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Entry version 178 (11 Dec 2019)
Sequence version 1 (01 Nov 1988)
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Protein

Chromogranin-A

Gene

CHGA

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Strongly inhibits glucose induced insulin release from the pancreas.1 Publication
Completely inhibits catecholamine release from chromaffin cells.1 Publication
Has antibacterial activity against M.luteus. Not active against E.coli.1 Publication
Inhibits catecholamine release from chromaffin cells and noradrenergic neurons by acting as a non-competitive nicotinic cholinergic antagonist (PubMed:9294131 and PubMed:9786174). Displays antibacterial activity against Gram-positive bacteria M.luteus and B.megaterium, and Gram-negative bacteria E.coli, and antifungal activity against a variety of filamentous fungi including A.fumigatus, N.hematococca, F.culmorum, F.oxyporum, T. mentagrophytes and several forms of Candida: C.albicans, C.tropicalis, C.glabrata and C.neoform (PubMed:15723172). Can induce mast cell migration, degranulation and production of cytokines and chemokines (By similarity).By similarity3 Publications
Has antibacterial activity against Gram-positive bacteria M.luteus, B.megaterium. Not active against Gram-positive bacteria B.cereus, B.subtilis, S.pyogenes, M.fortuitum, S.aureus and L.monocytogenes and against Gram-negative bacteria E.coli, E.cloacae, S.typhimurium, K.pneumoniae and P.aeruginosa. Possesses antifungal activity against N.crassa, A.fumigatus, A.brassicicola, N.hematococca, F.culmorum and F.oxyporum and against the yeast S.cerevisiae and C.albicans. Inactive against A.benhamiae.1 Publication
Has antifungal activity against N.crassa, A.fumigatus, A.brassicicola, N.hematococca, F.culmorum, F.oxyporum, A.benhamiae, C.neoformans, as well as against yeasts C.albicans, and C.tropicalis. Seems to be inactive against C.glabrata. Interacts with the fungal cell wall, crosses the plasma membrane and accumulates in fungal cells where it inhibits calcineurin activity.1 Publication
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 (PubMed:21436258).1 Publication

Miscellaneous

Binds calcium with a low-affinity.

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAntibiotic, Antimicrobial, Fungicide
LigandCalcium

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Chromogranin-A2 Publications
Short name:
CgA
Alternative name(s):
Pituitary secretory protein I1 Publication
Short name:
SP-I
Cleaved into the following 11 chains:
Vasostatin-11 Publication
Chromofungin1 Publication
Chromostatin1 Publication
Chromacin1 Publication
Pancreastatin1 Publication
WE-14By similarity
Catestatin1 Publication
GE-251 Publication
Serpinin1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CHGA
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBos taurus (Bovine)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9913 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaRuminantiaPecoraBovidaeBovinaeBos
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000009136 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane, Secreted

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 184 PublicationsAdd BLAST18
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000539819 – 449Chromogranin-AAdd BLAST431
<p>This subsection of the ‘PTM / Processing’ section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_000000539919 – 94Vasostatin-11 PublicationAdd BLAST76
PeptideiPRO_000043258765 – 88Chromofungin1 PublicationAdd BLAST24
PeptideiPRO_0000005400142 – 161Chromostatin1 PublicationAdd BLAST20
PeptideiPRO_0000005401191 – 212Chromacin1 PublicationAdd BLAST22
PeptideiPRO_0000005402266 – 312Pancreastatin1 PublicationAdd BLAST47
PeptideiPRO_0000005403334 – 347WE-14By similarityAdd BLAST14
PeptideiPRO_0000005404362 – 382Catestatin1 PublicationAdd BLAST21
PeptideiPRO_0000432673385 – 409GE-251 PublicationAdd BLAST25
PeptideiPRO_0000432674421 – 449Serpinin-RRGBy similarityAdd BLAST29
PeptideiPRO_0000432675421 – 446Serpinin1 PublicationAdd BLAST26
PeptideiPRO_0000432676424 – 446p-Glu serpinin precursorBy similarityAdd BLAST23

