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Protein

Somatostatin

Gene

SST

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

Functioni

Somatostatin inhibits the release of somatotropin.

GO - Molecular functioni

  • hormone activity Source: UniProtKB

GO - Biological processi

  • cell-cell signaling Source: UniProtKB
  • cell surface receptor signaling pathway Source: UniProtKB
  • digestion Source: UniProtKB
  • G-protein coupled receptor signaling pathway Source: UniProtKB
  • hormone-mediated apoptotic signaling pathway Source: UniProtKB
  • hyperosmotic response Source: Ensembl
  • negative regulation of cell proliferation Source: UniProtKB
  • regulation of cell migration Source: Ensembl
  • response to amino acid Source: Ensembl
  • response to drug Source: Ensembl
  • response to heat Source: Ensembl
  • response to nutrient Source: UniProtKB
  • response to steroid hormone Source: Ensembl
  • synaptic transmission Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hormone

Enzyme and pathway databases

ReactomeiREACT_14819. Peptide ligand-binding receptors.
REACT_19231. G alpha (i) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Somatostatin
Alternative name(s):
Growth hormone release-inhibiting factor
Cleaved into the following 2 chains:
Gene namesi
Name:SST
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:11329. SST.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • neuronal cell body Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Pharmaceutical usei

A synthetic analog known as octreotide or SMS 201-995 is available under the name Sandostatin (Novartis). It is used for the treatment of a variety of disorders including acromegaly and the symptomatic treatment of carcinoid tumors and vasoactive intestinal peptide tumors.

Organism-specific databases

PharmGKBiPA36153.

Chemistry

DrugBankiDB00847. Cysteamine.

Polymorphism and mutation databases

BioMutaiSST.
DMDMi47117741.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Add
BLAST
Propeptidei25 – 8864PRO_0000033086Add
BLAST
Peptidei89 – 11628Somatostatin-28PRO_0000033087Add
BLAST
Peptidei103 – 11614Somatostatin-14PRO_0000033088Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi105 ↔ 116Combined sources

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond

Proteomic databases

PaxDbiP61278.
PeptideAtlasiP61278.
PRIDEiP61278.

Miscellaneous databases

PMAP-CutDBP61278.

Expressioni

Gene expression databases

BgeeiP61278.
CleanExiHS_SST.
GenevisibleiP61278. HS.

Organism-specific databases

HPAiCAB000075.
HPA019472.

Interactioni

Protein-protein interaction databases

BioGridi112628. 2 interactions.
STRINGi9606.ENSP00000287641.

Structurei

Secondary structure

1
116
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi107 – 1148Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P2Wmodel-A1-116[»]
2MI1NMR-A103-116[»]
ProteinModelPortaliP61278.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the somatostatin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG44503.
GeneTreeiENSGT00510000047914.
HOGENOMiHOG000036630.
HOVERGENiHBG017816.
InParanoidiP61278.
KOiK05237.
OMAiRMELQRS.
OrthoDBiEOG7H4DXK.
PhylomeDBiP61278.
TreeFamiTF333185.

Family and domain databases

InterProiIPR004250. Somatostatin.
IPR018142. Somatostatin/Cortistatin_C.
[Graphical view]
PANTHERiPTHR10558. PTHR10558. 1 hit.
PfamiPF03002. Somatostatin. 1 hit.
[Graphical view]
PIRSFiPIRSF001814. Somatostatin. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P61278-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSCRLQCAL AALSIVLALG CVTGAPSDPR LRQFLQKSLA AAAGKQELAK
60 70 80 90 100
YFLAELLSEP NQTENDALEP EDLSQAAEQD EMRLELQRSA NSNPAMAPRE
110
RKAGCKNFFW KTFTSC
Length:116
Mass (Da):12,736
Last modified:July 21, 1986 - v1
Checksum:iAB49BB89DC9DD8DA
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111A → V.
Corresponds to variant rs35603672 [ dbSNP | Ensembl ].
VAR_034499
Natural varianti61 – 611N → T.
Corresponds to variant rs33934967 [ dbSNP | Ensembl ].
VAR_034500

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00306 Genomic DNA. Translation: AAA60566.1.
AK312177 mRNA. Translation: BAG35110.1.
CH471052 Genomic DNA. Translation: EAW78145.1.
BC032625 mRNA. Translation: AAH32625.1.
CCDSiCCDS3288.1.
PIRiA43614. RIHUS1.
RefSeqiNP_001039.1. NM_001048.3.
UniGeneiHs.12409.

Genome annotation databases

EnsembliENST00000287641; ENSP00000287641; ENSG00000157005.
GeneIDi6750.
KEGGihsa:6750.
UCSCiuc003frn.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Somatostatin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00306 Genomic DNA. Translation: AAA60566.1.
AK312177 mRNA. Translation: BAG35110.1.
CH471052 Genomic DNA. Translation: EAW78145.1.
BC032625 mRNA. Translation: AAH32625.1.
CCDSiCCDS3288.1.
PIRiA43614. RIHUS1.
RefSeqiNP_001039.1. NM_001048.3.
UniGeneiHs.12409.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P2Wmodel-A1-116[»]
2MI1NMR-A103-116[»]
ProteinModelPortaliP61278.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112628. 2 interactions.
STRINGi9606.ENSP00000287641.

Chemistry

BindingDBiP61278.
ChEMBLiCHEMBL1795130.
DrugBankiDB00847. Cysteamine.

Polymorphism and mutation databases

BioMutaiSST.
DMDMi47117741.

Proteomic databases

PaxDbiP61278.
PeptideAtlasiP61278.
PRIDEiP61278.

Protocols and materials databases

DNASUi6750.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000287641; ENSP00000287641; ENSG00000157005.
GeneIDi6750.
KEGGihsa:6750.
UCSCiuc003frn.3. human.

Organism-specific databases

CTDi6750.
GeneCardsiGC03M187386.
HGNCiHGNC:11329. SST.
HPAiCAB000075.
HPA019472.
MIMi182450. gene.
neXtProtiNX_P61278.
PharmGKBiPA36153.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG44503.
GeneTreeiENSGT00510000047914.
HOGENOMiHOG000036630.
HOVERGENiHBG017816.
InParanoidiP61278.
KOiK05237.
OMAiRMELQRS.
OrthoDBiEOG7H4DXK.
PhylomeDBiP61278.
TreeFamiTF333185.

Enzyme and pathway databases

ReactomeiREACT_14819. Peptide ligand-binding receptors.
REACT_19231. G alpha (i) signalling events.

Miscellaneous databases

ChiTaRSiSST. human.
GeneWikiiSomatostatin.
GenomeRNAii6750.
NextBioi26332.
PMAP-CutDBP61278.
PROiP61278.
SOURCEiSearch...

Gene expression databases

BgeeiP61278.
CleanExiHS_SST.
GenevisibleiP61278. HS.

Family and domain databases

InterProiIPR004250. Somatostatin.
IPR018142. Somatostatin/Cortistatin_C.
[Graphical view]
PANTHERiPTHR10558. PTHR10558. 1 hit.
PfamiPF03002. Somatostatin. 1 hit.
[Graphical view]
PIRSFiPIRSF001814. Somatostatin. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], STRUCTURE BY NMR OF 103-116, DISULFIDE BONDS.
  2. "Sequence of the human somatostatin I gene."
    Shen L.-P., Rutter W.J.
    Science 224:168-171(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Fetal brain.
  6. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSMS_HUMAN
AccessioniPrimary (citable) accession number: P61278
Secondary accession number(s): B2R5G3, P01166
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 24, 2015
This is version 103 of the entry and version 1 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

Keywords - Technical termi

3D-structure, Complete proteome, Pharmaceutical, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.