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P09496

- CLCA_HUMAN

UniProt

P09496 - CLCA_HUMAN

Protein

Clathrin light chain A

Gene

CLTA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    Functioni

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

    GO - Molecular functioni

    1. clathrin heavy chain binding Source: FlyBase
    2. peptide binding Source: Ensembl
    3. protein binding Source: IntAct
    4. structural molecule activity Source: InterPro

    GO - Biological processi

    1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
    2. axon guidance Source: Reactome
    3. endocytosis Source: Ensembl
    4. epidermal growth factor receptor signaling pathway Source: Reactome
    5. intracellular protein transport Source: InterPro
    6. membrane organization Source: Reactome
    7. negative regulation of epidermal growth factor receptor signaling pathway Source: Reactome
    8. neurotrophin TRK receptor signaling pathway Source: Reactome
    9. post-Golgi vesicle-mediated transport Source: Reactome

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_11035. Gap junction degradation.
    REACT_11049. Formation of annular gap junctions.
    REACT_121399. MHC class II antigen presentation.
    REACT_12435. Retrograde neurotrophin signalling.
    REACT_12484. EGFR downregulation.
    REACT_172599. WNT5A-dependent internalization of FZD4.
    REACT_19287. Lysosome Vesicle Biogenesis.
    REACT_19400. Golgi Associated Vesicle Biogenesis.
    REACT_22365. Recycling pathway of L1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Clathrin light chain A
    Short name:
    Lca
    Gene namesi
    Name:CLTA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:2090. CLTA.

    Subcellular locationi

    GO - Cellular componenti

    1. clathrin coat Source: UniProtKB
    2. clathrin-coated endocytic vesicle membrane Source: Reactome
    3. clathrin coat of coated pit Source: InterPro
    4. clathrin coat of trans-Golgi network vesicle Source: InterPro
    5. clathrin complex Source: FlyBase
    6. cytoplasmic membrane-bounded vesicle Source: BHF-UCL
    7. cytosol Source: Reactome
    8. intracellular membrane-bounded organelle Source: HPA
    9. membrane Source: UniProtKB
    10. plasma membrane Source: Reactome
    11. trans-Golgi network membrane Source: Reactome

    Keywords - Cellular componenti

    Coated pit, Cytoplasmic vesicle, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26616.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 248248Clathrin light chain APRO_0000205767Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei105 – 1051Phosphoserine1 Publication
    Modified residuei206 – 2061Phosphoserine2 Publications
    Modified residuei236 – 2361Phosphoserine1 Publication
    Modified residuei242 – 2421N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP09496.
    PaxDbiP09496.
    PRIDEiP09496.

    2D gel databases

    OGPiP09496.

    PTM databases

    PhosphoSiteiP09496.

    Miscellaneous databases

    PMAP-CutDBP09496.

    Expressioni

    Gene expression databases

    ArrayExpressiP09496.
    BgeeiP09496.
    CleanExiHS_CLTA.
    GenevestigatoriP09496.

    Organism-specific databases

    HPAiCAB002665.
    HPA050918.

    Interactioni

    Subunit structurei

    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.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TACC3Q9Y6A53EBI-1171169,EBI-2554984

    Protein-protein interaction databases

    BioGridi107621. 21 interactions.
    IntActiP09496. 21 interactions.
    MINTiMINT-1326541.
    STRINGi9606.ENSP00000242285.

    Structurei

    3D structure databases

    ProteinModelPortaliP09496.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni100 – 16263Involved in binding clathrin heavy chainAdd
    BLAST

    Sequence similaritiesi

    Belongs to the clathrin light chain family.Curated

    Phylogenomic databases

    eggNOGiNOG312397.
    HOGENOMiHOG000008147.
    HOVERGENiHBG003386.
    InParanoidiP09496.
    KOiK04644.
    OMAiMDDFDML.
    OrthoDBiEOG79KPH4.
    PhylomeDBiP09496.
    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 (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform Brain (identifier: P09496-1) [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

    MAELDPFGAP AGAPGGPALG NGVAGAGEED PAAAFLAQQE SEIAGIENDE    50
    AFAILDGGAP GPQPHGEPPG GPDAVDGVMN GEYYQESNGP TDSYAAISQV 100
    DRLQSEPESI RKWREEQMER LEALDANSRK QEAEWKEKAI KELEEWYARQ 150
    DEQLQKTKAN NRVADEAFYK QPFADVIGYV TNINHPCYSL EQAAEEAFVN 200
    DIDESSPGTE WERVARLCDF NPKSSKQAKD VSRMRSVLIS LKQAPLVH 248
    Length:248
    Mass (Da):27,077
    Last modified:July 1, 1989 - v1
    Checksum:i8D8A3B49E6353D93
    GO
    Isoform Non-brain (identifier: P09496-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         163-192: Missing.

