Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P05060 (SCG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Secretogranin-1
Alternative name(s):
Chromogranin-B
Short name=CgB
Secretogranin I
Short name=SgI

Cleaved into the following 2 chains:

  1. GAWK peptide
  2. CCB peptide
Gene names
Name:CHGB
Synonyms:SCG1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length677 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subcellular location

Secreted. Note: Neuroendocrine and endocrine secretory granules.

Tissue specificity

Expressed in the adrenal medulla, and in pheochromocytoma. Not expressed in liver. Ref.1

Post-translational modification

Extensively processed by limited proteolysis at conserved basic residues. Alternative processing are seen in different tissues By similarity.

O-glycosylated. Ref.14

Sequence similarities

Belongs to the chromogranin/secretogranin protein family.

Sequence caution

The sequence BAD92949.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Phosphoprotein
Sulfation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

secretory granule

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionhormone activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SMAD2Q157962EBI-712619,EBI-1040141

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.1 Ref.8
Chain21 – 677657Secretogranin-1
PRO_0000005438
Peptide440 – 51374GAWK peptide Ref.10
PRO_0000005439
Peptide617 – 67357CCB peptide Ref.11
PRO_0000005440

Regions

Region116 – 1205O-glycosylated at one site
Compositional bias163 – 1719Poly-Glu

Amino acid modifications

Modified residue791Phosphothreonine Probable
Modified residue991Phosphoserine Potential
Modified residue1001Phosphoserine Potential
Modified residue1491Phosphoserine Ref.12 Ref.13
Modified residue1831Phosphoserine By similarity
Modified residue2591Phosphoserine Ref.13
Modified residue2631Phosphoserine Ref.13
Modified residue2931Phosphoserine Potential
Modified residue2941Phosphoserine Potential
Modified residue3111Phosphoserine Ref.13
Modified residue3351Phosphoserine Ref.13
Modified residue3411Sulfotyrosine By similarity
Modified residue3771Phosphoserine By similarity
Modified residue3801Phosphoserine
Modified residue4051Phosphoserine Ref.12 Ref.13
Modified residue4711Sulfotyrosine Potential
Modified residue4741Sulfotyrosine Probable
Modified residue5331Phosphoserine Potential
Modified residue5341Phosphoserine Potential
Modified residue5661Sulfotyrosine Probable
Modified residue5681Sulfotyrosine Potential
Modified residue6171Phosphoserine Ref.13
Modified residue6241Sulfotyrosine By similarity
Modified residue6261Phosphoserine By similarity
Modified residue6311Phosphoserine By similarity
Disulfide bond36 ↔ 57

Natural variations

Natural variant931S → T. Ref.2 Ref.4
Corresponds to variant rs6085324 [ dbSNP | Ensembl ].
VAR_043578
Natural variant1171K → N.
Corresponds to variant rs236150 [ dbSNP | Ensembl ].
VAR_024414
Natural variant1451D → N.
Corresponds to variant rs6133278 [ dbSNP | Ensembl ].
VAR_028235
Natural variant1781R → Q. Ref.2 Ref.4
Corresponds to variant rs910122 [ dbSNP | Ensembl ].
VAR_020287
Natural variant2001N → H.
Corresponds to variant rs881118 [ dbSNP | Ensembl ].
VAR_028236
Natural variant2321R → Q.
Corresponds to variant rs6139873 [ dbSNP | Ensembl ].
VAR_028237
Natural variant2431T → A. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6 Ref.7
Corresponds to variant rs236151 [ dbSNP | Ensembl ].
VAR_024415
Natural variant3531A → G. Ref.2 Ref.4
Corresponds to variant rs236152 [ dbSNP | Ensembl ].
VAR_024416
Natural variant4131P → L.
Corresponds to variant rs742710 [ dbSNP | Ensembl ].
VAR_028238
Natural variant4171R → H. Ref.2 Ref.4
Corresponds to variant rs742711 [ dbSNP | Ensembl ].
VAR_022012

Experimental info

Sequence conflict241D → E in BAF82075. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P05060 [UniParc].

Last modified November 2, 2010. Version 2.
Checksum: BFDC97F7B21245B3

FASTA67778,276
        10         20         30         40         50         60 
MQPTLLLSLL GAVGLAAVNS MPVDNRNHNE GMVTRCIIEV LSNALSKSSA PPITPECRQV 

        70         80         90        100        110        120 
LKTSRKDVKD KETTENENTK FEVRLLRDPA DASEAHESSS RGEAGAPGEE DIQGPTKADT 

       130        140        150        160        170        180 
EKWAEGGGHS RERADEPQWS LYPSDSQVSE EVKTRHSEKS QREDEEEEEG ENYQKGERGE 

       190        200        210        220        230        240 
DSSEEKHLEE PGETQNAFLN ERKQASAIKK EELVARSETH AAGHSQEKTH SREKSSQESG 

       250        260        270        280        290        300 
EETGSQENHP QESKGQPRSQ EESEEGEEDA TSEVDKRRTR PRHHHGRSRP DRSSQGGSLP 

       310        320        330        340        350        360 
SEEKGHPQEE SEESNVSMAS LGEKRDHHST HYRASEEEPE YGEEIKGYPG VQAPEDLEWE 

       370        380        390        400        410        420 
RYRGRGSEEY RAPRPQSEES WDEEDKRNYP SLELDKMAHG YGEESEEERG LEPGKGRHHR 

       430        440        450        460        470        480 
GRGGEPRAYF MSDTREEKRF LGEGHHRVQE NQMDKARRHP QGAWKELDRN YLNYGEEGAP 

       490        500        510        520        530        540 
GKWQQQGDLQ DTKENREEAR FQDKQYSSHH TAEKRKRLGE LFNPYYDPLQ WKSSHFERRD 

       550        560        570        580        590        600 
NMNDNFLEGE EENELTLNEK NFFPEYNYDW WEKKPFSEDV NWGYEKRNLA RVPKLDLKRQ 

       610        620        630        640        650        660 
YDRVAQLDQL LHYRKKSAEF PDFYDSEEPV STHQEAENEK DRADQTVLTE DEKKELENLA 

