CHGA
entrez
1113
canonical
uniprot
P10645
canonical
ensembl
ENSG00000100604
resolver
ensembl
ENSG00000276781
resolver
ensp
ENSP00000216492
resolver
ensp
ENSP00000334023
resolver
ensp
ENSP00000478198
resolver
ensp
ENSP00000486710
resolver
ensp
ENSP00000573380
resolver
enst
ENST00000216492
resolver
enst
ENST00000334654
resolver
enst
ENST00000613166
resolver
enst
ENST00000630996
resolver
enst
ENST00000903321
resolver
genesymbol
CHGA
resolver
hgnc
HGNC:1929
resolver
uniprot
B2R9E9
resolver
uniprot
G5E968
resolver
uniprot
Q53FA8
resolver
uniprot
Q6NR84
resolver
uniprot
Q86T07
resolver
uniprot
Q96E84
resolver
uniprot
Q96GL7
resolver
uniprot
Q9BQB5
resolver
uniprot_entry
CMGA_HUMAN
resolver
uniprot_entry
G5E968_HUMAN
resolver
uniprot_entry
Q86T07_HUMAN
resolver
uniprot_sec
B2R9E9
resolver
uniprot_sec
Q53FA8
resolver
uniprot_sec
Q6NR84
resolver
uniprot_sec
Q96E84
resolver
uniprot_sec
Q96GL7
resolver
uniprot_sec
Q9BQB5
resolver
amino_acid_sequence
MRSAAVLALLLCAGQVTALPVNSPMNKGDTEVMKCIVEVISDTLSKPSPMPVSQECFETLRGDERILSILRHQNLLKELQDLALQGAKERAHQQKKHSGFEDELSEVLENQSSQAELKEAVEEPSSKDVMEKREDSKEAEKSGEATDGARPQALPEPMQESKAEGNNQAPGEEEEEEEEATNTHPPASLPSQKYPGPQAEGDSEGLSQGLVDREKGLSAEPGWQAKREEEEEEEEEAEAGEEAVPEEEGPTVVLNPHPSLGYKEIRKGESRSEALAVDGAGKPGAEEAQDPEGKGEQEHSQQKEEEEEMAVVPQGLFRGGKSGELEQEEERLSKEWEDSKRWSKMDQLAKELTAEKRLEGQEEEEDNRDSSMKLSFRARAYGFRGPGPQLRRGWRPSSREDSLEAGLPLQVRGYPEEKKEEEGSANRRPEDQELESLSAIEAELEKVAHQLQALRRG
uniprot
proteins
function
FUNCTION: [Pancreastatin]: Strongly inhibits glucose induced insulin release from the pancreas.; FUNCTION: [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, 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). {ECO:0000269|PubMed:15326220, ECO:0000269|PubMed:15723172, ECO:0000269|PubMed:21214543, ECO:0000269|PubMed:24723458, ECO:0000303|PubMed:18541522}.; FUNCTION: [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. {ECO:0000250|UniProtKB:P26339}.
uniprot
proteins
mass_dalton
50688
uniprot
proteins
post_translational_modification
PTM: Sulfated on tyrosine residues and/or contains sulfated glycans.; PTM: O-glycosylated with core 1 or possibly core 8 glycans (PubMed:19838169, PubMed:23234360, PubMed:9852066). Contains chondroitin sulfate (CS); CS attachment is pH-dependent, being observed at mildly acidic conditions of pH 5 but not at neutral pH, and promotes self-assembly in vitro (PubMed:25326458). {ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:23234360, ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:9852066}.; PTM: 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). {ECO:0000269|PubMed:10781584, ECO:0000269|PubMed:17991725}.
uniprot
proteins
protein_family
Chromogranin/secretogranin protein family
uniprot
proteins
pubmed
10781584
uniprot
proteins
pubmed
12442257
uniprot
proteins
pubmed
12508121
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14740315
uniprot
proteins
pubmed
14759560
uniprot
proteins
pubmed
14997482
uniprot
proteins
pubmed
15326220
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15723172
uniprot
proteins
pubmed
1577173
uniprot
proteins
pubmed
16807684
uniprot
proteins
pubmed
17438154
uniprot
proteins
pubmed
17991725
uniprot
proteins
pubmed
18541522
uniprot
proteins
pubmed
19838169
uniprot
proteins
pubmed
20116404
uniprot
proteins
pubmed
21214543
uniprot
proteins
pubmed
2165909
uniprot
proteins
pubmed
23234360
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2445752
uniprot
proteins
pubmed
24723458
uniprot
proteins
pubmed
25326458
uniprot
proteins
pubmed
2830133
uniprot
proteins
pubmed
3403545
uniprot
proteins
pubmed
3704195
uniprot
proteins
pubmed
37453717
uniprot
proteins
pubmed
7535395
uniprot
proteins
pubmed
8120054
uniprot
proteins
pubmed
9852066
uniprot
proteins
sequence_length
457
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Serpinin]: Secreted {ECO:0000250|UniProtKB:P26339}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:P26339}. Note=Pyroglutaminated serpinin localizes to secretory vesicle. {ECO:0000250|UniProtKB:P26339}.; SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:P10354}. Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle {ECO:0000250|UniProtKB:P10354}. Secreted {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:37453717}. Note=Associated with the secretory granule membrane through direct interaction to SCG3 that in turn binds to cholesterol-enriched lipid rafts in intragranular conditions. In pituitary gonadotropes, located in large secretory granules. {ECO:0000250|UniProtKB:P10354}.
uniprot
proteins