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi35 ↔ 561 Publication
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei99Phosphoserine1 Publication1
Modified residuei142Phosphoserine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>GlycosylationiCAR_000114185O-linked (GalNAc...) serine1 Publication1
Modified residuei191Phosphotyrosine1 Publication1
Modified residuei200PhosphoserineBy similarity1
GlycosylationiCAR_000203204O-linked (GalNAc...) serine1 Publication1
Modified residuei215PhosphoserineBy similarity1
GlycosylationiCAR_000115249O-linked (GalNAc...) threonine1 Publication1
Modified residuei295PhosphoserineBy similarity1
Modified residuei312Glycine amide1 Publication1
Modified residuei315Phosphoserine1 Publication1
Modified residuei325PhosphoserineBy similarity1
Modified residuei363PhosphoserineBy similarity1
Modified residuei364Methionine sulfoxide1 Publication1
Modified residuei390Phosphoserine1 Publication1
Modified residuei394Phosphoserine1 Publication1
Modified residuei416PhosphoserineBy similarity1
Modified residuei430PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

In secretory granules, is attacked at both N- and C-terminal sides by proteolytic enzymes generating numerous peptides of various activities. Proteolytic processing can give rise to additional longer forms of catestatin peptides which display a less potent catecholamine release-inhibitory activity (PubMed:10781584).1 Publication2 Publications

Keywords - PTMi

Amidation, Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Oxidation, Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P05059

PeptideAtlas

More...
PeptideAtlasi
P05059

PRoteomics IDEntifications database

More...
PRIDEi
P05059

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
92

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P05059

UniCarbKB; an annotated and curated database of glycan structures

More...
UniCarbKBi
P05059

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Highest concentration of GE-25 found in adrenal medulla with lower levels present in the pituitary, the intestinal mucosa and the pancreas. Also found in the brain.2 Publications

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with SCG3.

By similarity

Protein-protein interaction databases

Molecular INTeraction database

More...
MINTi
P05059

STRING: functional protein association networks

More...
STRINGi
9913.ENSBTAP00000012973

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1449
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P05059

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P05059

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410II3Z Eukaryota
ENOG410YGBX LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000111808

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P05059

KEGG Orthology (KO)

More...
KOi
K19990

Database of Orthologous Groups

More...
OrthoDBi
1127088at2759

TreeFam database of animal gene trees

More...
TreeFami
TF336596

Family and domain databases

Database of protein disorder

More...
DisProti
DP00118

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001819 Chromogranin_AB
IPR018054 Chromogranin_CS
IPR001990 Granin

The PANTHER Classification System

More...
PANTHERi
PTHR10583 PTHR10583, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01271 Granin, 2 hits

