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Q99828

- CIB1_HUMAN

UniProt

Q99828 - CIB1_HUMAN

Protein

Calcium and integrin-binding protein 1

Gene

CIB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 4 (20 Mar 2007)
      Previous versions | rss
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    Functioni

    Calcium-binding protein that plays a role in the regulation of numerous cellular processes, such as cell differentiation, cell division, cell proliferation, cell migration, thrombosis, angiogenesis, cardiac hypertrophy and apoptosis. Involved in bone marrow megakaryocyte differentiation by negatively regulating thrombopoietin-mediated signaling pathway. Participates in the endomitotic cell cycle of megakaryocyte, a form of mitosis in which both karyokinesis and cytokinesis are interrupted. Plays a role in integrin signaling by negatively regulating alpha-IIb/beta3 activation in thrombin-stimulated megakaryocytes preventing platelet aggregation. Up-regulates PTK2/FAK1 activity, and is also needed for the recruitment of PTK2/FAK1 to focal adhesions; it thus appears to play an important role in focal adhesion formation. Positively regulates cell migration on fibronectin in a CDC42-dependent manner, the effect being negatively regulated by PAK1. Functions as a negative regulator of stress activated MAP kinase (MAPK) signaling pathways. Down-regulates inositol 1,4,5-trisphosphate receptor-dependent calcium signaling. Involved in sphingosine kinase SPHK1 translocation to the plasma membrane in a N-myristoylation-dependent manner preventing TNF-alpha-induced apoptosis. Regulates serine/threonine-protein kinase PLK3 activity for proper completion of cell division progression. Plays a role in microtubule (MT) dynamics during neuronal development; disrupts the MT depolymerization activity of STMN2 attenuating NGF-induced neurite outgrowth and the MT reorganization at the edge of lamellipodia. Promotes cardiomyocyte hypertrophy via activation of the calcineurin/NFAT signaling pathway. Stimulates calcineurin PPP3R1 activity by mediating its anchoring to the sarcolemma. In ischemia-induced (pathological or adaptive) angiogenesis, stimulates endothelial cell proliferation, migration and microvessel formation by activating the PAK1 and ERK1/ERK2 signaling pathway. Promotes also cancer cell survival and proliferation. May regulate cell cycle and differentiation of spermatogenic germ cells, and/or differentiation of supporting Sertoli cells.
    Isoform 2: Plays a regulatory role in angiogenesis and tumor growth by mediating PKD/PRKD2-induced vascular endothelial growth factor A (VEGFA) secretion.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi116 – 127121Add
    BLAST
    Calcium bindingi161 – 172122Add
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: HGNC
    2. protein anchor Source: BHF-UCL
    3. protein binding Source: UniProtKB
    4. Ras GTPase binding Source: UniProtKB

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. apoptotic process Source: HGNC
    3. cell adhesion Source: ProtInc
    4. cell division Source: UniProtKB-KW
    5. cellular response to DNA damage stimulus Source: HGNC
    6. cellular response to growth factor stimulus Source: UniProtKB
    7. cellular response to nerve growth factor stimulus Source: UniProtKB
    8. cellular response to tumor necrosis factor Source: UniProtKB
    9. cytoplasmic microtubule organization Source: UniProtKB
    10. double-strand break repair Source: ProtInc
    11. endomitotic cell cycle Source: UniProtKB
    12. extrinsic apoptotic signaling pathway Source: BHF-UCL
    13. negative regulation of apoptotic process Source: UniProtKB
    14. negative regulation of cell proliferation Source: UniProtKB
    15. negative regulation of megakaryocyte differentiation Source: UniProtKB
    16. negative regulation of microtubule depolymerization Source: UniProtKB
    17. negative regulation of neuron projection development Source: UniProtKB
    18. negative regulation of protein kinase B signaling Source: UniProtKB
    19. negative regulation of protein phosphorylation Source: UniProtKB
    20. platelet formation Source: UniProtKB
    21. positive regulation of calcineurin-NFAT signaling cascade Source: BHF-UCL
    22. positive regulation of cell adhesion mediated by integrin Source: UniProtKB
    23. positive regulation of cell growth Source: UniProtKB
    24. positive regulation of cell-matrix adhesion Source: UniProtKB
    25. positive regulation of cell migration Source: UniProtKB
    26. positive regulation of cell migration involved in sprouting angiogenesis Source: UniProtKB
    27. positive regulation of cell proliferation Source: UniProtKB
    28. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    29. positive regulation of establishment of protein localization to plasma membrane Source: BHF-UCL
    30. positive regulation of gene expression involved in extracellular matrix organization Source: UniProtKB
    31. positive regulation of male germ cell proliferation Source: UniProtKB
    32. positive regulation of metalloenzyme activity Source: UniProtKB
    33. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    34. positive regulation of protein phosphorylation Source: UniProtKB
    35. positive regulation of protein serine/threonine kinase activity Source: UniProtKB
    36. positive regulation of protein targeting to membrane Source: UniProtKB
    37. positive regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
    38. regulation of cell division Source: UniProtKB
    39. regulation of cell proliferation Source: UniProtKB
    40. response to ischemia Source: UniProtKB
    41. spermatid development Source: UniProtKB
    42. thrombopoietin-mediated signaling pathway Source: UniProtKB

    Keywords - Biological processi

    Angiogenesis, Apoptosis, Cell adhesion, Cell cycle, Cell division, Differentiation, Spermatogenesis

    Keywords - Ligandi

    Calcium, Magnesium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calcium and integrin-binding protein 1
    Short name:
    CIB
    Alternative name(s):
    Calcium- and integrin-binding protein
    Short name:
    CIBP
    Calmyrin
    DNA-PKcs-interacting protein
    Kinase-interacting protein
    Short name:
    KIP
    SNK-interacting protein 2-28
    Short name:
    SIP2-28
    Gene namesi
    Name:CIB1
    Synonyms:CIB, KIP, PRKDCIP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:16920. CIB1.

    Subcellular locationi

    Membrane; Lipid-anchor. Cell membranesarcolemma. Cell membrane. Apical cell membrane. Cell projectionruffle membrane. Cell projectionfilopodium tip. Cell projectiongrowth cone. Cell projectionlamellipodium. Cytoplasm. Cytoplasmcytoskeleton. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmperinuclear region. Nucleus
    Note: Colocalized with PPP3R1 at the cell membrane of cardiomyocytes in the hypertrophic heart By similarity. Colocalized with NBR1 to the perinuclear region. Colocalizes with TAS1R2 in apical regions of taste receptor cells. Colocalized with RAC3 in the perinuclear area and at the cell periphery. Colocalized with PAK1 within membrane ruffles during cell spreading upon readhesion to fibronectin. Redistributed to the cytoskeleton upon platelet aggregation. Translocates from the cytosol to the plasma membrane in a calcium-dependent manner. Colocalized with STMN2 in the cell body, neurites and growth cones of neurons. Colocalized with STMN2 to the leading edge of lamellipodia. Colocalized with PLK3 at centrosomes in ductal breast carcinoma cells.By similarity
    Isoform 2 : Cytoplasmperinuclear region 1 Publication. Golgi apparatustrans-Golgi network 1 Publication

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB-SubCell
    2. cell periphery Source: UniProtKB
    3. centrosome Source: UniProtKB
    4. cytoplasm Source: UniProtKB
    5. endoplasmic reticulum Source: HGNC
    6. extracellular vesicular exosome Source: UniProt
    7. filopodium tip Source: UniProtKB
    8. Golgi apparatus Source: UniProtKB-SubCell
    9. growth cone Source: UniProtKB
    10. lamellipodium Source: UniProtKB
    11. membrane Source: HGNC
    12. neuronal cell body Source: UniProtKB
    13. neuron projection Source: UniProtKB
    14. nucleoplasm Source: HGNC
    15. nucleus Source: UniProtKB
    16. perinuclear region of cytoplasm Source: UniProtKB
    17. plasma membrane Source: UniProtKB
    18. ruffle membrane Source: UniProtKB-SubCell
    19. sarcolemma Source: BHF-UCL
    20. vesicle Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 21G → A: Inhibits translocation to the plasma membrane. Show increased apoptosis after TNF stimulation. 1 Publication
    Mutagenesisi78 – 781S → A: Loss of phosphorylation by PKD/PRKD2; in isoform 2. 1 Publication
    Mutagenesisi78 – 781S → E: Phosphomimetic; promotes tumor growth by an indirect mechanism; in isoform 2. 1 Publication
    Mutagenesisi114 – 1174IFDF → AAAA: Loss of binding to ITGAV.
    Mutagenesisi115 – 1151F → A: Loss of binding to ITGA2B. 1 Publication
    Mutagenesisi127 – 1271D → N: Cytoplasmic localization. 1 Publication
    Mutagenesisi131 – 1311L → A or T: Loss of binding to ITGA2B. 1 Publication
    Mutagenesisi152 – 1532LI → AA: Loss of binding to ITGA2B.
    Mutagenesisi153 – 1531I → A: Loss of binding to ITGA2B. 1 Publication
    Mutagenesisi167 – 1671T → A: No effect on phosphorylation by PKD/PRKD2; in isoform 2. 1 Publication
    Mutagenesisi172 – 1721E → Q: Cytoplasmic localization. 1 Publication
    Mutagenesisi173 – 1731F → A: Loss of binding to ITGA2B. 3 Publications
    Mutagenesisi173 – 1731F → A: Loss of binding to ITGA2B. Does not inhibit interaction with PAK1. 3 Publications

