Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Chromogranin-A

Gene

CHGA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Pancreastatin: Strongly inhibits glucose induced insulin release from the pancreas.
Catestatin: Inhibits catecholamine release from chromaffin cells and noradrenergic neurons by acting as a non-competitive nicotinic cholinergic antagonist (PubMed:15326220). Displays antibacterial activity against Gram-positive bacteria S.aureus and M.luteus, and Gram-negative bacteria E.coli and P.aeruginosa (PubMed:15723172 and PubMed:24723458). Can induce mast cell migration, degranulation and production of cytokines and chemokines (PubMed:21214543). Acts as a potent scavenger of free radicals in vitro (PubMed:24723458). May play a role in the regulation of cardiac function and blood pressure (PubMed:18541522).1 Publication4 Publications
Serpinin: Regulates granule biogenesis in endocrine cells by up-regulating the transcription of protease nexin 1 (SERPINE2) via a cAMP-PKA-SP1 pathway. This leads to inhibition of granule protein degradation in the Golgi complex which in turn promotes granule formation.By similarity

GO - Biological processi

  • defense response to fungus Source: UniProtKB-KW
  • defense response to Gram-negative bacterium Source: UniProtKB
  • defense response to Gram-positive bacterium Source: UniProtKB
  • innate immune response Source: UniProtKB
  • killing of cells of other organism Source: UniProtKB-KW
  • mast cell activation Source: UniProtKB
  • mast cell chemotaxis Source: UniProtKB
  • mast cell cytokine production Source: UniProtKB
  • mast cell degranulation Source: UniProtKB
  • negative regulation of catecholamine secretion Source: UniProtKB
  • positive regulation of dense core granule biogenesis Source: UniProtKB
  • regulation of blood pressure Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Fungicide

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Chromogranin-A
Short name:
CgA
Alternative name(s):
Pituitary secretory protein I
Short name:
SP-I
Cleaved into the following 18 chains:
Alternative name(s):
Vasostatin I
Alternative name(s):
Vasostatin II
Catestatin2 Publications
Alternative name(s):
SL211 Publication
GE-251 Publication
Gene namesi
Name:CHGA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componentsi: Chromosome 14, Unplaced

Organism-specific databases

HGNCiHGNC:1929. CHGA.

Subcellular locationi

Serpinin :
  • Secreted By similarity
  • Cytoplasmic vesiclesecretory vesicle By similarity

  • Note: Pyroglutaminated serpinin localizes to secretory vesicle.By similarity

GO - Cellular componenti

  • extracellular region Source: UniProtKB-SubCell
  • mast cell granule Source: GOC
  • perinuclear region of cytoplasm Source: UniProtKB
  • secretory granule Source: InterPro
  • transport vesicle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26461.

Polymorphism and mutation databases

BioMutaiCHGA.
DMDMi215274270.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18182 PublicationsAdd
BLAST
Chaini19 – 457439Chromogranin-APRO_0000005408Add
BLAST
Peptidei19 – 131113Vasostatin-21 PublicationPRO_0000005409Add
BLAST
Peptidei19 – 9476Vasostatin-11 PublicationPRO_0000005410Add
BLAST
Peptidei134 – 22592EA-921 PublicationPRO_0000005411Add
BLAST
Peptidei228 – 26033ES-431 PublicationPRO_0000005412Add
BLAST
Peptidei272 – 31948Pancreastatin1 PublicationPRO_0000005413Add
BLAST
Peptidei322 – 33918SS-181 PublicationPRO_0000005414Add
BLAST
Peptidei342 – 35514WE-141 PublicationPRO_0000005415Add
BLAST
Peptidei342 – 3498WA-81 PublicationPRO_0000005416
Peptidei358 – 37619LF-191 PublicationPRO_0000005417Add
BLAST
Peptidei370 – 39021Catestatin1 PublicationPRO_0000432682Add
BLAST
Peptidei380 – 39011AL-111 PublicationPRO_0000005418Add
BLAST
Peptidei393 – 41725GE-251 PublicationPRO_0000432683Add
BLAST
Peptidei393 – 41119GV-191 PublicationPRO_0000005419Add
BLAST
Peptidei413 – 45644GR-441 PublicationPRO_0000005420Add
BLAST
Peptidei420 – 45637ER-371 PublicationPRO_0000005421Add
BLAST
Peptidei429 – 45729Serpinin-RRGBy similarityPRO_0000432684Add
BLAST
Peptidei429 – 45426SerpininBy similarityPRO_0000432685Add
BLAST
Peptidei432 – 45423p-Glu serpinin precursorBy similarityPRO_0000432686Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi35 ↔ 561 Publication
Modified residuei142 – 1421PhosphoserineBy similarity
Glycosylationi181 – 1811O-linked (GalNAc...)1 PublicationCAR_000116
Glycosylationi183 – 1831O-linked (GalNAc...)1 PublicationCAR_000117
Modified residuei194 – 1941PhosphotyrosineBy similarity
Modified residuei203 – 2031Phosphoserine1 Publication
Modified residuei218 – 2181Phosphoserine1 Publication
Glycosylationi251 – 2511O-linked (GalNAc...)1 PublicationCAR_000118
Modified residuei270 – 2701Phosphoserine1 Publication
Modified residuei300 – 3001Phosphoserine1 Publication
Modified residuei319 – 3191Glycine amide2 Publications
Modified residuei322 – 3221Phosphoserine3 Publications
Modified residuei333 – 3331Phosphoserine1 Publication
Modified residuei372 – 3721Methionine sulfoxide1 Publication
Modified residuei398 – 3981PhosphoserineBy similarity
Modified residuei402 – 4021Phosphoserine1 Publication
Modified residuei432 – 4321Pyrrolidone carboxylic acidBy similarity
Modified residuei456 – 4561Arginine amide1 Publication

Post-translational modificationi

Sulfated on tyrosine residues and/or contains sulfated glycans.
O-glycosylated with core 1 or possibly core 8 glycans.3 Publications
Proteolytic processing gives rise to an additional longer form of catestatin (residues 358-390) which displays a less potent catecholamine release-inhibitory activity (PubMed:10781584). Plasmin-mediated proteolytic processing can give rise to additional shorter and longer forms of catestatin peptides (PubMed:17991725).2 Publications

Keywords - PTMi

Amidation, Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Oxidation, Phosphoprotein, Pyrrolidone carboxylic acid, Sulfation

Proteomic databases

PaxDbiP10645.
PRIDEiP10645.

PTM databases

PhosphoSiteiP10645.
UniCarbKBiP10645.

Miscellaneous databases

PMAP-CutDBQ6NR84.

Expressioni

Tissue specificityi

GE-25 is found in the brain.1 Publication

Gene expression databases

BgeeiP10645.
CleanExiHS_CHGA.
ExpressionAtlasiP10645. baseline and differential.
GenevisibleiP10645. HS.

Organism-specific databases

HPAiCAB000023.
CAB040544.
CAB055506.
CAB058688.
HPA017369.

Interactioni

Subunit structurei

Interacts with SCG3.By similarity

Protein-protein interaction databases

BioGridi107538. 8 interactions.
IntActiP10645. 3 interactions.
MINTiMINT-4846180.
STRINGi9606.ENSP00000216492.

Structurei

Secondary structure

1
457
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi380 – 3834Combined sources
Beta strandi385 – 3873Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LV4NMR-A370-390[»]
ProteinModelPortaliP10645.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10645.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni41 – 5919O-glycosylated at one site only in cerebrospinal fluidAdd
BLAST
Regioni181 – 19111O-glycosylated at one site only in cerebrospinal fluidAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG41926.
GeneTreeiENSGT00730000111266.
HOVERGENiHBG001272.
InParanoidiP10645.
OMAiVNSPMNK.
OrthoDBiEOG7V766Z.
PhylomeDBiP10645.
TreeFamiTF336596.

Family and domain databases

InterProiIPR001819. Chromogranin_AB.
IPR018054. Chromogranin_CS.
IPR001990. Granin.
[Graphical view]
PANTHERiPTHR10583. PTHR10583. 1 hit.
PfamiPF01271. Granin. 2 hits.
[Graphical view]
PRINTSiPR00659. CHROMOGRANIN.
PROSITEiPS00422. GRANINS_1. 1 hit.
PS00423. GRANINS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P10645-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSAAVLALL LCAGQVTALP VNSPMNKGDT EVMKCIVEVI SDTLSKPSPM
60 70 80 90 100
PVSQECFETL RGDERILSIL RHQNLLKELQ DLALQGAKER AHQQKKHSGF
110 120 130 140 150
EDELSEVLEN QSSQAELKEA VEEPSSKDVM EKREDSKEAE KSGEATDGAR
160 170 180 190 200
PQALPEPMQE SKAEGNNQAP GEEEEEEEEA TNTHPPASLP SQKYPGPQAE
210 220 230 240 250
GDSEGLSQGL VDREKGLSAE PGWQAKREEE EEEEEEAEAG EEAVPEEEGP
260 270 280 290 300
TVVLNPHPSL GYKEIRKGES RSEALAVDGA GKPGAEEAQD PEGKGEQEHS
310 320 330 340 350
QQKEEEEEMA VVPQGLFRGG KSGELEQEEE RLSKEWEDSK RWSKMDQLAK
360 370 380 390 400
ELTAEKRLEG QEEEEDNRDS SMKLSFRARA YGFRGPGPQL RRGWRPSSRE
410 420 430 440 450
DSLEAGLPLQ VRGYPEEKKE EEGSANRRPE DQELESLSAI EAELEKVAHQ

LQALRRG
Length:457
Mass (Da):50,688
Last modified:November 25, 2008 - v7
Checksum:i2F634E1A83FF0BB1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti41 – 411S → Y in AAA52018 (PubMed:2445752).Curated
Sequence conflicti54 – 541Q → K in AAA52018 (PubMed:2445752).Curated
Sequence conflicti87 – 871A → R in AAA52018 (PubMed:2445752).Curated
Sequence conflicti119 – 1191E → Q in AAA52018 (PubMed:2445752).Curated
Sequence conflicti167 – 1671N → K in AAA52018 (PubMed:2445752).Curated
Sequence conflicti200 – 2001E → K in AAA52018 (PubMed:2445752).Curated
Sequence conflicti219 – 2191A → V in AAA52018 (PubMed:2445752).Curated
Sequence conflicti339 – 3402SK → TN in AAA52018 (PubMed:2445752).Curated
Sequence conflicti370 – 3701S → R in AAA52018 (PubMed:2445752).Curated
Sequence conflicti373 – 3731K → R in AAA52018 (PubMed:2445752).Curated
Sequence conflicti380 – 3801A → G in AAA52018 (PubMed:2445752).Curated
Sequence conflicti394 – 3941W → S in AAA52018 (PubMed:2445752).Curated
Sequence conflicti397 – 3971S → N in AAA52018 (PubMed:2445752).Curated
Sequence conflicti416 – 4161E → Q in AAA52018 (PubMed:2445752).Curated

Mass spectrometryi

Molecular mass is 2051.89 Da from positions 357 - 373. Determined by MALDI. 1 Publication
Molecular mass is 3770 Da from positions 358 - 390. Determined by MALDI. 1 Publication
Molecular mass is 3787 Da from positions 358 - 390. Determined by MALDI. With methionine sulfoxide at Met-372.1 Publication
Molecular mass is 1070.54 Da from positions 369 - 377. Determined by MALDI. 1 Publication
Molecular mass is 840.45 Da from positions 378 - 384. Determined by MALDI. 1 Publication
Molecular mass is 1389.74 Da from positions 378 - 390. Determined by MALDI. 1 Publication
Molecular mass is 1419.8 Da from positions 378 - 390. Determined by MALDI. With variant Ser-382.1 Publication
Molecular mass is 1545.84 Da from positions 378 - 391. Determined by MALDI. 1 Publication
Molecular mass is 1575.9 Da from positions 378 - 391. Determined by MALDI. With variant Ser-382.1 Publication
Molecular mass is 1701.96 Da from positions 378 - 392. Determined by MALDI. 1 Publication
Molecular mass is 1318.71 Da from positions 380 - 391. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti61 – 611R → Q.
Corresponds to variant rs3742712 [ dbSNP | Ensembl ].
VAR_047417
Natural varianti176 – 1761E → K.
Corresponds to variant rs9658654 [ dbSNP | Ensembl ].
VAR_025636
Natural varianti264 – 2641E → D.1 Publication
Corresponds to variant rs9658655 [ dbSNP | Ensembl ].
VAR_025637
Natural varianti271 – 2711R → W.
Corresponds to variant rs9658662 [ dbSNP | Ensembl ].
VAR_025638
Natural varianti274 – 2741A → G.
Corresponds to variant rs9658663 [ dbSNP | Ensembl ].
VAR_025639
Natural varianti315 – 3151G → S.
Corresponds to variant rs9658664 [ dbSNP | Ensembl ].
VAR_025640
Natural varianti332 – 3321L → P.
Corresponds to variant rs9658665 [ dbSNP | Ensembl ].
VAR_025641
Natural varianti369 – 3691D → N.
Corresponds to variant rs2228575 [ dbSNP | Ensembl ].
VAR_025642
Natural varianti382 – 3821G → S Polymorphism; may be associated with a reduced risk for hypertension especially in men; reduces activity 4.7 fold; no effect on plasmin-mediated proteolytic processing; increase in ability to inhibit nicotine-evoked catecholamine secretion in vitro; displays alterations in baroreceptor function. 4 Publications
Corresponds to variant rs9658667 [ dbSNP | Ensembl ].
VAR_025643
Natural varianti388 – 3881P → L Polymorphism; increases activity 2.3 fold; decrease in plasmin-mediated proteolytic processing; decrease in ability to inhibit nicotine-evoked catecholamine secretion in vitro. 3 Publications
Corresponds to variant rs9658668 [ dbSNP | Ensembl ].
VAR_025644
Natural varianti392 – 3921R → Q Polymorphism; no effect on plasmin-mediated proteolytic processing; decrease in ability to inhibit nicotine-evoked catecholamine secretion in vitro. 2 Publications
VAR_072687
Natural varianti399 – 3991R → W.3 Publications
Corresponds to variant rs729940 [ dbSNP | Ensembl ].
VAR_025645

