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UniProtKB/Swiss-Prot entry P10144


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GRAB_HUMAN
Primary accession number P10144
Secondary accession number Q8N1D2
Integrated into Swiss-Prot on July 1, 1989
Sequence was last modified on July 1, 1989 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 106)
Name and origin of the protein
Protein name Granzyme B [Precursor]
Synonyms EC 3.4.21.79
Granzyme-2
T-cell serine protease 1-3E
Cytotoxic T-lymphocyte proteinase 2
Lymphocyte protease
SECT
Cathepsin G-like 1
CTSGL1
CTLA-1
Fragmentin-2
Human lymphocyte protein
HLP
C11
Gene name
Name: GZMB
Synonyms: CGL1, CSPB, CTLA1, GRB
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2953813 [NCBI, ExPASy, EBI, Israel, Japan]
Schmid J., Weissmann C.;
"Induction of mRNA for a serine protease and a beta-thromboglobulin-like protein in mitogen-stimulated human leukocytes.";
J. Immunol. 139:250-256(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ARG-55 AND ALA-94.
PubMed=3258865 [NCBI, ExPASy, EBI, Israel, Japan]
Caputo A., Fahey D., Lloyd C., Vozab R., McCairns E., Rowe P.B.;
"Structure and differential mechanisms of regulation of expression of a serine esterase gene in activated human T lymphocytes.";
J. Biol. Chem. 263:6363-6369(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3261871 [NCBI, ExPASy, EBI, Israel, Japan]
Trapani J.A., Klein J.L., White P.C., Dupont B.;
"Molecular cloning of an inducible serine esterase gene from human cytotoxic lymphocytes.";
Proc. Natl. Acad. Sci. U.S.A. 85:6924-6928(1988).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0888-7543(89)90093-1; PubMed=2788607 [NCBI, ExPASy, EBI, Israel, Japan]
Klein J.L., Shows T.B., Dupont B., Trapani J.A.;
"Genomic organization and chromosomal assignment for a serine protease gene (CSPB) expressed by human cytotoxic lymphocytes.";
Genomics 5:110-117(1989).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2365998 [NCBI, ExPASy, EBI, Israel, Japan]
Caputo A., Sauer D.E., Rowe P.B.;
"Nucleotide sequence and genomic organization of a human T lymphocyte serine protease gene.";
J. Immunol. 145:737-744(1990).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-94.
DOI=10.1016/0378-1119(90)90311-E; PubMed=2332171 [NCBI, ExPASy, EBI, Israel, Japan]
Haddad P., Clement M.-V., Bernard O., Larsen C.-J., Degos L., Sasportes M., Mathieu-Mahul D.;
"Structural organization of the hCTLA-1 gene encoding human granzyme B.";
Gene 87:265-271(1990).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-55.
DOI=10.1038/nature01348; PubMed=12508121 [NCBI, ExPASy, EBI, Israel, Japan]
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-247.
TISSUE=Pancreas;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-23.
DOI=10.1007/BF00195821; PubMed=2323780 [NCBI, ExPASy, EBI, Israel, Japan]
Dahl C.A., Bach F.H., Chan W., Huebner K., Russo G., Croce C.M., Herfurth T., Cairns J.S.;
"Isolation of a cDNA clone encoding a novel form of granzyme B from human NK cells and mapping to chromosome 14.";
Hum. Genet. 84:465-470(1990).
[10]
PROTEIN SEQUENCE OF 21-40, AND CHARACTERIZATION.
PubMed=3262682 [NCBI, ExPASy, EBI, Israel, Japan]
Hameed A., Lowrey D.M., Lichtenheld M., Podack E.R.;
"Characterization of three serine esterases isolated from human IL-2 activated killer cells.";
J. Immunol. 141:3142-3147(1988).
[11]
PROTEIN SEQUENCE OF 21-40, AND CHARACTERIZATION.
PubMed=3263427 [NCBI, ExPASy, EBI, Israel, Japan]
Kraehenbuhl O., Rey C., Jenne D.E., Lanzavecchia A., Groscurth P., Carrel S., Tschopp J.;
"Characterization of granzymes A and B isolated from granules of cloned human cytotoxic T lymphocytes.";
J. Immunol. 141:3471-3477(1988).
[12]
PROTEIN SEQUENCE OF 21-38.
PubMed=1985927 [NCBI, ExPASy, EBI, Israel, Japan]
Poe M., Blake J.T., Boulton D.A., Gammon M., Sigal N.H., Wu J.K., Zweerink H.J.;
"Human cytotoxic lymphocyte granzyme B. Its purification from granules and the characterization of substrate and inhibitor specificity.";
J. Biol. Chem. 266:98-103(1991).
[13]
PROTEIN SEQUENCE OF 19-33.
DOI=10.1110/ps.04682504; PubMed=15340161 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[14]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 21-247.
DOI=10.1515/BC.2000.148; PubMed=11209755 [NCBI, ExPASy, EBI, Israel, Japan]
Estebanez-Perpina E., Fuentes-Prior P., Belorgey D., Braun M., Kiefersauer R., Maskos K., Huber R., Rubin H., Bode W.;
"Crystal structure of the caspase activator human granzyme B, a proteinase highly specific for an Asp-P1 residue.";
Biol. Chem. 381:1203-1214(2000).
[15]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 21-247.
DOI=10.1016/S1074-5521(01)00018-7; PubMed=11325591 [NCBI, ExPASy, EBI, Israel, Japan]
Rotonda J., Garcia-Calvo M., Bull H.G., Geissler W.M., McKeever B.M., Willoughby C.A., Thornberry N.A., Becker J.W.;
"The three-dimensional structure of human granzyme B compared to caspase-3, key mediators of cell death with cleavage specificity for aspartic acid in P1.";
Chem. Biol. 8:357-368(2001).
[16]
VARIANTS ARG-55 AND HIS-247.
DOI=10.1007/s10038-003-0021-7; PubMed=12721789 [NCBI, ExPASy, EBI, Israel, Japan]
Saito S., Iida A., Sekine A., Kawauchi S., Higuchi S., Ogawa C., Nakamura Y.;
