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Protein

Cystatin-SA

Gene

CST2

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

Functioni

Thiol protease inhibitor.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei32 – 321Reactive site

GO - Molecular functioni

  • cysteine-type endopeptidase inhibitor activity Source: ProtInc

GO - Biological processi

  • detection of chemical stimulus involved in sensory perception of bitter taste Source: UniProtKB
  • negative regulation of endopeptidase activity Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Thiol protease inhibitor

Protein family/group databases

MEROPSiI25.009.

Names & Taxonomyi

Protein namesi
Recommended name:
Cystatin-SA
Alternative name(s):
Cystatin-2
Cystatin-S5
Gene namesi
Name:CST2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:2474. CST2.

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26975.

Polymorphism and mutation databases

BioMutaiCST2.
DMDMi118192.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20202 PublicationsAdd
BLAST
Chaini21 – 141121Cystatin-SAPRO_0000006652Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi94 ↔ 1041 Publication
Disulfide bondi118 ↔ 1381 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP09228.
PeptideAtlasiP09228.
PRIDEiP09228.

Expressioni

Tissue specificityi

Expressed in submandibular and sublingual saliva but not in parotid saliva (at protein level). Expressed in submandibular gland and parotid gland.2 Publications

Gene expression databases

BgeeiP09228.
CleanExiHS_CST2.
GenevisibleiP09228. HS.

Organism-specific databases

HPAiCAB024963.
HPA043706.
HPA044763.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ADAMTSL4Q6UY14-33EBI-8832659,EBI-10173507
NOTCH2NLQ7Z3S93EBI-8832659,EBI-945833
PSMA3P257883EBI-8832659,EBI-348380

Protein-protein interaction databases

BioGridi107852. 21 interactions.
IntActiP09228. 3 interactions.
STRINGi9606.ENSP00000307540.

Structurei

3D structure databases

ProteinModelPortaliP09228.
SMRiP09228. Positions 32-140.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi76 – 805Secondary area of contact

Sequence similaritiesi

Belongs to the cystatin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IZZH. Eukaryota.
ENOG4112CFJ. LUCA.
GeneTreeiENSGT00840000129787.
HOGENOMiHOG000231754.
HOVERGENiHBG009556.
InParanoidiP09228.
KOiK13898.
OMAiDDEVQHA.
OrthoDBiEOG7M98J9.
PhylomeDBiP09228.

Family and domain databases

InterProiIPR027214. Cystatin.
IPR000010. Cystatin_dom.
IPR018073. Prot_inh_cystat_CS.
[Graphical view]
PANTHERiPTHR11413. PTHR11413. 1 hit.
PfamiPF00031. Cystatin. 1 hit.
[Graphical view]
SMARTiSM00043. CY. 1 hit.
[Graphical view]
PROSITEiPS00287. CYSTATIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P09228-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAWPLCTLLL LLATQAVALA WSPQEEDRII EGGIYDADLN DERVQRALHF
60 70 80 90 100
VISEYNKATE DEYYRRLLRV LRAREQIVGG VNYFFDIEVG RTICTKSQPN
110 120 130 140
LDTCAFHEQP ELQKKQLCSF QIYEVPWEDR MSLVNSRCQE A
Length:141
Mass (Da):16,445
Last modified:July 1, 1989 - v1
Checksum:iEB54915B1B977AA2
GO

Mass spectrometryi

Molecular mass is 14336.9856±0.0158 Da from positions 21 - 141. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19673, M19671, M19672 Genomic DNA. Translation: AAA36116.1.
AF319564 Genomic DNA. Translation: AAK11570.1.
AL591074 Genomic DNA. Translation: CAC94784.1.
BC062679 mRNA. Translation: AAH62679.1.
CCDSiCCDS13161.1.
PIRiB29632.
RefSeqiNP_001313.1. NM_001322.2.
UniGeneiHs.669305.

Genome annotation databases

EnsembliENST00000304725; ENSP00000307540; ENSG00000170369.
GeneIDi1470.
KEGGihsa:1470.
UCSCiuc002wtq.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19673, M19671, M19672 Genomic DNA. Translation: AAA36116.1.
AF319564 Genomic DNA. Translation: AAK11570.1.
AL591074 Genomic DNA. Translation: CAC94784.1.
BC062679 mRNA. Translation: AAH62679.1.
CCDSiCCDS13161.1.
PIRiB29632.
RefSeqiNP_001313.1. NM_001322.2.
UniGeneiHs.669305.

3D structure databases

ProteinModelPortaliP09228.
SMRiP09228. Positions 32-140.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107852. 21 interactions.
IntActiP09228. 3 interactions.
STRINGi9606.ENSP00000307540.

Protein family/group databases

MEROPSiI25.009.

