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Q9Y5P4

- C43BP_HUMAN

UniProt

Q9Y5P4 - C43BP_HUMAN

Protein

Collagen type IV alpha-3-binding protein

Gene

COL4A3BP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Shelters ceramides and diacylglycerol lipids inside its START domain and mediates the intracellular trafficking of ceramides and diacylglycerol lipids in a non-vesicular manner.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei472 – 4721Ceramide
    Binding sitei493 – 4931Ceramide
    Binding sitei530 – 5301Ceramide
    Binding sitei579 – 5791Ceramide

    GO - Molecular functioni

    1. ceramide binding Source: UniProtKB
    2. ceramide transporter activity Source: UniProtKB
    3. phosphatidylinositol-4-phosphate binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein kinase activity Source: ProtInc

    GO - Biological processi

    1. cell morphogenesis Source: Ensembl
    2. cell proliferation Source: Ensembl
    3. ceramide metabolic process Source: Ensembl
    4. endoplasmic reticulum organization Source: Ensembl
    5. ER to Golgi ceramide transport Source: UniProtKB
    6. heart morphogenesis Source: Ensembl
    7. immune response Source: UniProtKB
    8. in utero embryonic development Source: Ensembl
    9. lipid homeostasis Source: Ensembl
    10. mitochondrion morphogenesis Source: Ensembl
    11. muscle contraction Source: Ensembl
    12. protein phosphorylation Source: ProtInc
    13. response to endoplasmic reticulum stress Source: Ensembl
    14. signal transduction Source: Ensembl
    15. small molecule metabolic process Source: Reactome
    16. sphingolipid biosynthetic process Source: Reactome
    17. sphingolipid metabolic process Source: Reactome

    Keywords - Biological processi

    Lipid transport, Transport

    Keywords - Ligandi

    Lipid-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.9. 2681.
    ReactomeiREACT_115810. Sphingolipid de novo biosynthesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen type IV alpha-3-binding protein
    Alternative name(s):
    Ceramide transfer protein
    Short name:
    hCERT
    Goodpasture antigen-binding protein
    Short name:
    GPBP
    START domain-containing protein 11
    Short name:
    StARD11
    StAR-related lipid transfer protein 11
    Gene namesi
    Name:COL4A3BP
    Synonyms:CERT, STARD11
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:2205. COL4A3BP.

    Subcellular locationi

    Cytoplasm. Golgi apparatus. Endoplasmic reticulum
    Note: Preferentially localized to the Golgi apparatus.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. endoplasmic reticulum membrane Source: Reactome
    3. Golgi apparatus Source: UniProtKB
    4. mitochondrion Source: Ensembl
    5. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Golgi apparatus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi132 – 1321S → A: Abolishes the phosphorylation. Strongly reduces the interaction with phosphatidylinositol 4-phosphate. Increases the ceramide transfer activity. 1 Publication
    Mutagenesisi324 – 3241D → A: Impairs the endoplasmic reticulum-to-Golgi ceramide trafficking and abolishes the interaction with VAPA. 1 Publication
    Mutagenesisi472 – 4721E → A: Reduces ceramide transfer. 1 Publication
    Mutagenesisi493 – 4931Q → A: No effect on ceramide transfer activity. 1 Publication
    Mutagenesisi499 – 4991W → A: Reduces affinity for membranes. Abolishes ceramide transfer; when associated with A-588. 1 Publication
    Mutagenesisi530 – 5301N → A: Reduces ceramide transfer. 1 Publication
    Mutagenesisi588 – 5881W → A: Abolishes ceramide transfer; when associated with A-499.

    Organism-specific databases

    PharmGKBiPA26720.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 624624Collagen type IV alpha-3-binding proteinPRO_0000220665Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei132 – 1321Phosphoserine; by PKD2 Publications
    Modified residuei315 – 3151Phosphoserine2 Publications
    Modified residuei377 – 3771Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylation on Ser-132 decreases the affinity toward phosphatidylinositol 4-phosphate at Golgi membranes and reduces ceramide transfer activity. Inactivated by hyperphosphorylation of serine residues by CSNK1G2/CK1 that triggers dissociation from the Golgi complex, thus down-regulating ER-to-Golgi transport of ceramide and sphingomyelin synthesis.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y5P4.
    PaxDbiQ9Y5P4.
    PRIDEiQ9Y5P4.

    PTM databases

    PhosphoSiteiQ9Y5P4.

    Expressioni

    Tissue specificityi

    Widely expressed.

