Calcineurin B homologous protein 1

Details

Name
Calcineurin B homologous protein 1
Synonyms
  • Calcineurin B-like protein
  • Calcium-binding protein CHP
  • Calcium-binding protein p22
  • CHP
  • EF-hand calcium-binding domain-containing protein p22
Gene Name
CHP1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0049480|Calcineurin B homologous protein 1
MGSRASTLLRDEELEEIKKETGFSHSQITRLYSRFTSLDKGENGTLSREDFQRIPELAIN
PLGDRIINAFFPEGEDQVNFRGFMRTLAHFRPIEDNEKSKDVNGPEPLNSRSNKLHFAFR
LYDLDKDEKISRDELLQVLRMMVGVNISDEQLGSIADRTIQEADQDGDSAISFTEFVKVL
EKVDVEQKMSIRFLH
Number of residues
195
Molecular Weight
22455.96
Theoretical pI
Not Available
GO Classification
Functions
calcium ion binding / calcium-dependent protein binding / kinase binding / microtubule binding / potassium channel regulator activity / protein kinase inhibitor activity / transporter activity
Processes
calcium ion regulated exocytosis / cellular response to acidic pH / cytoplasmic microtubule organization / hyaluronan catabolic process / membrane docking / membrane fusion / membrane organization / microtubule bundle formation / negative regulation of calcineurin-NFAT signaling cascade / negative regulation of NF-kappaB transcription factor activity / negative regulation of phosphatase activity / negative regulation of protein autophosphorylation / negative regulation of protein import into nucleus / negative regulation of protein kinase activity / negative regulation of protein phosphorylation / negative regulation of protein ubiquitination / positive regulation of protein glycosylation / positive regulation of protein targeting to membrane / positive regulation of protein transport / positive regulation of sodium / potassium ion transport / protein export from nucleus / protein oligomerization / protein stabilization / regulation of intracellular pH / regulation of neuron death / small GTPase mediated signal transduction
Components
cytoplasm / cytosol / endoplasmic reticulum / endoplasmic reticulum-Golgi intermediate compartment / extracellular exosome / focal adhesion / Golgi membrane / microtubule cytoskeleton / nucleus / plasma membrane / transport vesicle
General Function
Calcium-binding protein involved in different processes such as regulation of vesicular trafficking, plasma membrane Na(+)/H(+) exchanger and gene transcription. Involved in the constitutive exocytic membrane traffic. Mediates the association between microtubules and membrane-bound organelles of the endoplasmic reticulum and Golgi apparatus and is also required for the targeting and fusion of transcytotic vesicles (TCV) with the plasma membrane. Functions as an integral cofactor in cell pH regulation by controlling plasma membrane-type Na(+)/H(+) exchange activity. Affects the pH sensitivity of SLC9A1/NHE1 by increasing its sensitivity at acidic pH. Required for the stabilization and localization of SLC9A1/NHE1 at the plasma membrane. Inhibits serum- and GTPase-stimulated Na(+)/H(+) exchange. Plays a role as an inhibitor of ribosomal RNA transcription by repressing the nucleolar UBF1 transcriptional activity. May sequester UBF1 in the nucleoplasm and limit its translocation to the nucleolus. Associates to the ribosomal gene promoter. Acts as a negative regulator of the calcineurin/NFAT signaling pathway. Inhibits NFAT nuclear translocation and transcriptional activity by suppressing the calcium-dependent calcineurin phosphatase activity. Also negatively regulates the kinase activity of the apoptosis-induced kinase STK17B. Inhibits both STK17B auto- and substrate-phosphorylations in a calcium-dependent manner.
Specific Function
Calcium ion binding
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Nucleus
Gene sequence
>lcl|BSEQ0049481|Calcineurin B homologous protein 1 (CHP1)
ATGGGTTCTCGGGCCTCCACGTTACTGCGGGACGAAGAGCTCGAGGAGATCAAGAAGGAG
ACCGGCTTTTCCCACAGTCAAATCACTCGCCTCTACAGCCGGTTCACCAGCCTGGACAAA
GGAGAGAATGGGACTCTCAGCCGGGAAGATTTCCAGAGGATTCCAGAACTTGCCATCAAC
CCACTGGGGGACCGGATCATCAATGCCTTCTTTCCAGAGGGAGAGGACCAGGTAAACTTC
CGTGGATTCATGCGAACTTTGGCTCATTTCCGCCCCATTGAGGATAATGAAAAGAGCAAA
GATGTGAATGGACCCGAACCACTCAACAGCCGAAGCAACAAACTGCACTTTGCTTTTCGA
CTATATGATTTGGATAAAGATGAAAAGATCTCCCGTGATGAGCTGTTACAGGTGCTACGC
ATGATGGTCGGAGTAAATATCTCAGATGAGCAGCTGGGCAGCATCGCAGACAGGACCATT
CAGGAGGCTGATCAGGATGGGGACAGTGCCATATCTTTCACAGAATTTGTTAAGGTTTTG
GAGAAGGTGGATGTAGAACAGAAAATGAGCATCCGATTTCTTCACTAA
Chromosome Location
15
Locus
15q15.1
External Identifiers
ResourceLink
UniProtKB IDQ99653
UniProtKB Entry NameCHP1_HUMAN
HGNC IDHGNC:17433
General References
  1. Lin X, Barber DL: A calcineurin homologous protein inhibits GTPase-stimulated Na-H exchange. Proc Natl Acad Sci U S A. 1996 Oct 29;93(22):12631-6. [Article]
  2. 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 TO, 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: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [Article]
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  4. Lin X, Sikkink RA, Rusnak F, Barber DL: Inhibition of calcineurin phosphatase activity by a calcineurin B homologous protein. J Biol Chem. 1999 Dec 17;274(51):36125-31. [Article]
  5. Pang T, Su X, Wakabayashi S, Shigekawa M: Calcineurin homologous protein as an essential cofactor for Na+/H+ exchangers. J Biol Chem. 2001 May 18;276(20):17367-72. Epub 2001 Feb 28. [Article]
  6. Pang T, Hisamitsu T, Mori H, Shigekawa M, Wakabayashi S: Role of calcineurin B homologous protein in pH regulation by the Na+/H+ exchanger 1: tightly bound Ca2+ ions as important structural elements. Biochemistry. 2004 Mar 30;43(12):3628-36. [Article]
  7. Jimenez-Vidal M, Srivastava J, Putney LK, Barber DL: Nuclear-localized calcineurin homologous protein CHP1 interacts with upstream binding factor and inhibits ribosomal RNA synthesis. J Biol Chem. 2010 Nov 19;285(47):36260-6. doi: 10.1074/jbc.M110.165555. Epub 2010 Aug 18. [Article]
  8. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  9. Zhou H, Di Palma S, Preisinger C, Peng M, Polat AN, Heck AJ, Mohammed S: Toward a comprehensive characterization of a human cancer cell phosphoproteome. J Proteome Res. 2013 Jan 4;12(1):260-71. doi: 10.1021/pr300630k. Epub 2012 Dec 18. [Article]
  10. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
  11. Thinon E, Serwa RA, Broncel M, Brannigan JA, Brassat U, Wright MH, Heal WP, Wilkinson AJ, Mann DJ, Tate EW: Global profiling of co- and post-translationally N-myristoylated proteomes in human cells. Nat Commun. 2014 Sep 26;5:4919. doi: 10.1038/ncomms5919. [Article]
  12. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [Article]
  13. Mishima M, Wakabayashi S, Kojima C: Solution structure of the cytoplasmic region of Na+/H+ exchanger 1 complexed with essential cofactor calcineurin B homologous protein 1. J Biol Chem. 2007 Jan 26;282(4):2741-51. Epub 2006 Oct 18. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB11093Calcium citrateapproved, investigationalunknownagonistDetails
DB11348Calcium PhosphateapprovedunknownagonistDetails
DB14481Calcium phosphate dihydrateapprovedunknownDetails