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Showing Protein Chromogranin-A (HMDBP07615)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 2 metabolites
Identification
HMDB Protein ID HMDBP07615
Secondary Accession Numbers
  • 13324
Name Chromogranin-A
Synonyms
  1. AL-11
  2. CgA
  3. EA-92
  4. ER-37
  5. ES-43
  6. GR-44
  7. GV-19
  8. LF-19
  9. Pancreastatin
  10. Pituitary secretory protein I
  11. SP-I
  12. SS-18
  13. Vasostatin I
  14. Vasostatin II
  15. Vasostatin-1
  16. Vasostatin-2
  17. WA-8
  18. WE-14
Gene Name CHGA
Protein Type Unknown
Biological Properties
General Function Involved in regulation of blood pressure
Specific Function Pancreastatin strongly inhibits glucose induced insulin release from the pancreas
Pathways Not Available
Reactions Not Available
GO Classification Not Available
Cellular Location
  1. Secreted
Gene Properties
Chromosome Location Chromosome:1
Locus 14q32
SNPs CHGA
Gene Sequence 
>1374 bp
ATGCGCTCCGCCGCTGTCCTGGCTCTTCTGCTCTGCGCCGGGCAAGTCACTGCGCTCCCT
GTGAACAGCCCTATGAATAAAGGGGATACCGAGGTGATGAAATGCATCGTTGAGGTCATC
TCCGACACACTTTCCAAGCCCAGCCCCATGCCTGTCAGCCAGGAATGTTTTGAGACACTC
CGAGGAGATGAACGGATCCTTTCCATTCTGAGACATCAGAATTTACTGAAGGAGCTCCAA
GACCTCGCTCTCCAAGGCGCCAAGGAGAGGGCACATCAGCAGAAGAAACACAGCGGTTTT
GAAGATGAACTCTCAGAGGTTCTTGAGAACCAGAGCAGCCAGGCCGAGCTGAAAGAGGCG
GTGGAAGAGCCATCATCCAAGGATGTTATGGAGAAAAGAGAGGATTCCAAGGAGGCAGAG
AAAAGTGGTGAAGCCACAGACGGAGCCAGGCCCCAGGCCCTCCCGGAGCCCATGCAGGAG
TCCAAGGCTGAGGGGAACAATCAGGCCCCTGGGGAGGAAGAGGAGGAGGAGGAGGAGGCC
ACCAACACCCACCCTCCAGCCAGCCTCCCCAGCCAGAAATACCCAGGCCCACAGGCCGAG
GGGGACAGTGAGGGCCTCTCTCAGGGTCTGGTGGACAGAGAGAAGGGCCTGAGTGCAGAG
CCAGGGTGGCAGGCAAAGAGAGAAGAGGAGGAGGAGGAGGAGGAGGAGGCTGAGGCTGGA
GAGGAGGCTGTCCCCGAGGAAGAAGGCCCCACTGTAGTGCTGAACCCCCACCCGAGCCTT
GGCTACAAGGACATCCGGAAAGGCGAGAGTCGGTCGGAGGCTCTGGCTGTGGATGGAGCT
GGGAAGCCTGGGGCTGAGGAGGCTCAGGACCCCGAAGGGAAGGGAGAACAGGAGCACTCC
CAGCAGAAAGAGGAGGAGGAGGAGATGGCAGTGGTCCCGCAAGGCCTCTTCCGGGGTGGG
AAGAGCGGAGAGCTGGAGCAGGAGGAGGAGCGGCTCTCCAAGGAGTGGGAGGACTCCAAA
CGCTGGAGCAAGATGGACCAGCTGGCCAAGGAGCTGACGGCTGAGAAGCGGCTGGAGGGG
CAGGAGGAGGAGGAGGACAACCGGGACAGTTCCATGAAGCTCTCCTTCCGGGCCCGGGCC
TACGGCTTCAGGGGCCCTGGGCCGCAGCTGCGACGAGGCTGGAGGCCATCCTCCCGGGAG
GACAGCCTTGAGGCGGGCCTGCCCCTCCAGGTCCGAGGCTACCCCGAGGAGAAGAAAGAG
GAGGAGGGCAGCGCAAACCGCAGACCAGAGGACCAGGAGCTGGAGAGCCTGTCGGCCATT
GAGGCAGAGCTGGAGAAAGTGGCCCACCAGCTGCAGGCACTACGGCGGGGCTGA
Protein Properties
Number of Residues 457
Molecular Weight 50688.1
Theoretical pI 4.27
Pfam Domain Function
Signals
  • 1-18
Transmembrane Regions
  • None
Protein Sequence 
>Chromogranin-A
MRSAAVLALLLCAGQVTALPVNSPMNKGDTEVMKCIVEVISDTLSKPSPMPVSQECFETL
RGDERILSILRHQNLLKELQDLALQGAKERAHQQKKHSGFEDELSEVLENQSSQAELKEA
VEEPSSKDVMEKREDSKEAEKSGEATDGARPQALPEPMQESKAEGNNQAPGEEEEEEEEA
TNTHPPASLPSQKYPGPQAEGDSEGLSQGLVDREKGLSAEPGWQAKREEEEEEEEEAEAG
EEAVPEEEGPTVVLNPHPSLGYKEIRKGESRSEALAVDGAGKPGAEEAQDPEGKGEQEHS
QQKEEEEEMAVVPQGLFRGGKSGELEQEEERLSKEWEDSKRWSKMDQLAKELTAEKRLEG
QEEEEDNRDSSMKLSFRARAYGFRGPGPQLRRGWRPSSREDSLEAGLPLQVRGYPEEKKE
EEGSANRRPEDQELESLSAIEAELEKVAHQLQALRRG
GenBank ID Protein 62898323
UniProtKB/Swiss-Prot ID P10645
UniProtKB/Swiss-Prot Entry Name CMGA_HUMAN
PDB IDs
GenBank Gene ID AK223381
GeneCard ID CHGA
GenAtlas ID CHGA
HGNC ID HGNC:1929
References
General References
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  3. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed:12508121 ]
  4. Nilsson J, Ruetschi U, Halim A, Hesse C, Carlsohn E, Brinkmalm G, Larson G: Enrichment of glycopeptides for glycan structure and attachment site identification. Nat Methods. 2009 Nov;6(11):809-11. doi: 10.1038/nmeth.1392. Epub 2009 Oct 18. [PubMed:19838169 ]
  5. Beranova-Giorgianni S, Zhao Y, Desiderio DM, Giorgianni F: Phosphoproteomic analysis of the human pituitary. Pituitary. 2006;9(2):109-20. [PubMed:16807684 ]
  6. Giorgianni F, Beranova-Giorgianni S, Desiderio DM: Identification and characterization of phosphorylated proteins in the human pituitary. Proteomics. 2004 Mar;4(3):587-98. [PubMed:14997482 ]
  7. Konecki DS, Benedum UM, Gerdes HH, Huttner WB: The primary structure of human chromogranin A and pancreastatin. J Biol Chem. 1987 Dec 15;262(35):17026-30. [PubMed:2445752 ]
  8. Helman LJ, Ahn TG, Levine MA, Allison A, Cohen PS, Cooper MJ, Cohn DV, Israel MA: Molecular cloning and primary structure of human chromogranin A (secretory protein I) cDNA. J Biol Chem. 1988 Aug 15;263(23):11559-63. [PubMed:3403545 ]
  9. Mouland AJ, Bevan S, White JH, Hendy GN: Human chromogranin A gene. Molecular cloning, structural analysis, and neuroendocrine cell-specific expression. J Biol Chem. 1994 Mar 4;269(9):6918-26. [PubMed:8120054 ]
  10. Wilson BS, Phan SH, Lloyd RV: Chromogranin from normal human adrenal glands: purification by monoclonal antibody affinity chromatography and partial N-terminal amino acid sequence. Regul Pept. 1986 Feb;13(3-4):207-23. [PubMed:3704195 ]
  11. Tamamura H, Ohta M, Yoshizawa K, Ono Y, Funakoshi A, Miyasaka K, Tateishi K, Jimi A, Yajima H, Fujii N, et al.: Isolation and characterization of a tumor-derived human protein related to chromogranin A and its in vitro conversion to human pancreastatin-48. Eur J Biochem. 1990 Jul 20;191(1):33-9. [PubMed:2165909 ]
  12. Sekiya K, Ghatei MA, Minamino N, Bretherton-Watt D, Matsuo H, Bloom SR: Isolation of human pancreastatin fragment containing the active sequence from a glucagonoma. FEBS Lett. 1988 Feb 8;228(1):153-6. [PubMed:2830133 ]
  13. Curry WJ, Shaw C, Johnston CF, Thim L, Buchanan KD: Isolation and primary structure of a novel chromogranin A-derived peptide, WE-14, from a human midgut carcinoid tumour. FEBS Lett. 1992 Apr 27;301(3):319-21. [PubMed:1577173 ]
  14. Orr DF, Chen T, Johnsen AH, Chalk R, Buchanan KD, Sloan JM, Rao P, Shaw C: The spectrum of endogenous human chromogranin A-derived peptides identified using a modified proteomic strategy. Proteomics. 2002 Nov;2(11):1586-600. [PubMed:12442257 ]
  15. Gadroy P, Stridsberg M, Capon C, Michalski JC, Strub JM, Van Dorsselaer A, Aunis D, Metz-Boutigue MH: Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors. J Biol Chem. 1998 Dec 18;273(51):34087-97. [PubMed:9852066 ]
  16. Preece NE, Nguyen M, Mahata M, Mahata SK, Mahapatra NR, Tsigelny I, O'Connor DT: Conformational preferences and activities of peptides from the catecholamine release-inhibitory (catestatin) region of chromogranin A. Regul Pept. 2004 Apr 15;118(1-2):75-87. [PubMed:14759560 ]
  17. Wen G, Mahata SK, Cadman P, Mahata M, Ghosh S, Mahapatra NR, Rao F, Stridsberg M, Smith DW, Mahboubi P, Schork NJ, O'Connor DT, Hamilton BA: Both rare and common polymorphisms contribute functional variation at CHGA, a regulator of catecholamine physiology. Am J Hum Genet. 2004 Feb;74(2):197-207. Epub 2004 Jan 12. [PubMed:14740315 ]