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Q9NZU7

- CABP1_HUMAN

UniProt

Q9NZU7 - CABP1_HUMAN

Protein

Calcium-binding protein 1

Gene

CABP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 5 (31 May 2011)
      Previous versions | rss
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    Functioni

    Modulates calcium-dependent activity of inositol 1,4,5-triphosphate receptors (ITPRs). Inhibits agonist-induced intracellular calcium signaling. Enhances inactivation and does not support calcium-dependent facilitation of voltage-dependent P/Q-type calcium channels. Causes calcium-dependent facilitation and inhibits inactivation of L-type calcium channels by binding to the same sites as calmodulin in the C-terminal domain of CACNA1C, but resulting in an opposit effects on channel function. Suppresses the calcium-dependent inactivation of CACNA1D By similarity. Inhibits TRPC5 channels. Prevents NMDA receptor-induced cellular degeneration By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi238 – 2381Magnesium1 Publication
    Metal bindingi240 – 2401Magnesium1 Publication
    Metal bindingi242 – 2421Magnesium1 Publication
    Metal bindingi244 – 2441Magnesium; via carbonyl oxygen1 Publication
    Metal bindingi315 – 3151Calcium 11 Publication
    Metal bindingi317 – 3171Calcium 11 Publication
    Metal bindingi319 – 3191Calcium 11 Publication
    Metal bindingi321 – 3211Calcium 1; via carbonyl oxygen1 Publication
    Metal bindingi326 – 3261Calcium 11 Publication
    Metal bindingi352 – 3521Calcium 21 Publication
    Metal bindingi353 – 3531Calcium 2; via amide nitrogen1 Publication
    Metal bindingi354 – 3541Calcium 21 Publication
    Metal bindingi356 – 3561Calcium 21 Publication
    Metal bindingi357 – 3571Calcium 2; via amide nitrogen1 Publication
    Metal bindingi358 – 3581Calcium 2; via carbonyl oxygen1 Publication
    Metal bindingi360 – 3601Calcium 21 Publication
    Metal bindingi363 – 3631Calcium 21 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi238 – 249121Add
    BLAST
    Calcium bindingi315 – 326122Add
    BLAST
    Calcium bindingi352 – 363123Add
    BLAST

    GO - Molecular functioni

    1. calcium-dependent protein binding Source: UniProtKB
    2. calcium ion binding Source: ProtInc
    3. enzyme inhibitor activity Source: ProtInc
    4. nuclear localization sequence binding Source: UniProtKB
    5. protein binding Source: UniProtKB

    GO - Biological processi

    1. negative regulation of catalytic activity Source: GOC
    2. negative regulation of cell communication by electrical coupling Source: Ensembl
    3. negative regulation of protein import into nucleus Source: UniProtKB
    4. negative regulation of voltage-gated calcium channel activity Source: Ensembl

    Keywords - Ligandi

    Calcium, Magnesium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calcium-binding protein 1
    Short name:
    CaBP1
    Alternative name(s):
    Calbrain
    Caldendrin
    Gene namesi
    Name:CABP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:1384. CABP1.

    Subcellular locationi

    Cytoplasmcytoskeleton. Cytoplasmperinuclear region. Cell membrane; Lipid-anchor; Cytoplasmic side. Golgi apparatus. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density
    Note: L-CaBP1 is associated most likely with the cytoskeletal structures, whereas S-CaBP1 is localized at or near the plasma membrane.
    Isoform L-CaBP1 : Cytoplasmcytoskeleton
    Note: L-CaBP1 is associated most likely with the cytoskeletal structures.
    Isoform S-CaBP1 : Cytoplasmcell cortex. Cell membrane Curated; Lipid-anchor Curated
    Note: S-CaBP1 is localized at or near the plasma membrane.

