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P01034

- CYTC_HUMAN

UniProt

P01034 - CYTC_HUMAN

Protein

Cystatin-C

Gene

CST3

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

    As an inhibitor of cysteine proteinases, this protein is thought to serve an important physiological role as a local regulator of this enzyme activity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei37 – 371Reactive site

    GO - Molecular functioni

    1. beta-amyloid binding Source: BHF-UCL
    2. cysteine-type endopeptidase inhibitor activity Source: BHF-UCL
    3. endopeptidase inhibitor activity Source: UniProtKB
    4. protease binding Source: BHF-UCL
    5. protein binding Source: UniProtKB

    GO - Biological processi

    1. defense response Source: BHF-UCL
    2. extracellular fibril organization Source: BHF-UCL
    3. negative regulation of blood vessel remodeling Source: BHF-UCL
    4. negative regulation of collagen catabolic process Source: BHF-UCL
    5. negative regulation of elastin catabolic process Source: BHF-UCL
    6. negative regulation of endopeptidase activity Source: GOC
    7. negative regulation of extracellular matrix disassembly Source: BHF-UCL
    8. negative regulation of peptidase activity Source: BHF-UCL
    9. negative regulation of proteolysis Source: UniProt
    10. regulation of tissue remodeling Source: BHF-UCL

    Keywords - Molecular functioni

    Protease inhibitor, Thiol protease inhibitor

    Enzyme and pathway databases

    ReactomeiREACT_75925. Amyloids.

    Protein family/group databases

    MEROPSiI25.004.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cystatin-C
    Alternative name(s):
    Cystatin-3
    Gamma-trace
    Neuroendocrine basic polypeptide
    Post-gamma-globulin
    Gene namesi
    Name:CST3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:2475. CST3.

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: BHF-UCL
    2. extracellular space Source: BHF-UCL
    3. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Amyloid, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Amyloidosis 6 (AMYL6) [MIM:105150]: A hereditary generalized amyloidosis due to cystatin C amyloid deposition. Cystatin C amyloid accumulates in the walls of arteries, arterioles, and sometimes capillaries and veins of the brain, and in various organs including lymphoid tissue, spleen, salivary glands, and seminal vesicles. Amyloid deposition in the cerebral vessels results in cerebral amyloid angiopathy, cerebral hemorrhage and premature stroke. Cystatin C levels in the cerebrospinal fluid are abnormally low.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti94 – 941L → Q in AMYL6. 2 Publications
    Corresponds to variant rs28939068 [ dbSNP | Ensembl ].
    VAR_002207
    Macular degeneration, age-related, 11 (ARMD11) [MIM:611953]: A form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti25 – 251A → T Associated with ARMD11 and O-glycosylated in region between AA 22-28. 1 Publication
    Corresponds to variant rs1064039 [ dbSNP | Ensembl ].
    VAR_011893

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi25 – 251A → S: Shows a dual distribution to the Golgi apparatus and to the mitochondria. 1 Publication

    Keywords - Diseasei

    Age-related macular degeneration, Amyloidosis, Disease mutation

    Organism-specific databases

    MIMi105150. phenotype.
    611953. phenotype.
    Orphaneti100008. Hereditary cerebral hemorrhage with amyloidosis, Icelandic type.
    PharmGKBiPA26976.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 26264 PublicationsAdd
    BLAST
    Chaini27 – 146120Cystatin-C2 PublicationsPRO_0000006639Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi99 ↔ 109
    Disulfide bondi123 ↔ 143

    Post-translational modificationi

    The Thr-25 variant is O-glycosylated with a core 1 or possibly core 8 glycan. The signal peptide of the O-glycosylated Thr-25 variant is cleaved between Ala-20 and Val-21.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP01034.
    PaxDbiP01034.
    PeptideAtlasiP01034.
    PRIDEiP01034.

    2D gel databases

    DOSAC-COBS-2DPAGEP01034.
    UCD-2DPAGEP01034.

    PTM databases

    PhosphoSiteiP01034.

    Miscellaneous databases

    PMAP-CutDBP01034.

    Expressioni

    Tissue specificityi

    Expressed in submandibular and sublingual saliva but not in parotid saliva (at protein level). Expressed in various body fluids, such as the cerebrospinal fluid and plasma. Expressed in highest levels in the epididymis, vas deferens, brain, thymus, and ovary and the lowest in the submandibular gland.2 Publications

    Gene expression databases

    ArrayExpressiP01034.
    BgeeiP01034.
    CleanExiHS_CST3.
    GenevestigatoriP01034.

    Organism-specific databases

    HPAiCAB000118.
    HPA013143.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi107853. 6 interactions.
    IntActiP01034. 4 interactions.
    MINTiMINT-2857857.
    STRINGi9606.ENSP00000366124.

    Structurei

    Secondary structure

    1
    146
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi40 – 423
    Helixi47 – 6317
    Beta strandi67 – 10135
    Helixi106 – 1083
    Helixi115 – 1184
    Beta strandi121 – 13010
    Turni131 – 1344
    Beta strandi135 – 14511

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G96X-ray2.50A27-146[»]
    1R4CX-ray2.18A/B/C/D/E/F/G/H37-146[»]
    1TIJX-ray3.03A/B27-146[»]
    3GAXX-ray1.70A/B27-146[»]
    3NX0X-ray2.04A/B27-146[»]
    3PS8X-ray2.55A27-146[»]
    3QRDX-ray2.19A/B/C/D27-146[»]
    3S67X-ray2.26A27-146[»]
    3SVAX-ray3.02A27-146[»]
    ProteinModelPortaliP01034.
    SMRiP01034. Positions 37-146.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01034.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi81 – 855Secondary area of contact

    Sequence similaritiesi

    Belongs to the cystatin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG44865.
    HOGENOMiHOG000231754.
    HOVERGENiHBG009556.
    InParanoidiP01034.
    KOiK13899.
    OMAiKSSCQDA.
    OrthoDBiEOG7M98J9.
    PhylomeDBiP01034.

    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.

    P01034-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGPLRAPLL LLAILAVALA VSPAAGSSPG KPPRLVGGPM DASVEEEGVR    50
    RALDFAVGEY NKASNDMYHS RALQVVRARK QIVAGVNYFL DVELGRTTCT 100
    KTQPNLDNCP FHDQPHLKRK AFCSFQIYAV PWQGTMTLSK STCQDA 146
    Length:146
    Mass (Da):15,799
    Last modified:August 1, 1988 - v1
    Checksum:i75EF049CAE2E8B2B
    GO

    Mass spectrometryi

    Molecular mass is 13334.5829±0.0140 Da from positions 27 - 146. Determined by ESI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti25 – 251A → T Associated with ARMD11 and O-glycosylated in region between AA 22-28. 1 Publication
    Corresponds to variant rs1064039 [ dbSNP | Ensembl ].
    VAR_011893
    Natural varianti94 – 941L → Q in AMYL6. 2 Publications
    Corresponds to variant rs28939068 [ dbSNP | Ensembl ].
    VAR_002207

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05607 mRNA. Translation: CAA29096.1.
    M27891, M27889, M27890 Genomic DNA. Translation: AAA52164.1.
    X61681, X61682, X61683 Genomic DNA. Translation: CAA43856.2.
    X52255 Genomic DNA. Translation: CAA36497.1.
    AK312213 mRNA. Translation: BAG35146.1.
    BT006839 mRNA. Translation: AAP35485.1.
    CR541988 mRNA. Translation: CAG46785.1.
    CR542018 mRNA. Translation: CAG46815.1.
    AL121894 Genomic DNA. Translation: CAC05424.1.
    CH471133 Genomic DNA. Translation: EAX10137.1.
    CH471133 Genomic DNA. Translation: EAX10138.1.
    BC013083 mRNA. Translation: AAH13083.1.
    BC110305 mRNA. Translation: AAI10306.1.
    CCDSiCCDS13158.1.
    PIRiS10216. UDHU.
    RefSeqiNP_000090.1. NM_000099.3.
    NP_001275543.1. NM_001288614.1.
    UniGeneiHs.304682.

    Genome annotation databases

    EnsembliENST00000376925; ENSP00000366124; ENSG00000101439.
    ENST00000398409; ENSP00000381446; ENSG00000101439.
    ENST00000398411; ENSP00000381448; ENSG00000101439.
    GeneIDi1471.
    KEGGihsa:1471.
    UCSCiuc002wtm.3. human.

    Polymorphism databases

    DMDMi118183.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05607 mRNA. Translation: CAA29096.1 .
    M27891 , M27889 , M27890 Genomic DNA. Translation: AAA52164.1 .
    X61681 , X61682 , X61683 Genomic DNA. Translation: CAA43856.2 .
    X52255 Genomic DNA. Translation: CAA36497.1 .
    AK312213 mRNA. Translation: BAG35146.1 .
    BT006839 mRNA. Translation: AAP35485.1 .
    CR541988 mRNA. Translation: CAG46785.1 .
    CR542018 mRNA. Translation: CAG46815.1 .
    AL121894 Genomic DNA. Translation: CAC05424.1 .
    CH471133 Genomic DNA. Translation: EAX10137.1 .
    CH471133 Genomic DNA. Translation: EAX10138.1 .
    BC013083 mRNA. Translation: AAH13083.1 .
    BC110305 mRNA. Translation: AAI10306.1 .
    CCDSi CCDS13158.1.
    PIRi S10216. UDHU.
    RefSeqi NP_000090.1. NM_000099.3.
    NP_001275543.1. NM_001288614.1.
    UniGenei Hs.304682.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G96 X-ray 2.50 A 27-146 [» ]
    1R4C X-ray 2.18 A/B/C/D/E/F/G/H 37-146 [» ]
    1TIJ X-ray 3.03 A/B 27-146 [» ]
    3GAX X-ray 1.70 A/B 27-146 [» ]
    3NX0 X-ray 2.04 A/B 27-146 [» ]
    3PS8 X-ray 2.55 A 27-146 [» ]
    3QRD X-ray 2.19 A/B/C/D 27-146 [» ]
    3S67 X-ray 2.26 A 27-146 [» ]
    3SVA X-ray 3.02 A 27-146 [» ]
    ProteinModelPortali P01034.
    SMRi P01034. Positions 37-146.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107853. 6 interactions.
    IntActi P01034. 4 interactions.
    MINTi MINT-2857857.
    STRINGi 9606.ENSP00000366124.

    Protein family/group databases

    MEROPSi I25.004.

    PTM databases

    PhosphoSitei P01034.

    Polymorphism databases

    DMDMi 118183.

    2D gel databases

    DOSAC-COBS-2DPAGE P01034.
    UCD-2DPAGE P01034.

    Proteomic databases

    MaxQBi P01034.
    PaxDbi P01034.
    PeptideAtlasi P01034.
    PRIDEi P01034.

    Protocols and materials databases

    DNASUi 1471.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000376925 ; ENSP00000366124 ; ENSG00000101439 .
    ENST00000398409 ; ENSP00000381446 ; ENSG00000101439 .
    ENST00000398411 ; ENSP00000381448 ; ENSG00000101439 .
    GeneIDi 1471.
    KEGGi hsa:1471.
    UCSCi uc002wtm.3. human.

    Organism-specific databases

    CTDi 1471.
    GeneCardsi GC20M023608.
    HGNCi HGNC:2475. CST3.
    HPAi CAB000118.
    HPA013143.
    MIMi 105150. phenotype.
    604312. gene.
    611953. phenotype.
    neXtProti NX_P01034.
    Orphaneti 100008. Hereditary cerebral hemorrhage with amyloidosis, Icelandic type.
    PharmGKBi PA26976.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG44865.
    HOGENOMi HOG000231754.
    HOVERGENi HBG009556.
    InParanoidi P01034.
    KOi K13899.
    OMAi KSSCQDA.
    OrthoDBi EOG7M98J9.
    PhylomeDBi P01034.

    Enzyme and pathway databases

    Reactomei REACT_75925. Amyloids.

    Miscellaneous databases

    ChiTaRSi CST3. human.
    EvolutionaryTracei P01034.
    GeneWikii Cystatin_C.
    GenomeRNAii 1471.
    NextBioi 6039.
    PMAP-CutDB P01034.
    PROi P01034.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P01034.
    Bgeei P01034.
    CleanExi HS_CST3.
    Genevestigatori P01034.

    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. "Molecular cloning and sequence analysis of cDNA coding for the precursor of the human cysteine proteinase inhibitor cystatin C."
      Abrahamson M., Grubb A., Olafsson I., Lundwall A.
      FEBS Lett. 216:229-233(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    2. "The human cystatin C gene (CST3) is a member of the cystatin gene family which is localized on chromosome 20."
      Saitoh E., Sabatini L.M., Eddy R.L., Shows T.B., Azen E.A., Isemura S., Sanada K.
      Biochem. Biophys. Res. Commun. 162:1324-1331(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-25.
    3. "Stroke in Icelandic patients with hereditary amyloid angiopathy is related to a mutation in the cystatin C gene, an inhibitor of cysteine proteases."
      Levy E., Lopez-Otin C., Ghiso J., Geltner D., Frangione B.
      J. Exp. Med. 169:1771-1778(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT AMYL6 GLN-94.
      Tissue: Brain.
    4. "Structure and expression of the human cystatin C gene."
      Abrahamson M., Olafsson I., Palsdottir A., Ulvsbaeck M., Lundwall A., Jensson O., Grubb A.
      Biochem. J. 268:287-294(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Leukocyte.
    5. "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: Synovial cell.
    6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    8. "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].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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: Brain.
    11. "Human gamma-trace, a basic microprotein: amino acid sequence and presence in the adenohypophysis."
      Grubb A., Loefberg H.
      Proc. Natl. Acad. Sci. U.S.A. 79:3024-3027(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-146.
    12. "Human cystatin, a new protein inhibitor of cysteine proteinases."
      Brzin J., Popovic T., Turk V.
      Biochem. Biophys. Res. Commun. 118:103-109(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-76.
    13. "Protein inhibitors of cysteine proteinases. III. Amino-acid sequence of cystatin from chicken egg white."
      Turk V., Brzin J., Longer M., Ritonja A., Eropkin M., Borchart U., Machleidt W.
      Hoppe-Seyler's Z. Physiol. Chem. 364:1487-1496(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-73.
    14. "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 27-41.
    15. "The disulphide bridges of human cystatin C (gamma-trace) and chicken cystatin."
      Grubb A., Loefberg H., Barrett A.J.
      FEBS Lett. 170:370-374(1984)
      Cited for: DISULFIDE BONDS.
    16. "Cystatin C as a potential cerebrospinal fluid marker for the diagnosis of Creutzfeldt-Jakob disease."
      Sanchez J.C., Guillaume E., Lescuyer P., Allard L., Carrette O., Scherl A., Burgess J., Corthals G.L., Burkhard P.R., Hochstrasser D.F.
      Proteomics 4:2229-2233(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    17. "A dual Golgi- and mitochondria-localised Ala25Ser precursor cystatin C: an additional tool for characterising intracellular mis-localisation leading to increased AMD susceptibility."
      Ratnayaka A., Paraoan L., Spiller D.G., Hiscott P., Nelson G., White M.R., Grierson I.
      Exp. Eye Res. 84:1135-1139(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ALA-25.
    18. "Enrichment of glycopeptides for glycan structure and attachment site identification."
      Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
      Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS], STRUCTURE OF CARBOHYDRATES.
      Tissue: Cerebrospinal fluid.
    19. "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.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping."
      Janowski R., Kozak M., Jankowska E., Grzonka Z., Grubb A., Abrahamson M., Jaskolski M.
      Nat. Struct. Biol. 8:316-320(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 27-146.
    22. "3D domain-swapped human cystatin C with amyloid-like intermolecular beta-sheets."
      Janowski R., Kozak M., Abrahamson M., Grubb A., Jaskolski M.
      Proteins 61:570-578(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.03 ANGSTROMS) OF 27-146.
    23. "Hereditary cystatin C amyloid angiopathy: identification of the disease-causing mutation and specific diagnosis by polymerase chain reaction based analysis."
      Abrahamson M., Jonsdottir S., Olafsson I., Jensson O., Grubb A.
      Hum. Genet. 89:377-380(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AMYL6 GLN-94.
    24. "CST3 genotype associated with exudative age related macular degeneration."
      Zurdel J., Finckh U., Menzer G., Nitsch R.M., Richard G.
      Br. J. Ophthalmol. 86:214-219(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION OF VARIANT THR-25 WITH ARMD11.

    Entry informationi

    Entry nameiCYTC_HUMAN
    AccessioniPrimary (citable) accession number: P01034
    Secondary accession number(s): B2R5J9, D3DW42, Q6FGW9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 175 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

    Miscellaneous

    Potential cerebrospinal fluid marker for the diagnosis of Creutzfeldt-Jakob disease.

    Keywords - Technical termi

    3D-structure, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3