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P10645 (CMGA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chromogranin-A

Short name=CgA
Alternative name(s):
Pituitary secretory protein I
Short name=SP-I

Cleaved into the following 13 chains:

  1. Vasostatin-1
    Alternative name(s):
    Vasostatin I
  2. Vasostatin-2
    Alternative name(s):
    Vasostatin II
  3. EA-92
  4. ES-43
  5. Pancreastatin
  6. SS-18
  7. WA-8
  8. WE-14
  9. LF-19
  10. AL-11
  11. GV-19
  12. GR-44
  13. ER-37
Gene names
Name:CHGA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length457 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Pancreastatin strongly inhibits glucose induced insulin release from the pancreas.

Subunit structure

Interacts with SCG3 By similarity.

Subcellular location

Cytoplasmic vesiclesecretory vesicle lumen By similarity. Cytoplasmic vesiclesecretory vesicle membrane By similarity. Secreted. Note: Associated with the secretory granule membrane through direct interaction to SCG3 that in turn binds to cholesterol-enriched lipid rafts in intragranular conditions By similarity.

Post-translational modification

Sulfated on tyrosine residues and/or contains sulfated glycans.

O-glycosylated with core 1 or possibly core 8 glycans. Ref.16 Ref.20

Miscellaneous

Binds calcium with a low-affinity.

Sequence similarities

Belongs to the chromogranin/secretogranin protein family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.11
Chain19 – 457439Chromogranin-A
PRO_0000005408
Peptide19 – 131113Vasostatin-2
PRO_0000005409
Peptide19 – 9476Vasostatin-1
PRO_0000005410
Peptide134 – 22592EA-92
PRO_0000005411
Peptide228 – 26033ES-43
PRO_0000005412
Peptide272 – 31948Pancreastatin
PRO_0000005413
Peptide322 – 33918SS-18
PRO_0000005414
Peptide342 – 35514WE-14 Ref.14
PRO_0000005415
Peptide342 – 3498WA-8
PRO_0000005416
Peptide358 – 37619LF-19
PRO_0000005417
Peptide380 – 39011AL-11
PRO_0000005418
Peptide393 – 41119GV-19
PRO_0000005419
Peptide413 – 45644GR-44
PRO_0000005420
Peptide420 – 45637ER-37
PRO_0000005421

Regions

Region41 – 5919O-glycosylated at one site only in cerebrospinal fluid
Region181 – 19111O-glycosylated at one site only in cerebrospinal fluid

Amino acid modifications

Modified residue1421Phosphoserine By similarity
Modified residue1941Phosphotyrosine By similarity
Modified residue2031Phosphoserine Ref.18
Modified residue2181Phosphoserine Ref.16
Modified residue2701Phosphoserine Ref.16
Modified residue3001Phosphoserine Ref.18
Modified residue3191Glycine amide Ref.12 Ref.13
Modified residue3221Phosphoserine Ref.17 Ref.18
Modified residue3331Phosphoserine Ref.16
Modified residue3981Phosphoserine By similarity
Modified residue4021Phosphoserine Ref.18
Modified residue4561Arginine amide Ref.15
Glycosylation1811O-linked (GalNAc...) Ref.16
CAR_000116
Glycosylation1831O-linked (GalNAc...) Ref.16
CAR_000117
Glycosylation2511O-linked (GalNAc...) Ref.16
CAR_000118
Disulfide bond35 ↔ 56 Ref.1

Natural variations

Natural variant611R → Q.
Corresponds to variant rs3742712 [ dbSNP | Ensembl ].
VAR_047417
Natural variant1761E → K.
Corresponds to variant rs9658654 [ dbSNP | Ensembl ].
VAR_025636
Natural variant2641E → D. Ref.7
Corresponds to variant rs9658655 [ dbSNP | Ensembl ].
VAR_025637
Natural variant2711R → W.
Corresponds to variant rs9658662 [ dbSNP | Ensembl ].
VAR_025638
Natural variant2741A → G.
Corresponds to variant rs9658663 [ dbSNP | Ensembl ].
VAR_025639
Natural variant3151G → S.
Corresponds to variant rs9658664 [ dbSNP | Ensembl ].
VAR_025640
Natural variant3321L → P.
Corresponds to variant rs9658665 [ dbSNP | Ensembl ].
VAR_025641
Natural variant3691D → N.
Corresponds to variant rs2228575 [ dbSNP | Ensembl ].
VAR_025642
Natural variant3821G → S Reduces activity 4.7 fold. Ref.22
Corresponds to variant rs9658667 [ dbSNP | Ensembl ].
VAR_025643
Natural variant3881P → L Increases activity 2.3 fold. Ref.22
Corresponds to variant rs9658668 [ dbSNP | Ensembl ].
VAR_025644
Natural variant3991R → W. Ref.1 Ref.3 Ref.6
Corresponds to variant rs729940 [ dbSNP | Ensembl ].
VAR_025645

Experimental info

Sequence conflict411S → Y in AAA52018. Ref.1
Sequence conflict541Q → K in AAA52018. Ref.1
Sequence conflict871A → R in AAA52018. Ref.1
Sequence conflict1191E → Q in AAA52018. Ref.1
Sequence conflict1671N → K in AAA52018. Ref.1
Sequence conflict2001E → K in AAA52018. Ref.1
Sequence conflict2191A → V in AAA52018. Ref.1
Sequence conflict339 – 3402SK → TN in AAA52018. Ref.1
Sequence conflict3701S → R in AAA52018. Ref.1
Sequence conflict3731K → R in AAA52018. Ref.1
Sequence conflict3801A → G in AAA52018. Ref.1
Sequence conflict3941W → S in AAA52018. Ref.1
Sequence conflict3971S → N in AAA52018. Ref.1
Sequence conflict4161E → Q in AAA52018. Ref.1

Secondary structure

..... 457
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10645 [UniParc].

Last modified November 25, 2008. Version 7.
Checksum: 2F634E1A83FF0BB1

FASTA45750,688
        10         20         30         40         50         60 
MRSAAVLALL LCAGQVTALP VNSPMNKGDT EVMKCIVEVI SDTLSKPSPM PVSQECFETL 

        70         80         90        100        110        120 
RGDERILSIL RHQNLLKELQ DLALQGAKER AHQQKKHSGF EDELSEVLEN QSSQAELKEA 

       130        140        150        160        170        180 
VEEPSSKDVM EKREDSKEAE KSGEATDGAR PQALPEPMQE SKAEGNNQAP GEEEEEEEEA 

       190        200        210        220        230        240 
TNTHPPASLP SQKYPGPQAE GDSEGLSQGL VDREKGLSAE PGWQAKREEE EEEEEEAEAG 

       250        260        270        280        290        300 
EEAVPEEEGP TVVLNPHPSL GYKEIRKGES RSEALAVDGA GKPGAEEAQD PEGKGEQEHS 

       310        320        330        340        350        360 
QQKEEEEEMA VVPQGLFRGG KSGELEQEEE RLSKEWEDSK RWSKMDQLAK ELTAEKRLEG 

       370        380        390        400        410        420 
QEEEEDNRDS SMKLSFRARA YGFRGPGPQL RRGWRPSSRE DSLEAGLPLQ VRGYPEEKKE 