"Catalog of 680 variations among eight cytochrome p450 (CYP) genes, nine esterase genes, and two other genes in the Japanese population.";
J. Hum. Genet. 48:249-270(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M17016; AAA36627.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J03189; AAA36603.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J04071; AAA52118.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J03072; AAB59528.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M38193; AAA67124.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M28879; AAA75490.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136018; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
BC030195; AAH30195.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A61021; A61021.
RefSeq NP_004122.1; -.
UniGene Hs.1051
3D structure databases
PDB
1FQ3; X-ray; 3.10 A; A/B=21-247.[ExPASy / RCSB / EBI]
1IAU; X-ray; 2.00 A; A=21-247.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1FQ3; -.
1IAU; -.
ModBase P10144.
Protein family/group databases
MEROPS S01.010; -.
Enzyme and pathway databases
Reactome REACT_578; Apoptosis.
Organism-specific databases
GeneCards GC14M024170; -.
H-InvDB HIX0011578; -.
HGNC HGNC:4709; GZMB.
GenAtlas GZMB.
HPA CAB000376; -.
HPA003418; -.
MIM 123910; gene. [NCBI / EBI]
PharmGKB PA29087; -.
GeneCards P10144.
Gene expression databases
ArrayExpress P10144; -.
CleanEx HS_GZMB; -.
GermOnline ENSG00000100453; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0001772; Cellular component: immunological synapse (traceable author statement from UniProtKB).
GO:0005634; Cellular component: nucleus (traceable author statement from UniProtKB).
GO:0004278; Molecular function: granzyme B activity (inferred from experiment from Reactome).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0004252; Molecular function: serine-type endopeptidase activity (traceable author statement from UniProtKB).
GO:0006922; Biological process: cleavage of lamin (inferred from direct assay from UniProtKB).
GO:0019835; Biological process: cytolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0006508; Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
Graphical view of domain structure.
Pfam PF00089; Trypsin; 1.
Pfam graphical view of domain structure.
PRINTS PR00722; CHYMOTRYPSIN.
SMART SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.
PROSITE PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).
Proteomics databases
PRIDE P10144; -.
Genome annotation databases
Ensembl ENSG00000100453; Homo sapiens. [Contig view]
GeneID 3002; -.
KEGG hsa:3002; -.
Phylogenomic databases
HOVERGEN P10144; -.
Other
NextBio 11904; -.
SOURCE GZMB; Homo sapiens.
ProtoNet P10144.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Apoptosis; Cytolysis; Direct protein sequencing; Glycoprotein; Hydrolase; Polymorphism; Protease; Serine protease; Signal; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    18  18      
PROPEP   19    20  2     Activation peptide. PRO_0000027399
CHAIN   21   247  227     Granzyme B. PRO_0000027400
DOMAIN   21   245  225     Peptidase S1. 
ACT_SITE   64    64        Charge relay system. 
ACT_SITE   108   108        Charge relay system. 
ACT_SITE   203   203        Charge relay system. 
CARBOHYD   71    71        N-linked (GlcNAc...). 
CARBOHYD   104   104        N-linked (GlcNAc...) (Potential). 
DISULFID   49    65         
DISULFID   142   209         
DISULFID   173   188         
VARIANT   55    55  1     Q -> R (in dbSNP:rs8192917 [NCBI]). VAR_018371 [3D]
VARIANT   94    94  1     P -> A (in dbSNP:rs11539752 [NCBI]). VAR_047409 [3D]
VARIANT   247   247  1     Y -> H (in dbSNP:rs2236338 [NCBI]). VAR_018381 
CONFLICT   72    72        V -> G (in Ref. 3; AAA52118). 
CONFLICT   212   212        V -> C (in Ref. 4; AAB59528). 
STRAND   35    41  7      
STRAND   46    55  10      
STRAND   58    61  4      
HELIX   63    65  3      
STRAND   68    75  8      
STRAND   87    96  10      
TURN   102   104  3      
STRAND   110   116  7      
STRAND   141   148  8      
STRAND   150   154  5      
STRAND   161   166  6      
HELIX   170   176  7      
TURN   177   180  4      
TURN   183   185  3      
STRAND   186   189  4      
STRAND   205   209  5      
STRAND   212   220  9      
STRAND   228   232  5      
HELIX   233   236  4      
HELIX   237   245  9      
Sequence information
Length: 247 AA [This is the length of the unprocessed precursor] Molecular weight: 27688 Da [This is the MW of the unprocessed precursor] CRC64: 684FF605D6F2F4FB [This is a checksum on the sequence]
        10         20         30         40         50         60 
MQPILLLLAF LLLPRADAGE IIGGHEAKPH SRPYMAYLMI WDQKSLKRCG GFLIQDDFVL 

        70         80         90        100        110        120 
TAAHCWGSSI NVTLGAHNIK EQEPTQQFIP VKRPIPHPAY NPKNFSNDIM LLQLERKAKR 

       130        140        150        160        170        180 
TRAVQPLRLP SNKAQVKPGQ TCSVAGWGQT APLGKHSHTL QEVKMTVQED RKCESDLRHY 

       190        200        210        220        230        240 
YDSTIELCVG DPEIKKTSFK GDSGGPLVCN KVAQGIVSYG RNNGMPPRAC TKVSSFVHWI 


KKTMKRY 

P10144 in FASTA format

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View entry in raw text format (no links)
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