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Protein

Cystatin-C

Gene

CST3

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

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: UniProtKB
  3. endopeptidase inhibitor activity Source: UniProtKB
  4. identical protein binding Source: IntAct
  5. protease binding Source: BHF-UCL

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: UniProtKB
  10. regulation of tissue remodeling Source: BHF-UCL
Complete GO annotation...

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 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:2475. CST3.

Subcellular locationi

  1. Secreted 1 Publication

GO - Cellular componenti

  1. extracellular region Source: BHF-UCL
  2. extracellular space Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Amyloid, Secreted

Pathology & Biotechi

Involvement in diseasei

Amyloidosis 6 (AMYL6)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:105150
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)1 Publication

Disease susceptibility is associated with variations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:611953
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.

Polymorphism and mutation databases

BioMutaiCST3.
DMDMi118183.

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

BgeeiP01034.
CleanExiHS_CST3.
ExpressionAtlasiP01034. baseline and differential.
GenevestigatoriP01034.

Organism-specific databases

HPAiCAB000118.
HPA013143.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-948622,EBI-948622

Protein-protein interaction databases

BioGridi107853. 7 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 – 423Combined sources
Helixi47 – 6317Combined sources
Beta strandi67 – 10135Combined sources
Helixi106 – 1083Combined sources
Helixi115 – 1184Combined sources
Beta strandi121 – 13010Combined sources
Turni131 – 1344Combined sources
Beta strandi135 – 14511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00570000079039.
HOGENOMiHOG000231754.
HOVERGENiHBG009556.
InParanoidiP01034.
KOiK13899.
OMAiYTVPWLG.
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

        10         20         30         40         50
MAGPLRAPLL LLAILAVALA VSPAAGSSPG KPPRLVGGPM DASVEEEGVR
60 70 80 90 100
RALDFAVGEY NKASNDMYHS RALQVVRARK QIVAGVNYFL DVELGRTTCT
110 120 130 140
KTQPNLDNCP FHDQPHLKRK AFCSFQIYAV PWQGTMTLSK STCQDA
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:
EMBLi
GenBanki
DDBJi
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 and mutation databases

BioMutaiCST3.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi107853. 7 interactions.
IntActiP01034. 4 interactions.
MINTiMINT-2857857.
STRINGi9606.ENSP00000366124.

Protein family/group databases

MEROPSiI25.004.

PTM databases

PhosphoSiteiP01034.

Polymorphism and mutation databases

BioMutaiCST3.
DMDMi118183.

2D gel databases

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

Proteomic databases

MaxQBiP01034.
PaxDbiP01034.
PeptideAtlasiP01034.
PRIDEiP01034.

Protocols and materials databases

DNASUi1471.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1471.
GeneCardsiGC20M023608.
HGNCiHGNC:2475. CST3.
HPAiCAB000118.
HPA013143.
MIMi105150. phenotype.
604312. gene.
611953. phenotype.
neXtProtiNX_P01034.
Orphaneti100008. Hereditary cerebral hemorrhage with amyloidosis, Icelandic type.
PharmGKBiPA26976.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG44865.
GeneTreeiENSGT00570000079039.
HOGENOMiHOG000231754.
HOVERGENiHBG009556.
InParanoidiP01034.
KOiK13899.
OMAiYTVPWLG.
OrthoDBiEOG7M98J9.
PhylomeDBiP01034.

Enzyme and pathway databases

ReactomeiREACT_75925. Amyloids.

Miscellaneous databases

ChiTaRSiCST3. human.
EvolutionaryTraceiP01034.
GeneWikiiCystatin_C.
GenomeRNAii1471.
NextBioi6039.
PMAP-CutDBP01034.
PROiP01034.
SOURCEiSearch...

Gene expression databases

BgeeiP01034.
CleanExiHS_CST3.
ExpressionAtlasiP01034. baseline and differential.
GenevestigatoriP01034.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "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.
  23. "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.
  24. "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.
  25. "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: April 29, 2015
This is version 180 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

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 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.