    Organism-specific databases

    PharmGKBiPA38423.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 191190Calcium and integrin-binding protein 1PRO_0000073531Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine1 Publication
    Modified residuei78 – 781Phosphoserine; by PKD/PRKD2; in isoform 21 Publication

    Post-translational modificationi

    Phosphorylation of isoform 2 at Ser-78 by PRKD2 increases its ability to stimulate tumor angiogenesis.1 Publication

    Keywords - PTMi

    Lipoprotein, Myristate, Phosphoprotein

    Proteomic databases

    MaxQBiQ99828.
    PaxDbiQ99828.
    PRIDEiQ99828.

    PTM databases

    PhosphoSiteiQ99828.

    Expressioni

    Tissue specificityi

    Detected in platelets and in cell lines of megakaryocytic and erythrocytic lineages. Both isoform 1 and isoform 2 are detected in various cancer cell lines, with isoform 2 being the predominant form (at protein level). Ubiquitously expressed.5 Publications

    Inductioni

    Up-regulated during breast cancer progression.

    Gene expression databases

    BgeeiQ99828.
    CleanExiHS_CIB1.
    GenevestigatoriQ99828.

    Organism-specific databases

    HPAiCAB012991.
    HPA048825.

    Interactioni

    Subunit structurei

    Monomer. Interacts with MYO1C. Interacts (via C-terminal region) with PPP3R1 and CACNA1C; the interactions increase upon cardiomyocytes hypertrophy By similarity. Interacts with the heterodimeric integrin alpha-IIb/beta3 (ITGA2B-ITGB3). Interacts with ITGA2B (via cytoplasmic domain); the interaction is direct and calcium-dependent. Interacts with the protein kinases PLK2/SNK and PRKDC (via the region immediately upstream of the kinase domain). Interacts with PLK3; the interaction inhibits PLK3 kinase activity. Interacts with PSEN2. Interacts (via C-terminus) with F8. Interacts with NBR1 (via C-terminus). Interacts with FEZ1 (via C-terminus). Interacts with UBR5 (via C-terminus); the interaction is sensitive to DNA damage, and may target CIB1 for ubiquitin-mediated degradation. Interacts with IFI6. Interacts with BCL2. Interacts with ITPR3; the interaction occurs in a calcium-dependent manner. Interacts with PTK2/FAK1. Interacts with MAP3K5; the interaction inhibits MAP3K5 activation by phosphorylation, and its subsequent interaction with TRAF2. Isoform 2 interacts with PRKD2 (via N-terminal AP-rich region), PTK2/FAK1 and PAK1. Interacts with TAS1R2 (via C-terminus); the interaction is independent of the myristoylation state of CIB1. Interacts (via C-terminal region) with STMN2 (via the N-terminal region); the interaction is direct, occurs in a calcium-dependent manner and attenuates the STMN2-induced neurite outgrowth inhibition. Interacts with SPHK1, the interaction occurs in a calcium-dependent manner. Interacts with ITGA2B (via C-terminal cytoplasmic tail); the interaction occurs upon platelet aggregation and is stabilized/increased in a calcium and magnesium-dependent manner. Interacts with PAK1 (via N-terminal region); the interaction is direct and occurs in a calcium-dependent manner. Interacts with RAC3 (via C-terminal region); the interaction induces their association with the cytoskeleton upon alpha-IIb/beta3 integrin-mediated adhesion. Interacts with ITGA5 and ITGAV.By similarity32 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    WASLO004017EBI-372594,EBI-957615

    Protein-protein interaction databases

    BioGridi115774. 18 interactions.
    DIPiDIP-31260N.
    IntActiQ99828. 15 interactions.
    MINTiMINT-95290.
    STRINGi9606.ENSP00000333873.

    Structurei

    Secondary structure

    1
    191
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi14 – 163
    Turni18 – 203
    Helixi24 – 3512
    Helixi40 – 423
    Helixi45 – 506
    Helixi55 – 595
    Helixi62 – 654
    Helixi70 – 778
    Beta strandi81 – 866
    Helixi88 – 9811
    Helixi104 – 11512
    Beta strandi120 – 1234
    Helixi125 – 13511
    Beta strandi137 – 1393
    Beta strandi145 – 1473
    Helixi149 – 16012
    Beta strandi165 – 1684
    Helixi170 – 17910
    Helixi181 – 19010

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DGUNMR-A9-191[»]
    1DGVNMR-A9-191[»]
    1XO5X-ray1.99A/B9-191[»]
    1Y1AX-ray2.30A/B9-191[»]
    2L4HNMR-A1-191[»]
    2L4INMR-A1-191[»]
    2LM5NMR-A1-191[»]
    ProteinModelPortaliQ99828.
    SMRiQ99828. Positions 9-191.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99828.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini103 – 13836EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini148 – 18336EF-hand 2PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The EF-hands may also bind magnesium ions in the presence of high Mg2+ levels and low Ca2+ levels.

    Sequence similaritiesi

    Contains 2 EF-hand domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG257993.
    HOVERGENiHBG107344.
    InParanoidiQ99828.
    KOiK17259.
    OMAiYKRFSEL.
    OrthoDBiEOG7KM5V7.
    PhylomeDBiQ99828.
    TreeFamiTF313865.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    [Graphical view]
    PfamiPF13499. EF-hand_7. 1 hit.
    [Graphical view]
    SMARTiSM00054. EFh. 2 hits.
    [Graphical view]
    PROSITEiPS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q99828-1) [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

    MGGSGSRLSK ELLAEYQDLT FLTKQEILLA HRRFCELLPQ EQRSVESSLR    50
    AQVPFEQILS LPELKANPFK ERICRVFSTS PAKDSLSFED FLDLLSVFSD 100
    TATPDIKSHY AFRIFDFDDD GTLNREDLSR LVNCLTGEGE DTRLSASEMK 150
    QLIDNILEES DIDRDGTINL SEFQHVISRS PDFASSFKIV L 191
    Length:191
    Mass (Da):21,703
    Last modified:March 20, 2007 - v4
    Checksum:i9AA19A0DE7AA1E05
    GO
    Isoform 2 (identifier: Q99828-2) [UniParc]FASTAAdd to Basket

    Also known as: CIB1a

    The sequence of this isoform differs from the canonical sequence as follows:
         29-29: L → LSVYVVLAPHLVDNEQQARSGNEHTGRPIAENTDSSPLSTR

    Show »
    Length:231
    Mass (Da):26,032
    Checksum:i0D38C53F1478119E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti136 – 1361T → M in CAG33236. 1 PublicationCurated
    Sequence conflicti171 – 1711S → F in AEZ06077. (PubMed:23503467)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti44 – 441S → T.3 Publications
    Corresponds to variant rs3210935 [ dbSNP | Ensembl ].
    VAR_019565
    Natural varianti106 – 1061I → T.
    Corresponds to variant rs11551250 [ dbSNP | Ensembl ].
    VAR_048636

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei29 – 291L → LSVYVVLAPHLVDNEQQARS GNEHTGRPIAENTDSSPLST R in isoform 2. 1 PublicationVSP_053740

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U82226 mRNA. Translation: AAC51106.1.
    U85611 mRNA. Translation: AAB53387.1.
    AB021866 Genomic DNA. Translation: BAA36281.1.
    JQ246073 mRNA. Translation: AEZ06077.1.
    U83236 mRNA. Translation: AAB39758.1.
    CR456955 mRNA. Translation: CAG33236.1.
    AB451276 mRNA. Translation: BAG70090.1.
    AB451406 mRNA. Translation: BAG70220.1.
    CH471101 Genomic DNA. Translation: EAX02090.1.
    BC000846 mRNA. Translation: AAH00846.1.
    CCDSiCCDS10360.1. [Q99828-1]
    RefSeqiNP_001264693.1. NM_001277764.1. [Q99828-2]
    NP_006375.2. NM_006384.3. [Q99828-1]
    UniGeneiHs.715556.

