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Protein

Secretogranin-2

Gene

Scg2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Secretogranin-2 is a neuroendocrine secretory granule protein, which may be the precursor for other biologically active peptides.

GO - Molecular functioni

  • chemoattractant activity Source: HGNC
  • cytokine activity Source: HGNC

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Secretogranin-2
Alternative name(s):
Chromogranin-C
Secretogranin II
Short name:
SgII
Cleaved into the following 2 chains:
Secretoneurin
Short name:
SN
Gene namesi
Name:Scg2
Synonyms:Chgc, Scg-2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:103033. Scg2.

Subcellular locationi

  • Secreted

  • Note: Neuroendocrine and endocrine secretory granules.

GO - Cellular componenti

  • dense core granule Source: MGI
  • extracellular space Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030By similarityAdd
BLAST
Chaini31 – 617587Secretogranin-2PRO_0000005455Add
BLAST
Peptidei184 – 21633SecretoneurinPRO_0000005456Add
BLAST
Peptidei527 – 56640ManserinBy similarityPRO_0000432737Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei153 – 1531SulfotyrosineBy similarity
Modified residuei176 – 1761PhosphoserineBy similarity
Modified residuei270 – 2701PhosphoserineBy similarity
Modified residuei434 – 4341PhosphoserineBy similarity
Modified residuei532 – 5321PhosphoserineCombined sources
Modified residuei555 – 5551PhosphoserineCombined sources
Modified residuei556 – 5561PhosphoserineCombined sources

Keywords - PTMi

Cleavage on pair of basic residues, Phosphoprotein, Sulfation

Proteomic databases

MaxQBiQ03517.
PaxDbiQ03517.
PeptideAtlasiQ03517.
PRIDEiQ03517.

PTM databases

iPTMnetiQ03517.
PhosphoSiteiQ03517.

Expressioni

Gene expression databases

BgeeiQ03517.
CleanExiMM_SCG2.
ExpressionAtlasiQ03517. baseline and differential.
GenevisibleiQ03517. MM.

Interactioni

GO - Molecular functioni

  • cytokine activity Source: HGNC

Protein-protein interaction databases

BioGridi203090. 1 interaction.
IntActiQ03517. 1 interaction.
MINTiMINT-4133926.
STRINGi10090.ENSMUSP00000062556.

Structurei

3D structure databases

ProteinModelPortaliQ03517.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IFXN. Eukaryota.
ENOG4111F4G. LUCA.
GeneTreeiENSGT00390000010895.
HOGENOMiHOG000059543.
HOVERGENiHBG054148.
InParanoidiQ03517.
OMAiEIVEEQY.
OrthoDBiEOG7K0ZC3.
PhylomeDBiQ03517.
TreeFamiTF334018.

Family and domain databases

InterProiIPR001990. Granin.
[Graphical view]
PfamiPF01271. Granin. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q03517-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGAKAYRLG AVLLLIHLIF LISGAEAASF QRNQLLQKEP DLRLENVQKF
60 70 80 90 100
PSPEMIRALE YIEKLRQQAH REESSPDYNP YQGVSVPLQL KENGEESHLA
110 120 130 140 150
ESSRDALSED EWMRIILEAL RQAENEPPSA PKENKPYALN LEKNFPVDTP
160 170 180 190 200
DDYETQQWPE RKLKHMRFPL MYEENSRENP FKRTNEIVEE QYTPQSLATL
210 220 230 240 250
ESVFQELGKL TGPSNQKRER VDEEQKLYTD DEDDVYKTNN IAYEDVVGGE
260 270 280 290 300
DWSPIEEKIE TQTQEEVRDS KENTEKNEQI NEEMKRSGQL GLPDEENRRE
310 320 330 340 350
SKDQLSEDAS KVITYLRRLV NAVGSGRSQS GPNGDRAARL LQKPLDSQSI
360 370 380 390 400
YQLIEISRNL QIPPEDLIEM LKAGEKPNGL VEPEQDLELA VDLDDIPEAD
410 420 430 440 450
LDRPDMFQSK MLSKGGYPKA PGRGMVEALP DGLSVEDILN VLGMENVVNQ
460 470 480 490 500
KSPYFPNQYS QDKALMRLPY GPGKSRANQI PKVAWIPDVE SRQAPYENLN
510 520 530 540 550
DQELGEYLAR MLVKYPELLN TNQLKRVPSP VSSEDDLQEE EQLEQAIKEH
560 570 580 590 600
LGPGSSQEME RLAKVSKRIP VGSLKNEDTP NRQYLDEDML LKVLEYLNQE
610
QAEQGREHLA KRAMENM
Length:617
Mass (Da):70,644
Last modified:October 1, 1993 - v1
Checksum:i42D0D5D5546F4BDD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti238 – 2381T → A in BAB22476 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68837 Genomic DNA. Translation: CAA48727.1.
AK002953 mRNA. Translation: BAB22476.2.
CCDSiCCDS15089.1.
PIRiS27389.
RefSeqiNP_033155.1. NM_009129.2.
UniGeneiMm.5038.