    Show »
    Length:218
    Mass (Da):23,662
    Checksum:i05C5037569FB6E8D
    GO
    Isoform 3 (identifier: P09496-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         181-192: Missing.

    Show »
    Length:236
    Mass (Da):25,676
    Checksum:iDAD1A01F3FD51284
    GO
    Isoform 4 (identifier: P09496-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         162-180: RVADEAFYKQPFADVIGYV → S

    Note: No experimental confirmation available.

    Show »
    Length:230
    Mass (Da):24,993
    Checksum:iB9644FCE2C09A116
    GO
    Isoform 5 (identifier: P09496-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         73-124: Missing.
         163-192: Missing.

    Note: No experimental confirmation available. Gene prediction based on EST data.

    Show »
    Length:166
    Mass (Da):17,687
    Checksum:i1F8381B9C1F55136
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti207 – 2071P → Q in ABB76683. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei73 – 12452Missing in isoform 5. CuratedVSP_047168Add
    BLAST
    Alternative sequencei162 – 18019RVADE…VIGYV → S in isoform 4. 1 PublicationVSP_043239Add
    BLAST
    Alternative sequencei163 – 19230Missing in isoform Non-brain and isoform 5. 4 PublicationsVSP_001095Add
    BLAST
    Alternative sequencei181 – 19212Missing in isoform 3. 1 PublicationVSP_024238Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20471 mRNA. Translation: AAA51817.1.
    M20472 mRNA. Translation: AAA59505.1.
    DQ270158 mRNA. Translation: ABB76683.1.
    BT007170 mRNA. Translation: AAP35834.1.
    AK291078 mRNA. Translation: BAF83767.1.
    AK295692 mRNA. Translation: BAG58543.1.
    AL158830 Genomic DNA. Translation: CAD13387.1.
    AL158830 Genomic DNA. Translation: CAD13388.1.
    AL161792 Genomic DNA. No translation available.
    CH471071 Genomic DNA. Translation: EAW58312.1.
    BC009201 mRNA. Translation: AAH09201.1.
    BC019287 mRNA. Translation: AAH19287.1.
    CCDSiCCDS43802.1. [P09496-3]
    CCDS55306.1. [P09496-4]
    CCDS55307.1. [P09496-5]
    CCDS6600.1. [P09496-2]
    CCDS6601.1. [P09496-1]
    PIRiA31775.
    RefSeqiNP_001070145.1. NM_001076677.2. [P09496-3]
    NP_001171689.1. NM_001184760.1. [P09496-4]
    NP_001171691.1. NM_001184762.1. [P09496-5]
    NP_001824.1. NM_001833.3. [P09496-2]
    NP_009027.1. NM_007096.3. [P09496-1]
    UniGeneiHs.522114.

    Genome annotation databases

    EnsembliENST00000242285; ENSP00000242285; ENSG00000122705. [P09496-1]
    ENST00000345519; ENSP00000242284; ENSG00000122705. [P09496-2]
    ENST00000396603; ENSP00000379848; ENSG00000122705. [P09496-3]
    ENST00000433436; ENSP00000401019; ENSG00000122705. [P09496-1]
    ENST00000470744; ENSP00000419746; ENSG00000122705. [P09496-4]
    ENST00000538225; ENSP00000442869; ENSG00000122705. [P09496-4]
    ENST00000540080; ENSP00000437508; ENSG00000122705. [P09496-5]
    GeneIDi1211.
    KEGGihsa:1211.
    UCSCiuc003zzc.3. human. [P09496-1]
    uc003zzd.3. human. [P09496-3]
    uc003zze.3. human. [P09496-2]
    uc011lpk.2. human. [P09496-4]

    Polymorphism databases

    DMDMi116501.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20471 mRNA. Translation: AAA51817.1 .
    M20472 mRNA. Translation: AAA59505.1 .
    DQ270158 mRNA. Translation: ABB76683.1 .
    BT007170 mRNA. Translation: AAP35834.1 .
    AK291078 mRNA. Translation: BAF83767.1 .
    AK295692 mRNA. Translation: BAG58543.1 .
    AL158830 Genomic DNA. Translation: CAD13387.1 .
    AL158830 Genomic DNA. Translation: CAD13388.1 .
    AL161792 Genomic DNA. No translation available.
    CH471071 Genomic DNA. Translation: EAW58312.1 .
    BC009201 mRNA. Translation: AAH09201.1 .
    BC019287 mRNA. Translation: AAH19287.1 .
    CCDSi CCDS43802.1. [P09496-3 ]
    CCDS55306.1. [P09496-4 ]
    CCDS55307.1. [P09496-5 ]
    CCDS6600.1. [P09496-2 ]
    CCDS6601.1. [P09496-1 ]
    PIRi A31775.
    RefSeqi NP_001070145.1. NM_001076677.2. [P09496-3 ]
    NP_001171689.1. NM_001184760.1. [P09496-4 ]
    NP_001171691.1. NM_001184762.1. [P09496-5 ]
    NP_001824.1. NM_001833.3. [P09496-2 ]
    NP_009027.1. NM_007096.3. [P09496-1 ]
    UniGenei Hs.522114.

    3D structure databases

    ProteinModelPortali P09496.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107621. 21 interactions.
    IntActi P09496. 21 interactions.
    MINTi MINT-1326541.
    STRINGi 9606.ENSP00000242285.

    PTM databases

    PhosphoSitei P09496.

    Polymorphism databases

    DMDMi 116501.

    2D gel databases

    OGPi P09496.

    Proteomic databases

    MaxQBi P09496.
    PaxDbi P09496.
    PRIDEi P09496.

    Protocols and materials databases

    DNASUi 1211.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000242285 ; ENSP00000242285 ; ENSG00000122705 . [P09496-1 ]
    ENST00000345519 ; ENSP00000242284 ; ENSG00000122705 . [P09496-2 ]
    ENST00000396603 ; ENSP00000379848 ; ENSG00000122705 . [P09496-3 ]
    ENST00000433436 ; ENSP00000401019 ; ENSG00000122705 . [P09496-1 ]
    ENST00000470744 ; ENSP00000419746 ; ENSG00000122705 . [P09496-4 ]
    ENST00000538225 ; ENSP00000442869 ; ENSG00000122705 . [P09496-4 ]
    ENST00000540080 ; ENSP00000437508 ; ENSG00000122705 . [P09496-5 ]
    GeneIDi 1211.
    KEGGi hsa:1211.
    UCSCi uc003zzc.3. human. [P09496-1 ]
    uc003zzd.3. human. [P09496-3 ]
    uc003zze.3. human. [P09496-2 ]
    uc011lpk.2. human. [P09496-4 ]

    Organism-specific databases

    CTDi 1211.
    GeneCardsi GC09P036180.
    HGNCi HGNC:2090. CLTA.
    HPAi CAB002665.
    HPA050918.
    MIMi 118960. gene.
    neXtProti NX_P09496.
    PharmGKBi PA26616.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG312397.
    HOGENOMi HOG000008147.
    HOVERGENi HBG003386.
    InParanoidi P09496.
    KOi K04644.
    OMAi MDDFDML.
    OrthoDBi EOG79KPH4.
    PhylomeDBi P09496.
    TreeFami TF313162.

    Enzyme and pathway databases

    Reactomei REACT_11035. Gap junction degradation.
    REACT_11049. Formation of annular gap junctions.
    REACT_121399. MHC class II antigen presentation.
    REACT_12435. Retrograde neurotrophin signalling.
    REACT_12484. EGFR downregulation.
    REACT_172599. WNT5A-dependent internalization of FZD4.
    REACT_19287. Lysosome Vesicle Biogenesis.
    REACT_19400. Golgi Associated Vesicle Biogenesis.
    REACT_22365. Recycling pathway of L1.

    Miscellaneous databases

    ChiTaRSi CLTA. human.
    GenomeRNAii 1211.
    NextBioi 4985.
    PMAP-CutDB P09496.
    PROi P09496.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P09496.
    Bgeei P09496.
    CleanExi HS_CLTA.
    Genevestigatori P09496.

    Family and domain databases

    InterProi IPR000996. Clathrin_L-chain.
    [Graphical view ]
    PANTHERi PTHR10639. PTHR10639. 1 hit.
    Pfami PF01086. Clathrin_lg_ch. 1 hit.
    [Graphical view ]
    PROSITEi PS00224. CLATHRIN_LIGHT_CHN_1. 1 hit.
    PS00581. CLATHRIN_LIGHT_CHN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure of human clathrin light chains. Conservation of light chain polymorphism in three mammalian species."
      Jackson A.P., Parham P.
      J. Biol. Chem. 263:16688-16695(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BRAIN AND NON-BRAIN).
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      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.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM NON-BRAIN).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS NON-BRAIN AND 4).
      Tissue: Hippocampus.
    4. 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
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    5. "DNA sequence and analysis of human chromosome 9."
      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.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 NON-BRAIN).
      Tissue: Lung.
    8. "Calcyon, a novel partner of clathrin light chain, stimulates clathrin-mediated endocytosis."
      Xiao J., Dai R., Negyessy L., Bergson C.
      J. Biol. Chem. 281:15182-15193(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CALY.
    9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206 AND SER-236, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      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.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105 AND SER-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCLCA_HUMAN
    AccessioniPrimary (citable) accession number: P09496
    Secondary accession number(s): A8K4W3
    , B4DIN1, F5H6N3, Q2XPN5, Q53XZ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 142 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3