    Gene expression databases

    ArrayExpressiQ9Y5P4.
    BgeeiQ9Y5P4.
    CleanExiHS_COL4A3BP.
    GenevestigatoriQ9Y5P4.

    Organism-specific databases

    HPAiHPA035645.

    Interactioni

    Subunit structurei

    Interacts with COL4A3. Interacts with VAPA and VAPB. Interaction with VAPB is less efficient than with VAPA.1 Publication

    Protein-protein interaction databases

    BioGridi115396. 15 interactions.
    IntActiQ9Y5P4. 13 interactions.
    MINTiMINT-1441568.
    STRINGi9606.ENSP00000369862.

    Structurei

    Secondary structure

    1
    624
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi26 – 338
    Turni36 – 383
    Beta strandi40 – 489
    Beta strandi51 – 566
    Beta strandi58 – 625
    Beta strandi64 – 718
    Beta strandi75 – 784
    Beta strandi85 – 906
    Beta strandi93 – 986
    Helixi102 – 11918
    Helixi397 – 40711
    Beta strandi413 – 4153
    Beta strandi418 – 4247
    Beta strandi427 – 4326
    Beta strandi444 – 4518
    Helixi455 – 4639
    Helixi465 – 4673
    Helixi468 – 4714
    Beta strandi474 – 48512
    Beta strandi488 – 4958
    Beta strandi499 – 5024
    Beta strandi504 – 51512
    Beta strandi518 – 5225
    Beta strandi525 – 5328
    Beta strandi542 – 5465
    Beta strandi548 – 55912
    Beta strandi563 – 5653
    Helixi570 – 5723
    Beta strandi573 – 58412
    Helixi591 – 61727
    Beta strandi618 – 6203

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2E3MX-ray2.20A347-624[»]
    2E3NX-ray1.40A347-624[»]
    2E3OX-ray1.55A347-624[»]
    2E3PX-ray1.40A/B347-624[»]
    2E3QX-ray2.08A347-624[»]
    2E3RX-ray1.65A/B347-624[»]
    2E3SX-ray1.94A347-624[»]
    2RSGNMR-A24-117[»]
    2Z9YX-ray1.80A347-624[»]
    2Z9ZX-ray1.74A347-624[»]
    3H3QX-ray2.00A/B347-624[»]
    3H3RX-ray1.85A/B347-624[»]
    3H3SX-ray1.66A/B347-624[»]
    3H3TX-ray2.40A/B347-624[»]
    4HHVX-ray1.75A/B20-121[»]
    ProteinModelPortaliQ9Y5P4.
    SMRiQ9Y5P4. Positions 20-121, 391-624.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y5P4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini23 – 11795PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini389 – 618230STARTPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili263 – 30341Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi321 – 3277FFAT

    Domaini

    The START domain recognizes ceramides and diacylglycerol lipids, interacts with membranes, and mediates the intermembrane transfer of ceramides and diacylglycerol lipids.1 Publication
    The PH domain targets the Golgi apparatus.1 Publication
    The FFAT motif is required for interaction with VAPA and VAPB.1 Publication

    Sequence similaritiesi

    Contains 1 PH domain.PROSITE-ProRule annotation
    Contains 1 START domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG238964.
    HOVERGENiHBG050753.
    InParanoidiQ9Y5P4.
    KOiK08283.
    OMAiWPTSMPS.
    OrthoDBiEOG7G7KNJ.
    PhylomeDBiQ9Y5P4.
    TreeFamiTF106160.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    3.30.530.20. 1 hit.
    InterProiIPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR023393. START-like_dom.
    IPR002913. START_lipid-bd_dom.
    [Graphical view]
    PfamiPF00169. PH. 1 hit.
    PF01852. START. 1 hit.
    [Graphical view]
    SMARTiSM00233. PH. 1 hit.
    SM00234. START. 1 hit.
    [Graphical view]
    PROSITEiPS50003. PH_DOMAIN. 1 hit.
    PS50848. START. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y5P4-1) [UniParc]FASTAAdd to Basket

    Also known as: CERTL

    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

    MSDNQSWNSS GSEEDPETES GPPVERCGVL SKWTNYIHGW QDRWVVLKNN    50
    ALSYYKSEDE TEYGCRGSIC LSKAVITPHD FDECRFDISV NDSVWYLRAQ 100
    DPDHRQQWID AIEQHKTESG YGSESSLRRH GSMVSLVSGA SGYSATSTSS 150
    FKKGHSLREK LAEMETFRDI LCRQVDTLQK YFDACADAVS KDELQRDKVV 200
    EDDEDDFPTT RSDGDFLHST NGNKEKLFPH VTPKGINGID FKGEAITFKA 250
    TTAGILATLS HCIELMVKRE DSWQKRLDKE TEKKRRTEEA YKNAMTELKK 300
    KSHFGGPDYE EGPNSLINEE EFFDAVEAAL DRQDKIEEQS QSEKVRLHWP 350
    TSLPSGDAFS SVGTHRFVQK PYSRSSSMSS IDLVSASDDV HRFSSQVEEM 400
    VQNHMTYSLQ DVGGDANWQL VVEEGEMKVY RREVEENGIV LDPLKATHAV 450
    KGVTGHEVCN YFWNVDVRND WETTIENFHV VETLADNAII IYQTHKRVWP 500
    ASQRDVLYLS VIRKIPALTE NDPETWIVCN FSVDHDSAPL NNRCVRAKIN 550
    VAMICQTLVS PPEGNQEISR DNILCKITYV ANVNPGGWAP ASVLRAVAKR 600
    EYPKFLKRFT SYVQEKTAGK PILF 624
    Length:624
    Mass (Da):70,835
    Last modified:November 1, 1999 - v1
    Checksum:iA125162492AC5A0E
    GO
    Isoform 2 (identifier: Q9Y5P4-2) [UniParc]FASTAAdd to Basket

    Also known as: Delta26, GPBPD26

    The sequence of this isoform differs from the canonical sequence as follows:
         371-396: Missing.

    Show »
    Length:598
    Mass (Da):68,007
    Checksum:iFC52E241DE7C5D85
    GO
    Isoform 3 (identifier: Q9Y5P4-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MQHSCIPTPP...GLLLGCRASM

    Show »
    Length:752
    Mass (Da):83,708
    Checksum:i277A14A581D94EDF
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti138 – 1381S → C Found in a patient with mental retardation. 1 Publication
    VAR_069403
    Natural varianti599 – 5991K → R.
    Corresponds to variant rs55882089 [ dbSNP | Ensembl ].
    VAR_061815

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MQHSCIPTPPSPFSAPPAFL PVVTRESRRGLSSGGSAGRN AGVTATAAAADGWKGRLPSP LVLLPRSARCQARRRRGGRT SSLLLLPPTPERALFASPSP DPSPRGLGASSGAAEGAGAG LLLGCRASM in isoform 3. 1 PublicationVSP_041022
    Alternative sequencei371 – 39626Missing in isoform 2. 4 PublicationsVSP_006276Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF136450 mRNA. Translation: AAD30288.1.
    AF232930 mRNA. Translation: AAG42046.1.
    AF232935 Genomic DNA. Translation: AAG42051.1.
    AY453385 mRNA. Translation: AAR26717.1.
    AY453386 mRNA. Translation: AAR26718.1.
    AK091851 mRNA. Translation: BAC03762.1.
    AK096854 mRNA. Translation: BAG53379.1.
    AK292087 mRNA. Translation: BAF84776.1.
    AC008897 Genomic DNA. No translation available.
    AC112183 Genomic DNA. No translation available.
    AC116341 Genomic DNA. No translation available.
    CH471084 Genomic DNA. Translation: EAW95757.1.
    CH471084 Genomic DNA. Translation: EAW95760.1.
    BC000102 mRNA. Translation: AAH00102.1.
    AB036934 Genomic DNA. Translation: BAB58974.1.
    AB036936 Genomic DNA. Translation: BAB58977.1.
    CCDSiCCDS4028.1. [Q9Y5P4-1]
    CCDS4029.1. [Q9Y5P4-2]
    CCDS47235.1. [Q9Y5P4-3]
    RefSeqiNP_001123577.1. NM_001130105.1. [Q9Y5P4-3]
    NP_005704.1. NM_005713.2. [Q9Y5P4-1]
    NP_112729.1. NM_031361.2. [Q9Y5P4-2]
    XP_006714576.1. XM_006714513.1. [Q9Y5P4-1]
    UniGeneiHs.270437.

    Genome annotation databases

    EnsembliENST00000261415; ENSP00000261415; ENSG00000113163. [Q9Y5P4-2]
    ENST00000380494; ENSP00000369862; ENSG00000113163. [Q9Y5P4-3]
    ENST00000405807; ENSP00000383996; ENSG00000113163. [Q9Y5P4-1]
    GeneIDi10087.
    KEGGihsa:10087.
    UCSCiuc003kds.3. human. [Q9Y5P4-2]
    uc003kdt.3. human. [Q9Y5P4-3]
    uc003kdu.2. human. [Q9Y5P4-1]

    Polymorphism databases

    DMDMi20978413.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF136450 mRNA. Translation: AAD30288.1 .
    AF232930 mRNA. Translation: AAG42046.1 .
    AF232935 Genomic DNA. Translation: AAG42051.1 .
    AY453385 mRNA. Translation: AAR26717.1 .
    AY453386 mRNA. Translation: AAR26718.1 .
    AK091851 mRNA. Translation: BAC03762.1 .
    AK096854 mRNA. Translation: BAG53379.1 .
    AK292087 mRNA. Translation: BAF84776.1 .
    AC008897 Genomic DNA. No translation available.
    AC112183 Genomic DNA. No translation available.
    AC116341 Genomic DNA. No translation available.
    CH471084 Genomic DNA. Translation: EAW95757.1 .
    CH471084 Genomic DNA. Translation: EAW95760.1 .
    BC000102 mRNA. Translation: AAH00102.1 .
    AB036934 Genomic DNA. Translation: BAB58974.1 .
    AB036936 Genomic DNA. Translation: BAB58977.1 .
    CCDSi CCDS4028.1. [Q9Y5P4-1 ]
    CCDS4029.1. [Q9Y5P4-2 ]
    CCDS47235.1. [Q9Y5P4-3 ]
    RefSeqi NP_001123577.1. NM_001130105.1. [Q9Y5P4-3 ]
    NP_005704.1. NM_005713.2. [Q9Y5P4-1 ]
    NP_112729.1. NM_031361.2. [Q9Y5P4-2 ]
    XP_006714576.1. XM_006714513.1. [Q9Y5P4-1 ]
    UniGenei Hs.270437.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2E3M X-ray 2.20 A 347-624 [» ]
    2E3N X-ray 1.40 A 347-624 [» ]
    2E3O X-ray 1.55 A 347-624 [» ]
    2E3P X-ray 1.40 A/B 347-624 [» ]
    2E3Q X-ray 2.08 A 347-624 [» ]
    2E3R X-ray 1.65 A/B 347-624 [» ]
    2E3S X-ray 1.94 A 347-624 [» ]
    2RSG NMR - A 24-117 [» ]
    2Z9Y X-ray 1.80 A 347-624 [» ]
    2Z9Z X-ray 1.74 A 347-624 [» ]
    3H3Q X-ray 2.00 A/B 347-624 [» ]
    3H3R X-ray 1.85 A/B 347-624 [» ]
    3H3S X-ray 1.66 A/B 347-624 [» ]
    3H3T X-ray 2.40 A/B 347-624 [» ]
    4HHV X-ray 1.75 A/B 20-121 [» ]
    ProteinModelPortali Q9Y5P4.
    SMRi Q9Y5P4. Positions 20-121, 391-624.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115396. 15 interactions.
    IntActi Q9Y5P4. 13 interactions.
    MINTi MINT-1441568.
    STRINGi 9606.ENSP00000369862.

    PTM databases

    PhosphoSitei Q9Y5P4.

    Polymorphism databases

    DMDMi 20978413.

    Proteomic databases

    MaxQBi Q9Y5P4.
    PaxDbi Q9Y5P4.
    PRIDEi Q9Y5P4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261415 ; ENSP00000261415 ; ENSG00000113163 . [Q9Y5P4-2 ]
    ENST00000380494 ; ENSP00000369862 ; ENSG00000113163 . [Q9Y5P4-3 ]
    ENST00000405807 ; ENSP00000383996 ; ENSG00000113163 . [Q9Y5P4-1 ]
    GeneIDi 10087.
    KEGGi hsa:10087.
    UCSCi uc003kds.3. human. [Q9Y5P4-2 ]
    uc003kdt.3. human. [Q9Y5P4-3 ]
    uc003kdu.2. human. [Q9Y5P4-1 ]

    Organism-specific databases

    CTDi 10087.
    GeneCardsi GC05M074664.
    HGNCi HGNC:2205. COL4A3BP.
    HPAi HPA035645.
    MIMi 604677. gene.
    neXtProti NX_Q9Y5P4.
    PharmGKBi PA26720.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG238964.
    HOVERGENi HBG050753.
    InParanoidi Q9Y5P4.
    KOi K08283.
    OMAi WPTSMPS.
    OrthoDBi EOG7G7KNJ.
    PhylomeDBi Q9Y5P4.
    TreeFami TF106160.