       430        440        450 
EEGSANRRPE DQELESLSAI EAELEKVAHQ LQALRRG 

« Hide

References

« Hide 'large scale' references
[1]"The primary structure of human chromogranin A and pancreastatin."
Konecki D.S., Benedum U.M., Gerdes H.-H., Huttner W.B.
J. Biol. Chem. 262:17026-17030(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], DISULFIDE BOND, VARIANT TRP-399.
[2]"Molecular cloning and primary structure of human chromogranin A (secretory protein I) cDNA."
Helman L.J., Ahn T.G., Levine M.A., Allison A., Cohen P.S., Cooper M.J., Cohn D.V., Israel M.A.
J. Biol. Chem. 263:11559-11563(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Human chromogranin A gene. Molecular cloning, structural analysis, and neuroendocrine cell-specific expression."
Mouland A.J., Bevan S., White J.H., Hendy G.N.
J. Biol. Chem. 269:6918-6926(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TRP-399.
Tissue: Liver.
[4]Mouland A.J., Bevan S., White J.H., Hendy G.N.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 384-397.
[5]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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 T.-O., 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT TRP-399.
Tissue: Stomach.
[7]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASP-264.
Tissue: Gastric mucosa.
[8]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., 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. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels 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.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"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].
Tissue: Brain.
[11]"Chromogranin from normal human adrenal glands: purification by monoclonal antibody affinity chromatography and partial N-terminal amino acid sequence."
Wilson B.S., Phan S.H., Lloyd R.V.
Regul. Pept. 13:207-223(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-46.
Tissue: Adrenal gland.
[12]"Isolation and characterization of a tumor-derived human protein related to chromogranin A and its in vitro conversion to human pancreastatin-48."
Tamamura H., Ohta M., Yoshizawa K., Ono Y., Funakoshi A., Miyasaka K., Tateishi K., Jimi A., Yajima H., Fujii N., Funakoshi S.
Eur. J. Biochem. 191:33-39(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 134-319, AMIDATION AT GLY-319.
Tissue: Pancreas.
[13]"Isolation of human pancreastatin fragment containing the active sequence from a glucagonoma."
Sekiya K., Ghatei M.A., Minamino N., Bretherton-Watt D., Matsuo H., Bloom S.R.
FEBS Lett. 228:153-156(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 291-319, AMIDATION AT GLY-319.
Tissue: Pancreas.
[14]"Isolation and primary structure of a novel chromogranin A-derived peptide, WE-14, from a human midgut carcinoid tumour."
Curry W.J., Shaw C., Johnston C.F., Thim L., Buchanan K.D.
FEBS Lett. 301:319-321(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 342-355.
[15]"The spectrum of endogenous human chromogranin A-derived peptides identified using a modified proteomic strategy."
Orr D.F., Chen T., Johnsen A.H., Chalk R., Buchanan K.D., Sloan J.M., Rao P., Shaw C.
Proteomics 2:1586-1600(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF DERIVED PEPTIDES, AMIDATION AT ARG-456 (PEPTIDE GR-44 AND PEPTIDE ER-37).
[16]"Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors."
Gadroy P., Stridsberg M., Capon C., Michalski J.-C., Strub J.-M., van Dorsselaer A., Aunis D., Metz-Boutigue M.-H.
J. Biol. Chem. 273:34087-34097(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT THR-181; THR-183 AND THR-251, PHOSPHORYLATION AT SER-218; SER-270 AND SER-333.
[17]"Identification and characterization of phosphorylated proteins in the human pituitary."
Giorgianni F., Beranova-Giorgianni S., Desiderio D.M.
Proteomics 4:587-598(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-322.
Tissue: Pituitary.
[18]"Phosphoproteomic analysis of the human pituitary."
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.
Pituitary 9:109-120(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-300; SER-322 AND SER-402, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Pituitary.
[19]"Enrichment of glycopeptides for glycan structure and attachment site identification."
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS], STRUCTURE OF CARBOHYDRATES.
Tissue: Cerebrospinal fluid.
[20]"LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins."
Halim A., Ruetschi U., Larson G., Nilsson J.
J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
[21]"Conformational preferences and activities of peptides from the catecholamine release-inhibitory (catestatin) region of chromogranin A."
Preece N.E., Nguyen M., Mahata M., Mahata S.K., Mahapatra N.R., Tsigelny I., O'Connor D.T.
Regul. Pept. 118:75-87(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 370-390.
[22]"Both rare and common polymorphisms contribute functional variation at CHGA, a regulator of catecholamine physiology."
Wen G., Mahata S.K., Cadman P., Mahata M., Ghosh S., Mahapatra N.R., Rao F., Stridsberg M., Smith D.W., Mahboubi P., Schork N.J., O'Connor D.T., Hamilton B.A.
Am. J. Hum. Genet. 74:197-207(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SER-382 AND LEU-388.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03483 mRNA. Translation: AAA52017.1.
J03915 mRNA. Translation: AAA52018.1.
U03749 expand/collapse EMBL AC list , U03742, U03743, U03744, U03748, U03745, U03746, U03747 Genomic DNA. Translation: AAB53685.1.
BT006869 mRNA. Translation: AAP35515.1.
AK223381 mRNA. Translation: BAD97101.1.
AL117192 Genomic DNA. No translation available.
AK313757 mRNA. Translation: BAG36496.1.
CH471061 Genomic DNA. Translation: EAW81505.1.
BC001059 mRNA. Translation: AAH01059.1.
BC006459 mRNA. Translation: AAH06459.1.
BC009384 mRNA. Translation: AAH09384.2.
BC012755 mRNA. Translation: AAH12755.2.
CCDSCCDS9906.1.
PIRA28468. A54376.
RefSeqNP_001266.1. NM_001275.3.
UniGeneHs.150793.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LV4NMR-A370-390[»]
ProteinModelPortalP10645.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107538. 6 interactions.
IntActP10645. 3 interactions.
MINTMINT-4846180.
STRING9606.ENSP00000216492.

PTM databases

PhosphoSiteP10645.
UniCarbKBP10645.

Polymorphism databases

DMDM215274270.

Proteomic databases

PaxDbP10645.
PRIDEP10645.

Protocols and materials databases

DNASU1113.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216492; ENSP00000216492; ENSG00000100604.
GeneID1113.
KEGGhsa:1113.
UCSCuc001ybc.4. human.

Organism-specific databases

CTD1113.
GeneCardsGC14P093389.
HGNCHGNC:1929. CHGA.
HPACAB000023.
CAB040544.
CAB055506.
CAB058688.
HPA017369.
MIM118910. gene.
neXtProtNX_P10645.
PharmGKBPA26461.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41926.
HOVERGENHBG001272.
InParanoidP10645.
OMAVNSPMNK.
OrthoDBEOG7V766Z.
PhylomeDBP10645.
TreeFamTF336596.

Gene expression databases

ArrayExpressP10645.
BgeeP10645.
CleanExHS_CHGA.
GenevestigatorP10645.

Family and domain databases

InterProIPR001819. Chromogranin_AB.
IPR018054. Chromogranin_CS.
IPR001990. Granin.
[Graphical view]
PANTHERPTHR10583. PTHR10583. 1 hit.
PfamPF01271. Granin. 2 hits.
[Graphical view]
PRINTSPR00659. CHROMOGRANIN.
PROSITEPS00422. GRANINS_1. 1 hit.
PS00423. GRANINS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCHGA. human.
EvolutionaryTraceP10645.
GeneWikiChromogranin_A.
GenomeRNAi1113.
NextBio4618.
PMAP-CutDBQ6NR84.
PROP10645.
SOURCESearch...

Entry information

Entry nameCMGA_HUMAN
AccessionPrimary (citable) accession number: P10645
Secondary accession number(s): B2R9E9 expand/collapse secondary AC list , Q53FA8, Q6NR84, Q96E84, Q96GL7, Q9BQB5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 158 of the entry and version 7 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM