F.M.;
RT "Huntingtin-interacting protein 1 (Hip1) and Hip1-related protein (Hip1R)
RT bind the conserved sequence of clathrin light chains and thereby influence
RT clathrin assembly in vitro and actin distribution in vivo.";
RL J. Biol. Chem. 280:6109-6117(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-187, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Clathrin is the major protein of the polyhedral coat of
CC coated pits and vesicles.
CC -!- SUBUNIT: Clathrin coats are formed from molecules containing 3 heavy
CC chains and 3 light chains. Interacts (via N-terminus) with HIP1.
CC Interacts with HIP1R. {ECO:0000269|PubMed:11889126,
CC ECO:0000269|PubMed:15533940}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral membrane
CC protein; Cytoplasmic side. Membrane, coated pit; Peripheral membrane
CC protein; Cytoplasmic side. Note=Cytoplasmic face of coated pits and
CC vesicles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Brain;
CC IsoId=P09497-1; Sequence=Displayed;
CC Name=Non-brain;
CC IsoId=P09497-2; Sequence=VSP_001098;
CC -!- SIMILARITY: Belongs to the clathrin light chain family. {ECO:0000305}.
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DR EMBL; M20469; AAA51818.1; -; mRNA.
DR EMBL; M20470; AAA59506.1; -; mRNA.
DR EMBL; BT007028; AAP35675.1; -; mRNA.
DR EMBL; CR536577; CAG38814.1; -; mRNA.
DR EMBL; CH471195; EAW85079.1; -; Genomic_DNA.
DR EMBL; BC006332; AAH06332.1; -; mRNA.
DR EMBL; BC006457; AAH06457.1; -; mRNA.
DR CCDS; CCDS4402.1; -. [P09497-2]
DR CCDS; CCDS4403.1; -. [P09497-1]
DR PIR; B31775; B31775.
DR RefSeq; NP_001825.1; NM_001834.3. [P09497-2]
DR RefSeq; NP_009028.1; NM_007097.3. [P09497-1]
DR AlphaFoldDB; P09497; -.
DR SMR; P09497; -.
DR BioGRID; 107622; 135.
DR IntAct; P09497; 94.
DR MINT; P09497; -.
DR STRING; 9606.ENSP00000309415; -.
DR TCDB; 8.A.137.1.2; the clathrin (clathrin) family.
DR GlyGen; P09497; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P09497; -.
DR PhosphoSitePlus; P09497; -.
DR BioMuta; CLTB; -.
DR OGP; P09497; -.
DR EPD; P09497; -.
DR jPOST; P09497; -.
DR MassIVE; P09497; -.
DR MaxQB; P09497; -.
DR PaxDb; P09497; -.
DR PeptideAtlas; P09497; -.
DR PRIDE; P09497; -.
DR ProteomicsDB; 52240; -. [P09497-1]
DR ProteomicsDB; 52241; -. [P09497-2]
DR Antibodypedia; 29088; 235 antibodies from 27 providers.
DR DNASU; 1212; -.
DR Ensembl; ENST00000310418.9; ENSP00000309415.4; ENSG00000175416.16. [P09497-1]
DR Ensembl; ENST00000345807.7; ENSP00000310812.4; ENSG00000175416.16. [P09497-2]
DR GeneID; 1212; -.
DR KEGG; hsa:1212; -.
DR MANE-Select; ENST00000310418.9; ENSP00000309415.4; NM_007097.5; NP_009028.1.
DR UCSC; uc003meh.4; human. [P09497-1]
DR CTD; 1212; -.
DR DisGeNET; 1212; -.
DR GeneCards; CLTB; -.
DR HGNC; HGNC:2091; CLTB.
DR HPA; ENSG00000175416; Low tissue specificity.
DR MIM; 118970; gene.
DR neXtProt; NX_P09497; -.
DR OpenTargets; ENSG00000175416; -.
DR PharmGKB; PA26617; -.
DR VEuPathDB; HostDB:ENSG00000175416; -.
DR eggNOG; KOG4031; Eukaryota.
DR GeneTree; ENSGT00940000160186; -.
DR HOGENOM; CLU_091462_1_0_1; -.
DR InParanoid; P09497; -.
DR OMA; QWETICK; -.
DR OrthoDB; 1577821at2759; -.
DR PhylomeDB; P09497; -.
DR TreeFam; TF313162; -.
DR PathwayCommons; P09497; -.
DR Reactome; R-HSA-190873; Gap junction degradation.
DR Reactome; R-HSA-196025; Formation of annular gap junctions.
DR Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-HSA-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-HSA-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; P09497; -.
DR SIGNOR; P09497; -.
DR BioGRID-ORCS; 1212; 21 hits in 1086 CRISPR screens.
DR ChiTaRS; CLTB; human.
DR GenomeRNAi; 1212; -.
DR Pharos; P09497; Tbio.
DR PRO; PR:P09497; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P09497; protein.
DR Bgee; ENSG00000175416; Expressed in lower esophagus mucosa and 203 other tissues.
DR ExpressionAtlas; P09497; baseline and differential.
DR Genevisible; P09497; HS.
DR GO; GO:0060170; C:ciliary membrane; IEA:Ensembl.
DR GO; GO:0030118; C:clathrin coat; ISS:UniProtKB.
DR GO; GO:0030132; C:clathrin coat of coated pit; IEA:InterPro.
DR GO; GO:0030130; C:clathrin coat of trans-Golgi network vesicle; IEA:InterPro.
DR GO; GO:0030125; C:clathrin vesicle coat; IBA:GO_Central.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; NAS:ARUK-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0099631; C:postsynaptic endocytic zone cytoplasmic component; IBA:GO_Central.
DR GO; GO:0098835; C:presynaptic endocytic zone membrane; IEA:Ensembl.
DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR GO; GO:0032050; F:clathrin heavy chain binding; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IEA:Ensembl.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR InterPro; IPR000996; Clathrin_L-chain.
DR PANTHER; PTHR10639; PTHR10639; 1.
DR Pfam; PF01086; Clathrin_lg_ch; 1.
DR PROSITE; PS00224; CLATHRIN_LIGHT_CHN_1; 1.
DR PROSITE; PS00581; CLATHRIN_LIGHT_CHN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Calcium; Coated pit;
KW Cytoplasmic vesicle; Disulfide bond; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..229
FT /note="Clathrin light chain B"
FT /id="PRO_0000205771"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..155
FT /note="Involved in binding clathrin heavy chain"
FT COMPBIAS 63..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04975"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04975"
FT MOD_RES 187
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 204
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6IRU5"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09496"
FT DISULFID 199..209
FT /evidence="ECO:0000250"
FT VAR_SEQ 156..173
FT /note="Missing (in isoform Non-brain)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2,
FT ECO:0000303|Ref.3"
FT /id="VSP_001098"
FT CONFLICT 5
FT /note="F -> I (in Ref. 3; CAG38814)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 229 AA; 25190 MW; 07DBA19D44648F6F CRC64;
MADDFGFFSS SESGAPEAAE EDPAAAFLAQ QESEIAGIEN DEGFGAPAGS HAAPAQPGPT
SGAGSEDMGT TVNGDVFQEA NGPADGYAAI AQADRLTQEP ESIRKWREEQ RKRLQELDAA
SKVTEQEWRE KAKKDLEEWN QRQSEQVEKN KINNRIADKA FYQQPDADII GYVASEEAFV
KESKEETPGT EWEKVAQLCD FNPKSSKQCK DVSRLRSVLM SLKQTPLSR
