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Protein

Secretogranin-1

Gene

Chgb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Secretogranin-1 is a neuroendocrine secretory granule protein, which may be the precursor for other biologically active peptides.

Names & Taxonomyi

Protein namesi
Recommended name:
Secretogranin-1
Alternative name(s):
Chromogranin-B
Short name:
CgB
Secretogranin I
Short name:
SgI
Cleaved into the following 2 chains:
Gene namesi
Name:Chgb
Synonyms:Scg-1, Scg1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:88395. Chgb.

Subcellular locationi

  • Secreted

  • Note: Neuroendocrine and endocrine secretory granules.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Add
BLAST
Chaini21 – 677657Secretogranin-1PRO_0000005441Add
BLAST
Peptidei575 – 58511PE-111 PublicationPRO_0000432731Add
BLAST
Peptidei617 – 67761CCB peptideBy similarityPRO_0000411988Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi36 ↔ 57By similarity
Modified residuei93 – 931PhosphoserineBy similarity
Modified residuei99 – 991PhosphoserineSequence analysis
Modified residuei100 – 1001PhosphoserineSequence analysis
Glycosylationi115 – 1151O-linked (GalNAc...)Curated
Modified residuei129 – 1291PhosphoserineBy similarity
Modified residuei147 – 1471PhosphoserineBy similarity
Modified residuei171 – 1711SulfotyrosineSequence analysis
Modified residuei190 – 1901PhosphoserineBy similarity
Modified residuei220 – 2201PhosphoserineCombined sources
Modified residuei256 – 2561PhosphoserineBy similarity
Modified residuei260 – 2601PhosphoserineBy similarity
Modified residuei300 – 3001PhosphoserineSequence analysis
Modified residuei301 – 3011PhosphoserineSequence analysis
Modified residuei318 – 3181PhosphoserineBy similarity
Modified residuei342 – 3421PhosphoserineCombined sources
Modified residuei348 – 3481SulfotyrosineBy similarity
Modified residuei365 – 3651PhosphoserineBy similarity
Modified residuei375 – 3751PhosphoserineBy similarity
Modified residuei378 – 3781PhosphoserineBy similarity
Modified residuei469 – 4691SulfotyrosineSequence analysis
Modified residuei472 – 4721SulfotyrosineCurated
Modified residuei493 – 4931PhosphoserineCombined sources
Modified residuei532 – 5321PhosphoserineSequence analysis
Modified residuei543 – 5431PhosphoserineSequence analysis
Modified residuei566 – 5661SulfotyrosineCurated
Modified residuei568 – 5681SulfotyrosineSequence analysis
Modified residuei624 – 6241SulfotyrosineBy similarity
Modified residuei626 – 6261PhosphoserineCombined sources

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation

Proteomic databases

PaxDbiP16014.
PeptideAtlasiP16014.
PRIDEiP16014.

PTM databases

iPTMnetiP16014.
PhosphoSiteiP16014.

Miscellaneous databases

PMAP-CutDBP16014.

Expressioni

Gene expression databases

BgeeiP16014.
CleanExiMM_CHGB.
ExpressionAtlasiP16014. baseline and differential.
GenevisibleiP16014. MM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
SOD1P004416EBI-990820,EBI-990792From a different organism.

Protein-protein interaction databases

IntActiP16014. 2 interactions.
STRINGi10090.ENSMUSP00000028826.

Structurei

3D structure databases

ProteinModelPortaliP16014.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IVJ3. Eukaryota.
ENOG410ZHMS. LUCA.
HOGENOMiHOG000132984.
HOVERGENiHBG057317.
InParanoidiP16014.
KOiK19991.
OMAiNWGYEKR.
OrthoDBiEOG74N5GF.
PhylomeDBiP16014.
TreeFamiTF336596.

Family and domain databases

InterProiIPR001819. Chromogranin_AB.
IPR018054. Chromogranin_CS.
IPR001990. Granin.
[Graphical view]
PANTHERiPTHR10583. PTHR10583. 1 hit.
PfamiPF01271. Granin. 1 hit.
[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.

P16014-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQPAMLLGLL GAAALAAVSS APVDNRDHNE EMVTRCIIEV LSNALSKSSV
60 70 80 90 100
PTITPECRQV LKKSGKEVKG EEKGENQNSK FEVRLLRDPA DASGTRWASS
110 120 130 140 150
REDAGAPVED SQGQTKVGNE KWTEGGGHSR EGVDDQESLR PSNQQASKEA
160 170 180 190 200
KIYHSEERVG KEREKEEGKI YPMGEHREDA GEEKKHIEDS GEKPNTFSNK
210 220 230 240 250
RSEASAKKKD ESVARADAHS MELEEKTHSR EQSSQESGEE TRRQEKPQEL
260 270 280 290 300
TDQDQSQEES QEGEEGEEGE EGEEGEEDSA SEVTKRRPRH HHGRSGSNKS
310 320 330 340 350
SYEGHPLSEE RRPSPKESKE ADVATVRLGE KRSHHLAHYR ASEEEPEYGE
360 370 380 390 400
ESRSYRGLQY RGRGSEEDRA PRPRSEESQE REYKRNHPDS ELESTANRHG
410 420 430 440 450
EETEEERSYE GANGRQHRGR GREPGAHSAL DTREEKRLLD EGHYPVRESP
460 470 480 490 500
IDTAKRYPQS KWQEQEKNYL NYGEEGDQGR WWQQEEQLGP EESREEVRFP
510 520 530 540 550
DRQYEPYPIT EKRKRLGALF NPYFDPLQWK NSDFEKRGNP DDSFLEDEGE
560 570 580 590 600
DRNGVTLTEK NSFPEYNYDW WERRPFSEDV NWGYEKRSFA RAPQLDLKRQ
610 620 630 640 650
YDGVAELDQL LHYRKKADEF PDFYDSEEQM GPHQEANDEK ARADQRVLTA
660 670
EEKKELENLA AMDLELQKIA EKFSQRG
Length:677
Mass (Da):77,969
Last modified:February 1, 1991 - v2
Checksum:iC73291E781E4F9B9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti422 – 4243REP → LGA in CAA35792 (PubMed:2320426).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53028 mRNA. Translation: CAA37199.1.
X51429 mRNA. Translation: CAA35792.1.
BC014736 mRNA. Translation: AAH14736.1.
CCDSiCCDS16777.1.
PIRiS09078.
RefSeqiNP_031720.1. NM_007694.4.
UniGeneiMm.255241.

Genome annotation databases

EnsembliENSMUST00000028826; ENSMUSP00000028826; ENSMUSG00000027350.
GeneIDi12653.
KEGGimmu:12653.
UCSCiuc008mnf.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53028 mRNA. Translation: CAA37199.1.
X51429 mRNA. Translation: CAA35792.1.
BC014736 mRNA. Translation: AAH14736.1.
CCDSiCCDS16777.1.
PIRiS09078.
RefSeqiNP_031720.1. NM_007694.4.
UniGeneiMm.255241.

3D structure databases

ProteinModelPortaliP16014.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP16014. 2 interactions.
STRINGi10090.ENSMUSP00000028826.

PTM databases

iPTMnetiP16014.
PhosphoSiteiP16014.

Proteomic databases

PaxDbiP16014.
PeptideAtlasiP16014.
PRIDEiP16014.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028826; ENSMUSP00000028826; ENSMUSG00000027350.
GeneIDi12653.
KEGGimmu:12653.
UCSCiuc008mnf.1. mouse.

Organism-specific databases

CTDi1114.
MGIiMGI:88395. Chgb.

Phylogenomic databases

eggNOGiENOG410IVJ3. Eukaryota.
ENOG410ZHMS. LUCA.
HOGENOMiHOG000132984.
HOVERGENiHBG057317.
InParanoidiP16014.
KOiK19991.
OMAiNWGYEKR.
OrthoDBiEOG74N5GF.
PhylomeDBiP16014.
TreeFamiTF336596.

Miscellaneous databases

ChiTaRSiChgb. mouse.
PMAP-CutDBP16014.
PROiP16014.
SOURCEiSearch...

Gene expression databases

BgeeiP16014.
CleanExiMM_CHGB.
ExpressionAtlasiP16014. baseline and differential.
GenevisibleiP16014. MM.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of mouse chromogranin B deduced from cDNA sequence."
    Linard C.G., Mbikay M., Seidah N.G., Chretien M.
    Nucleic Acids Res. 18:1298-1298(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Pituitary.
  2. "The organisation of the mouse chromogranin B (secretogranin I) gene."
    Pohl T.M., Phillips E., Song K., Gerdes H.-H., Huttner W.B., Ruether U.
    FEBS Lett. 262:219-224(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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: Eye.
  4. "Proteolytic processing of chromogranin B and secretogranin II by prohormone convertases."
    Laslop A., Weiss C., Savaria D., Eiter C., Tooze S.A., Seidah N.G., Winkler H.
    J. Neurochem. 70:374-383(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF PE-11.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220; SER-342; SER-493 AND SER-626, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney and Pancreas.

Entry informationi

Entry nameiSCG1_MOUSE
AccessioniPrimary (citable) accession number: P16014
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: February 1, 1991
Last modified: July 6, 2016
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.