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P07477

- TRY1_HUMAN

UniProt

P07477 - TRY1_HUMAN

Protein

Trypsin-1

Gene

PRSS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 1 (01 Apr 1988)
      Previous versions | rss
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    Functioni

    Has activity against the synthetic substrates Boc-Phe-Ser-Arg-Mec, Boc-Leu-Thr-Arg-Mec, Boc-Gln-Ala-Arg-Mec and Boc-Val-Pro-Arg-Mec. The single-chain form is more active than the two-chain form against all of these substrates.1 Publication

    Catalytic activityi

    Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.

    Cofactori

    Binds 1 calcium ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei63 – 631Charge relay system
    Metal bindingi75 – 751Calcium
    Metal bindingi77 – 771Calcium; via carbonyl oxygen
    Metal bindingi80 – 801Calcium; via carbonyl oxygen
    Metal bindingi85 – 851Calcium
    Active sitei107 – 1071Charge relay system
    Sitei194 – 1941Required for specificityBy similarity
    Active sitei200 – 2001Charge relay system

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. serine-type endopeptidase activity Source: UniProtKB

    GO - Biological processi

    1. cobalamin metabolic process Source: Reactome
    2. digestion Source: UniProtKB-KW
    3. extracellular matrix disassembly Source: Reactome
    4. extracellular matrix organization Source: Reactome
    5. small molecule metabolic process Source: Reactome
    6. vitamin metabolic process Source: Reactome
    7. water-soluble vitamin metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Digestion

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_118682. Activation of Matrix Metalloproteinases.
    REACT_163862. Cobalamin (Cbl, vitamin B12) transport and metabolism.

    Protein family/group databases

    MEROPSiS01.127.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trypsin-1 (EC:3.4.21.4)
    Alternative name(s):
    Beta-trypsin
    Cationic trypsinogen
    Serine protease 1
    Trypsin I
    Cleaved into the following 2 chains:
    Gene namesi
    Name:PRSS1
    Synonyms:TRP1, TRY1, TRYP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:9475. PRSS1.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. extracellular region Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Pancreatitis, hereditary (PCTT) [MIM:167800]: A disease characterized by pancreas inflammation, permanent destruction of the pancreatic parenchyma, maldigestion, and severe abdominal pain attacks.11 Publications
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti16 – 161A → V in PCTT; disrupts signal sequence cleavage site. 1 Publication
    VAR_011693
    Natural varianti22 – 221D → G in PCTT; increased rate of activation. 1 Publication
    VAR_011652
    Natural varianti23 – 231K → R in PCTT; increased rate of activation. 1 Publication
    VAR_011653
    Natural varianti29 – 291N → I in PCTT. 4 Publications
    VAR_006720
    Natural varianti29 – 291N → T in PCTT. 1 Publication
    VAR_012712
    Natural varianti54 – 541N → S in PCTT; associated with Ile-29; the double mutant shows increased autocatalytic activation which is solely due to the Ile-29 mutation. 1 Publication
    VAR_037908
    Natural varianti79 – 791E → K in PCTT; Lys-79 trypsin activates anionic trypsinogen PRSS2 2-fold while the common pancreatitis-associated mutants His-122 or Ile-29 have no such effect. 1 Publication
    Corresponds to variant rs28934902 [ dbSNP | Ensembl ].
    VAR_037909
    Natural varianti104 – 1041L → P in PCTT. 1 Publication
    VAR_011654
    Natural varianti116 – 1161R → C in PCTT. 1 Publication
    VAR_011655
    Natural varianti122 – 1221R → C in PCTT; suppresses an autocleavage site. 1 Publication
    VAR_012713
    Natural varianti122 – 1221R → H in PCTT; suppresses an autocleavage site which is probably part of a fail-safe mechanism by which trypsin, which is activated within the pancreas, may be inactivated; loss of this cleavage site would permit autodigestion resulting in pancreatitis. 5 Publications
    VAR_006721
    Natural varianti139 – 1391C → F in PCTT. 1 Publication
    VAR_011656

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi154 – 1541Y → F: Lack of sulfation. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi167800. phenotype.
    Orphaneti676. Hereditary chronic pancreatitis.
    PharmGKBiPA33828.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 15152 PublicationsAdd
    BLAST
    Propeptidei16 – 238Activation peptidePRO_0000028197
    Chaini24 – 247224Trypsin-1PRO_0000028198Add
    BLAST
    Chaini24 – 12299Alpha-trypsin chain 1PRO_0000313570Add
    BLAST
    Chaini123 – 247125Alpha-trypsin chain 2PRO_0000313571Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi30 ↔ 160
    Disulfide bondi48 ↔ 64
    Disulfide bondi139 ↔ 206
    Modified residuei154 – 1541Sulfotyrosine1 Publication
    Disulfide bondi171 ↔ 185
    Disulfide bondi196 ↔ 220

    Post-translational modificationi

    Occurs in a single-chain form and a two-chain form, produced by proteolytic cleavage after Arg-122.

    Keywords - PTMi

    Disulfide bond, Sulfation, Zymogen

    Proteomic databases

    MaxQBiP07477.
    PaxDbiP07477.
    PeptideAtlasiP07477.
    PRIDEiP07477.

    PTM databases

    PhosphoSiteiP07477.

    Miscellaneous databases

    PMAP-CutDBP07477.

    Expressioni

    Gene expression databases

    ArrayExpressiP07477.
    BgeeiP07477.
    GenevestigatoriP07477.

    Organism-specific databases

    HPAiCAB025487.
    CAB025538.

    Interactioni

    Protein-protein interaction databases

    BioGridi111626. 6 interactions.
    IntActiP07477. 4 interactions.

    Structurei

    Secondary structure

    1
    247
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi38 – 5417
    Beta strandi57 – 604
    Helixi62 – 643
    Beta strandi70 – 745
    Beta strandi76 – 805
    Beta strandi86 – 9510
    Turni101 – 1033
    Beta strandi109 – 1157
    Beta strandi120 – 1223
    Beta strandi138 – 1447
    Beta strandi149 – 1513
    Beta strandi159 – 1657
    Helixi168 – 1747
    Turni176 – 1783
    Beta strandi183 – 1875
    Beta strandi192 – 1943
    Beta strandi203 – 2064
    Beta strandi209 – 2168
    Beta strandi218 – 2225
    Beta strandi227 – 2315
    Helixi232 – 2354
    Helixi236 – 24510

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FXYX-ray2.15A127-247[»]
    1TRNX-ray2.20A/B24-247[»]
    2RA3X-ray1.46A/B24-247[»]
    ProteinModelPortaliP07477.
    SMRiP07477. Positions 24-247.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07477.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini24 – 244221Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG5640.
    HOVERGENiHBG013304.
    InParanoidiP07477.
    KOiK01312.
    PhylomeDBiP07477.
    TreeFamiTF331065.

    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.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P07477-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNPLLILTFV AAALAAPFDD DDKIVGGYNC EENSVPYQVS LNSGYHFCGG    50
    SLINEQWVVS AGHCYKSRIQ VRLGEHNIEV LEGNEQFINA AKIIRHPQYD 100
    RKTLNNDIML IKLSSRAVIN ARVSTISLPT APPATGTKCL ISGWGNTASS 150
    GADYPDELQC LDAPVLSQAK CEASYPGKIT SNMFCVGFLE GGKDSCQGDS 200
    GGPVVCNGQL QGVVSWGDGC AQKNKPGVYT KVYNYVKWIK NTIAANS 247
    Length:247
    Mass (Da):26,558
    Last modified:April 1, 1988 - v1
    Checksum:iDD49A487B8062813
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4 – 41L → F in AAI28227. (PubMed:15489334)Curated