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00659 CHROMOGRANIN

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00422 GRANINS_1, 1 hit
PS00423 GRANINS_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P05059-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRSAAVLALL LCAGQVIALP VNSPMNKGDT EVMKCIVEVI SDTLSKPSPM
60 70 80 90 100
PVSKECFETL RGDERILSIL RHQNLLKELQ DLALQGAKER THQQKKHSSY
110 120 130 140 150
EDELSEVLEK PNDQAEPKEV TEEVSSKDAA EKRDDFKEVE KSDEDSDGDR
160 170 180 190 200
PQASPGLGPG PKVEEDNQAP GEEEEAPSNA HPLASLPSPK YPGPQAKEDS
210 220 230 240 250
EGPSQGPASR EKGLSAEQGR QTEREEEEEK WEEAEAREKA VPEEESPPTA
260 270 280 290 300
AFKPPPSLGN KETQRAAPGW PEDGAGKMGA EEAKPPEGKG EWAHSRQEEE
310 320 330 340 350
EMARAPQVLF RGGKSGEPEQ EEQLSKEWED AKRWSKMDQL AKELTAEKRL
360 370 380 390 400
EGEEEEEEDP DRSMRLSFRA RGYGFRGPGL QLRRGWRPNS REDSVEAGLP
410 420 430 440
LQVRGYPEEK KEEEGSANRR PEDQELESLS AIEAELEKVA HQLEELRRG
Length:449
Mass (Da):50,015
Last modified:November 1, 1988 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iF304EDC587AA70A3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti112N → T in AAA30765 (PubMed:3474638).Curated1
Sequence conflicti136F → S in CAA27636 (PubMed:3755681).Curated1
Sequence conflicti136F → S in AAI05516 (Ref. 6) Curated1
Sequence conflicti154 – 155SP → PQ in CAA27841 (PubMed:3018587).Curated2
Sequence conflicti159P → R in CAA27841 (PubMed:3018587).Curated1
Sequence conflicti191Y → H in AAB21297 (PubMed:1779968).Curated1
Sequence conflicti254P → A in AAB21297 (PubMed:1779968).Curated1
Sequence conflicti293A → S in AAC48700 (PubMed:9074643).Curated1
Sequence conflicti311R → H in CAA27636 (PubMed:3755681).Curated1
Sequence conflicti311R → H in AAI05516 (Ref. 6) Curated1
Sequence conflicti311R → H AA sequence (PubMed:1710890).Curated1
Sequence conflicti319E → K in CAA27636 (PubMed:3755681).Curated1
Sequence conflicti319E → K in AAI05516 (Ref. 6) Curated1
Sequence conflicti319E → K AA sequence (PubMed:1710890).Curated1
Sequence conflicti379G → R in AAA30765 (PubMed:3474638).Curated1
Sequence conflicti391R → Q in CAA27636 (PubMed:3755681).Curated1
Sequence conflicti391R → Q in AAI05516 (Ref. 6) Curated1

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 8584.9 Da. Determined by MALDI. 1 Publication
Molecular mass is 2426 Da. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
S79270 S79268 Genomic DNA Translation: AAB21297.1
X04012 mRNA Translation: CAA27636.1
X04298 mRNA Translation: CAA27841.1
M16971 mRNA Translation: AAA30765.1
U73523 mRNA Translation: AAC48700.1
BC105515 mRNA Translation: AAI05516.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A41520

NCBI Reference Sequences

More...
RefSeqi
NP_851348.1, NM_181005.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
281070

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bta:281070

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S79270 S79268 Genomic DNA Translation: AAB21297.1
X04012 mRNA Translation: CAA27636.1
X04298 mRNA Translation: CAA27841.1
M16971 mRNA Translation: AAA30765.1
U73523 mRNA Translation: AAC48700.1
BC105515 mRNA Translation: AAI05516.1
PIRiA41520
RefSeqiNP_851348.1, NM_181005.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CFKmodel-A359-389[»]
1N2YNMR-A368-380[»]
SMRiP05059
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

MINTiP05059
STRINGi9913.ENSBTAP00000012973

PTM databases

GlyConnecti92
iPTMnetiP05059
UniCarbKBiP05059

Proteomic databases

PaxDbiP05059
PeptideAtlasiP05059
PRIDEiP05059

Genome annotation databases

GeneIDi281070
KEGGibta:281070

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1113

Phylogenomic databases

eggNOGiENOG410II3Z Eukaryota
ENOG410YGBX LUCA
HOGENOMiHOG000111808
InParanoidiP05059
KOiK19990
OrthoDBi1127088at2759
TreeFamiTF336596

Miscellaneous databases

EvolutionaryTraceiP05059

Family and domain databases

DisProtiDP00118
InterProiView protein in InterPro
IPR001819 Chromogranin_AB
IPR018054 Chromogranin_CS
IPR001990 Granin
PANTHERiPTHR10583 PTHR10583, 1 hit
PfamiView protein in Pfam
PF01271 Granin, 2 hits
PRINTSiPR00659 CHROMOGRANIN
PROSITEiView protein in PROSITE
PS00422 GRANINS_1, 1 hit
PS00423 GRANINS_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCMGA_BOVIN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P05059
Secondary accession number(s): P79392, Q2KJ52
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: November 1, 1988
Last modified: December 11, 2019
This is version 178 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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