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P01034 (CYTC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 170. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cystatin-C
Alternative name(s):
Cystatin-3
Gamma-trace
Neuroendocrine basic polypeptide
Post-gamma-globulin
Gene names
Name:CST3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length146 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Homodimer.

Subcellular location

Secreted Ref.19.

Tissue specificity

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. Ref.16 Ref.19

Post-translational modification

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.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.23

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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.24

Miscellaneous

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

Sequence similarities

Belongs to the cystatin family.

Mass spectrometry

Molecular mass is 13334.5829±0.0140 Da from positions 27 - 146. Determined by ESI. Ref.19

Ontologies

Keywords
   Cellular componentAmyloid
Secreted
   Coding sequence diversityPolymorphism
   DiseaseAge-related macular degeneration
Amyloidosis
Disease mutation
   DomainSignal
   Molecular functionProtease inhibitor
Thiol protease inhibitor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processSertoli cell development

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Inferred from electronic annotation. Source: Ensembl

brain development

Inferred from electronic annotation. Source: Ensembl

cell activation

Inferred from electronic annotation. Source: Ensembl

cellular response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

circadian sleep/wake cycle, REM sleep

Inferred from electronic annotation. Source: Ensembl

defense response

Inferred from direct assay PubMed 6203523. Source: BHF-UCL

embryo implantation

Inferred from electronic annotation. Source: Ensembl

extracellular fibril organization

Inferred from genetic interaction PubMed 18026102. Source: BHF-UCL

eye development

Inferred from electronic annotation. Source: Ensembl

negative regulation of blood vessel remodeling

Inferred from expression pattern PubMed 10545518. Source: BHF-UCL

negative regulation of cell death

Inferred from electronic annotation. Source: Ensembl

negative regulation of collagen catabolic process

Inferred from expression pattern PubMed 10545518. Source: BHF-UCL

negative regulation of elastin catabolic process

Inferred from mutant phenotype PubMed 10545518. Source: BHF-UCL

negative regulation of endopeptidase activity

Inferred from direct assay PubMed 15127951PubMed 6203523PubMed 7890620. Source: GOC

negative regulation of extracellular matrix disassembly

Inferred from expression pattern PubMed 10545518. Source: BHF-UCL

negative regulation of histolysis

Inferred by curator PubMed 7890620. Source: BHF-UCL

negative regulation of peptidase activity

Inferred from direct assay PubMed 6203523PubMed 7890620. Source: BHF-UCL

positive regulation of DNA replication

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of programmed cell death

Inferred from electronic annotation. Source: Ensembl

regulation of tissue remodeling

Inferred from expression pattern PubMed 10545518. Source: BHF-UCL

response to axon injury

Inferred from electronic annotation. Source: Ensembl

response to carbohydrate

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to nutrient levels

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

salivary gland development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentbasement membrane

Inferred from electronic annotation. Source: Ensembl

cell projection

Inferred from electronic annotation. Source: Ensembl

contractile fiber

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

extracellular region

Inferred from mutant phenotype PubMed 18026102. Source: BHF-UCL

extracellular space

Inferred from direct assay PubMed 18613859. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708. Source: UniProt

lysosome

Inferred from electronic annotation. Source: Ensembl

multivesicular body

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

nuclear membrane

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionbeta-amyloid binding

Inferred from physical interaction PubMed 18026102. Source: BHF-UCL

cysteine-type endopeptidase inhibitor activity

Inferred from direct assay PubMed 6203523PubMed 7890620. Source: BHF-UCL

endopeptidase inhibitor activity

Inferred from direct assay PubMed 15127951. Source: UniProtKB

protease binding

Inferred from physical interaction PubMed 6203523PubMed 7890620. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.11 Ref.12 Ref.13 Ref.14
Chain27 – 146120Cystatin-C Ref.1 Ref.3
PRO_0000006639