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03483 mRNA. Translation: AAA52017.1.
J03915 mRNA. Translation: AAA52018.1.
U03749
, 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.
CCDSiCCDS9906.1.
PIRiA54376. A28468.
RefSeqiNP_001266.1. NM_001275.3.
NP_001288619.1. NM_001301690.1.
UniGeneiHs.150793.

Genome annotation databases

EnsembliENST00000216492; ENSP00000216492; ENSG00000100604.
ENST00000613166; ENSP00000478198; ENSG00000276781.
GeneIDi1113.
KEGGihsa:1113.
UCSCiuc001ybc.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03483 mRNA. Translation: AAA52017.1.
J03915 mRNA. Translation: AAA52018.1.
U03749
, 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.
CCDSiCCDS9906.1.
PIRiA54376. A28468.
RefSeqiNP_001266.1. NM_001275.3.
NP_001288619.1. NM_001301690.1.
UniGeneiHs.150793.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LV4NMR-A370-390[»]
ProteinModelPortaliP10645.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107538. 8 interactions.
IntActiP10645. 3 interactions.
MINTiMINT-4846180.
STRINGi9606.ENSP00000216492.

PTM databases

PhosphoSiteiP10645.
UniCarbKBiP10645.

Polymorphism and mutation databases

BioMutaiCHGA.
DMDMi215274270.

Proteomic databases

PaxDbiP10645.
PRIDEiP10645.

Protocols and materials databases

DNASUi1113.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216492; ENSP00000216492; ENSG00000100604.
ENST00000613166; ENSP00000478198; ENSG00000276781.
GeneIDi1113.
KEGGihsa:1113.
UCSCiuc001ybc.4. human.

Organism-specific databases

CTDi1113.
GeneCardsiGC14P093389.
HGNCiHGNC:1929. CHGA.
HPAiCAB000023.
CAB040544.
CAB055506.
CAB058688.
HPA017369.
MIMi118910. gene.
neXtProtiNX_P10645.
PharmGKBiPA26461.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG41926.
GeneTreeiENSGT00730000111266.
HOVERGENiHBG001272.
InParanoidiP10645.
OMAiVNSPMNK.
OrthoDBiEOG7V766Z.
PhylomeDBiP10645.
TreeFamiTF336596.

Miscellaneous databases

ChiTaRSiCHGA. human.
EvolutionaryTraceiP10645.
GeneWikiiChromogranin_A.
GenomeRNAii1113.
NextBioi4618.
PMAP-CutDBQ6NR84.
PROiP10645.
SOURCEiSearch...

Gene expression databases

BgeeiP10645.
CleanExiHS_CHGA.
ExpressionAtlasiP10645. baseline and differential.
GenevisibleiP10645. HS.

Family and domain databases

InterProiIPR001819. Chromogranin_AB.
IPR018054. Chromogranin_CS.
IPR001990. Granin.
[Graphical view]
PANTHERiPTHR10583. PTHR10583. 1 hit.
PfamiPF01271. Granin. 2 hits.
[Graphical view]
PRINTSiPR00659. CHROMOGRANIN.
PROSITEiPS00422. GRANINS_1. 1 hit.
PS00423. GRANINS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. "Molecular characterization of immunoreactivities of peptides derived from chromogranin A (GE-25) and from secretogranin II (secretoneurin) in human and bovine cerebrospinal fluid."
    Kirchmair R., Benzer A., Troger J., Miller C., Marksteiner J., Saria A., Gasser R.W., Hogue-Angeletti R., Fischer-Colbrie R., Winkler H.
    Neuroscience 63:1179-1187(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF GE-25, TISSUE SPECIFICITY.
  17. "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.
  18. "Formation of the catecholamine release-inhibitory peptide catestatin from chromogranin A. Determination of proteolytic cleavage sites in hormone storage granules."
    Taylor C.V., Taupenot L., Mahata S.K., Mahata M., Wu H., Yasothornsrikul S., Toneff T., Caporale C., Jiang Q., Parmer R.J., Hook V.Y., O'Connor D.T.
    J. Biol. Chem. 275:22905-22915(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY, PROTEOLYTIC PROCESSING, OXIDATION AT MET-372.
  19. "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.
  20. "New antimicrobial activity for the catecholamine release-inhibitory peptide from chromogranin A."
    Briolat J., Wu S.D., Mahata S.K., Gonthier B., Bagnard D., Chasserot-Golaz S., Helle K.B., Aunis D., Metz-Boutigue M.H.
    Cell. Mol. Life Sci. 62:377-385(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (CATESTATIN).
  21. 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.
  22. "Catestatin is a novel endogenous peptide that regulates cardiac function and blood pressure."
    Mahapatra N.R.
    Cardiovasc. Res. 80:330-338(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  23. "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.
  24. "Catestatin: a multifunctional peptide from chromogranin A."
    Mahata S.K., Mahata M., Fung M.M., O'Connor D.T.
    Regul. Pept. 162:33-43(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  25. "Catestatin, a neuroendocrine antimicrobial peptide, induces human mast cell migration, degranulation and production of cytokines and chemokines."
    Aung G., Niyonsaba F., Ushio H., Kajiwara N., Saito H., Ikeda S., Ogawa H., Okumura K.
    Immunology 132:527-539(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (CATESTATIN).
  26. "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.
  27. "Antioxidant properties of a human neuropeptide and its protective effect on free radical-induced DNA damage."
    Mohseni S., Emtenani S., Emtenani S., Asoodeh A.
    J. Pept. Sci. 20:429-437(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (CATESTATIN).
  28. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  29. "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.
  30. "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.
  31. "The catecholamine release-inhibitory 'catestatin' fragment of chromogranin a: naturally occurring human variants with different potencies for multiple chromaffin cell nicotinic cholinergic responses."
    Mahata S.K., Mahata M., Wen G., Wong W.B., Mahapatra N.R., Hamilton B.A., O'Connor D.T.
    Mol. Pharmacol. 66:1180-1191(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SER-382; LEU-388 AND GLN-392, CHARACTERIZATION OF VARIANTS SER-382; LEU-388 AND GLN-392, FUNCTION (CATESTATIN).
  32. "Catecholamine release-inhibitory peptide catestatin (chromogranin A(352-372)): naturally occurring amino acid variant Gly364Ser causes profound changes in human autonomic activity and alters risk for hypertension."
    Rao F., Wen G., Gayen J.R., Das M., Vaingankar S.M., Rana B.K., Mahata M., Kennedy B.P., Salem R.M., Stridsberg M., Abel K., Smith D.W., Eskin E., Schork N.J., Hamilton B.A., Ziegler M.G., Mahata S.K., O'Connor D.T.
    Circulation 115:2271-2281(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SER-382, CHARACTERIZATION OF VARIANT SER-382.
  33. "Proteolytic cleavage of human chromogranin a containing naturally occurring catestatin variants: differential processing at catestatin region by plasmin."
    Biswas N., Vaingankar S.M., Mahata M., Das M., Gayen J.R., Taupenot L., Torpey J.W., O'Connor D.T., Mahata S.K.
    Endocrinology 149:749-757(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SER-382; LEU-388 AND GLN-392, CHARACTERIZATION OF VARIANTS SER-382; LEU-388 AND GLN-392, PROTEOLYTIC PROCESSING, MASS SPECTROMETRY.

Entry informationi

Entry nameiCMGA_HUMAN
AccessioniPrimary (citable) accession number: P10645
Secondary accession number(s): B2R9E9
, Q53FA8, Q6NR84, Q96E84, Q96GL7, Q9BQB5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 25, 2008
Last modified: June 24, 2015
This is version 166 of the entry and version 7 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

Binds calcium with a low-affinity.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.