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Protein

Secretogranin-2

Gene

SCG2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. chemoattractant activity Source: HGNC
  2. cytokine activity Source: HGNC

GO - Biological processi

  1. angiogenesis Source: HGNC
  2. endothelial cell migration Source: HGNC
  3. eosinophil chemotaxis Source: HGNC
  4. induction of positive chemotaxis Source: HGNC
  5. inflammatory response Source: HGNC
  6. intracellular signal transduction Source: HGNC
  7. MAPK cascade Source: HGNC
  8. negative regulation of endothelial cell apoptotic process Source: BHF-UCL
  9. negative regulation of endothelial cell proliferation Source: HGNC
  10. negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
  11. positive chemotaxis Source: BHF-UCL
  12. positive regulation of endothelial cell proliferation Source: HGNC
  13. protein secretion Source: ProtInc
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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:10575. SCG2.

Subcellular locationi

Secreted
Note: Neuroendocrine and endocrine secretory granules.

GO - Cellular componenti

  1. extracellular space Source: HGNC
  2. secretory granule Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34987.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence AnalysisAdd
BLAST
Propeptidei28 – 303Sequence AnalysisPRO_0000005452
Chaini31 – 617587Secretogranin-2PRO_0000005453Add
BLAST
Peptidei182 – 21433SecretoneurinPRO_0000005454Add
BLAST
Peptidei527 – 56640ManserinBy similarityPRO_0000432735Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei151 – 1511Sulfotyrosine1 Publication

Post-translational modificationi

O-glycosylated.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Glycoprotein, Sulfation

Proteomic databases

MaxQBiP13521.
PaxDbiP13521.
PRIDEiP13521.

PTM databases

PhosphoSiteiP13521.

Expressioni

Gene expression databases

BgeeiP13521.
CleanExiHS_SCG2.
ExpressionAtlasiP13521. baseline and differential.
GenevestigatoriP13521.

Organism-specific databases

HPAiCAB002519.
HPA011893.

Interactioni

Protein-protein interaction databases

BioGridi113611. 5 interactions.
IntActiP13521. 6 interactions.
MINTiMINT-2864303.
STRINGi9606.ENSP00000304133.

Structurei

3D structure databases

ProteinModelPortaliP13521.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni182 – 20019O-glycosylated at one siteAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG47177.
GeneTreeiENSGT00390000010895.
HOGENOMiHOG000059543.
HOVERGENiHBG054148.
InParanoidiP13521.
OMAiEIVEEQY.
OrthoDBiEOG7K0ZC3.
PhylomeDBiP13521.
TreeFamiTF334018.

Family and domain databases

InterProiIPR018054. Chromogranin_CS.
IPR001990. Granin.
[Graphical view]
PfamiPF01271. Granin. 1 hit.
[Graphical view]
PROSITEiPS00422. GRANINS_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P13521-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEAKTHWLG AALSLIPLIF LISGAEAASF QRNQLLQKEP DLRLENVQKF
60 70 80 90 100
PSPEMIRALE YIENLRQQAH KEESSPDYNP YQGVSVPLQQ KENGDESHLP
110 120 130 140 150
ERDSLSEEDW MRIILEALRQ AENEPQSAPK ENKPYALNSE KNFPMDMSDD
160 170 180 190 200
YETQQWPERK LKHMQFPPMY EENSRDNPFK RTNEIVEEQY TPQSLATLES
210 220 230 240 250
VFQELGKLTG PNNQKRERMD EEQKLYTDDE DDIYKANNIA YEDVVGGEDW
260 270 280 290 300
NPVEEKIESQ TQEEVRDSKE NIEKNEQIND EMKRSGQLGI QEEDLRKESK
310 320 330 340 350
DQLSDDVSKV IAYLKRLVNA AGSGRLQNGQ NGERATRLFE KPLDSQSIYQ
360 370 380 390 400
LIEISRNLQI PPEDLIEMLK TGEKPNGSVE PERELDLPVD LDDISEADLD
410 420 430 440 450
HPDLFQNRML SKSGYPKTPG RAGTEALPDG LSVEDILNLL GMESAANQKT
460 470 480 490 500
SYFPNPYNQE KVLPRLPYGA GRSRSNQLPK AAWIPHVENR QMAYENLNDK
510 520 530 540 550
DQELGEYLAR MLVKYPEIIN SNQVKRVPGQ GSSEDDLQEE EQIEQAIKEH
560 570 580 590 600
LNQGSSQETD KLAPVSKRFP VGPPKNDDTP NRQYWDEDLL MKVLEYLNQE
610
KAEKGREHIA KRAMENM
Length:617
Mass (Da):70,941
Last modified:April 3, 2007 - v2
Checksum:iA81C9C091DE9DF6B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti273 – 2731E → G in AAA36607 (PubMed:2745426).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti61 – 611Y → H.
Corresponds to variant rs16864976 [ dbSNP | Ensembl ].
VAR_031555
Natural varianti196 – 1961A → V.
Corresponds to variant rs1438157 [ dbSNP | Ensembl ].
VAR_048755
Natural varianti294 – 2941D → G.1 Publication
Corresponds to variant rs17852053 [ dbSNP | Ensembl ].
VAR_031556
Natural varianti421 – 4211R → G.1 Publication
Corresponds to variant rs17856669 [ dbSNP | Ensembl ].
VAR_031557
Natural varianti535 – 5351D → G.1 Publication
Corresponds to variant rs17852054 [ dbSNP | Ensembl ].
VAR_031558
Natural varianti564 – 5641P → L.
Corresponds to variant rs36043001 [ dbSNP | Ensembl ].
VAR_031559

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25756 mRNA. Translation: AAA36607.1.
AK312452 mRNA. Translation: BAG35359.1.
AC012512 Genomic DNA. Translation: AAY24243.1.
CH471063 Genomic DNA. Translation: EAW70811.1.
BC022509 mRNA. Translation: AAH22509.1.
CCDSiCCDS2457.1.
PIRiA34174.
RefSeqiNP_003460.2. NM_003469.4.
UniGeneiHs.516726.

Genome annotation databases

EnsembliENST00000305409; ENSP00000304133; ENSG00000171951.
GeneIDi7857.
KEGGihsa:7857.
UCSCiuc002vnm.3. human.

Polymorphism databases

DMDMi143811457.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25756 mRNA. Translation: AAA36607.1.
AK312452 mRNA. Translation: BAG35359.1.
AC012512 Genomic DNA. Translation: AAY24243.1.
CH471063 Genomic DNA. Translation: EAW70811.1.
BC022509 mRNA. Translation: AAH22509.1.
CCDSiCCDS2457.1.
PIRiA34174.
RefSeqiNP_003460.2. NM_003469.4.
UniGeneiHs.516726.

3D structure databases

ProteinModelPortaliP13521.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113611. 5 interactions.
IntActiP13521. 6 interactions.
MINTiMINT-2864303.
STRINGi9606.ENSP00000304133.

PTM databases

PhosphoSiteiP13521.

Polymorphism databases

DMDMi143811457.

Proteomic databases

MaxQBiP13521.
PaxDbiP13521.
PRIDEiP13521.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000305409; ENSP00000304133; ENSG00000171951.
GeneIDi7857.
KEGGihsa:7857.
UCSCiuc002vnm.3. human.

Organism-specific databases

CTDi7857.
GeneCardsiGC02M224425.
H-InvDBHIX0002882.
HGNCiHGNC:10575. SCG2.
HPAiCAB002519.
HPA011893.
MIMi118930. gene.
neXtProtiNX_P13521.
PharmGKBiPA34987.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG47177.
GeneTreeiENSGT00390000010895.
HOGENOMiHOG000059543.
HOVERGENiHBG054148.
InParanoidiP13521.
OMAiEIVEEQY.
OrthoDBiEOG7K0ZC3.
PhylomeDBiP13521.
TreeFamiTF334018.

Miscellaneous databases

ChiTaRSiSCG2. human.
GeneWikiiSCG2.
GenomeRNAii7857.
NextBioi30297.
PROiP13521.
SOURCEiSearch...

Gene expression databases

BgeeiP13521.
CleanExiHS_SCG2.
ExpressionAtlasiP13521. baseline and differential.
GenevestigatoriP13521.

Family and domain databases

InterProiIPR018054. Chromogranin_CS.
IPR001990. Granin.
[Graphical view]
PfamiPF01271. Granin. 1 hit.
[Graphical view]
PROSITEiPS00422. GRANINS_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The primary structure of human secretogranin II, a widespread tyrosine-sulfated secretory granule protein that exhibits low pH- and calcium-induced aggregation."
    Gerdes H.-H., Rosa P., Phillips E., Baeuerle P.A., Frank R., Argos P., Huttner W.B.
    J. Biol. Chem. 264:12009-12015(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SULFATION AT TYR-151.
    Tissue: Pituitary.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Caudate nucleus.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS GLY-294; GLY-421 AND GLY-535.
    Tissue: Brain.
  6. "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(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 182-214.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Pituitary.
  8. "LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins."
    Halim A., Ruetschi U., Larson G., Nilsson J.
    J. Proteome Res. 12:573-584(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiSCG2_HUMAN
AccessioniPrimary (citable) accession number: P13521
Secondary accession number(s): B2R662, Q53T11, Q8TBH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: April 3, 2007
Last modified: April 1, 2015
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Binds calcium with a low-affinity.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.