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Cystatin-B (CPI-B) (Liver thiol proteinase inhibitor) (Stefin-B)

 CYTB_HUMAN              Reviewed;          98 AA.
P04080;
01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
28-MAR-2018, entry version 201.
RecName: Full=Cystatin-B;
AltName: Full=CPI-B;
AltName: Full=Liver thiol proteinase inhibitor;
AltName: Full=Stefin-B;
Name=CSTB; Synonyms=CST6, STFB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
PROTEIN SEQUENCE.
PubMed=3902020; DOI=10.1016/0006-291X(85)90216-5;
Ritonja A., Machleidt W., Barrett A.J.;
"Amino acid sequence of the intracellular cysteine proteinase
inhibitor cystatin B from human liver.";
Biochem. Biophys. Res. Commun. 131:1187-1192(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=8596935; DOI=10.1126/science.271.5256.1731;
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.;
"Mutations in the gene encoding cystatin B in progressive myoclonus
epilepsy (EPM1).";
Science 271:1731-1734(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Bhat K.S.;
Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10830953; DOI=10.1038/35012518;
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., 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.;
"The DNA sequence of human chromosome 21.";
Nature 405:311-319(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
SUBCELLULAR LOCATION.
PubMed=11139332; DOI=10.1006/excr.2000.5085;
Riccio M., Di Giaimo R., Pianetti S., Palmieri P.P., Melli M.,
Santi S.;
"Nuclear localization of cystatin B, the cathepsin inhibitor
implicated in myoclonus epilepsy (EPM1).";
Exp. Cell Res. 262:84-94(2001).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[12]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
PubMed=2347312;
Stubbs M.T., Laber B., Bode W., Huber R., Jerala R., Lenarcic B.,
Turk V.;
"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.";
EMBO J. 9:1939-1947(1990).
[13]
VARIANT EPM1 ARG-4.
PubMed=9012407;
Lalioti M.D., Mirotsou M., Buresi C., Peitsch M.C., Rossier C.,
Ouazzani R., Baldy-Moulinier M., Bottani A., Malafosse A.,
Antonarakis S.E.;
"Identification of mutations in cystatin B, the gene responsible for
the Unverricht-Lundborg type of progressive myoclonus epilepsy
(EPM1).";
Am. J. Hum. Genet. 60:342-351(1997).
-!- FUNCTION: This is an intracellular thiol proteinase inhibitor.
Tightly binding reversible inhibitor of cathepsins L, H and B.
-!- SUBUNIT: Able to form dimers stabilized by noncovalent forces.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11139332}.
Nucleus {ECO:0000269|PubMed:11139332}.
-!- 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. {ECO:0000269|PubMed:9012407}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the cystatin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CSTBID40181ch21q22.html";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; U46692; AAA99014.1; -; Genomic_DNA.
EMBL; L03558; AAA35727.1; -; mRNA.
EMBL; AF208234; AAF44059.1; -; Genomic_DNA.
EMBL; AP001752; BAA95541.1; -; Genomic_DNA.
EMBL; BC003370; AAH03370.1; -; mRNA.
EMBL; BC010532; AAH10532.1; -; mRNA.
CCDS; CCDS13701.1; -.
PIR; A01278; UDHUB.
RefSeq; NP_000091.1; NM_000100.3.
UniGene; Hs.695; -.
PDB; 1STF; X-ray; 2.37 A; I=1-98.
PDB; 2OCT; X-ray; 1.40 A; A/B=1-98.
PDB; 4N6V; X-ray; 1.80 A; 0/1/2/3/4/5/6/7/8/9=8-98.
PDBsum; 1STF; -.
PDBsum; 2OCT; -.
PDBsum; 4N6V; -.
ProteinModelPortal; P04080; -.
SMR; P04080; -.
BioGrid; 107858; 24.
IntAct; P04080; 13.
MINT; P04080; -.
STRING; 9606.ENSP00000291568; -.
MEROPS; I25.003; -.
TCDB; 1.C.91.1.1; the stefin b pore-forming protein (stefin b) family.
iPTMnet; P04080; -.
PhosphoSitePlus; P04080; -.
SwissPalm; P04080; -.
BioMuta; CSTB; -.
DMDM; 1706278; -.
EPD; P04080; -.
PaxDb; P04080; -.
PeptideAtlas; P04080; -.
PRIDE; P04080; -.
TopDownProteomics; P04080; -.
DNASU; 1476; -.
Ensembl; ENST00000291568; ENSP00000291568; ENSG00000160213.
GeneID; 1476; -.
KEGG; hsa:1476; -.
CTD; 1476; -.
DisGeNET; 1476; -.
EuPathDB; HostDB:ENSG00000160213.5; -.
GeneCards; CSTB; -.
GeneReviews; CSTB; -.
HGNC; HGNC:2482; CSTB.
HPA; CAB047320; -.
HPA; HPA017380; -.
HPA; HPA058557; -.
MalaCards; CSTB; -.
MIM; 254800; phenotype.
MIM; 601145; gene.
neXtProt; NX_P04080; -.
OpenTargets; ENSG00000160213; -.
Orphanet; 308; Unverricht-Lundborg disease.
PharmGKB; PA26984; -.
eggNOG; ENOG410IZK7; Eukaryota.
eggNOG; ENOG41121QW; LUCA.
GeneTree; ENSGT00390000015607; -.
HOGENOM; HOG000294175; -.
HOVERGEN; HBG002292; -.
InParanoid; P04080; -.
KO; K13907; -.
OMA; SLPHEDK; -.
OrthoDB; EOG091G12NK; -.
PhylomeDB; P04080; -.
TreeFam; TF333174; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
ChiTaRS; CSTB; human.
EvolutionaryTrace; P04080; -.
GeneWiki; Cystatin_B; -.
GenomeRNAi; 1476; -.
PRO; PR:P04080; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000160213; -.
CleanEx; HS_CST6; -.
CleanEx; HS_CSTB; -.
ExpressionAtlas; P04080; baseline and differential.
Genevisible; P04080; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:UniProtKB.
GO; GO:0004866; F:endopeptidase inhibitor activity; TAS:ProtInc.
GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
GO; GO:0010466; P:negative regulation of peptidase activity; IDA:BHF-UCL.
GO; GO:0045861; P:negative regulation of proteolysis; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
CDD; cd00042; CY; 1.
InterPro; IPR000010; Cystatin_dom.
InterPro; IPR018073; Prot_inh_cystat_CS.
InterPro; IPR001713; Prot_inh_stefin.
PANTHER; PTHR11414; PTHR11414; 1.
Pfam; PF00031; Cystatin; 1.
PRINTS; PR00295; STEFINA.
SMART; SM00043; CY; 1.
PROSITE; PS00287; CYSTATIN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation; Epilepsy; Nucleus;
Protease inhibitor; Reference proteome; Thiol protease inhibitor.
CHAIN 1 98 Cystatin-B.
/FTId=PRO_0000207136.
MOTIF 46 50 Secondary area of contact.
SITE 4 4 Reactive site.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
VARIANT 4 4 G -> R (in EPM1; dbSNP:rs74315443).
{ECO:0000269|PubMed:9012407}.
/FTId=VAR_002206.
CONFLICT 31 31 E -> Y (in Ref. 1; AA sequence).
{ECO:0000305}.
HELIX 14 31 {ECO:0000244|PDB:2OCT}.
STRAND 39 58 {ECO:0000244|PDB:2OCT}.
STRAND 60 62 {ECO:0000244|PDB:1STF}.
STRAND 64 74 {ECO:0000244|PDB:2OCT}.
STRAND 80 89 {ECO:0000244|PDB:2OCT}.
SEQUENCE 98 AA; 11140 MW; B8076220E19D0483 CRC64;
MMCGAPSATQ PATAETQHIA DQVRSQLEEK ENKKFPVFKA VSFKSQVVAG TNYFIKVHVG
DEDFVHLRVF QSLPHENKPL TLSNYQTNKA KHDELTYF


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