    GO - Cellular componenti

    1. cell cortex Source: UniProtKB-SubCell
    2. cell junction Source: UniProtKB-KW
    3. cytoplasmic side of plasma membrane Source: Ensembl
    4. cytosol Source: Ensembl
    5. dendrite Source: Ensembl
    6. extracellular space Source: UniProt
    7. Golgi membrane Source: MGI
    8. neuronal cell body Source: Ensembl
    9. nucleus Source: Ensembl
    10. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    11. plasma membrane Source: MGI
    12. postsynaptic density Source: UniProtKB
    13. postsynaptic membrane Source: UniProtKB-KW
    14. protein complex Source: Ensembl

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane, Postsynaptic cell membrane, Synapse

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi238 – 2381D → A: Loss of magnesium-binding. Loss of binding to ITPRs; when associated with A-240; A-315; A-317; A-352 and A-354. 2 Publications
    Mutagenesisi240 – 2401D → A: Loss of magnesium-binding. Loss of binding to ITPRs; when associated with A-238; A-315; A-317; A-352 and A-354. 2 Publications
    Mutagenesisi242 – 2421D → A: Loss of magnesium-binding. 1 Publication
    Mutagenesisi249 – 2491D → A: No effect on magnesium-binding. 1 Publication
    Mutagenesisi315 – 3151D → A: Loss of binding to ITPRs; when associated with A-238; A-240; A-317; A-352 and A-354. 1 Publication
    Mutagenesisi317 – 3171N → A: Loss of binding to ITPRs; when associated with A-238; A-240; A-315; A-352 and A-354. 1 Publication
    Mutagenesisi323 – 3231S → A: Loss of phosphorylation and loss of calcium release by InsP(3). 1 Publication
    Mutagenesisi352 – 3521D → A: Loss of binding to ITPRs; when associated with A-238; A-240; A-315; A-317 and A-354. 1 Publication
    Mutagenesisi354 – 3541N → A: Loss of binding to ITPRs; when associated with A-238; A-240; A-315; A-317 and A-352. 1 Publication

    Organism-specific databases

    PharmGKBiPA26000.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedSequence Analysis
    Chaini2 – 370369Calcium-binding protein 1PRO_0000073513Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineSequence Analysis
    Modified residuei323 – 3231Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated. The phosphorylation regulates the activity.1 Publication

    Keywords - PTMi

    Lipoprotein, Myristate, Phosphoprotein

    Proteomic databases

    PaxDbiQ9NZU7.
    PRIDEiQ9NZU7.

    PTM databases

    PhosphoSiteiQ9NZU7.

    Expressioni

    Tissue specificityi

    Retina and brain. Somatodendritic compartment of neurons. Calbrain was found exclusively in brain where it is abundant in the hippocampus, habenular area in the epithalamus and in the cerebellum.

    Gene expression databases

    ArrayExpressiQ9NZU7.
    BgeeiQ9NZU7.
    CleanExiHS_CABP1.
    GenevestigatoriQ9NZU7.

    Organism-specific databases

    HPAiHPA051438.

    Interactioni

    Subunit structurei

    Homodimer; when bound to calcium or magnesium. Interacts (via C-terminus) with ITPR1, ITPR2 and ITPR3. This binding is calcium dependent and the interaction correlates with calcium concentration. An additional calcium-independent interaction with the N-terminus of ITPR1 results in a decreased InsP3 binding to the receptor. Interacts with CACNA1A (via C-terminal CDB motif) in the pre- and postsynaptic membranes. Interacts with CACNA1C (via C-terminal C and IQ motifs). The binding to the C motif is calcium independent whereas the binding to IQ requires the presence of calcium and is mutually exclusive with calmodulin binding. Interacts with CACNA1D By similarity. Interacts with TRPC5 (via C-terminus). Interacts (via EF-hands 1 and 2) at microtubules with MAP1LC3B. Interacts with MYO1C By similarity. Interacts (via EF-hands 1 and 2) with NSMF (via the central NLS-containing motif region), the interaction occurs in a calcium dependent manner after synaptic NMDA receptor stimulation and prevents nuclear import of NSMF By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CACNA1CQ139364EBI-907894,EBI-1038838

    Protein-protein interaction databases

    BioGridi114863. 8 interactions.
    DIPiDIP-35477N.
    IntActiQ9NZU7. 4 interactions.
    STRINGi9606.ENSP00000317310.

    Structurei

    Secondary structure

    1
    370
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi224 – 24017
    Beta strandi242 – 2443
    Helixi247 – 25610
    Helixi263 – 27412
    Beta strandi277 – 2793
    Helixi283 – 29412
    Helixi299 – 3024
    Helixi304 – 31411
    Beta strandi319 – 3224
    Helixi324 – 33512
    Beta strandi337 – 3393
    Helixi341 – 35111
    Beta strandi353 – 3597
    Helixi361 – 3677

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2K7BNMR-A219-294[»]
    2K7CNMR-A299-370[»]
    2K7DNMR-A299-370[»]
    2LANNMR-A219-370[»]
    2LAPNMR-A219-370[»]
    3OX5X-ray2.90A/B/C/D/E/F219-370[»]
    3OX6X-ray2.40A/B/C/D/E/F219-370[»]
    ProteinModelPortaliQ9NZU7.
    SMRiQ9NZU7. Positions 219-370.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NZU7.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini225 – 26036EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini261 – 29636EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini302 – 33736EF-hand 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini339 – 37032EF-hand 4PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi45 – 484Poly-Pro
    Compositional biasi74 – 796Poly-Ala
    Compositional biasi86 – 16479Pro-richAdd
    BLAST

    Domaini

    EF-1 binds magnesium constitutively under physiological conditions, EF-3 and EF-4 bind calcium cooperatively and EF-2 binds neither calcium nor magnesium.

    Sequence similaritiesi

    Contains 4 EF-hand domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5126.
    HOGENOMiHOG000233018.
    HOVERGENiHBG012180.
    OrthoDBiEOG7XM303.
    PhylomeDBiQ9NZU7.
    TreeFamiTF334804.

    Family and domain databases

    Gene3Di1.10.238.10. 2 hits.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    [Graphical view]
    PfamiPF00036. EF-hand_1. 3 hits.
    [Graphical view]
    SMARTiSM00054. EFh. 3 hits.
    [Graphical view]
    PROSITEiPS00018. EF_HAND_1. 3 hits.
    PS50222. EF_HAND_2. 4 hits.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Note: Experimental confirmation may be lacking for some isoforms.

    Isoform Caldendrin (identifier: Q9NZU7-4) [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

    MGGGDGAAFK RPGDGARLQR VLGLGSRREP RSLPAGGPAP RRTAPPPPGH    50
    ASAGPAAMSS HIAKSESKTS LLKAAAAAAS GGSRAPRHGP ARDPGLPSRR 100
    LPGSCPATPQ SSGDPSSRRP LCRPAPREEG ARGSQRVLPQ AHCRPREALP 150
    AAASRPSPSS PLPPARGRDG EERGLSPALG LRGSLRARGR GDSVPAAASE 200
    ADPFLHRLRP MLSSAFGQDR SLRPEEIEEL REAFREFDKD KDGYINCRDL 250
    GNCMRTMGYM PTEMELIELS QQINMNLGGH VDFDDFVELM GPKLLAETAD 300
    MIGVKELRDA FREFDTNGDG EISTSELREA MRKLLGHQVG HRDIEEIIRD 350
    VDLNGDGRVD FEEFVRMMSR 370
    Length:370
    Mass (Da):39,838
    Last modified:May 31, 2011 - v5
    Checksum:i3444721152E01AA7
    GO
    Isoform L-CaBP1 (identifier: Q9NZU7-1) [UniParc]FASTAAdd to Basket

    Also known as: Caldendrin-S2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-143: Missing.
         144-218: RPREALPAAA...RPMLSSAFGQ → MGNCVKYPLR...RKGFAENRQP

    Note: Myristoylated on Gly-2.

    Show »
    Length:227
    Mass (Da):25,979
    Checksum:iFF3F7A9B575486AB
    GO
    Isoform S-CaBP1 (identifier: Q9NZU7-2) [UniParc]FASTAAdd to Basket

    Also known as: Caldendrin-S1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-203: Missing.
         204-218: FLHRLRPMLSSAFGQ → MGNCVKYPLRNLSRK

    Note: Myristoylated on Gly-2.

    Show »
    Length:167
    Mass (Da):19,430
    Checksum:iB8C19D9E24D384FD
    GO
    Isoform Calbrain (identifier: Q9NZU7-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-300: Missing.

    Note: It is currently uncertain whether calbrain represent a spliced isoform.

    Show »
    Length:70
    Mass (Da):8,139
    Checksum:i2807BEB35ADCDA48
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti140 – 1401Q → R in AAH30201. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 300300Missing in isoform Calbrain. 1 PublicationVSP_037936Add
    BLAST
    Alternative sequencei1 – 203203Missing in isoform S-CaBP1. 1 PublicationVSP_037937Add
    BLAST
    Alternative sequencei1 – 143143Missing in isoform L-CaBP1. 1 PublicationVSP_037938Add
    BLAST
    Alternative sequencei144 – 21875RPREA…SAFGQ → MGNCVKYPLRNLSRKMCQEE QTSYMVVQTSEEGLAADAEL PGPLLMLAQNCAVMHNLLGP ACIFLRKGFAENRQP in isoform L-CaBP1. 1 PublicationVSP_037939Add
    BLAST
    Alternative sequencei204 – 21815FLHRL…SAFGQ → MGNCVKYPLRNLSRK in isoform S-CaBP1. 1 PublicationVSP_037940Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X94700 mRNA. Translation: CAA64361.1.
    AF169148 mRNA. Translation: AAF25782.1.
    AF169149 mRNA. Translation: AAF25783.1.
    AC069234 Genomic DNA. No translation available.
    BC030201 mRNA. Translation: AAH30201.2.
    CCDSiCCDS31913.1. [Q9NZU7-4]
    CCDS9204.1. [Q9NZU7-2]
    CCDS9205.1. [Q9NZU7-1]
    RefSeqiNP_001028849.1. NM_001033677.1. [Q9NZU7-4]
    NP_004267.2. NM_004276.4. [Q9NZU7-2]
    NP_112482.1. NM_031205.3. [Q9NZU7-1]
    UniGeneiHs.458482.

    Genome annotation databases

    EnsembliENST00000288616; ENSP00000288616; ENSG00000157782. [Q9NZU7-1]
    ENST00000316803; ENSP00000317310; ENSG00000157782. [Q9NZU7-4]
    ENST00000351200; ENSP00000288615; ENSG00000157782. [Q9NZU7-2]
    GeneIDi9478.
    KEGGihsa:9478.
    UCSCiuc001tyu.3. human. [Q9NZU7-4]
    uc001tyv.4. human. [Q9NZU7-1]
    uc001tyw.4. human. [Q9NZU7-2]

    Polymorphism databases

    DMDMi334302962.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X94700 mRNA. Translation: CAA64361.1 .
    AF169148 mRNA. Translation: AAF25782.1 .
    AF169149 mRNA. Translation: AAF25783.1 .
    AC069234 Genomic DNA. No translation available.
    BC030201 mRNA. Translation: AAH30201.2 .
    CCDSi CCDS31913.1. [Q9NZU7-4 ]
    CCDS9204.1. [Q9NZU7-2 ]
    CCDS9205.1. [Q9NZU7-1 ]
    RefSeqi NP_001028849.1. NM_001033677.1. [Q9NZU7-4 ]
    NP_004267.2. NM_004276.4. [Q9NZU7-2 ]
    NP_112482.1. NM_031205.3. [Q9NZU7-1 ]
    UniGenei Hs.458482.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2K7B NMR - A 219-294 [» ]
    2K7C NMR - A 299-370 [» ]
    2K7D NMR - A 299-370 [» ]
    2LAN NMR - A 219-370 [» ]
    2LAP NMR - A 219-370 [» ]
    3OX5 X-ray 2.90 A/B/C/D/E/F 219-370 [» ]
    3OX6 X-ray 2.40 A/B/C/D/E/F 219-370 [» ]
    ProteinModelPortali Q9NZU7.
    SMRi Q9NZU7. Positions 219-370.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114863. 8 interactions.
    DIPi DIP-35477N.
    IntActi Q9NZU7. 4 interactions.
    STRINGi 9606.ENSP00000317310.

