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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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20202 PublicationsAdd
BLAST
Chaini21 – 646626Secretogranin-1PRO_0000005434Add
BLAST
Chaini476 – 56691Secretogranin-1(476-566)PRO_0000326263Add
BLAST
Peptidei544 – 55411PE-11By similarityPRO_0000432729Add
BLAST
Peptidei567 – 58014Peptide BAM-1745PRO_0000005436Add
BLAST
Peptidei584 – 64663CCB peptidePRO_0000411987Add
BLAST
Peptidei634 – 64613SecretolytinPRO_0000005437Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi36 ↔ 57By similarity
Modified residuei74 – 741PhosphoserineSequence analysis
Modified residuei79 – 791PhosphothreonineCurated
Modified residuei92 – 921PhosphothreonineSequence analysis
Modified residuei93 – 931PhosphoserineBy similarity
Modified residuei99 – 991PhosphoserineSequence analysis
Modified residuei100 – 1001PhosphoserineSequence analysis
Modified residuei104 – 1041PhosphoserineSequence analysis
Glycosylationi113 – 1131O-linked (GalNAc...)1 Publication
Modified residuei123 – 1231PhosphoserineBy similarity
Modified residuei146 – 1461PhosphoserineCurated
Modified residuei168 – 1681Phosphoserine1 Publication
Glycosylationi190 – 1901O-linked (GalNAc...)1 Publication
Modified residuei205 – 2051PhosphoserineBy similarity
Modified residuei276 – 2761PhosphoserineSequence analysis
Modified residuei277 – 2771PhosphoserineSequence analysis
Modified residuei295 – 2951PhosphoserineSequence analysis
Modified residuei315 – 3151SulfotyrosineBy similarity
Modified residuei351 – 3511Phosphoserine1 Publication
Modified residuei354 – 3541Phosphoserine1 Publication
Modified residuei374 – 3741PhosphotyrosineBy similarity
Modified residuei375 – 3751PhosphoserineSequence analysis
Modified residuei378 – 3781PhosphoserineSequence analysisBy similarity
Modified residuei438 – 4381SulfotyrosineSequence analysis
Modified residuei441 – 4411SulfotyrosineCurated
Modified residuei476 – 4761Pyrrolidone carboxylic acid; in secretogranin-1(476-566)1 Publication
Modified residuei502 – 5021PhosphoserineSequence analysis
Modified residuei503 – 5031PhosphoserineSequence analysis
Modified residuei514 – 5141PhosphoserineSequence analysis
Modified residuei535 – 5351SulfotyrosineCurated
Modified residuei537 – 5371SulfotyrosineSequence analysis
Modified residuei567 – 5671Pyrrolidone carboxylic acid; in peptide BAM-17452 Publications
Modified residuei584 – 5841Phosphoserine1 Publication
Modified residuei591 – 5911SulfotyrosineBy similarity
Modified residuei593 – 5931Phosphoserine1 Publication
Modified residuei598 – 5981Phosphoserine1 Publication
Modified residuei634 – 6341Pyrrolidone carboxylic acid; in Secretolytin; partial1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Sitei161 – 1622Cleavage; major site
Sitei275 – 2762Cleavage; major site
Sitei278 – 2792Cleavage; major site
Sitei324 – 3252Cleavage; major site
Sitei629 – 6302Cleavage; major site

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)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi617 – 6248Poly-Glu

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641N → S in CAA38846 (PubMed:2025642).Curated
Sequence conflicti70 – 701N → D in AAC48720 (PubMed:9136897).Curated
Sequence conflicti93 – 986SEAPGL → FRSPRAS in CAA39109 (PubMed:1350945).Curated
Sequence conflicti181 – 1811T → M in AAC48720 (PubMed:9136897).Curated
Sequence conflicti261 – 2611H → R in AAC48720 (PubMed:9136897).Curated
Sequence conflicti386 – 3861P → R in AAC48720 (PubMed:9136897).Curated
Sequence conflicti481 – 4811H → L in CAA39109 (PubMed:1350945).Curated

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti597 – 5971M → V.2 Publications

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.