Polymorphism and mutation databases

BioMutaiCST2.
DMDMi118192.

Proteomic databases

PaxDbiP09228.
PeptideAtlasiP09228.
PRIDEiP09228.

Protocols and materials databases

DNASUi1470.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000304725; ENSP00000307540; ENSG00000170369.
GeneIDi1470.
KEGGihsa:1470.
UCSCiuc002wtq.2. human.

Organism-specific databases

CTDi1470.
GeneCardsiCST2.
HGNCiHGNC:2474. CST2.
HPAiCAB024963.
HPA043706.
HPA044763.
MIMi123856. gene.
neXtProtiNX_P09228.
PharmGKBiPA26975.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IZZH. Eukaryota.
ENOG4112CFJ. LUCA.
GeneTreeiENSGT00840000129787.
HOGENOMiHOG000231754.
HOVERGENiHBG009556.
InParanoidiP09228.
KOiK13898.
OMAiDDEVQHA.
OrthoDBiEOG7M98J9.
PhylomeDBiP09228.

Miscellaneous databases

GeneWikiiCST2.
GenomeRNAii1470.
PROiP09228.
SOURCEiSearch...

Gene expression databases

BgeeiP09228.
CleanExiHS_CST2.
GenevisibleiP09228. HS.

Family and domain databases

InterProiIPR027214. Cystatin.
IPR000010. Cystatin_dom.
IPR018073. Prot_inh_cystat_CS.
[Graphical view]
PANTHERiPTHR11413. PTHR11413. 1 hit.
PfamiPF00031. Cystatin. 1 hit.
[Graphical view]
SMARTiSM00043. CY. 1 hit.
[Graphical view]
PROSITEiPS00287. CYSTATIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human cysteine-proteinase inhibitors: nucleotide sequence analysis of three members of the cystatin gene family."
    Saitoh E., Kim H.-S., Smithies O., Maeda N.
    Gene 61:329-338(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Acquisition of complex patterns of differential expression in epithelial cell populations during the evolution of type 2 cystatin genes."
    Dickinson D.P., Hewett-Emmett D., Thiesse M.
    Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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.
    , 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].
  4. "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: Thyroid.
  5. "Identification of full-sized forms of salivary (S-type) cystatins (cystatin SN, cystatin SA, cystatin S, and two phosphorylated forms of cystatin S) in human whole saliva and determination of phosphorylation sites of cystatin S."
    Isemura S., Saitoh E., Sanada K., Minakata K.
    J. Biochem. 110:648-654(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 21-40.
    Tissue: Saliva.
  6. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 21-35.
  7. "Characterization and amino acid sequence of a new acidic cysteine proteinase inhibitor (cystatin SA) structurally closely related to cystatin S, from human whole saliva."
    Isemura S., Saitoh E., Sanada K.
    J. Biochem. 102:693-704(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-141.
  8. "Characterization and amino acid sequence of a new acidic cysteine proteinase inhibitor (cystatin SA) structurally closely related to cystatin S, from human whole saliva."
    Isemura S., Saitoh E., Sanada K., Isemura M., Ito S.
    (In) Turk V. (eds.); Cysteine proteinases and their inhibitors, pp.497-505, Walter de Gruyter, Berlin and New York (1986)
    Cited for: PRELIMINARY PROTEIN SEQUENCE OF 25-141.
  9. "Cystatin superfamily. Evidence that family II cystatin genes are evolutionarily related to family III cystatin genes."
    Saitoh E., Isemura S., Sanada K., Kim H.-S., Smithies O., Maeda N.
    Biol. Chem. Hoppe-Seyler 369:191-197(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-141.
  10. "Expression of type 2 cystatin genes CST1-CST5 in adult human tissues and the developing submandibular gland."
    Dickinson D.P., Thiesse M., Hicks M.J.
    DNA Cell Biol. 21:47-65(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  11. "Confident assignment of intact mass tags to human salivary cystatins using top-down Fourier-transform ion cyclotron resonance mass spectrometry."
    Ryan C.M., Souda P., Halgand F., Wong D.T., Loo J.A., Faull K.F., Whitelegge J.P.
    J. Am. Soc. Mass Spectrom. 21:908-917(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
    Tissue: Saliva.
  12. "Human basal tear peptidome characterization by CID, HCD, and ETD followed by in silico and in vitro analyses for antimicrobial peptide identification."
    Azkargorta M., Soria J., Ojeda C., Guzman F., Acera A., Iloro I., Suarez T., Elortza F.
    J. Proteome Res. 14:2649-2658(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Tear.

Entry informationi

Entry nameiCYTT_HUMAN
AccessioniPrimary (citable) accession number: P09228
Secondary accession number(s): Q9UCQ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: June 8, 2016
This is version 144 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.