Regions

Motif81 – 855Secondary area of contact

Sites

Site371Reactive site

Amino acid modifications

Disulfide bond99 ↔ 109 Ref.15 Ref.19
Disulfide bond123 ↔ 143 Ref.15 Ref.19

Natural variations

Natural variant251A → T Associated with ARMD11 and O-glycosylated in region between AA 22-28. Ref.2 Ref.24
Corresponds to variant rs1064039 [ dbSNP | Ensembl ].
VAR_011893
Natural variant941L → Q in AMYL6. Ref.3 Ref.23
Corresponds to variant rs28939068 [ dbSNP | Ensembl ].
VAR_002207

Experimental info

Mutagenesis251A → S: Shows a dual distribution to the Golgi apparatus and to the mitochondria. Ref.17

Secondary structure

............... 146
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01034 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 75EF049CAE2E8B2B

FASTA14615,799
        10         20         30         40         50         60 
MAGPLRAPLL LLAILAVALA VSPAAGSSPG KPPRLVGGPM DASVEEEGVR RALDFAVGEY 

        70         80         90        100        110        120 
NKASNDMYHS RALQVVRARK QIVAGVNYFL DVELGRTTCT KTQPNLDNCP FHDQPHLKRK 

       130        140 
AFCSFQIYAV PWQGTMTLSK STCQDA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRUDHU. S10216.
RefSeqNP_000090.1. NM_000099.3.
NP_001275543.1. NM_001288614.1.
UniGeneHs.304682.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP01034.
SMRP01034. Positions 37-146.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107853. 6 interactions.
IntActP01034. 4 interactions.
MINTMINT-2857857.
STRING9606.ENSP00000366124.

Protein family/group databases

MEROPSI25.004.

PTM databases

PhosphoSiteP01034.

Polymorphism databases

DMDM118183.

2D gel databases

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

Proteomic databases

PaxDbP01034.
PeptideAtlasP01034.
PRIDEP01034.

Protocols and materials databases

DNASU1471.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000376925; ENSP00000366124; ENSG00000101439.
ENST00000398409; ENSP00000381446; ENSG00000101439.
ENST00000398411; ENSP00000381448; ENSG00000101439.
GeneID1471.
KEGGhsa:1471.
UCSCuc002wtm.3. human.

Organism-specific databases

CTD1471.
GeneCardsGC20M023608.
HGNCHGNC:2475. CST3.
HPACAB000118.
HPA013143.
MIM105150. phenotype.
604312. gene.
611953. phenotype.
neXtProtNX_P01034.
Orphanet100008. Hereditary cerebral hemorrhage with amyloidosis, Icelandic type.
PharmGKBPA26976.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG44865.
HOGENOMHOG000231754.
HOVERGENHBG009556.
InParanoidP01034.
KOK13899.
OMAYTVPWLG.
OrthoDBEOG7M98J9.
PhylomeDBP01034.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.

Gene expression databases

ArrayExpressP01034.
BgeeP01034.
CleanExHS_CST3.
GenevestigatorP01034.

Family and domain databases

InterProIPR027214. Cystatin.
IPR000010. Prot_inh_cystat.
IPR018073. Prot_inh_cystat_CS.
[Graphical view]
PANTHERPTHR11413. PTHR11413. 1 hit.
PfamPF00031. Cystatin. 1 hit.
[Graphical view]
SMARTSM00043. CY. 1 hit.
[Graphical view]
PROSITEPS00287. CYSTATIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCST3. human.
EvolutionaryTraceP01034.
GeneWikiCystatin_C.
GenomeRNAi1471.
NextBio6039.
PMAP-CutDBP01034.
PROP01034.
SOURCESearch...

Entry information

Entry nameCYTC_HUMAN
AccessionPrimary (citable) accession number: P01034
Secondary accession number(s): B2R5J9, D3DW42, Q6FGW9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1988
Last modified: April 16, 2014
This is version 170 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM