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Protein

Tryptase alpha/beta-1

Gene

TPSAB1

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

Functioni

Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. May play a role in innate immunity. Isoform 2 cleaves large substrates, such as fibronectin, more efficiently than isoform 1, but seems less efficient toward small substrates (PubMed:18854315).By similarity1 Publication

Catalytic activityi

Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa, but with more restricted specificity than trypsin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei74 – 741Charge relay system
Active sitei121 – 1211Charge relay system
Active sitei224 – 2241Charge relay system

GO - Molecular functioni

  • serine-type endopeptidase activity Source: UniProtKB
  • serine-type peptidase activity Source: ProtInc

GO - Biological processi

  • defense response Source: ProtInc
  • extracellular matrix disassembly Source: Reactome
  • extracellular matrix organization Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BRENDAi3.4.21.59. 2681.
ReactomeiR-HSA-1592389. Activation of Matrix Metalloproteinases.

Protein family/group databases

MEROPSiS01.143.

Names & Taxonomyi

Protein namesi
Recommended name:
Tryptase alpha/beta-1 (EC:3.4.21.59)
Short name:
Tryptase-1
Alternative name(s):
Tryptase I
Tryptase alpha-1
Gene namesi
Name:TPSAB1
Synonyms:TPS1, TPS2, TPSB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:12019. TPSAB1.

Subcellular locationi

  • Secreted

  • Note: Released from the secretory granules upon mast cell activation.By similarity

GO - Cellular componenti

  • extracellular region Source: Reactome
  • extracellular space Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36698.

Chemistry

ChEMBLiCHEMBL2095193.
GuidetoPHARMACOLOGYi2424.

Polymorphism and mutation databases

DMDMi18202508.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Propeptidei19 – 3012Activation peptideBy similarityPRO_0000027479Add
BLAST
Chaini31 – 275245Tryptase alpha/beta-1PRO_0000027480Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi59 ↔ 75
Glycosylationi132 – 1321N-linked (GlcNAc...)Sequence analysis
Disulfide bondi155 ↔ 230
Disulfide bondi188 ↔ 211
Disulfide bondi220 ↔ 248
Glycosylationi233 – 2331N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ15661.
PRIDEiQ15661.

PTM databases

PhosphoSiteiQ15661.

Expressioni

Tissue specificityi

Isoform 1 and isoform 2 are expressed in lung, stomach, spleen, heart and skin; in these tissues, isoform 1 is predominant. Isoform 2 is expressed in aorta, spleen, and breast tumor, with highest levels in the endothelial cells of some blood vessels surrounding the aorta, as well as those surrounding the tumor and low levels, if any, in mast cells (at protein level).1 Publication

Gene expression databases

BgeeiQ15661.
CleanExiHS_TPSAB1.
ExpressionAtlasiQ15661. baseline and differential.
GenevisibleiQ15661. HS.

Organism-specific databases

HPAiCAB016369.
CAB022175.
HPA049153.
HPA049554.

Interactioni

Subunit structurei

Homotetramer. The active tetramer is converted to inactive monomers at neutral and acidic pH in the absence of heparin. Low concentrations of inactive monomers become active monomers at pH 6.0 in the presence of heparin. When the concentration of active monomers is higher, they convert to active monomers and then to active tetramers. These monomers are active and functionally distinct from the tetrameric enzyme. In contrast to the hidden active sites in the tetrameric form, the active site of the monomeric form is accessible for macromolecular proteins and inhibitors eg: fibrinogen which is a substrate for the monomeric but not for the tetrameric form. The monomeric form forms a complex with SERPINB6.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
NCK1P163332EBI-1761369,EBI-389883
PIK3R1P279862EBI-1761369,EBI-79464

Protein-protein interaction databases

BioGridi113029. 2 interactions.
IntActiQ15661. 2 interactions.
STRINGi9606.ENSP00000343577.

Chemistry

BindingDBiQ15661.

Structurei

Secondary structure

1
275
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi32 – 365Combined sources
Beta strandi45 – 6521Combined sources
Beta strandi68 – 714Combined sources
Helixi73 – 764Combined sources
Helixi83 – 853Combined sources
Beta strandi86 – 894Combined sources
Turni95 – 984Combined sources
Beta strandi104 – 1096Combined sources
Turni116 – 1183Combined sources
Beta strandi123 – 1297Combined sources
Beta strandi135 – 1373Combined sources
Beta strandi155 – 1606Combined sources
Beta strandi176 – 1794Combined sources
Helixi185 – 1939Combined sources
Beta strandi196 – 1983Combined sources
Beta strandi209 – 2124Combined sources
Beta strandi215 – 2184Combined sources
Turni221 – 2255Combined sources
Beta strandi227 – 2326Combined sources
Beta strandi235 – 24410Combined sources
Beta strandi246 – 2505Combined sources
Beta strandi255 – 2595Combined sources
Helixi260 – 2634Combined sources
Helixi264 – 2707Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LTOX-ray2.20A/B/C/D31-275[»]
2F9NX-ray1.60A/B/C/D31-275[»]
2F9OX-ray2.10A/B/C/D31-275[»]
2F9PX-ray2.30A/B/C/D31-275[»]
2ZEBX-ray2.50A/B/C/D31-273[»]
2ZECX-ray2.06A/B/C/D31-273[»]
4A6LX-ray2.05A/B/C/D31-275[»]
4MPUX-ray1.65A/B31-275[»]
4MPVX-ray2.31A/B31-275[»]
4MPWX-ray1.95A/B31-275[»]
4MPXX-ray2.00A/B31-275[»]
4MQAX-ray2.25A/B31-275[»]
5F03X-ray1.94A/B31-275[»]
ProteinModelPortaliQ15661.
SMRiQ15661. Positions 31-273.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15661.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 272242Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family. Tryptase subfamily.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118810.
HOVERGENiHBG013304.
InParanoidiQ15661.
KOiK01340.
OrthoDBiEOG75B84T.
PhylomeDBiQ15661.
TreeFamiTF351676.

Family and domain databases

InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15661-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLNLLLLALP VLASRAYAAP APGQALQRVG IVGGQEAPRS KWPWQVSLRV
60 70 80 90 100
HGPYWMHFCG GSLIHPQWVL TAAHCVGPDV KDLAALRVQL REQHLYYQDQ
110 120 130 140 150
LLPVSRIIVH PQFYTAQIGA DIALLELEEP VNVSSHVHTV TLPPASETFP
160 170 180 190 200
PGMPCWVTGW GDVDNDERLP PPFPLKQVKV PIMENHICDA KYHLGAYTGD
210 220 230 240 250
DVRIVRDDML CAGNTRRDSC QGDSGGPLVC KVNGTWLQAG VVSWGEGCAQ
260 270
PNRPGIYTRV TYYLDWIHHY VPKKP
Length:275
Mass (Da):30,515
Last modified:November 1, 1996 - v1
Checksum:iADC48FDC51F37112
GO
Isoform 2 (identifier: Q15661-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     79-87: Missing.

Show »
Length:266
Mass (Da):29,533
Checksum:i04F79FEB4ABF517D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti129 – 1291E → K in ACZ98912 (PubMed:19748655).Curated

Polymorphismi

There are two alleles alpha and beta-I. The sequence shown is that of allele beta-I.3 Publications

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3 – 31N → S in allele alpha.
VAR_064277
Natural varianti15 – 151R → P.3 Publications
Corresponds to variant rs61729112 [ dbSNP | Ensembl ].
VAR_064278
Natural varianti18 – 181A → V.1 Publication
Corresponds to variant rs1800984 [ dbSNP | Ensembl ].
VAR_014557
Natural varianti23 – 231G → V in allele alpha. 1 Publication
Corresponds to variant rs1141965 [ dbSNP | Ensembl ].
VAR_014558
Natural varianti28 – 281R → Q in allele alpha.
Corresponds to variant rs1064770 [ dbSNP | Ensembl ].
VAR_064279
Natural varianti29 – 291V → A in allele alpha.
Corresponds to variant rs1064771 [ dbSNP | Ensembl ].
VAR_064280
Natural varianti51 – 511H → R in allele alpha.
Corresponds to variant rs1060281 [ dbSNP | Ensembl ].
VAR_064281
Natural varianti52 – 521G → D in allele alpha.
Corresponds to variant rs17841227 [ dbSNP | Ensembl ].
VAR_064282
Natural varianti53 – 531P → R in allele alpha.
Corresponds to variant rs17841226 [ dbSNP | Ensembl ].
VAR_064283
Natural varianti76 – 761V → L in allele alpha.
Corresponds to variant rs71384640 [ dbSNP | Ensembl ].
VAR_064284
Natural varianti85 – 851A → T.3 Publications
Corresponds to variant rs1141968 [ dbSNP | Ensembl ].
VAR_014559
Natural varianti115 – 1151T → I in allele alpha.
Corresponds to variant rs1064774 [ dbSNP | Ensembl ].
VAR_064285
Natural varianti116 – 1161A → I in allele alpha; requires 2 nucleotide substitutions.
VAR_064286
Natural varianti118 – 1181I → T in allele alpha.
Corresponds to variant rs71376589 [ dbSNP | Ensembl ].
VAR_064287
Natural varianti132 – 1321N → K.2 Publications
Corresponds to variant rs1800991 [ dbSNP | Ensembl ].
VAR_016102
Natural varianti133 – 1331V → I in allele alpha.
Corresponds to variant rs1064779 [ dbSNP | Ensembl ].
VAR_064288
Natural varianti136 – 1361H → R in allele alpha.
Corresponds to variant rs1064780 [ dbSNP | Ensembl ].
VAR_051830
Natural varianti141 – 1411T → A.1 Publication
Corresponds to variant rs1800992 [ dbSNP | Ensembl ].
VAR_014560
Natural varianti141 – 1411T → M in allele alpha.
VAR_064289
Natural varianti162 – 1621D → N.1 Publication
Corresponds to variant rs2234641 [ dbSNP | Ensembl ].
VAR_014561
Natural varianti168 – 1681R → P in allele alpha.
Corresponds to variant rs1141969 [ dbSNP | Ensembl ].
VAR_064290
Natural varianti170 – 1701P → S.2 Publications
Corresponds to variant rs2234904 [ dbSNP | Ensembl ].
VAR_014562
Natural varianti205 – 2051V → I in allele alpha.
Corresponds to variant rs1060284 [ dbSNP | Ensembl ].
VAR_064291
Natural varianti215 – 2151T → S.3 Publications
Corresponds to variant rs2234905 [ dbSNP | Ensembl ].
VAR_014563
Natural varianti216 – 2161R → Q.3 Publications
Corresponds to variant rs2234906 [ dbSNP | Ensembl ].
VAR_014564
Natural varianti221 – 2211Q → K.3 Publications
Corresponds to variant rs17841224 [ dbSNP | Ensembl ].
VAR_064292
Natural varianti245 – 2451G → D in allele alpha.
Corresponds to variant rs1060292 [ dbSNP | Ensembl ].
VAR_064293
Natural varianti263 – 2631Y → N.1 Publication
Corresponds to variant rs2234646 [ dbSNP | Ensembl ].
VAR_064294

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei79 – 879Missing in isoform 2. CuratedVSP_005375

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30038 mRNA. Translation: AAA86934.1.
M33494 Genomic DNA. Translation: AAC83172.1.
M33491 mRNA. Translation: AAA36778.1.
AF098328 Genomic DNA. Translation: AAD17846.1.
AF099144 Genomic DNA. Translation: AAD17860.1.
AF206665 mRNA. Translation: AAG35695.1.
AF206666 mRNA. Translation: AAG35696.1.
AF206667 mRNA. Translation: AAG35697.1.
FJ931116 Genomic DNA. Translation: ACZ98910.1.
FJ931118 mRNA. Translation: ACZ98912.1.
AC120498 Genomic DNA. No translation available.
BC074974 mRNA. Translation: AAH74974.1.
CCDSiCCDS10431.1. [Q15661-1]
PIRiA35863.
A45754.
C35863.
RefSeqiNP_003285.2. NM_003294.3. [Q15661-1]
UniGeneiHs.405479.
Hs.592982.

Genome annotation databases

EnsembliENST00000338844; ENSP00000343577; ENSG00000172236. [Q15661-1]
GeneIDi7177.
KEGGihsa:7177.
UCSCiuc002ckz.4. human. [Q15661-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30038 mRNA. Translation: AAA86934.1.
M33494 Genomic DNA. Translation: AAC83172.1.
M33491 mRNA. Translation: AAA36778.1.
AF098328 Genomic DNA. Translation: AAD17846.1.
AF099144 Genomic DNA. Translation: AAD17860.1.
AF206665 mRNA. Translation: AAG35695.1.
AF206666 mRNA. Translation: AAG35696.1.
AF206667 mRNA. Translation: AAG35697.1.
FJ931116 Genomic DNA. Translation: ACZ98910.1.
FJ931118 mRNA. Translation: ACZ98912.1.
AC120498 Genomic DNA. No translation available.
BC074974 mRNA. Translation: AAH74974.1.
CCDSiCCDS10431.1. [Q15661-1]
PIRiA35863.
A45754.
C35863.
RefSeqiNP_003285.2. NM_003294.3. [Q15661-1]
UniGeneiHs.405479.
Hs.592982.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LTOX-ray2.20A/B/C/D31-275[»]
2F9NX-ray1.60A/B/C/D31-275[»]
2F9OX-ray2.10A/B/C/D31-275[»]
2F9PX-ray2.30A/B/C/D31-275[»]
2ZEBX-ray2.50A/B/C/D31-273[»]
2ZECX-ray2.06A/B/C/D31-273[»]
4A6LX-ray2.05A/B/C/D31-275[»]
4MPUX-ray1.65A/B31-275[»]
4MPVX-ray2.31A/B31-275[»]
4MPWX-ray1.95A/B31-275[»]
4MPXX-ray2.00A/B31-275[»]
4MQAX-ray2.25A/B31-275[»]
5F03X-ray1.94A/B31-275[»]
ProteinModelPortaliQ15661.
SMRiQ15661. Positions 31-273.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113029. 2 interactions.
IntActiQ15661. 2 interactions.
STRINGi9606.ENSP00000343577.

Chemistry

BindingDBiQ15661.
ChEMBLiCHEMBL2095193.
GuidetoPHARMACOLOGYi2424.

Protein family/group databases

MEROPSiS01.143.

PTM databases

PhosphoSiteiQ15661.

Polymorphism and mutation databases

DMDMi18202508.

Proteomic databases

PaxDbiQ15661.
PRIDEiQ15661.

Protocols and materials databases

DNASUi7177.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000338844; ENSP00000343577; ENSG00000172236. [Q15661-1]
GeneIDi7177.
KEGGihsa:7177.
UCSCiuc002ckz.4. human. [Q15661-1]

Organism-specific databases

CTDi7177.
GeneCardsiTPSAB1.
H-InvDBHIX0012676.
HGNCiHGNC:12019. TPSAB1.
HPAiCAB016369.
CAB022175.
HPA049153.
HPA049554.
MIMi191080. gene.
neXtProtiNX_Q15661.
PharmGKBiPA36698.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118810.
HOVERGENiHBG013304.
InParanoidiQ15661.
KOiK01340.
OrthoDBiEOG75B84T.
PhylomeDBiQ15661.
TreeFamiTF351676.

Enzyme and pathway databases

BRENDAi3.4.21.59. 2681.
ReactomeiR-HSA-1592389. Activation of Matrix Metalloproteinases.

Miscellaneous databases

ChiTaRSiTPSAB1. human.
EvolutionaryTraceiQ15661.
GenomeRNAii7177.
NextBioi28132.
PROiQ15661.
SOURCEiSearch...

Gene expression databases

BgeeiQ15661.
CleanExiHS_TPSAB1.
ExpressionAtlasiQ15661. baseline and differential.
GenevisibleiQ15661. HS.

Family and domain databases

InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of complementary DNA for human tryptase."
    Miller J.S., Westin E.H., Schwartz L.B.
    J. Clin. Invest. 84:1188-1195(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS THR-85; SER-215; GLN-216 AND LYS-221.
    Tissue: Lung.
  2. Schwartz L.B.
    Submitted (MAR-1990) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 89-93 AND 108.
  3. "Human mast cell tryptase: multiple cDNAs and genes reveal a multigene serine protease family."
    Vanderslice P., Ballinger S.M., Tam E.K., Goldstein S.M., Craik C.S., Caughey G.H.
    Proc. Natl. Acad. Sci. U.S.A. 87:3811-3815(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ALLELE BETA-I) (ISOFORM 1).
  4. "Characterization of genes encoding known and novel human mast cell tryptases on chromosome 16p13.3."
    Pallaoro M., Fejzo M.S., Shayesteh L., Blount J.L., Caughey G.H.
    J. Biol. Chem. 274:3355-3362(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES ALPHA AND BETA-I) (ISOFORM 1).
  5. "Alternate mRNA splicing in multiple human tryptase genes is predicted to regulate tetramer formation."
    Jackson N.E., Wang H.W., Bryant K.J., McNeil H.P., Husain A., Liu K., Tedla N., Thomas P.S., King G.C., Hettiaratchi A., Cairns J., Hunt J.E.
    J. Biol. Chem. 283:34178-34187(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 16-275 (ALLELE ALPHA; ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 54-275 (ALLELE BETA-I; ISOFORM 2), VARIANTS PRO-15 AND THR-85, FUNCTION, FIBRONECTIN CLEAVAGE, TISSUE SPECIFICITY.
  6. "Human subjects are protected from mast cell tryptase deficiency despite frequent inheritance of loss-of-function mutations."
    Trivedi N.N., Tamraz B., Chu C., Kwok P.Y., Caughey G.H.
    J. Allergy Clin. Immunol. 124:1099-1105(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS PRO-15; SER-170; SER-215; GLN-216 AND LYS-221.
  7. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORM 1), VARIANT LYS-132.
  9. "Human pituitary tryptase: molecular forms, NH2-terminal sequence, immunocytochemical localization, and specificity with prohormone and fluorogenic substrates."
    Cromlish J.A., Seidah N.G., Marcinkiewcz M., Hamelin J., Johnson D.A., Chretein M.
    J. Biol. Chem. 262:1363-1373(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 31-50, PROTEIN SEQUENCE OF 31-38.
    Tissue: Lung.
  10. "Intracellular serpin SERPINB6 (PI6) is abundantly expressed by human mast cells and forms complexes with beta-tryptase monomers."
    Strik M.C., Wolbink A., Wouters D., Bladergroen B.A., Verlaan A.R., van Houdt I.S., Hijlkema S., Hack C.E., Kummer J.A.
    Blood 103:2710-2717(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FORMATION OF A COMPLEX WITH SERPINB6.
  11. "Active monomers of human beta-tryptase have expanded substrate specificities."
    Fukuoka Y., Schwartz L.B.
    Int. Immunopharmacol. 7:1900-1908(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  12. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-233.
    Tissue: Liver.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "The crystal structure of human alpha1-tryptase reveals a blocked substrate-binding region."
    Marquardt U., Zettl F., Huber R., Bode W., Sommerhoff C.
    J. Mol. Biol. 321:491-502(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 31-275.
  15. "Characterization of two highly polymorphic human tryptase loci and comparison with a newly discovered monkey tryptase ortholog."
    Guida M., Riedy M., Lee D., Hall J.
    Pharmacogenetics 10:389-396(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PRO-15; VAL-18; VAL-23; THR-85; LYS-132; ALA-141; ASN-162; SER-170; SER-215; GLN-216; LYS-221 AND ASN-263.

Entry informationi

Entry nameiTRYB1_HUMAN
AccessioniPrimary (citable) accession number: Q15661
Secondary accession number(s): D2E6R9
, D2E6S1, P15157, Q15663, Q6B052, Q9H2Y4, Q9H2Y5, Q9UQI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 150 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

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 one 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.