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P01036

- CYTS_HUMAN

UniProt

P01036 - CYTS_HUMAN

Protein

Cystatin-S

Gene

CST4

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

    This protein strongly inhibits papain and ficin, partially inhibits stem bromelain and bovine cathepsin C, but does not inhibit porcine cathepsin B or clostripain. Papain is inhibited non-competitively.

    Sites

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

    GO - Molecular functioni

    1. cysteine-type endopeptidase inhibitor activity Source: UniProt

    GO - Biological processi

    1. detection of chemical stimulus involved in sensory perception of bitter taste Source: UniProt
    2. negative regulation of endopeptidase activity Source: GOC
    3. negative regulation of proteolysis Source: UniProt
    4. retina homeostasis Source: UniProt

    Keywords - Molecular functioni

    Protease inhibitor, Thiol protease inhibitor

    Protein family/group databases

    MEROPSiI25.008.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cystatin-S
    Alternative name(s):
    Cystatin-4
    Cystatin-SA-III
    Salivary acidic protein 1
    Gene namesi
    Name:CST4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:2476. CST4.

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular space Source: UniProt
    2. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26977.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 20204 PublicationsAdd
    BLAST
    Chaini21 – 141121Cystatin-SPRO_0000006650Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei21 – 211Phosphoserine3 Publications
    Modified residuei23 – 231Phosphoserine5 Publications
    Disulfide bondi94 ↔ 104By similarity
    Disulfide bondi118 ↔ 138By similarity

    Post-translational modificationi

    Phosphorylated at both its N- and C-terminal regions.5 Publications

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    PaxDbiP01036.
    PeptideAtlasiP01036.
    PRIDEiP01036.

    PTM databases

    PhosphoSiteiP01036.

    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

    BgeeiP01036.
    CleanExiHS_CST4.
    GenevestigatoriP01036.

    Organism-specific databases

    HPAiHPA043706.
    HPA044763.

    Interactioni

    Protein-protein interaction databases

    BioGridi107854. 1 interaction.
    STRINGi9606.ENSP00000217423.

    Structurei

    3D structure databases

    ProteinModelPortaliP01036.
    SMRiP01036. 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

    eggNOGiNOG44865.
    HOGENOMiHOG000231754.
    HOVERGENiHBG009556.
    InParanoidiP01036.
    KOiK13900.
    OMAiDAENDEM.
    OrthoDBiEOG7M98J9.
    PhylomeDBiP01036.

    Family and domain databases

    InterProiIPR027214. Cystatin.
    IPR000010. Prot_inh_cystat.
    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.

    P01036-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARPLCTLLL LMATLAGALA SSSKEENRII PGGIYDADLN DEWVQRALHF    50
    AISEYNKATE DEYYRRPLQV LRAREQTFGG VNYFFDVEVG RTICTKSQPN 100
    LDTCAFHEQP ELQKKQLCSF EIYEVPWEDR MSLVNSRCQE A 141
    Length:141
    Mass (Da):16,214
    Last modified:July 1, 1993 - v3
    Checksum:i65B1FEB8F074DEA6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti135 – 1351N → D AA sequence (PubMed:6501254)Curated

    Mass spectrometryi

    Molecular mass is 14175.8569±0.0564 Da from positions 21 - 141. Determined by ESI. 1 Publication
    Molecular mass is 14255.8567±0.0899 Da from positions 21 - 141. Determined by ESI. Monophosphorylated at Ser-23, also called form S1.1 Publication
    Molecular mass is 14335.811±0.0775 Da from positions 21 - 141. Determined by ESI. Diphosphorylated at Ser-21 and Ser-23, also called form S2.1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti36 – 361D → N.
    Corresponds to variant rs3210291 [ dbSNP | Ensembl ].
    VAR_048852
    Natural varianti77 – 771T → N in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036549

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54667 mRNA. Translation: CAA38478.1.
    S51222, S51214, S51219 Genomic DNA. Translation: AAB24493.1.
    AF319565 Genomic DNA. Translation: AAK11571.1.
    AL359433 Genomic DNA. Translation: CAC07196.1.
    BC065714 mRNA. Translation: AAH65714.1.
    BC074952 mRNA. Translation: AAH74952.1.
    BC074953 mRNA. Translation: AAH74953.1.
    CCDSiCCDS13159.1.
    PIRiS17667. UDHUP1.
    RefSeqiNP_001890.1. NM_001899.2.
    UniGeneiHs.654549.

    Genome annotation databases

    EnsembliENST00000217423; ENSP00000217423; ENSG00000101441.
    GeneIDi1472.
    KEGGihsa:1472.
    UCSCiuc002wto.1. human.

    Polymorphism databases

    DMDMi399336.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54667 mRNA. Translation: CAA38478.1 .
    S51222 , S51214 , S51219 Genomic DNA. Translation: AAB24493.1 .
    AF319565 Genomic DNA. Translation: AAK11571.1 .
    AL359433 Genomic DNA. Translation: CAC07196.1 .
    BC065714 mRNA. Translation: AAH65714.1 .
    BC074952 mRNA. Translation: AAH74952.1 .
    BC074953 mRNA. Translation: AAH74953.1 .
    CCDSi CCDS13159.1.
    PIRi S17667. UDHUP1.
    RefSeqi NP_001890.1. NM_001899.2.
    UniGenei Hs.654549.

    3D structure databases

    ProteinModelPortali P01036.
    SMRi P01036. Positions 32-140.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107854. 1 interaction.
    STRINGi 9606.ENSP00000217423.

    Protein family/group databases

    MEROPSi I25.008.

    PTM databases

    PhosphoSitei P01036.

    Polymorphism databases

    DMDMi 399336.

    Proteomic databases

    PaxDbi P01036.
    PeptideAtlasi P01036.
    PRIDEi P01036.

    Protocols and materials databases

    DNASUi 1472.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000217423 ; ENSP00000217423 ; ENSG00000101441 .
    GeneIDi 1472.
    KEGGi hsa:1472.
    UCSCi uc002wto.1. human.

    Organism-specific databases

    CTDi 1472.
    GeneCardsi GC20M023666.
    HGNCi HGNC:2476. CST4.
    HPAi HPA043706.
    HPA044763.
    MIMi 123857. gene.
    neXtProti NX_P01036.
    PharmGKBi PA26977.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG44865.
    HOGENOMi HOG000231754.
    HOVERGENi HBG009556.
    InParanoidi P01036.
    KOi K13900.
    OMAi DAENDEM.
    OrthoDBi EOG7M98J9.
    PhylomeDBi P01036.

    Miscellaneous databases

    GeneWikii CST4.
    GenomeRNAii 1472.
    NextBioi 6043.
    PROi P01036.
    SOURCEi Search...

    Gene expression databases

    Bgeei P01036.
    CleanExi HS_CST4.
    Genevestigatori P01036.

    Family and domain databases

    InterProi IPR027214. Cystatin.
    IPR000010. Prot_inh_cystat.
    IPR018073. Prot_inh_cystat_CS.
    [Graphical view ]
    PANTHERi PTHR11413. PTHR11413. 1 hit.
    Pfami PF00031. Cystatin. 1 hit.
    [Graphical view ]
    SMARTi SM00043. CY. 1 hit.
    [Graphical view ]
    PROSITEi PS00287. CYSTATIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human salivary cystatin S. Cloning, sequence analysis, hybridization in situ and immunocytochemistry."
      Bobek L.A., Aguirre A., Levine M.J.
      Biochem. J. 278:627-635(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Submandibular gland.
    2. "Characterization of two members (CST4 and CST5) of the cystatin gene family and molecular evolution of cystatin genes."
      Saitoh E., Isemura S., Sanada K., Ohnishi K.
      Agents Actions 38:340-348(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "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].
    4. "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].
    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: Thyroid.
    6. "Identification of a long form of cystatin from human saliva by rapid microbore HPLC mapping."
      Hawke D.H., Yuan P.M., Wilson K.J., Hunkapiller M.W.
      Biochem. Biophys. Res. Commun. 145:1248-1253(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-51.
    7. "Large-scale purification and characterization of the major phosphoproteins and mucins of human submandibular-sublingual saliva."
      Ramasubbu N., Reddy M.S., Bergey E.J., Haraszthy G.G., Soni S.-D., Levine M.J.
      Biochem. J. 280:341-352(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-55, PHOSPHORYLATION AT SER-23.
      Tissue: Saliva.
    8. "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 21-36, PHOSPHORYLATION AT SER-21 AND SER-23.
      Tissue: Saliva.
    9. "The effects of human salivary cystatins and statherin on hydroxyapatite crystallization."
      Johnsson M., Richardson C.F., Bergey E.J., Levine M.J., Nancollas G.H.
      Arch. Oral Biol. 36:631-636(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-36, PHOSPHORYLATION AT SER-23.
      Tissue: Saliva.
    10. "Isolation and amino acid sequence of SAP-1, an acidic protein of human whole saliva, and sequence homology with human gamma-trace."
      Isemura S., Saitoh E., Sanada K.
      J. Biochem. 96:489-498(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-141.
    11. "Cystatin S: a cysteine proteinase inhibitor of human saliva."
      Isemura S., Saitoh E., Ito S., Isemura M., Sanada K.
      J. Biochem. 96:1311-1314(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: INHIBITOR SPECIFICITY.
    12. "Salivary cystatin SA-III, a potential precursor of the acquired enamel pellicle, is phosphorylated at both its amino- and carboxyl-terminal regions."
      Lamkin M.S., Jensen J.L., Setayesh M.R., Troxler R.F., Oppenheim F.G.
      Arch. Biochem. Biophys. 288:664-670(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    13. "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: PHOSPHORYLATION AT SER-21 AND SER-23, DISULFIDE BONDS, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
      Tissue: Saliva.
    14. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-77.

    Entry informationi

    Entry nameiCYTS_HUMAN
    AccessioniPrimary (citable) accession number: P01036
    Secondary accession number(s): Q9UBI5, Q9UCS9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 147 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

    External Data

    Dasty 3