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Protein

Clathrin light chain B

Gene

Cltb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiR-MMU-190873. Gap junction degradation.
R-MMU-196025. Formation of annular gap junctions.
R-MMU-432720. Lysosome Vesicle Biogenesis.
R-MMU-5099900. WNT5A-dependent internalization of FZD4.

Names & Taxonomyi

Protein namesi
Recommended name:
Clathrin light chain B
Short name:
Lcb
Gene namesi
Name:Cltb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1921575. Cltb.

Subcellular locationi

GO - Cellular componenti

  • ciliary membrane Source: MGI
  • clathrin coat Source: UniProtKB
  • clathrin coat of coated pit Source: InterPro
  • clathrin coat of trans-Golgi network vesicle Source: InterPro
  • clathrin vesicle coat Source: GO_Central
  • cytoplasm Source: MGI
  • intracellular membrane-bounded organelle Source: MGI
  • plasma membrane Source: MGI
  • trans-Golgi network Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Coated pit, Cytoplasmic vesicle, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 229229Clathrin light chain BPRO_0000205772Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei11 – 111PhosphoserineBy similarity
Modified residuei13 – 131PhosphoserineBy similarity
Modified residuei187 – 1871PhosphothreonineBy similarity
Disulfide bondi199 ↔ 209By similarity
Modified residuei204 – 2041N6-acetyllysineCombined sources
Modified residuei217 – 2171PhosphoserineBy similarity
Modified residuei223 – 2231N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

EPDiQ6IRU5.
MaxQBiQ6IRU5.
PeptideAtlasiQ6IRU5.
PRIDEiQ6IRU5.

2D gel databases

REPRODUCTION-2DPAGEQ6IRU5.

PTM databases

iPTMnetiQ6IRU5.
PhosphoSiteiQ6IRU5.

Expressioni

Gene expression databases

BgeeiQ6IRU5.
CleanExiMM_CLTB.
ExpressionAtlasiQ6IRU5. baseline and differential.
GenevisibleiQ6IRU5. MM.

Interactioni

Subunit structurei

Clathrin coats are formed from molecules containing 3 heavy chains and 3 light chains. Interacts (via N-terminus) with HIP1. Interacts with HIP1R.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi216666. 1 interaction.
IntActiQ6IRU5. 2 interactions.
MINTiMINT-4997457.

Structurei

3D structure databases

ProteinModelPortaliQ6IRU5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni93 – 15563Involved in binding clathrin heavy chainAdd
BLAST

Sequence similaritiesi

Belongs to the clathrin light chain family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000010441.
HOGENOMiHOG000008147.
HOVERGENiHBG003386.
InParanoidiQ6IRU5.
KOiK04645.
OMAiQNPIQLQ.
OrthoDBiEOG79KPH4.
PhylomeDBiQ6IRU5.
TreeFamiTF313162.

Family and domain databases

InterProiIPR000996. Clathrin_L-chain.
[Graphical view]
PANTHERiPTHR10639. PTHR10639. 1 hit.
PfamiPF01086. Clathrin_lg_ch. 1 hit.
[Graphical view]
PROSITEiPS00224. CLATHRIN_LIGHT_CHN_1. 1 hit.
PS00581. CLATHRIN_LIGHT_CHN_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6IRU5-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAEDFGFFSS SESGAPEAAE EDPAAAFLAQ QESEIAGIEN DPGFGAPAAS
60 70 80 90 100
QVASAQPGLA SGAGSEDMST TVNGDVFQEA NGPADGYAAI AQADRLTQEP
110 120 130 140 150
ESIRKWREEQ KKRLQELDAA SKVTEQEWRE KAKKDLEEWN QRQSEQVEKN
160 170 180 190 200
KINNRIADKA FYQQPDADTI GYVASEEAFV KESKEETPGT EWEKVAQLCD
210 220
FNPKSSKQCK DVSRLRSVLM SLKQTPLSR
Length:229
Mass (Da):25,172
Last modified:July 5, 2004 - v1
Checksum:i62C87F71DB9F782A
GO
Isoform 2 (identifier: Q6IRU5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     156-173: Missing.

Note: No experimental confirmation available.
Show »
Length:211
Mass (Da):23,174
Checksum:iDE25CC6106552C14
GO
Isoform 3 (identifier: Q6IRU5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     156-229: Missing.

Note: No experimental confirmation available.
Show »
Length:155
Mass (Da):16,834
Checksum:i7A5CBD04ECF17B68
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei156 – 22974Missing in isoform 3. 1 PublicationVSP_013383Add
BLAST
Alternative sequencei156 – 17318Missing in isoform 2. 1 PublicationVSP_013382Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009844 mRNA. Translation: BAB26539.1.
AK029382 mRNA. Translation: BAC26430.1.
AK045989 mRNA. Translation: BAC32563.1.
BC070404 mRNA. Translation: AAH70404.1.
CCDSiCCDS26533.1. [Q6IRU5-2]
RefSeqiNP_083146.1. NM_028870.3. [Q6IRU5-2]
XP_006517481.1. XM_006517418.2. [Q6IRU5-1]
UniGeneiMm.290026.

Genome annotation databases

EnsembliENSMUST00000049575; ENSMUSP00000053371; ENSMUSG00000047547. [Q6IRU5-1]
ENSMUST00000091609; ENSMUSP00000089198; ENSMUSG00000047547. [Q6IRU5-2]
GeneIDi74325.
KEGGimmu:74325.
UCSCiuc007qon.1. mouse. [Q6IRU5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009844 mRNA. Translation: BAB26539.1.
AK029382 mRNA. Translation: BAC26430.1.
AK045989 mRNA. Translation: BAC32563.1.
BC070404 mRNA. Translation: AAH70404.1.
CCDSiCCDS26533.1. [Q6IRU5-2]
RefSeqiNP_083146.1. NM_028870.3. [Q6IRU5-2]
XP_006517481.1. XM_006517418.2. [Q6IRU5-1]
UniGeneiMm.290026.

3D structure databases

ProteinModelPortaliQ6IRU5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi216666. 1 interaction.
IntActiQ6IRU5. 2 interactions.
MINTiMINT-4997457.

PTM databases

iPTMnetiQ6IRU5.
PhosphoSiteiQ6IRU5.

2D gel databases

REPRODUCTION-2DPAGEQ6IRU5.

Proteomic databases

EPDiQ6IRU5.
MaxQBiQ6IRU5.
PeptideAtlasiQ6IRU5.
PRIDEiQ6IRU5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000049575; ENSMUSP00000053371; ENSMUSG00000047547. [Q6IRU5-1]
ENSMUST00000091609; ENSMUSP00000089198; ENSMUSG00000047547. [Q6IRU5-2]
GeneIDi74325.
KEGGimmu:74325.
UCSCiuc007qon.1. mouse. [Q6IRU5-1]

Organism-specific databases

CTDi1212.
MGIiMGI:1921575. Cltb.

Phylogenomic databases

GeneTreeiENSGT00390000010441.
HOGENOMiHOG000008147.
HOVERGENiHBG003386.
InParanoidiQ6IRU5.
KOiK04645.
OMAiQNPIQLQ.
OrthoDBiEOG79KPH4.
PhylomeDBiQ6IRU5.
TreeFamiTF313162.

Enzyme and pathway databases

ReactomeiR-MMU-190873. Gap junction degradation.
R-MMU-196025. Formation of annular gap junctions.
R-MMU-432720. Lysosome Vesicle Biogenesis.
R-MMU-5099900. WNT5A-dependent internalization of FZD4.

Miscellaneous databases

ChiTaRSiCltb. mouse.
PROiQ6IRU5.
SOURCEiSearch...

Gene expression databases

BgeeiQ6IRU5.
CleanExiMM_CLTB.
ExpressionAtlasiQ6IRU5. baseline and differential.
GenevisibleiQ6IRU5. MM.

Family and domain databases

InterProiIPR000996. Clathrin_L-chain.
[Graphical view]
PANTHERiPTHR10639. PTHR10639. 1 hit.
PfamiPF01086. Clathrin_lg_ch. 1 hit.
[Graphical view]
PROSITEiPS00224. CLATHRIN_LIGHT_CHN_1. 1 hit.
PS00581. CLATHRIN_LIGHT_CHN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Strain: C57BL/6J.
    Tissue: Corpora quadrigemina, Head and Tongue.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Brain.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Lung and Pancreas.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-204, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiCLCB_MOUSE
AccessioniPrimary (citable) accession number: Q6IRU5
Secondary accession number(s): Q8BR04, Q8CDX9, Q9CV35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: July 5, 2004
Last modified: July 6, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.