Genome annotation databases

EnsembliENSMUST00000049972; ENSMUSP00000062556; ENSMUSG00000050711.
GeneIDi20254.
KEGGimmu:20254.
UCSCiuc007bqr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68837 Genomic DNA. Translation: CAA48727.1.
AK002953 mRNA. Translation: BAB22476.2.
CCDSiCCDS15089.1.
PIRiS27389.
RefSeqiNP_033155.1. NM_009129.2.
UniGeneiMm.5038.

3D structure databases

ProteinModelPortaliQ03517.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203090. 1 interaction.
IntActiQ03517. 1 interaction.
MINTiMINT-4133926.
STRINGi10090.ENSMUSP00000062556.

PTM databases

iPTMnetiQ03517.
PhosphoSiteiQ03517.

Proteomic databases

MaxQBiQ03517.
PaxDbiQ03517.
PeptideAtlasiQ03517.
PRIDEiQ03517.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000049972; ENSMUSP00000062556; ENSMUSG00000050711.
GeneIDi20254.
KEGGimmu:20254.
UCSCiuc007bqr.1. mouse.

Organism-specific databases

CTDi7857.
MGIiMGI:103033. Scg2.

Phylogenomic databases

eggNOGiENOG410IFXN. Eukaryota.
ENOG4111F4G. LUCA.
GeneTreeiENSGT00390000010895.
HOGENOMiHOG000059543.
HOVERGENiHBG054148.
InParanoidiQ03517.
OMAiEIVEEQY.
OrthoDBiEOG7K0ZC3.
PhylomeDBiQ03517.
TreeFamiTF334018.

Miscellaneous databases

ChiTaRSiScg2. mouse.
PROiQ03517.
SOURCEiSearch...

Gene expression databases

BgeeiQ03517.
CleanExiMM_SCG2.
ExpressionAtlasiQ03517. baseline and differential.
GenevisibleiQ03517. MM.

Family and domain databases

InterProiIPR001990. Granin.
[Graphical view]
PfamiPF01271. Granin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 119-516.
    Strain: C57BL/6J.
    Tissue: Brain.
  3. "Formation and sequence analysis of secretoneurin, a neuropeptide derived from secretogranin II, in mammalian, bird, reptile, amphibian and fish brains."
    Leitner B., Schneitler C., Klocker H., Volknandt W., Zimmermann H., Winkler H., Fischer-Colbrie R.
    Neurosci. Lett. 248:105-108(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 184-216.
  4. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 452-463, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-532; SER-555 AND SER-556, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue and Pancreas.

Entry informationi

Entry nameiSCG2_MOUSE
AccessioniPrimary (citable) accession number: Q03517
Secondary accession number(s): Q80Y79, Q9CW80
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: July 6, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds calcium with a low-affinity.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.