    Genome annotation databases

    EnsembliENST00000328649; ENSP00000333873; ENSG00000185043. [Q99828-1]
    GeneIDi10519.
    KEGGihsa:10519.
    UCSCiuc002bpb.4. human. [Q99828-1]

    Polymorphism databases

    DMDMi134047806.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U82226 mRNA. Translation: AAC51106.1 .
    U85611 mRNA. Translation: AAB53387.1 .
    AB021866 Genomic DNA. Translation: BAA36281.1 .
    JQ246073 mRNA. Translation: AEZ06077.1 .
    U83236 mRNA. Translation: AAB39758.1 .
    CR456955 mRNA. Translation: CAG33236.1 .
    AB451276 mRNA. Translation: BAG70090.1 .
    AB451406 mRNA. Translation: BAG70220.1 .
    CH471101 Genomic DNA. Translation: EAX02090.1 .
    BC000846 mRNA. Translation: AAH00846.1 .
    CCDSi CCDS10360.1. [Q99828-1 ]
    RefSeqi NP_001264693.1. NM_001277764.1. [Q99828-2 ]
    NP_006375.2. NM_006384.3. [Q99828-1 ]
    UniGenei Hs.715556.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DGU NMR - A 9-191 [» ]
    1DGV NMR - A 9-191 [» ]
    1XO5 X-ray 1.99 A/B 9-191 [» ]
    1Y1A X-ray 2.30 A/B 9-191 [» ]
    2L4H NMR - A 1-191 [» ]
    2L4I NMR - A 1-191 [» ]
    2LM5 NMR - A 1-191 [» ]
    ProteinModelPortali Q99828.
    SMRi Q99828. Positions 9-191.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115774. 18 interactions.
    DIPi DIP-31260N.
    IntActi Q99828. 15 interactions.
    MINTi MINT-95290.
    STRINGi 9606.ENSP00000333873.

    PTM databases

    PhosphoSitei Q99828.

    Polymorphism databases

    DMDMi 134047806.

    Proteomic databases

    MaxQBi Q99828.
    PaxDbi Q99828.
    PRIDEi Q99828.

    Protocols and materials databases

    DNASUi 10519.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000328649 ; ENSP00000333873 ; ENSG00000185043 . [Q99828-1 ]
    GeneIDi 10519.
    KEGGi hsa:10519.
    UCSCi uc002bpb.4. human. [Q99828-1 ]

    Organism-specific databases

    CTDi 10519.
    GeneCardsi GC15M090773.
    H-InvDB HIX0012576.
    HGNCi HGNC:16920. CIB1.
    HPAi CAB012991.
    HPA048825.
    MIMi 602293. gene.
    neXtProti NX_Q99828.
    PharmGKBi PA38423.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG257993.
    HOVERGENi HBG107344.
    InParanoidi Q99828.
    KOi K17259.
    OMAi YKRFSEL.
    OrthoDBi EOG7KM5V7.
    PhylomeDBi Q99828.
    TreeFami TF313865.

    Miscellaneous databases

    ChiTaRSi CIB1. human.
    EvolutionaryTracei Q99828.
    GeneWikii CIB1.
    GenomeRNAii 10519.
    NextBioi 35528000.
    PROi Q99828.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q99828.
    CleanExi HS_CIB1.
    Genevestigatori Q99828.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    [Graphical view ]
    Pfami PF13499. EF-hand_7. 1 hit.
    [Graphical view ]
    SMARTi SM00054. EFh. 2 hits.
    [Graphical view ]
    PROSITEi PS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a novel calcium-binding protein that interacts with the integrin alphaIIb cytoplasmic domain."
      Naik U.P., Patel P.M., Parise L.V.
      J. Biol. Chem. 272:4651-4654(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH ITGA2B, TISSUE SPECIFICITY, CALCIUM-BINDING.
      Tissue: Fetal liver.
    2. "Interaction between DNA-dependent protein kinase and a novel protein, KIP."
      Wu X., Lieber M.R.
      Mutat. Res. 385:13-20(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH PRKDC, TISSUE SPECIFICITY, VARIANT THR-44.
    3. "Genomic structure of mouse and human genes for DNA-PKcs interacting protein (KIP)."
      Hattori A., Seki N., Hayashi A., Kozuma S., Saito T.
      DNA Seq. 10:415-418(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-44.
    4. "A novel splice variant of calcium and integrin-binding protein 1 mediates protein kinase D2-stimulated tumour growth by regulating angiogenesis."
      Armacki M., Joodi G., Nimmagadda S.C., de Kimpe L., Pusapati G.V., Vandoninck S., Van Lint J., Illing A., Seufferlein T.
      Oncogene 33:1167-1180(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORM 2), INTERACTION WITH PRKD2; PTK2 AND PAK1, SUBCELLULAR LOCATION (ISOFORM 2), TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-78, MUTAGENESIS OF SER-78 AND THR-167.
      Tissue: Brain.
    5. "SNK, a Ser/Thr protein kinase, associated proteins."
      Yuan O.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-44.
    6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    7. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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).
      Tissue: Cervix.
    10. "Calcium-dependent properties of CIB binding to the integrin alphaIIb cytoplasmic domain and translocation to the platelet cytoskeleton."
      Shock D.D., Naik U.P., Brittain J.E., Alahari S.K., Sondek J., Parise L.V.
      Biochem. J. 342:729-735(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ITGA2B, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    11. "A myristoylated calcium-binding protein that preferentially interacts with the Alzheimer's disease presenilin 2 protein."
      Stabler S.M., Ostrowski L.L., Janicki S.M., Monteiro M.J.
      J. Cell Biol. 145:1277-1292(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MYRISTOYLATION AT GLY-2, INTERACTION WITH PSEN2.
    12. "The interaction of the calcium- and integrin-binding protein (CIBP) with the coagulation factor VIII."
      Fang X., Chen C., Wang Q., Gu J., Chi C.
      Thromb. Res. 102:177-185(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH F8.
    13. "NBR1 interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB) and shows developmentally restricted expression in the neural tube."
      Whitehouse C., Chambers J., Howe K., Cobourne M., Sharpe P., Solomon E.
      Eur. J. Biochem. 269:538-545(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NBR1 AND FEZ1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    14. "The small GTPase Rac3 interacts with the integrin-binding protein CIB and promotes integrin alpha(IIb)beta(3)-mediated adhesion and spreading."
      Haataja L., Kaartinen V., Groffen J., Heisterkamp N.
      J. Biol. Chem. 277:8321-8328(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RAC3, SUBCELLULAR LOCATION.
    15. "EDD, the human hyperplastic discs protein, has a role in progesterone receptor coactivation and potential involvement in DNA damage response."
      Henderson M.J., Russell A.J., Hird S., Munoz M., Clancy J.L., Lehrbach G.M., Calanni S.T., Jans D.A., Sutherland R.L., Watts C.K.
      J. Biol. Chem. 277:26468-26478(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBR5.
    16. "Molecular basis of CIB binding to the integrin alpha IIb cytoplasmic domain."
      Barry W.T., Boudignon-Proudhon C., Shock D.D., McFadden A., Weiss J.M., Sondek J., Parise L.V.
      J. Biol. Chem. 277:28877-28883(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ITGA2B, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-115; LEU-131; ILE-153 AND PHE-173.
    17. "Association of CIB with GPIIb/IIIa during outside-in signaling is required for platelet spreading on fibrinogen."
      Naik U.P., Naik M.U.
      Blood 102:1355-1362(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "Metal ion binding properties and conformational states of calcium- and integrin-binding protein."
      Yamniuk A.P., Nguyen L.T., Hoang T.T., Vogel H.J.
      Biochemistry 43:2558-2568(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ITGA2B, CALCIUM-BINDING, MAGNESIUM-BINDING.
    19. "Calcium binding sequences in calmyrin regulates interaction with presenilin-2."
      Zhu J., Stabler S.M., Ames J.B., Baskakov I., Monteiro M.J.
      Exp. Cell Res. 300:440-454(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PSEN2, MUTAGENESIS OF ASP-127 AND GLU-172.
    20. "Calcium-and integrin-binding protein regulates focal adhesion kinase activity during platelet spreading on immobilized fibrinogen."
      Naik M.U., Naik U.P.
      Blood 102:3629-3636(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PTK2/FAK1.
    21. "Calcium-binding calmyrin forms stable covalent dimers in vitro, but in vivo is found in monomeric form."
      Sobczak A., Blazejczyk M., Piszczek G., Zhao G., Kuznicki J., Wojda U.
      Acta Biochim. Pol. 52:469-476(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    22. "G1P3, an interferon inducible gene 6-16, is expressed in gastric cancers and inhibits mitochondrial-mediated apoptosis in gastric cancer cell line TMK-1 cell."
      Tahara E. Jr., Tahara H., Kanno M., Naka K., Takeda Y., Matsuzaki T., Yamazaki R., Ishihara H., Yasui W., Barrett J.C., Ide T., Tahara E.
      Cancer Immunol. Immunother. 54:729-740(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH IFI6 AND BCL2.
    23. "Essential role of CIB1 in regulating PAK1 activation and cell migration."
      Leisner T.M., Liu M., Jaffer Z.M., Chernoff J., Parise L.V.
      J. Cell Biol. 170:465-476(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PAK1.
    24. "Calcium- and magnesium-dependent interactions between calcium- and integrin-binding protein and the integrin alphaIIb cytoplasmic domain."
      Yamniuk A.P., Vogel H.J.
      Protein Sci. 14:1429-1437(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ITGA2B, CALCIUM-BINDING, MAGNESIUM-BINDING.
    25. "CIB1, a ubiquitously expressed Ca2+-binding protein ligand of the InsP3 receptor Ca2+ release channel."
      White C., Yang J., Monteiro M.J., Foskett J.K.
      J. Biol. Chem. 281:20825-20833(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ITPR3.
    26. "CIB1 is an endogenous inhibitor of agonist-induced integrin alphaIIbbeta3 activation."
      Yuan W., Leisner T.M., McFadden A.W., Wang Z., Larson M.K., Clark S., Boudignon-Proudhon C., Lam S.C., Parise L.V.
      J. Cell Biol. 172:169-175(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PAK1, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-173.
    27. "Sweet taste receptor interacting protein CIB1 is a general inhibitor of InsP3-dependent Ca2+ release in vivo."
      Hennigs J.K., Burhenne N., Staehler F., Winnig M., Walter B., Meyerhof W., Schmale H.
      J. Neurochem. 106:2249-2262(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TAS1R2, SUBCELLULAR LOCATION.
    28. "CIB1 functions as a Ca(2+)-sensitive modulator of stress-induced signaling by targeting ASK1."
      Yoon K.W., Cho J.H., Lee J.K., Kang Y.H., Chae J.S., Kim Y.M., Kim J., Kim E.K., Kim S.E., Baik J.H., Naik U.P., Cho S.G., Choi E.J.
      Proc. Natl. Acad. Sci. U.S.A. 106:17389-17394(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MAP3K5.
    29. "Auxiliary Ca2+ binding sites can influence the structure of CIB1."
      Yamniuk A.P., Anderson K.L., Fraser M.E., Vogel H.J.
      Protein Sci. 18:1128-1134(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, CALCIUM-BINDING.
    30. "Translocation of sphingosine kinase 1 to the plasma membrane is mediated by calcium- and integrin-binding protein 1."
      Jarman K.E., Moretti P.A., Zebol J.R., Pitson S.M.
      J. Biol. Chem. 285:483-492(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SPHK1, SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-2.
    31. Cited for: SUBCELLULAR LOCATION.
    32. "Calmyrin1 binds to SCG10 protein (stathmin2) to modulate neurite outgrowth."
      Sobczak A., Debowska K., Blazejczyk M., Kreutz M.R., Kuznicki J., Wojda U.
      Biochim. Biophys. Acta 1813:1025-1037(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STMN2, SUBCELLULAR LOCATION.
