2ct9 Summary


The crystal structure of calcineurin B homologous proein 1 (CHP1)

The structure was published by Naoe, Y., Arita, K., Hashimoto, H., Kanazawa, H., Sato, M., and Shimizu, T., in 2005 in a paper entitled "Structural characterization of calcineurin B homologous protein 1" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 2005.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of Calcium-binding protein p22.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Calcium-binding protein p22 P61023 (1-195) (CHP1_RAT)search Rattus norvegicussearch 100% 208 95%
B Calcium-binding protein p22 P61023 (1-195) (CHP1_RAT)search Rattus norvegicussearch 100% 208 95%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P61023 (1 - 195) Calcium-binding protein p22 Rattus norvegicus

Chain Structural classification (CATH) Sequence family (Pfam)
A, B (P61023) EF-handsearch PF13405: EF-hand domainsearch, PF13499: EF-hand domain pairsearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A, B (P61023) protein transportsearch negative regulation of calcineurin-NFAT signaling cascadesearch negative regulation of phosphatase activitysearch negative regulation of protein kinase activitysearch regulation of intracellular pHsearch protein oligomerizationsearch cytoplasmic microtubule organizationsearch negative regulation of NF-kappaB transcription factor activitysearch protein stabilizationsearch positive regulation of protein targeting to membranesearch membrane fusionsearch positive regulation of protein glycosylationsearch calcium ion-dependent exocytosissearch positive regulation of sodium:proton antiporter activitysearch transcytosissearch regulation of neuron deathsearch protein export from nucleussearch cellular response to acidic pHsearch membrane organizationsearch negative regulation of protein ubiquitinationsearch transportsearch membrane dockingsearch negative regulation of protein import into nucleussearch negative regulation of protein phosphorylationsearch positive regulation of protein transportsearch negative regulation of protein autophosphorylationsearch microtubule bundle formationsearch calcium-mediated signalingsearch protein bindingsearch microtubule bindingsearch metal ion bindingsearch transporter activitysearch calcium ion bindingsearch kinase bindingsearch calcium-dependent protein bindingsearch protein kinase inhibitor activitysearch cytosolsearch cytoplasmsearch plasma membranesearch Golgi membranesearch cytoskeletonsearch nucleussearch membranesearch microtubule cytoskeletonsearch endoplasmic reticulum-Golgi intermediate compartmentsearch focal adhesionsearch transport vesiclesearch extracellular vesicular exosomesearch endoplasmic reticulumsearch

Chain InterPro annotation
A, B EF-hand domainsearch EF-hand domain pairsearch EF-Hand 1, calcium-binding sitesearch