    Mass spectrometryi

    Molecular mass is 24348±2 Da from positions 24 - 247. Determined by ESI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti16 – 161A → V in PCTT; disrupts signal sequence cleavage site. 1 Publication
    VAR_011693
    Natural varianti22 – 221D → G in PCTT; increased rate of activation. 1 Publication
    VAR_011652
    Natural varianti23 – 231K → R in PCTT; increased rate of activation. 1 Publication
    VAR_011653
    Natural varianti29 – 291N → I in PCTT. 4 Publications
    VAR_006720
    Natural varianti29 – 291N → T in PCTT. 1 Publication
    VAR_012712
    Natural varianti54 – 541N → S in PCTT; associated with Ile-29; the double mutant shows increased autocatalytic activation which is solely due to the Ile-29 mutation. 1 Publication
    VAR_037908
    Natural varianti79 – 791E → K in PCTT; Lys-79 trypsin activates anionic trypsinogen PRSS2 2-fold while the common pancreatitis-associated mutants His-122 or Ile-29 have no such effect. 1 Publication
    Corresponds to variant rs28934902 [ dbSNP | Ensembl ].
    VAR_037909
    Natural varianti104 – 1041L → P in PCTT. 1 Publication
    VAR_011654
    Natural varianti116 – 1161R → C in PCTT. 1 Publication
    VAR_011655
    Natural varianti122 – 1221R → C in PCTT; suppresses an autocleavage site. 1 Publication
    VAR_012713
    Natural varianti122 – 1221R → H in PCTT; suppresses an autocleavage site which is probably part of a fail-safe mechanism by which trypsin, which is activated within the pancreas, may be inactivated; loss of this cleavage site would permit autodigestion resulting in pancreatitis. 5 Publications
    VAR_006721
    Natural varianti137 – 1371T → M in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036299
    Natural varianti139 – 1391C → F in PCTT. 1 Publication
    VAR_011656

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22612 mRNA. Translation: AAA61231.1.
    L36092 Genomic DNA. Translation: AAC80207.1.
    AK312199 mRNA. Translation: BAG35132.1.
    AC231380 Genomic DNA. No translation available.
    CH236959 Genomic DNA. Translation: EAL23773.1.
    CH471198 Genomic DNA. Translation: EAW51925.1.
    BC128226 mRNA. Translation: AAI28227.1.
    AF314534 Genomic DNA. Translation: AAG30943.1.
    U70137 Genomic DNA. Translation: AAC50728.1.
    AF315309 Genomic DNA. Translation: AAG30947.1.
    AF315310 Genomic DNA. Translation: AAG30948.1.
    AF315311 Genomic DNA. Translation: AAG30949.1.
    CCDSiCCDS5872.1.
    PIRiA25852.
    S50020.
    S50021.
    RefSeqiNP_002760.1. NM_002769.4.
    UniGeneiHs.449281.

    Genome annotation databases

    EnsembliENST00000311737; ENSP00000308720; ENSG00000204983.
    GeneIDi5644.
    KEGGihsa:5644.
    UCSCiuc003wak.2. human.

    Polymorphism databases

    DMDMi136408.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22612 mRNA. Translation: AAA61231.1 .
    L36092 Genomic DNA. Translation: AAC80207.1 .
    AK312199 mRNA. Translation: BAG35132.1 .
    AC231380 Genomic DNA. No translation available.
    CH236959 Genomic DNA. Translation: EAL23773.1 .
    CH471198 Genomic DNA. Translation: EAW51925.1 .
    BC128226 mRNA. Translation: AAI28227.1 .
    AF314534 Genomic DNA. Translation: AAG30943.1 .
    U70137 Genomic DNA. Translation: AAC50728.1 .
    AF315309 Genomic DNA. Translation: AAG30947.1 .
    AF315310 Genomic DNA. Translation: AAG30948.1 .
    AF315311 Genomic DNA. Translation: AAG30949.1 .
    CCDSi CCDS5872.1.
    PIRi A25852.
    S50020.
    S50021.
    RefSeqi NP_002760.1. NM_002769.4.
    UniGenei Hs.449281.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FXY X-ray 2.15 A 127-247 [» ]
    1TRN X-ray 2.20 A/B 24-247 [» ]
    2RA3 X-ray 1.46 A/B 24-247 [» ]
    ProteinModelPortali P07477.
    SMRi P07477. Positions 24-247.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111626. 6 interactions.
    IntActi P07477. 4 interactions.

    Chemistry

    BindingDBi P07477.
    ChEMBLi CHEMBL209.
    GuidetoPHARMACOLOGYi 2397.

    Protein family/group databases

    MEROPSi S01.127.

    PTM databases

    PhosphoSitei P07477.

    Polymorphism databases

    DMDMi 136408.

    Proteomic databases

    MaxQBi P07477.
    PaxDbi P07477.
    PeptideAtlasi P07477.
    PRIDEi P07477.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000311737 ; ENSP00000308720 ; ENSG00000204983 .
    GeneIDi 5644.
    KEGGi hsa:5644.
    UCSCi uc003wak.2. human.