    PTM databases

    PhosphoSitei Q9NZU7.

    Polymorphism databases

    DMDMi 334302962.

    Proteomic databases

    PaxDbi Q9NZU7.
    PRIDEi Q9NZU7.

    Protocols and materials databases

    DNASUi 9478.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000288616 ; ENSP00000288616 ; ENSG00000157782 . [Q9NZU7-1 ]
    ENST00000316803 ; ENSP00000317310 ; ENSG00000157782 . [Q9NZU7-4 ]
    ENST00000351200 ; ENSP00000288615 ; ENSG00000157782 . [Q9NZU7-2 ]
    GeneIDi 9478.
    KEGGi hsa:9478.
    UCSCi uc001tyu.3. human. [Q9NZU7-4 ]
    uc001tyv.4. human. [Q9NZU7-1 ]
    uc001tyw.4. human. [Q9NZU7-2 ]

    Organism-specific databases

    CTDi 9478.
    GeneCardsi GC12P121078.
    HGNCi HGNC:1384. CABP1.
    HPAi HPA051438.
    MIMi 605563. gene.
    neXtProti NX_Q9NZU7.
    PharmGKBi PA26000.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5126.
    HOGENOMi HOG000233018.
    HOVERGENi HBG012180.
    OrthoDBi EOG7XM303.
    PhylomeDBi Q9NZU7.
    TreeFami TF334804.

    Miscellaneous databases

    ChiTaRSi CABP1. human.
    EvolutionaryTracei Q9NZU7.
    GenomeRNAii 9478.
    NextBioi 35520.
    PROi Q9NZU7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NZU7.
    Bgeei Q9NZU7.
    CleanExi HS_CABP1.
    Genevestigatori Q9NZU7.