    33. "Calcium- and integrin-binding protein 1 regulates microtubule organization and centrosome segregation through polo like kinase 3 during cell cycle progression."
      Naik M.U., Naik U.P.
      Int. J. Biochem. Cell Biol. 43:120-129(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PLK3, SUBCELLULAR LOCATION (ISOFORM 1).
    34. "Calcium-dependent inhibition of polo-like kinase 3 activity by CIB1 in breast cancer cells."
      Naik M.U., Pham N.T., Beebe K., Dai W., Naik U.P.
      Int. J. Cancer 128:587-596(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PLK3.
    35. "Contra-regulation of calcium- and integrin-binding protein 1-induced cell migration on fibronectin by PAK1 and MAP kinase signaling."
      Naik M.U., Naik U.P.
      J. Cell. Biochem. 112:3289-3299(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION (ISOFORM 1).
    36. "Calcium- and integrin-binding protein 1 regulates endomitosis and its interaction with Polo-like kinase 3 is enhanced in endomitotic Dami cells."
      Kostyak J.C., Naik U.P.
      PLoS ONE 6:E14513-E14513(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PLK3.
    37. "Biophysical and structural studies of the human calcium- and integrin-binding protein family: understanding their functional similarities and differences."
      Huang H., Bogstie J.N., Vogel H.J.
      Biochem. Cell Biol. 90:646-656(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ITGA2B.
    38. "Identification of novel integrin binding partners for calcium and integrin binding protein 1 (CIB1): structural and thermodynamic basis of CIB1 promiscuity."
      Freeman T.C. Jr., Black J.L., Bray H.G., Dagliyan O., Wu Y.I., Tripathy A., Dokholyan N.V., Leisner T.M., Parise L.V.
      Biochemistry 52:7082-7090(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ITGA5 AND ITGAV, MUTAGENESIS OF 114-ILE--PHE-117; 152-LEU-ILE-153 AND PHE-173.
    39. "CIB1 prevents nuclear GAPDH accumulation and non-apoptotic tumor cell death via AKT and ERK signaling."
      Leisner T.M., Moran C., Holly S.P., Parise L.V.
      Oncogene 32:4017-4027(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    40. "Structures of the platelet calcium- and integrin-binding protein and the alphaIIb-integrin cytoplasmic domain suggest a mechanism for calcium-regulated recognition; homology modelling and NMR studies."
      Hwang P.M., Vogel H.J.
      J. Mol. Recognit. 13:83-92(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 9-191.
    41. "Structural and biochemical characterization of CIB1 delineates a new family of EF-hand-containing proteins."
      Gentry H.R., Singer A.U., Betts L., Yang C., Ferrara J.D., Sondek J., Parise L.V.
      J. Biol. Chem. 280:8407-8415(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 9-191 IN COMPLEX WITH CALCIUM IONS, SUBUNIT.
    42. "The crystal structure of calcium- and integrin-binding protein 1: insights into redox regulated functions."
      Blamey C.J., Ceccarelli C., Naik U.P., Bahnson B.J.
      Protein Sci. 14:1214-1221(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 9-191.
    43. "Solution structures of Ca2+-CIB1 and Mg2+-CIB1 and their interactions with the platelet integrin alphaIIb cytoplasmic domain."
      Huang H., Ishida H., Yamniuk A.P., Vogel H.J.
      J. Biol. Chem. 286:17181-17192(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-191 IN COMPLEXES WITH CALCIUM IONS AND MAGNESIUM ION, INTERACTION WITH ITGA2B.
    44. "Structural basis for the activation of platelet integrin alphaIIbbeta3 by calcium- and integrin-binding protein 1."
      Huang H., Vogel H.J.
      J. Am. Chem. Soc. 134:3864-3872(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-191 IN COMPLEX WITH ITGA2B PEPTIDE AND CALCIUM IONS, INTERACTION WITH ITGA2B.

    Entry informationi

    Entry nameiCIB1_HUMAN
    AccessioniPrimary (citable) accession number: Q99828
    Secondary accession number(s): B5BU40
    , H6WJF3, O00693, O00735, Q6IB49, Q96J54, Q99971
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: March 20, 2007
    Last modified: October 1, 2014
    This is version 143 of the entry and version 4 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

    Miscellaneous

    The binding of either calcium or magnesium significantly increases the structural stability of the protein in comparison to apo-CIB (calcium- and magnesium-free form).1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: 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