Hmdb loader
Identification
HMDB Protein ID HMDBP07584
Secondary Accession Numbers
  • 13292
Name Calcium homeostasis endoplasmic reticulum protein
Synonyms
  1. ERPROT 213-21
  2. SR-related CTD-associated factor 6
Gene Name CHERP
Protein Type Unknown
Biological Properties
General Function Involved in nucleic acid binding
Specific Function Involved in calcium homeostasis, growth and proliferation
Pathways Not Available
Reactions Not Available
GO Classification
Component
cell part
intracellular
Function
binding
nucleic acid binding
rna binding
Process
rna metabolic process
metabolic process
macromolecule metabolic process
cellular macromolecule metabolic process
rna processing
Cellular Location
  1. Cytoplasm
  2. Cytoplasm
  3. perinuclear region
  4. Endoplasmic reticulum
Gene Properties
Chromosome Location Chromosome:1
Locus 19p13.1
SNPs CHERP
Gene Sequence
>2751 bp
ATGGAGATGCCGCTGCCCCCCGATGACCAGGAGCTTCGAAATGTCATCGACAAGCTCGCC
CAGTTCGTGGCTCGCAATGGGCCCGAGTTTGAGAAGATGACTATGGAGAAGCAGAAGGAC
AACCCCAAATTCTCGTTTCTTTTCGGAGGCGAATTCTACAGTTACTACAAGTGCAAGCTG
GCGCTGGAGCAGCAGCAGCTCATCTGCAAGCAGCAGACCCCGGAGCTGGAGCCAGCCGCC
ACCATGCCACCCCTGCCACAGCCCCCGCTGGCCCCCGCCGCGCCCATCCCGCCGGCCCAG
GGCGCGCCATCCATGGACGAGCTCATCCAGCAGAGCCAGTGGAACCTCCAGCAGCAGGAG
CAGCACTTGCTGGCGCTCAGACAGGAGCAAGTGACAGCGGCCGTGGCCCACGCGGTGGAG
CAGCAGATGCAGAAGCTTCTGGAGGAGACCCAGCTAGACATGAACGAGTTTGACAACCTC
CTGCAGCCCATCATCGACACGTGCACCAAGGACGCCATCTCGGCCGGGAAGAACTGGATG
TTCAGCAATGCCAAGTCCCCGCCGCACTGTGAGCTGATGGCCGGCCACCTCCGGAACCGC
ATCACGGCTGATGGGGCACACTTCGAGCTGCGGCTGCACCTCATCTACCTGATCAATGAC
GTGCTGCACCACTGCCAGCGCAAGCAGGCCCGGGAGCTGCTGGCCGCCCTGCAGAAGGTC
GTGGTGCCCATCTACTGCACCAGCTTCTTGGCCGTGGAGGAAGACAAGCAGCAGAAGATC
GCCCGGCTCCTGCAGCTCTGGGAGAAAAACGGCTACTTCGATGACTCCATCATTCAGCAG
CTACAGAGCCCAGCCCTGGGGCTTGGTCAGTACCAGGCCACCCTCATCAACGAGTACTCC
TCAGTGGTCCAGCCGGTGCAGCTGGCCTTCCAGCAGCAGATCCAGACCCTCAAGACGCAG
CACGAGGAGTTTGTCACCAGCCTGGCCCAGCAGCAGCAGCAGCAGCAACAGCAGCAGCAG
CAGCTCCAGATGCCGCAGATGGAGGCTGAAGTCAAGGCCACGCCTCCACCGCCTGCTCCA
CCCCCGGCCCCAGCACCTGCCCCTGCCATCCCGCCCACCACCCAGCCTGATGACAGCAAG
CCTCCCATCCAGATGCCTGGCTCTTCAGAGTACGAAGCTCCAGGAGGGGTCCAGGATCCT
GCAGCTGCCGGCCCCCGGGGCCCCGGGCCACACGACCAGATCCCACCAAACAAGCCCCCT
TGGTTTGACCAGCCTCACCCCGTGGCTCCTTGGGGCCAGCAGCAGCCGCCAGAGCAGCCA
CCCTACCCGCACCACCAGGGCGGCCCACCCCACTGCCCCCCCTGGAACAACAGCCATGAG
GGCATGTGGGGCGAGCAGCGCGGTGACCCCGGCTGGAACGGCCAGCGCGACGCGCCCTGG
AACAACCAGCCCGACGCCGCCTGGAACAGCCAGTTCGAGGGCCCCTGGAACAGCCAGCAC
GAGCAGCCGCCCTGGGGCGGGGGCCAGCGCGAGCCACCCTTCCGCATGCAGCGGCCCCCA
CACTTCCGGGGGCCCTTCCCGCCCCACCAGCAGCACCCGCAGTTCAACCAGCCTCCGCAC
CCCCACAACTTCAACCGCTTCCCGCCCCGCTTCATGCAGGACGACTTCCCGCCACGGCAC
CCCTTCGAGCGGCCGCCCTATCCCCACCGCTTCGACTACCCCCAGGGGGACTTCCCTGCC
GAAATGGGGCCCCCTCACCACCACCCTGGCCACCGCATGCCTCATCCTGGCATCAACGAG
CACCCGCCTTGGGCTGGACCCCAGCACCCTGACTTCGGCCCTCCCCCCCATGGCTTCAAC
GGGCAGCCCCCACACATGCGGCGACAGGGCCCACCCCACATCAACCACGATGACCCCAGC
CTGGTCCCCAATGTGCCCTACTTCGATCTCCCTGCTGGGCTGATGGCCCCCCTCGTGAAG
CTGGAAGATCACGAGTACAAGCCTTTGGACCCTAAAGACATCCGCCTCCCACCCCCCATG
CCGCCCAGCGAGAGGCTGCTGGCTGCAGTGGAGGCCTTCTACAGCCCCCCGTCCCACGAC
AGGCCCAGGAACAGTGAAGGCTGGGAGCAGAACGGCCTCTATGAGTTCTTCCGAGCAAAA
ATGCGGGCCCGGCGGAGGAAAGGCCAGGAGAAGAGGAACAGCGGACCCTCGAGGTCTCGG
AGCAGATCCAAGAGTCGAGGGCGTTCTTCCTCCCGCTCCAACTCAAGATCCTCCAAGTCT
TCAGGCTCGTACTCAAGGTCAAGGTCGCGCTCCTGCTCCCGTTCCTACTCCCGCTCCAGA
TCTAGAAGTCGGAGCAGGTCGCGCTCCTCCAGAAGCCGCTCCCGGTCCCAGTCGCGGTCC
CGGTCCAAGTCGTACTCCCCAGGAAGAAGACGCCGGTCACGGTCCAGGAGCCCCACCCCG
CCTTCCTCTGCTGGTCTGGGTTCTAATTCGGCGCCTCCCATCCCTGACTCAAGGCTCGGA
GAAGAGAACAAAGGCCATCAGATGCTGGTGAAGATGGGCTGGAGCGGCTCAGGCGGCCTC
GGTGCGAAGGAGCAAGGGATCCAGGACCCCATCAAGGGCGGGGACGTCCGGGATAAGTGG
GACCAGTATAAAGGCGTGGGCGTGGCTCTGGATGACCCCTATGAGAACTACCGCAGGAAC
AAGAGCTACTCCTTCATCGCCCGCATGAAGGCCAGGGACGAGTGTAAGTAG
Protein Properties
Number of Residues 916
Molecular Weight 103701.6
Theoretical pI 9.39
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Calcium homeostasis endoplasmic reticulum protein
MEMPLPPDDQELRNVIDKLAQFVARNGPEFEKMTMEKQKDNPKFSFLFGGEFYSYYKCKL
ALEQQQLICKQQTPELEPAATMPPLPQPPLAPAAPIPPAQGAPSMDELIQQSQWNLQQQE
QHLLALRQEQVTAAVAHAVEQQMQKLLEETQLDMNEFDNLLQPIIDTCTKDAISAGKNWM
FSNAKSPPHCELMAGHLRNRITADGAHFELRLHLIYLINDVLHHCQRKQARELLAALQKV
VVPIYCTSFLAVEEDKQQKIARLLQLWEKNGYFDDSIIQQLQSPALGLGQYQATLINEYS
SVVQPVQLAFQQQIQTLKTQHEEFVTSLAQQQQQQQQQQQQLQMPQMEAEVKATPPPPAP
PPAPAPAPAIPPTTQPDDSKPPIQMPGSSEYEAPGGVQDPAAAGPRGPGPHDQIPPNKPP
WFDQPHPVAPWGQQQPPEQPPYPHHQGGPPHCPPWNNSHEGMWGEQRGDPGWNGQRDAPW
NNQPDAAWNSQFEGPWNSQHEQPPWGGGQREPPFRMQRPPHFRGPFPPHQQHPQFNQPPH
PHNFNRFPPRFMQDDFPPRHPFERPPYPHRFDYPQGDFPAEMGPPHHHPGHRMPHPGINE