       670 
AMDLELQKIA EKFSQRG 

« Hide

References

« Hide 'large scale' references
[1]"The primary structure of human secretogranin I (chromogranin B): comparison with chromogranin A reveals homologous terminal domains and a large intervening variable region."
Benedum U.M., Lamouroux A., Konecki D.S., Hille A., Baeuerle P.A., Frank R., Lottspeich F., Mallet J., Huttner W.B.
EMBO J. 6:1203-1211(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-34; 85-93; 334-340 AND 347-355, TISSUE SPECIFICITY, VARIANT ALA-243.
Tissue: Adrenal medulla.
[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. expand/collapse author list , 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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS THR-93; GLN-178; ALA-243; GLY-353 AND HIS-417.
Tissue: Adrenal gland.
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-243.
[4]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS THR-93; GLN-178; ALA-243; GLY-353 AND HIS-417.
Tissue: Brain.
[5]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ALA-243.
[7]"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], VARIANT ALA-243.
Tissue: Lung.
[8]"Chromogranin B: isolation from pheochromocytoma, N-terminal sequence, tissue distribution and secretory vesicle processing."
Gill B.M., Barbosa J.A., Dinh T.Q., Garrod S., O'Connor D.T.
Regul. Pept. 33:223-235(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-48.
[9]"Identification of a new chromogranin B fragment (314-365) in endocrine tumors."
Woussen-Colle M.-C., Gourlet P., Vandermeers A., Vandermeers-Piret M.-C., D'Haens J., Velkeniers B., Robberecht P.
Peptides 16:231-236(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 334-385.
[10]"GAWK, a novel human pituitary polypeptide: isolation, immunocytochemical localization and complete amino acid sequence."
Benjannet S., Leduc R., Lazure C., Seidah N.G., Marcinkiewicz M., Chretien M.
Biochem. Biophys. Res. Commun. 126:602-609(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 440-513.
Tissue: Pituitary.
[11]"Chromogranin B (secretogranin I), a putative precursor of two novel pituitary peptides through processing at paired basic residues."
Benjannet S., Leduc R., Adrouche N., Falgueyret J.P., Marcinkiewicz M., Seidah N.G., Mbikay M., Lazure C., Chretien M.
FEBS Lett. 224:142-148(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 617-673.
Tissue: Pituitary.
[12]"Identification and characterization of phosphorylated proteins in the human pituitary."
Giorgianni F., Beranova-Giorgianni S., Desiderio D.M.
Proteomics 4:587-598(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-149 AND SER-405.
Tissue: Pituitary.
[13]"Phosphoproteomic analysis of the human pituitary."
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.
Pituitary 9:109-120(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-259; SER-263; SER-311; SER-335; SER-405 AND SER-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Pituitary.
[14]"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(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00064 mRNA. Translation: CAA68271.1.
AK289386 mRNA. Translation: BAF82075.1.
CR456726 mRNA. Translation: CAG33007.1.
AB209712 mRNA. Translation: BAD92949.1. Different initiation.
AL035461 Genomic DNA. Translation: CAB55272.1.
AL035461 Genomic DNA. Translation: CAC34360.1.
CH471133 Genomic DNA. Translation: EAX10410.1.
BC000375 mRNA. Translation: AAH00375.1.
PIRCNHUB. A29264.
RefSeqNP_001810.2. NM_001819.2.
UniGeneHs.516874.

3D structure databases

ProteinModelPortalP05060.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107539. 29 interactions.
IntActP05060. 31 interactions.
MINTMINT-1414600.
STRING9606.ENSP00000368244.

PTM databases

PhosphoSiteP05060.

Polymorphism databases

DMDM311033509.

Proteomic databases

PaxDbP05060.
PeptideAtlasP05060.
PRIDEP05060.

Protocols and materials databases

DNASU1114.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378961; ENSP00000368244; ENSG00000089199.
GeneID1114.
KEGGhsa:1114.
UCSCuc002wmg.3. human.

Organism-specific databases

CTD1114.
GeneCardsGC20P005891.
H-InvDBHIX0015625.
HGNCHGNC:1930. CHGB.
HPACAB009403.
HPA008759.
HPA012602.
MIM118920. gene.
neXtProtNX_P05060.
PharmGKBPA26462.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39839.
HOVERGENHBG057317.
InParanoidP05060.
OMANWGYEKR.
OrthoDBEOG74N5GF.
PhylomeDBP05060.
TreeFamTF336596.

Gene expression databases

BgeeP05060.
CleanExHS_CHGB.
GenevestigatorP05060.

Family and domain databases

InterProIPR001819. Chromogranin_AB.
IPR018054. Chromogranin_CS.
IPR001990. Granin.
[Graphical view]
PANTHERPTHR10583. PTHR10583. 1 hit.
PfamPF01271. Granin. 1 hit.
[Graphical view]
PRINTSPR00659. CHROMOGRANIN.
PROSITEPS00422. GRANINS_1. 1 hit.
PS00423. GRANINS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCHGB. human.
GeneWikiSecretoneurin.
GenomeRNAi1114.
NextBio4622.
PROP05060.
SOURCESearch...

Entry information

Entry nameSCG1_HUMAN
AccessionPrimary (citable) accession number: P05060
Secondary accession number(s): A8K021 expand/collapse secondary AC list , Q59EU9, Q6IBS6, Q9BQV6, Q9UC25, Q9UJA6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: November 2, 2010
Last modified: April 16, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM