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Q9NRR2

- TRYG1_HUMAN

UniProt

Q9NRR2 - TRYG1_HUMAN

Protein

Tryptase gamma

Gene

TPSG1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      Previous versions | rss
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    Functioni

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei78 – 781Charge relay systemBy similarity
    Active sitei125 – 1251Charge relay systemBy similarity
    Active sitei222 – 2221Charge relay systemBy similarity

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: InterPro
    2. serine-type peptidase activity Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Protein family/group databases

    MEROPSiS01.028.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tryptase gamma (EC:3.4.21.-)
    Alternative name(s):
    Serine protease 31
    Transmembrane tryptase
    Cleaved into the following 2 chains:
    Gene namesi
    Name:TPSG1
    Synonyms:PRSS31, TMT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:14134. TPSG1.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37849.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 321302Tryptase gammaPRO_0000027498Add
    BLAST
    Chaini20 – 3617Tryptase gamma light chainPRO_0000027499Add
    BLAST
    Chaini38 – 321284Tryptase gamma heavy chainPRO_0000027500Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi26 ↔ 145Interchain (between light and heavy chains)PROSITE-ProRule annotation
    Disulfide bondi63 ↔ 79PROSITE-ProRule annotation
    Glycosylationi85 – 851N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi159 ↔ 228PROSITE-ProRule annotation
    Disulfide bondi192 ↔ 210PROSITE-ProRule annotation
    Disulfide bondi218 ↔ 246PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiQ9NRR2.
    PRIDEiQ9NRR2.

    Expressioni

    Tissue specificityi

    Expressed in many tissues.

    Gene expression databases

    BgeeiQ9NRR2.
    CleanExiHS_TPSG1.
    GenevestigatoriQ9NRR2.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000234798.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NRR2.
    SMRiQ9NRR2. Positions 38-269.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei284 – 30421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini38 – 270233Peptidase 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, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5640.
    HOGENOMiHOG000251820.
    HOVERGENiHBG013304.
    InParanoidiQ9NRR2.
    KOiK09615.
    OrthoDBiEOG75B84T.
    PhylomeDBiQ9NRR2.
    TreeFamiTF351676.

    Family and domain databases

    InterProiIPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [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.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9NRR2-1 [UniParc]FASTAAdd to Basket

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    MALGACGLLL LLAVPGVSLR TLQPGCGRPQ VSDAGGRIVG GHAAPAGAWP    50
    WQASLRLRRM HVCGGSLLSP QWVLTAAHCF SGSLNSSDYQ VHLGELEITL 100
    SPHFSTVRQI ILHSSPSGQP GTSGDIALVE LSVPVTLSSR ILPVCLPEAS 150
    DDFCPGIRCW VTGWGYTREG EPLPPPYSLR EVKVSVVDTE TCRRDYPGPG 200
    GSILQPDMLC ARGPGDACQD DSGGPLVCQV NGAWVQAGTV SWGEGCGRPN 250
    RPGVYTRVPA YVNWIRRHIT ASGGSESGYP RLPLLAGLFL PGLFLLLVSC 300
    VLLAKCLLHP SADGTPFPAP D 321
    Length:321
    Mass (Da):33,815
    Last modified:May 18, 2010 - v3
    Checksum:iD2F7A5A1D66F59C7
    GO

    Polymorphismi

    There are two alleles; gamma-I and gamma-II which differ by 5 residues.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti60 – 601M → V in allele gamma-II. 2 Publications
    Corresponds to variant rs760357 [ dbSNP | Ensembl ].
    VAR_012097
    Natural varianti126 – 1261I → M in allele gamma-II. 1 Publication
    VAR_012098
    Natural varianti132 – 1321S → T in allele gamma-II. 1 Publication
    VAR_012099
    Natural varianti160 – 1601W → S.1 Publication
    Corresponds to variant rs4984638 [ dbSNP | Ensembl ].
    VAR_025012
    Natural varianti204 – 2041L → I in allele gamma-II. 1 Publication
    VAR_012100
    Natural varianti239 – 2391T → I.4 Publications
    Corresponds to variant rs11248860 [ dbSNP | Ensembl ].
    VAR_061773
    Natural varianti288 – 2881L → F in allele gamma-II. 2 Publications
    Corresponds to variant rs1004041 [ dbSNP | Ensembl ].
    VAR_012101

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF175522 mRNA. Translation: AAF03695.1.
    AF175759 Genomic DNA. Translation: AAF03697.1.
    AF191031 Genomic DNA. Translation: AAF76457.1.
    AF195508 Genomic DNA. Translation: AAF76458.1.
    AE006466 Genomic DNA. Translation: AAK61269.1.
    AC120498 Genomic DNA. No translation available.
    AF223563 Genomic DNA. Translation: AAG48852.2.
    CCDSiCCDS10430.1.
    RefSeqiNP_036599.3. NM_012467.3.
    UniGeneiHs.592076.

    Genome annotation databases

    EnsembliENST00000234798; ENSP00000234798; ENSG00000116176.
    GeneIDi25823.
    KEGGihsa:25823.
    UCSCiuc002ckw.2. human.

    Polymorphism databases

    DMDMi296453005.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF175522 mRNA. Translation: AAF03695.1 .
    AF175759 Genomic DNA. Translation: AAF03697.1 .
    AF191031 Genomic DNA. Translation: AAF76457.1 .
    AF195508 Genomic DNA. Translation: AAF76458.1 .
    AE006466 Genomic DNA. Translation: AAK61269.1 .
    AC120498 Genomic DNA. No translation available.
    AF223563 Genomic DNA. Translation: AAG48852.2 .
    CCDSi CCDS10430.1.
    RefSeqi NP_036599.3. NM_012467.3.
    UniGenei Hs.592076.

    3D structure databases

    ProteinModelPortali Q9NRR2.
    SMRi Q9NRR2. Positions 38-269.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000234798.

    Chemistry

    ChEMBLi CHEMBL4955.

    Protein family/group databases

    MEROPSi S01.028.

    Polymorphism databases

    DMDMi 296453005.

    Proteomic databases

    PaxDbi Q9NRR2.
    PRIDEi Q9NRR2.

    Protocols and materials databases

    DNASUi 25823.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000234798 ; ENSP00000234798 ; ENSG00000116176 .
    GeneIDi 25823.
    KEGGi hsa:25823.
    UCSCi uc002ckw.2. human.

    Organism-specific databases

    CTDi 25823.
    GeneCardsi GC16M001271.
    H-InvDB HIX0038548.
    HGNCi HGNC:14134. TPSG1.
    MIMi 609341. gene.
    neXtProti NX_Q9NRR2.
    PharmGKBi PA37849.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5640.
    HOGENOMi HOG000251820.
    HOVERGENi HBG013304.
    InParanoidi Q9NRR2.
    KOi K09615.
    OrthoDBi EOG75B84T.
    PhylomeDBi Q9NRR2.
    TreeFami TF351676.

    Miscellaneous databases

    GeneWikii TPSG1.
    GenomeRNAii 25823.
    NextBioi 47087.
    PROi Q9NRR2.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9NRR2.
    CleanExi HS_TPSG1.
    Genevestigatori Q9NRR2.

    Family and domain databases

    InterProi IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a new member of the tryptase family of mouse and human mast cell proteases which possesses a novel COOH-terminal hydrophobic extension."
      Wong G.W., Tang Y., Feyfant E., Sali A., Li L., Li Y., Huang C., Friend D.S., Krilis S.A., Stevens R.L.
      J. Biol. Chem. 274:30784-30793(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT ILE-239.
    2. "Characterization of human gamma-tryptases, novel members of the chromosome 16p mast cell tryptase and prostasin gene families."
      Caughey G.H., Raymond W.W., Blount J.L., Hau L.W., Pallaoro M., Wolters P.J., Verghese G.M.
      J. Immunol. 164:6566-6575(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-60; MET-126; THR-132; SER-160; ILE-204; ILE-239 AND PHE-288.
    3. "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16."
      Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.
      Hum. Mol. Genet. 10:339-352(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS VAL-60; ILE-239 AND PHE-288.
    4. "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].
    5. "Organization and alternative splicing of CACNA1H."
      Mittman S., Agnew W.S.
      Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 220-321, VARIANT ILE-239.

    Entry informationi

    Entry nameiTRYG1_HUMAN
    AccessioniPrimary (citable) accession number: Q9NRR2
    Secondary accession number(s): Q96RZ8
    , Q9C015, Q9NRQ8, Q9UBB2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 109 of the entry and version 3 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

    Complete proteome, 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. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3