    Enzyme and pathway databases

    BRENDAi 2.7.11.9. 2681.
    Reactomei REACT_115810. Sphingolipid de novo biosynthesis.

    Miscellaneous databases

    EvolutionaryTracei Q9Y5P4.
    GeneWikii COL4A3BP.
    GenomeRNAii 10087.
    NextBioi 38145.
    PROi Q9Y5P4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y5P4.
    Bgeei Q9Y5P4.
    CleanExi HS_COL4A3BP.
    Genevestigatori Q9Y5P4.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    3.30.530.20. 1 hit.
    InterProi IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR023393. START-like_dom.
    IPR002913. START_lipid-bd_dom.
    [Graphical view ]
    Pfami PF00169. PH. 1 hit.
    PF01852. START. 1 hit.
    [Graphical view ]
    SMARTi SM00233. PH. 1 hit.
    SM00234. START. 1 hit.
    [Graphical view ]
    PROSITEi PS50003. PH_DOMAIN. 1 hit.
    PS50848. START. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of a novel type of serine/threonine kinase that specifically phosphorylates the human goodpasture antigen."
      Raya A., Revert F., Navarro S., Saus J.
      J. Biol. Chem. 274:12642-12649(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
    2. "Goodpasture antigen-binding protein, the kinase that phosphorylates the Goodpasture antigen, is an alternatively spliced variant implicated in autoimmune pathogenesis."
      Raya A., Revert-Ros F., Martinez-Martinez P., Navarro S., Rosello E., Vieites B., Granero F., Forteza J., Saus J.
      J. Biol. Chem. 275:40392-40399(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
    3. "Molecular machinery for non-vesicular trafficking of ceramide."
      Hanada K., Kumagai K., Yasuda S., Miura Y., Kawano M., Fukasawa M., Nishijima M.
      Nature 426:803-809(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, DOMAIN, SUBCELLULAR LOCATION.
    4. "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 2 AND 3).
      Tissue: Lung and Synovium.
    5. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(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 2).
      Tissue: Placenta.
    8. "Homo sapiens genomic sequence, containing DINB1 and GPBP gene."
      Ogi T., Yamamoto Y., Ohmori H.
      Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77.
    9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Efficient trafficking of ceramide from the endoplasmic reticulum to the Golgi apparatus requires a VAMP-associated protein-interacting FFAT motif of CERT."
      Kawano M., Kumagai K., Nishijima M., Hanada K.
      J. Biol. Chem. 281:30279-30288(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VAPA AND VAPB, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-324.
    11. "Regulation of secretory transport by protein kinase D-mediated phosphorylation of the ceramide transfer protein."
      Fugmann T., Hausser A., Schoeffler P., Schmid S., Pfizenmaier K., Olayioye M.A.
      J. Cell Biol. 178:15-22(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-132, FUNCTION, MUTAGENESIS OF SER-132.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Casein kinase I{gamma}2 down-regulates trafficking of ceramide in the synthesis of sphingomyelin."
      Tomishige N., Kumagai K., Kusuda J., Nishijima M., Hanada K.
      Mol. Biol. Cell 20:348-357(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CSNK1G2/CK1.
    14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Structural basis for specific lipid recognition by CERT responsible for nonvesicular trafficking of ceramide."
      Kudo N., Kumagai K., Tomishige N., Yamaji T., Wakatsuki S., Nishijima M., Hanada K., Kato R.
      Proc. Natl. Acad. Sci. U.S.A. 105:488-493(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 347-624 IN COMPLEXES WITH CERAMIDES AND DIACYLGLYCEROL, MUTAGENESIS OF GLU-472; GLN-493 AND ASN-530, FUNCTION, SUBCELLULAR LOCATION.
    17. "Crystal structures of the CERT START domain with inhibitors provide insights into the mechanism of ceramide transfer."
      Kudo N., Kumagai K., Matsubara R., Kobayashi S., Hanada K., Wakatsuki S., Kato R.
      J. Mol. Biol. 396:245-251(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 347-624 IN COMPLEXES WITH CERAMIDE AND INHIBITOR, MUTAGENESIS OF TRP-499, FUNCTION.
    18. Cited for: VARIANT CYS-138.

    Entry informationi

    Entry nameiC43BP_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y5P4
    Secondary accession number(s): A8K7S2
    , B3KUB7, Q53YV1, Q53YV2, Q96Q85, Q96Q88, Q9H2S7, Q9H2S8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 15, 2002
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 128 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

    Caution

    Was originally reported to have a protein kinase activity and to phosphorylate on Ser and Thr residues the Goodpasture autoantigen (in vitro).1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3