    Family and domain databases

    Gene3Di 1.10.238.10. 2 hits.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    [Graphical view ]
    Pfami PF00036. EF-hand_1. 3 hits.
    [Graphical view ]
    SMARTi SM00054. EFh. 3 hits.
    [Graphical view ]
    PROSITEi PS00018. EF_HAND_1. 3 hits.
    PS50222. EF_HAND_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Calbrain, a novel two EF-hand calcium-binding protein that suppresses Ca2+/calmodulin-dependent protein kinase II activity in the brain."
      Yamaguchi K., Yamaguchi F., Miyamoto O., Sugimoto K., Konishi R., Hatase O.
      J. Biol. Chem. 274:3610-3616(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CALBRAIN).
      Tissue: Cerebellum.
    2. "Five members of a novel Ca(2+)-binding protein (CABP) subfamily with similarity to calmodulin."
      Haeseleer F., Sokal I., Verlinde C.L.M.J., Erdjument-Bromage H., Tempst P., Pronin A.N., Benovic J.L., Fariss R.N., Palczewski K.
      J. Biol. Chem. 275:1247-1260(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS L-CABP1 AND S-CABP1), MYRISTOYLATION (ISOFORMS L-CABP1 AND S-CABP1).
      Tissue: Retina.
    3. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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 CALDENDRIN).
    5. "Caldendrin, a novel neuronal calcium-binding protein confined to the somato-dendritic compartment."
      Seidenbecher C.I., Langnaese K., Sanmarti-Vila L., Boeckers T.M., Smalla K.-H., Sabel B.A., Garner C.C., Gundelfinger E.D., Kreutz M.R.
      J. Biol. Chem. 273:21324-21331(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM CALDENDRIN).
    6. "Identification of a family of calcium sensors as protein ligands of inositol trisphosphate receptor Ca(2+) release channels."
      Yang J., McBride S., Mak D.-O.D., Vardi N., Palczewski K., Haeseleer F., Foskett J.K.
      Proc. Natl. Acad. Sci. U.S.A. 99:7711-7716(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ITPR1; ITPR2 AND ITPR3, MUTAGENESIS OF ASP-238; ASP-240; ASP-315; ASN-317; ASP-352 AND ASN-354.
    7. "Differential modulation of Ca(v)2.1 channels by calmodulin and Ca2+-binding protein 1."
      Lee A., Westenbroek R.E., Haeseleer F., Palczewski K., Scheuer T., Catterall W.A.
      Nat. Neurosci. 5:210-217(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CACNA1A.
    8. Cited for: PHOSPHORYLATION AT SER-323, MUTAGENESIS OF SER-323, SUBCELLULAR LOCATION, INTERACTION WITH ITPR1.
    9. "Calcium-binding protein 1 is an inhibitor of agonist-evoked, inositol 1,4,5-trisphosphate-mediated calcium signaling."
      Haynes L.P., Tepikin A.V., Burgoyne R.D.
      J. Biol. Chem. 279:547-555(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    10. "Caldendrin but not calmodulin binds to light chain 3 of MAP1A/B: an association with the microtubule cytoskeleton highlighting exclusive binding partners for neuronal Ca(2+)-sensor proteins."
      Seidenbecher C.I., Landwehr M., Smalla K.H., Kreutz M., Dieterich D.C., Zuschratter W., Reissner C., Hammarback J.A., Bockers T.M., Gundelfinger E.D., Kreutz M.R.
      J. Mol. Biol. 336:957-970(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAP1LC3B.
    11. "Ca2+-binding protein-1 facilitates and forms a postsynaptic complex with Cav1.2 (L-type) Ca2+ channels."
      Zhou H., Kim S.-A., Kirk E.A., Tippens A.L., Sun H., Haeseleer F., Lee A.
      J. Neurosci. 24:4698-4708(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CACNA1C.
    12. "Molecular mechanism for divergent regulation of Cav1.2 Ca2+ channels by calmodulin and Ca2+-binding protein-1."
      Zhou H., Yu K., McCoy K.L., Lee A.
      J. Biol. Chem. 280:29612-29619(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CACNA1C.
    13. "Inhibition of TRPC5 channels by Ca2+-binding protein 1 in Xenopus oocytes."
      Kinoshita-Kawada M., Tang J., Xiao R., Kaneko S., Foskett J.K., Zhu M.X.
      Pflugers Arch. 450:345-354(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TRPC5.
    14. "Structural analysis of Mg2+ and Ca2+ binding to CaBP1, a neuron-specific regulator of calcium channels."
      Wingard J.N., Chan J., Bosanac I., Haeseleer F., Palczewski K., Ikura M., Ames J.B.
      J. Biol. Chem. 280:37461-37470(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, CALCIUM-BINDING, MAGNESIUM-BINDING.
    15. "Structural insights into Ca2+-dependent regulation of inositol 1,4,5-trisphosphate receptors by CaBP1."
      Li C., Chan J., Haeseleer F., Mikoshiba K., Palczewski K., Ikura M., Ames J.B.
      J. Biol. Chem. 284:2472-2481(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 219-294 AND 299-370 IN COMPLEX WITH MAGNESIUM AND CALCIUM, MUTAGENESIS OF ASP-238; ASP-240; ASP-242 AND ASP-249.

    Entry informationi

    Entry nameiCABP1_HUMAN
    AccessioniPrimary (citable) accession number: Q9NZU7
    Secondary accession number(s): O95663, Q8N6H5, Q9NZU8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: May 31, 2011
    Last modified: October 1, 2014
    This is version 124 of the entry and version 5 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3