HPPWAGPQHPDFGPPPHGFNGQPPHMRRQGPPHINHDDPSLVPNVPYFDLPAGLMAPLVK
LEDHEYKPLDPKDIRLPPPMPPSERLLAAVEAFYSPPSHDRPRNSEGWEQNGLYEFFRAK
MRARRRKGQEKRNSGPSRSRSRSKSRGRSSSRSNSRSSKSSGSYSRSRSRSCSRSYSRSR
SRSRSRSRSSRSRSRSQSRSRSKSYSPGRRRRSRSRSPTPPSSAGLGSNSAPPIPDSRLG
EENKGHQMLVKMGWSGSGGLGAKEQGIQDPIKGGDVRDKWDQYKGVGVALDDPYENYRRN
KSYSFIARMKARDECK
GenBank ID Protein 119226260
UniProtKB/Swiss-Prot ID Q8IWX8
UniProtKB/Swiss-Prot Entry Name CHERP_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_006387.5
GeneCard ID CHERP
GenAtlas ID CHERP
HGNC ID HGNC:16930
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  4. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  5. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  6. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed:15057824 ]
  7. Imbert G, Saudou F, Yvert G, Devys D, Trottier Y, Garnier JM, Weber C, Mandel JL, Cancel G, Abbas N, Durr A, Didierjean O, Stevanin G, Agid Y, Brice A: Cloning of the gene for spinocerebellar ataxia 2 reveals a locus with high sensitivity to expanded CAG/glutamine repeats. Nat Genet. 1996 Nov;14(3):285-91. [PubMed:8896557 ]
  8. Laplante JM, O'Rourke F, Lu X, Fein A, Olsen A, Feinstein MB: Cloning of human Ca2+ homoeostasis endoplasmic reticulum protein (CHERP): regulated expression of antisense cDNA depletes CHERP, inhibits intracellular Ca2+ mobilization and decreases cell proliferation. Biochem J. 2000 May 15;348 Pt 1:189-99. [PubMed:10794731 ]
  9. O'Rourke F, Soons K, Flaumenhauft R, Watras J, Baio-Larue C, Matthews E, Feinstein MB: Ca2+ release by inositol 1,4,5-trisphosphate is blocked by the K(+)-channel blockers apamin and tetrapentylammonium ion, and a monoclonal antibody to a 63 kDa membrane protein: reversal of blockade by K+ ionophores nigericin and valinomycin and purification of the 63 kDa antibody-binding protein. Biochem J. 1994 Jun 15;300 ( Pt 3):673-83. [PubMed:8010949 ]
  10. O'Rourke FA, LaPlante JM, Feinstein MB: Antisense-mediated loss of calcium homoeostasis endoplasmic reticulum protein (CHERP; ERPROT213-21) impairs Ca2+ mobilization, nuclear factor of activated T-cells (NFAT) activation and cell proliferation in Jurkat T-lymphocytes. Biochem J. 2003 Jul 1;373(Pt 1):133-43. [PubMed:12656674 ]