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Protein

Cystatin-SN

Gene

CST1

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

Functioni

Human saliva appears to contain several cysteine proteinase inhibitors that are immunologically related to cystatin S but that differ in their specificity due to amino acid sequence differences. Cystatin SN, with a pI of 7.5, is a much better inhibitor of papain and dipeptidyl peptidase I than is cystatin S, although both inhibit ficin equally well.

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

MEROPSiI25.010.

Names & Taxonomyi

Protein namesi
Recommended name:
Cystatin-SN
Alternative name(s):
Cystain-SA-I
Cystatin-1
Salivary cystatin-SA-1
Gene namesi
Name:CST1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:2473. CST1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26972.

Polymorphism and mutation databases

BioMutaiCST1.
DMDMi311033460.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20203 PublicationsAdd
BLAST
Chaini21 – 141121Cystatin-SNPRO_0000006649Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP01037.
PaxDbiP01037.
PRIDEiP01037.

PTM databases

iPTMnetiP01037.
PhosphoSiteiP01037.

Expressioni

Tissue specificityi

Expressed in submandibular and sublingual saliva but not in parotid saliva (at protein level). Expressed in saliva, tears, urine and seminal fluid.1 Publication

Gene expression databases

BgeeiP01037.
CleanExiHS_CST1.
GenevisibleiP01037. HS.

Organism-specific databases

HPAiCAB026769.
HPA043706.
HPA044763.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
SGTAO437653EBI-1056240,EBI-347996

Protein-protein interaction databases

BioGridi107851. 34 interactions.
IntActiP01037. 1 interaction.
STRINGi9606.ENSP00000305731.

Structurei

3D structure databases

ProteinModelPortaliP01037.
SMRiP01037. 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.
InParanoidiP01037.
KOiK13897.
OMAiEYNKATK.
OrthoDBiEOG7M98J9.
PhylomeDBiP01037.

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.

P01037-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQYLSTLLL LLATLAVALA WSPKEEDRII PGGIYNADLN DEWVQRALHF
60 70 80 90 100
AISEYNKATK DDYYRRPLRV LRARQQTVGG VNYFFDVEVG RTICTKSQPN
110 120 130 140
LDTCAFHEQP ELQKKQLCSF EIYEVPWENR RSLVKSRCQE S
Length:141
Mass (Da):16,388
Last modified:November 2, 2010 - v3
Checksum:i9F9934704D6C077D
GO

Mass spectrometryi

Molecular mass is 14303.1553±0.0675 Da from positions 21 - 141. Determined by ESI. 1 Publication
Molecular mass is 14319.171±0.0523 Da from positions 21 - 141. Determined by ESI. Variant Leu-31.1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4 – 41Y → H.2 Publications
Corresponds to variant rs6076122 [ dbSNP | Ensembl ].
VAR_028932
Natural varianti31 – 311P → L.
Corresponds to variant rs2070856 [ dbSNP | Ensembl ].
VAR_028933
Natural varianti129 – 1291N → D.
Corresponds to variant rs3188319 [ dbSNP | Ensembl ].
VAR_028934
Natural varianti131 – 1311R → M.
Corresponds to variant rs3188320 [ dbSNP | Ensembl ].
VAR_028935
Natural varianti135 – 1351K → N.
Corresponds to variant rs3188322 [ dbSNP | Ensembl ].
VAR_028936

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19169 Genomic DNA. Translation: AAA36115.1.
J03870 mRNA. Translation: AAA60299.1.
AL591074 Genomic DNA. Translation: CAC94783.1.
BC021225 mRNA. Translation: AAH21225.1.
CCDSiCCDS13160.1.
PIRiA28110. UDHUP2.
RefSeqiNP_001889.2. NM_001898.2.
UniGeneiHs.123114.

Genome annotation databases

EnsembliENST00000304749; ENSP00000305731; ENSG00000170373.
ENST00000398402; ENSP00000381439; ENSG00000170373.
GeneIDi1469.
KEGGihsa:1469.
UCSCiuc002wtp.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19169 Genomic DNA. Translation: AAA36115.1.
J03870 mRNA. Translation: AAA60299.1.
AL591074 Genomic DNA. Translation: CAC94783.1.
BC021225 mRNA. Translation: AAH21225.1.
CCDSiCCDS13160.1.
PIRiA28110. UDHUP2.
RefSeqiNP_001889.2. NM_001898.2.
UniGeneiHs.123114.

3D structure databases

ProteinModelPortaliP01037.
SMRiP01037. Positions 32-140.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107851. 34 interactions.
IntActiP01037. 1 interaction.
STRINGi9606.ENSP00000305731.

Protein family/group databases

MEROPSiI25.010.

PTM databases

iPTMnetiP01037.
PhosphoSiteiP01037.

Polymorphism and mutation databases

BioMutaiCST1.
DMDMi311033460.

Proteomic databases

MaxQBiP01037.
PaxDbiP01037.
PRIDEiP01037.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000304749; ENSP00000305731; ENSG00000170373.
ENST00000398402; ENSP00000381439; ENSG00000170373.
GeneIDi1469.
KEGGihsa:1469.
UCSCiuc002wtp.3. human.

Organism-specific databases

CTDi1469.
GeneCardsiCST1.
HGNCiHGNC:2473. CST1.
HPAiCAB026769.
HPA043706.
HPA044763.
MIMi123855. gene.
neXtProtiNX_P01037.
PharmGKBiPA26972.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IZZH. Eukaryota.
ENOG4112CFJ. LUCA.
GeneTreeiENSGT00840000129787.
HOGENOMiHOG000231754.
HOVERGENiHBG009556.
InParanoidiP01037.
KOiK13897.
OMAiEYNKATK.
OrthoDBiEOG7M98J9.
PhylomeDBiP01037.

Miscellaneous databases

ChiTaRSiCST1. human.
GeneWikiiCST1.
GenomeRNAii1469.
PROiP01037.
SOURCEiSearch...

Gene expression databases

BgeeiP01037.
CleanExiHS_CST1.
GenevisibleiP01037. 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], VARIANT HIS-4.
  2. "Purification, molecular cloning, and sequencing of salivary cystatin SA-1."
    Al-Hashimi I., Dickinson D.P., Levine M.J.
    J. Biol. Chem. 263:9381-9387(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT HIS-4.
  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: Skin.
  5. "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 [MRNA] OF 21-141.
  6. "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.
  7. "Newly identified proteins in human nasal lavage fluid from non-smokers and smokers using two-dimensional gel electrophoresis and peptide mass fingerprinting."
    Ghafouri B., Stahlbom B., Tagesson C., Lindahl M.
    Proteomics 2:112-120(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 21-32.
  8. "Characterization of a new cysteine proteinase inhibitor of human saliva, cystatin SN, which is immunologically related to cystatin S."
    Isemura S., Saitoh E., Sanada K.
    FEBS Lett. 198:145-149(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 29-141.
  9. "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.
  10. "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: PROTEIN SEQUENCE OF 105-141, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Tear.
  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.

Entry informationi

Entry nameiCYTN_HUMAN
AccessioniPrimary (citable) accession number: P01037
Secondary accession number(s): Q96LE6, Q9UCQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 2, 2010
Last modified: June 8, 2016
This is version 162 of the entry and version 3 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. 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

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.