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P04080 (CYTB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 169. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cystatin-B
Alternative name(s):
CPI-B
Liver thiol proteinase inhibitor
Stefin-B
Gene names
Name:CSTB
Synonyms:CST6, STFB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length98 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This is an intracellular thiol proteinase inhibitor. Tightly binding reversible inhibitor of cathepsins L, H and B.

Subunit structure

Able to form dimers stabilized by noncovalent forces.

Subcellular location

Cytoplasm. Nucleus Ref.6.

Involvement in disease

Epilepsy, progressive myoclonic 1 (EPM1) [MIM:254800]: An autosomal recessive disorder characterized by severe, stimulus-sensitive myoclonus and tonic-clonic seizures. The onset, occurring between 6 and 13 years of age, is characterized by convulsions. Myoclonus begins 1 to 5 years later. The twitchings occur predominantly in the proximal muscles of the extremities and are bilaterally symmetrical, although asynchronous. At first small, they become late in the clinical course so violent that the victim is thrown to the floor. Mental deterioration and eventually dementia develop.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11

Sequence similarities

Belongs to the cystatin family.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   DiseaseDisease mutation
Epilepsy
   Molecular functionProtease inhibitor
Thiol protease inhibitor
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadult locomotory behavior

Inferred from electronic annotation. Source: Ensembl

negative regulation of endopeptidase activity

Inferred from direct assay PubMed 3488317PubMed 6203523. Source: GOC

negative regulation of peptidase activity

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

negative regulation of proteolysis

Inferred from direct assay PubMed 3488317. Source: UniProt

regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

extracellular space

Inferred from direct assay PubMed 23580065PubMed 3488317. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708PubMed 23376485. Source: UniProt

nucleolus

Inferred from direct assay. Source: HPA

   Molecular_functioncysteine-type endopeptidase inhibitor activity

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

endopeptidase inhibitor activity

Traceable author statement PubMed 3053245. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protease binding

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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 9898Cystatin-B
PRO_0000207136

Regions

Motif46 – 505Secondary area of contact

Sites

Site41Reactive site

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7 Ref.9

Natural variations

Natural variant41G → R in EPM1. Ref.11
VAR_002206

Experimental info

Sequence conflict311E → Y AA sequence Ref.1

Secondary structure

........... 98
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04080 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: B8076220E19D0483

FASTA9811,140
        10         20         30         40         50         60 
MMCGAPSATQ PATAETQHIA DQVRSQLEEK ENKKFPVFKA VSFKSQVVAG TNYFIKVHVG 

        70         80         90 
DEDFVHLRVF QSLPHENKPL TLSNYQTNKA KHDELTYF 

« Hide

References

« Hide 'large scale' references
[1]"Amino acid sequence of the intracellular cysteine proteinase inhibitor cystatin B from human liver."
Ritonja A., Machleidt W., Barrett A.J.
Biochem. Biophys. Res. Commun. 131:1187-1192(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
[2]"Mutations in the gene encoding cystatin B in progressive myoclonus epilepsy (EPM1)."
Pennacchio L.A., Lehesjoki A.-E., Stone N.E., Willour V.L., Virteneva K., Miao J., D'Amato E., Ramirez L., Faham J., Koskiniemi M., Warringtion J.A., Norio R., la Chapelle A., Cox D.R., Myers R.M.
Science 271:1731-1734(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[3]Bhat K.S.
Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"The DNA sequence of human chromosome 21."
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. expand/collapse author list , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
Nature 405:311-319(2000) [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: Placenta.
[6]"Nuclear localization of cystatin B, the cathepsin inhibitor implicated in myoclonus epilepsy (EPM1)."
Riccio M., Di Giaimo R., Pianetti S., Palmieri P.P., Melli M., Santi S.
Exp. Cell Res. 262:84-94(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"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].
[9]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction."
Stubbs M.T., Laber B., Bode W., Huber R., Jerala R., Lenarcic B., Turk V.
EMBO J. 9:1939-1947(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[11]"Identification of mutations in cystatin B, the gene responsible for the Unverricht-Lundborg type of progressive myoclonus epilepsy (EPM1)."
Lalioti M.D., Mirotsou M., Buresi C., Peitsch M.C., Rossier C., Ouazzani R., Baldy-Moulinier M., Bottani A., Malafosse A., Antonarakis S.E.
Am. J. Hum. Genet. 60:342-351(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EPM1 ARG-4.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U46692 Genomic DNA. Translation: AAA99014.1.
L03558 mRNA. Translation: AAA35727.1.
AF208234 Genomic DNA. Translation: AAF44059.1.
AP001752 Genomic DNA. Translation: BAA95541.1.
BC003370 mRNA. Translation: AAH03370.1.
BC010532 mRNA. Translation: AAH10532.1.
CCDSCCDS13701.1.
PIRUDHUB. A01278.
RefSeqNP_000091.1. NM_000100.3.
UniGeneHs.695.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1STFX-ray2.37I1-98[»]
2OCTX-ray1.40A/B1-98[»]
4N6VX-ray1.800/1/2/3/4/5/6/7/8/98-98[»]
ProteinModelPortalP04080.
SMRP04080. Positions 1-98.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107858. 18 interactions.
IntActP04080. 7 interactions.
MINTMINT-1504629.
STRING9606.ENSP00000291568.

Protein family/group databases

MEROPSI25.003.
TCDB1.C.91.1.1. the stefin b pore-forming protein (stefin b) family.

PTM databases

PhosphoSiteP04080.

Polymorphism databases

DMDM1706278.

Proteomic databases

MaxQBP04080.
PaxDbP04080.
PeptideAtlasP04080.
PRIDEP04080.

Protocols and materials databases

DNASU1476.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000291568; ENSP00000291568; ENSG00000160213.
GeneID1476.
KEGGhsa:1476.
UCSCuc002zdr.4. human.

Organism-specific databases

CTD1476.
GeneCardsGC21M045192.
GeneReviewsCSTB.
HGNCHGNC:2482. CSTB.
HPACAB047318.
CAB047320.
HPA017380.
MIM254800. phenotype.
601145. gene.
neXtProtNX_P04080.
Orphanet308. Unverricht-Lundborg disease.
PharmGKBPA26984.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG29074.
HOGENOMHOG000294175.
HOVERGENHBG002292.
InParanoidP04080.
KOK13907.
OMAKHDELAY.
OrthoDBEOG7FR7JX.
PhylomeDBP04080.
TreeFamTF333174.

Gene expression databases

ArrayExpressP04080.
BgeeP04080.
CleanExHS_CST6.
HS_CSTB.
GenevestigatorP04080.

Family and domain databases

InterProIPR000010. Prot_inh_cystat.
IPR018073. Prot_inh_cystat_CS.
IPR001713. Prot_inh_stefinA.
[Graphical view]
PfamPF00031. Cystatin. 1 hit.
[Graphical view]
PRINTSPR00295. STEFINA.
SMARTSM00043. CY. 1 hit.
[Graphical view]
PROSITEPS00287. CYSTATIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCSTB. human.
EvolutionaryTraceP04080.
GeneWikiCystatin_B.
GenomeRNAi1476.
NextBio6061.
PROP04080.
SOURCESearch...

Entry information

Entry nameCYTB_HUMAN
AccessionPrimary (citable) accession number: P04080
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 169 of the entry and version 2 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 21

Human chromosome 21: entries, gene names and cross-references to MIM