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Protein

Secretogranin-1

Gene

CHGB

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 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. The 16 pairs of basic AA distributed throughout its sequence may be used as proteolytic cleavage sites.
Secretolytin has antibacterial activity.

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 5 chains:
Gene namesi
Name:CHGB
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

Secretogranin-1 :

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 202 PublicationsAdd BLAST20
ChainiPRO_000000543421 – 646Secretogranin-1Add BLAST626
ChainiPRO_0000326263476 – 566Secretogranin-1(476-566)Add BLAST91
PeptideiPRO_0000432729544 – 554PE-11By similarityAdd BLAST11
PeptideiPRO_0000005436567 – 580Peptide BAM-1745Add BLAST14
PeptideiPRO_0000411987584 – 646CCB peptideAdd BLAST63
PeptideiPRO_0000005437634 – 646SecretolytinAdd BLAST13

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi36 ↔ 57By similarity
Modified residuei74PhosphoserineSequence analysis1
Modified residuei79PhosphothreonineCurated1
Modified residuei92PhosphothreonineSequence analysis1
Modified residuei93PhosphoserineBy similarity1
Modified residuei99PhosphoserineSequence analysis1
Modified residuei100PhosphoserineSequence analysis1
Modified residuei104PhosphoserineSequence analysis1
Glycosylationi113O-linked (GalNAc...)1 Publication1
Modified residuei123PhosphoserineBy similarity1
Modified residuei146PhosphoserineCurated1
Modified residuei168Phosphoserine1 Publication1
Glycosylationi190O-linked (GalNAc...)1 Publication1
Modified residuei205PhosphoserineBy similarity1
Modified residuei276PhosphoserineSequence analysis1
Modified residuei277PhosphoserineSequence analysis1
Modified residuei295PhosphoserineSequence analysis1
Modified residuei315SulfotyrosineBy similarity1
Modified residuei351Phosphoserine1 Publication1
Modified residuei354Phosphoserine1 Publication1
Modified residuei374PhosphotyrosineBy similarity1
Modified residuei375PhosphoserineSequence analysis1
Modified residuei378PhosphoserineSequence analysisBy similarity1
Modified residuei438SulfotyrosineSequence analysis1
Modified residuei441SulfotyrosineCurated1
Modified residuei476Pyrrolidone carboxylic acid; in secretogranin-1(476-566)1 Publication1
Modified residuei502PhosphoserineSequence analysis1
Modified residuei503PhosphoserineSequence analysis1
Modified residuei514PhosphoserineSequence analysis1
Modified residuei535SulfotyrosineCurated1
Modified residuei537SulfotyrosineSequence analysis1
Modified residuei567Pyrrolidone carboxylic acid; in peptide BAM-17452 Publications1
Modified residuei584Phosphoserine1 Publication1
Modified residuei591SulfotyrosineBy similarity1
Modified residuei593Phosphoserine1 Publication1
Modified residuei598Phosphoserine1 Publication1
Modified residuei634Pyrrolidone carboxylic acid; in Secretolytin; partial1 Publication1

Post-translational modificationi

O-glycosylated by the trisaccharide, GalNAc-Gal-NeuAc, on 2 sites in the N-terminal. May be glycated.1 Publication
Extensively phosphorylated.1 Publication
Differentially processed on numerous sites throughout the sequence depending on tissue type.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei161 – 162Cleavage; major site2
Sitei275 – 276Cleavage; major site2
Sitei278 – 279Cleavage; major site2
Sitei324 – 325Cleavage; major site2
Sitei629 – 630Cleavage; major site2

Keywords - PTMi

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

Proteomic databases

PaxDbiP23389.
PRIDEiP23389.

PTM databases

iPTMnetiP23389.

Expressioni

Gene expression databases

BgeeiENSBTAG00000011782.

Interactioni

Protein-protein interaction databases

MINTiMINT-1214903.
STRINGi9913.ENSBTAP00000015645.

Structurei

3D structure databases

DisProtiDP00124.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi617 – 624Poly-Glu8

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IVJ3. Eukaryota.
ENOG410ZHMS. LUCA.
HOGENOMiHOG000132984.
HOVERGENiHBG057317.
InParanoidiP23389.
KOiK19991.
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.

P23389-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQPAALLGLL GATVVAAVSS MPVDIRNHNE EVVTHCIIEV LSNALLKSSA
60 70 80 90 100
PPITPECRQV LKKNGKELKN EEKSENENTR FEVRLLRDPA DTSEAPGLSS
110 120 130 140 150
REDSGEGDAQ VPTVADTESG GHSRERAGEP PGSQVAKEAK TRYSKSEGQN
160 170 180 190 200
REEEMVKYQK RERGEVGSEE RLSEGPGKAQ TAFLNQRNQT PAKKEELVSR
210 220 230 240 250
YDTQSARGLE KSHSRERSSQ ESGEETKSQE NWPQELQRHP EGQEAPGESE
260 270 280 290 300
EDASPEVDKR HSRPRHHHGR SRPDRSSQEG NPPLEEESHV GTGNSDEEKA
310 320 330 340 350
RHPAHFRALE EGAEYGEEVR RHSAAQAPGD LQGARFGGRG RGEHQALRRP
360 370 380 390 400
SEESLEQENK RHGLSPDLNM AQGYSEESEE ERGPAPGPSY RARGGEAAAY
410 420 430 440 450
STLGQTDEKR FLGETHHRVQ ESQRDKARRR LPGELRNYLD YGEEKGEEAA
460 470 480 490 500
RGKWQPQGDP RDADENREEA RLRGKQYAPH HITEKRLGEL LNPFYDPSQW
510 520 530 540 550
KSSRFERKDP MDDSFLEGEE ENGLTLNEKN FFPEYNYDWW EKKPFEEDVN
560 570 580 590 600
WGYEKRNPVP KLDLKRQYDR VAELDQLLHY RKKSAEFPDF YDSEEQMSPQ
610 620 630 640
HTAENEEEKA GQGVLTEEEE KELENLAAMD LELQKIAEKF SGTRRG
Length:646
Mass (Da):73,340
Last modified:December 1, 2000 - v2
Checksum:i420DB1178FD9E415
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti64N → S in CAA38846 (PubMed:2025642).Curated1
Sequence conflicti70N → D in AAC48720 (PubMed:9136897).Curated1
Sequence conflicti93 – 98SEAPGL → FRSPRAS in CAA39109 (PubMed:1350945).Curated6
Sequence conflicti181T → M in AAC48720 (PubMed:9136897).Curated1
Sequence conflicti261H → R in AAC48720 (PubMed:9136897).Curated1
Sequence conflicti386P → R in AAC48720 (PubMed:9136897).Curated1
Sequence conflicti481H → L in CAA39109 (PubMed:1350945).Curated1

Mass spectrometryi

Molecular mass is 2053 Da from positions 161 - 178. Determined by MALDI. Monophosphorylated.1 Publication
Molecular mass is 2338 Da from positions 276 - 299. Determined by MALDI. Monophosphorylated.1 Publication
Molecular mass is 6952 Da from positions 300 - 360. Determined by MALDI. Monophosphorylated and monosulfated.1 Publication
Molecular mass is 5304 Da from positions 361 - 409. Determined by MALDI. Monophosphorylated.1 Publication
Molecular mass is 2417 Da from positions 427 - 445. Determined by MALDI. Monosulfated.1 Publication
Molecular mass is 1223 Da from positions 476 - 485. Determined by MALDI. Pyroglutamate.1 Publication
Molecular mass is 3933 Da from positions 486 - 516. Determined by MALDI. Diphosphorylated.1 Publication
Molecular mass is 1919 Da from positions 530 - 542. Determined by MALDI. Monosulfated.1 Publication
Molecular mass is 1746 Da from positions 567 - 580. Determined by MALDI. Pyroglutamate.1 Publication
Molecular mass is 1746 Da from positions 567 - 580. Determined by FAB. Pyroglutamate.1 Publication
Molecular mass is 997.5 Da from positions 590 - 596. Determined by MALDI. Monophosphorylated.1 Publication
Molecular mass is 3042 Da from positions 584 - 609. Determined by MALDI. Non-phosphorylatecd. Val-597.1 Publication
Molecular mass is 3122 Da from positions 584 - 609. Determined by MALDI. Monophosphorylatecd. Val-597.1 Publication
Molecular mass is 3154 Da from positions 584 - 609. Determined by MALDI. Monophosphorylatecd. Met-597.1 Publication
Molecular mass is 3170 Da from positions 584 - 609. Determined by MALDI. Monophosphorylatecd. Oxidized Met-597.1 Publication
Molecular mass is 3202 Da from positions 584 - 609. Determined by MALDI. Diphosphorylatecd. Val-597.1 Publication
Molecular mass is 3250 Da from positions 584 - 609. Determined by MALDI. Diphosphorylatecd. Oxidized Met-597.1 Publication
Molecular mass is 1460.3±0.4 Da from positions 624 - 646. Determined by ESI. Pyroglutamate.1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti597M → V.2 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55027 mRNA. Translation: CAA38846.1.
U88551 mRNA. Translation: AAC48720.1.
X55489 mRNA. Translation: CAA39109.1.
PIRiS15901.
RefSeqiNP_851349.1. NM_181006.2.
UniGeneiBt.5448.

Genome annotation databases

GeneIDi281071.
KEGGibta:281071.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55027 mRNA. Translation: CAA38846.1.
U88551 mRNA. Translation: AAC48720.1.
X55489 mRNA. Translation: CAA39109.1.
PIRiS15901.
RefSeqiNP_851349.1. NM_181006.2.
UniGeneiBt.5448.

3D structure databases

DisProtiDP00124.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1214903.
STRINGi9913.ENSBTAP00000015645.

PTM databases

iPTMnetiP23389.

Proteomic databases

PaxDbiP23389.
PRIDEiP23389.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281071.
KEGGibta:281071.

Organism-specific databases

CTDi1114.

Phylogenomic databases

eggNOGiENOG410IVJ3. Eukaryota.
ENOG410ZHMS. LUCA.
HOGENOMiHOG000132984.
HOVERGENiHBG057317.
InParanoidiP23389.
KOiK19991.
TreeFamiTF336596.

Gene expression databases

BgeeiENSBTAG00000011782.

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...

Entry informationi

Entry nameiSCG1_BOVIN
AccessioniPrimary (citable) accession number: P23389
Secondary accession number(s): O02707
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: December 1, 2000
Last modified: September 7, 2016
This is version 120 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, Direct protein sequencing, Reference proteome

Documents

  1. 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.