    Organism-specific databases

    CTDi 5644.
    GeneCardsi GC07P142711.
    GeneReviewsi PRSS1.
    HGNCi HGNC:9475. PRSS1.
    HPAi CAB025487.
    CAB025538.
    MIMi 167800. phenotype.
    276000. gene.
    neXtProti NX_P07477.
    Orphaneti 676. Hereditary chronic pancreatitis.
    PharmGKBi PA33828.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5640.
    HOVERGENi HBG013304.
    InParanoidi P07477.
    KOi K01312.
    PhylomeDBi P07477.
    TreeFami TF331065.

    Enzyme and pathway databases

    Reactomei REACT_118682. Activation of Matrix Metalloproteinases.
    REACT_163862. Cobalamin (Cbl, vitamin B12) transport and metabolism.

    Miscellaneous databases

    EvolutionaryTracei P07477.
    GeneWikii Trypsin_1.
    GenomeRNAii 5644.
    NextBioi 21926.
    PMAP-CutDB P07477.
    PROi P07477.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07477.
    Bgeei P07477.
    Genevestigatori P07477.

    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.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, characterization and nucleotide sequences of two cDNAs encoding human pancreatic trypsinogens."
      Emi M., Nakamura Y., Ogawa M., Yamamoto T., Nishide T., Mori T., Matsubara K.
      Gene 41:305-310(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The complete 685-kilobase DNA sequence of the human beta T cell receptor locus."
      Rowen L., Koop B.F., Hood L.
      Science 272:1755-1762(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Prostate.
    4. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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].
    8. "Chronic pancreatitis associated with an activation peptide mutation that facilitates trypsin activation."
      Teich N., Ockenga J., Hoffmeister A., Manns M., Mossner J., Keim V.
      Gastroenterology 119:461-465(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 15-67, VARIANT PCTT GLY-22.
    9. "Identification of one- and two-chain forms of trypsinogen 1 produced by a human gastric adenocarcinoma cell line."
      Koshikawa N., Yasumitsu H., Nagashima Y., Umeda M., Miyazaki K.
      Biochem. J. 303:187-190(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 16-43 AND 123-142, FUNCTION, POST-TRANSLATIONAL PROCESSING.
      Tissue: Gastric adenocarcinoma.
    10. "Immunoreactive anionic and cationic trypsin in human serum."
      Kimland M., Russick C., Marks W.H., Borgstroem A.
      Clin. Chim. Acta 184:31-46(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 16-43.
    11. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 68-151, VARIANT PCTT HIS-122.
    12. "Mutational screening of patients with nonalcoholic chronic pancreatitis: identification of further trypsinogen variants."
      Teich N., Bauer N., Mossner J., Keim V.
      Am. J. Gastroenterol. 97:341-346(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 68-151, VARIANTS PCTT ILE-29; PRO-104; CYS-116; HIS-122 AND PHE-139.
    13. Lubec G., Afjehi-Sadat L.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 73-92, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    14. "Human cationic trypsinogen is sulfated on Tyr154."
      Sahin-Toth M., Kukor Z., Nemoda Z.
      FEBS J. 273:5044-5050(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SULFATION AT TYR-154, MUTAGENESIS OF TYR-154.
    15. "Crystal structure of human trypsin 1: unexpected phosphorylation of Tyr151."
      Gaboriaud C., Serre L., Guy-Crotte O., Forest E., Fontecilla-Camps J.-C.
      J. Mol. Biol. 259:995-1010(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), MASS SPECTROMETRY.
    16. "Mutations in the cationic trypsinogen gene are associated with recurrent acute and chronic pancreatitis."
      Gorry M.C., Gabbaizedeh D., Furey W., Gates L.K. Jr., Preston R.A., Aston C.E., Zhang Y., Ulrich C., Ehrlich G.D., Whitcomb D.C.
      Gastroenterology 113:1063-1068(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PCTT ILE-29 AND HIS-122.
    17. "Mutations of the cationic trypsinogen in hereditary pancreatitis."
      Teich N., Mossner J., Keim V.
      Hum. Mutat. 12:39-43(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PCTT ILE-29.
    18. "A signal peptide cleavage site mutation in the cationic trypsinogen gene is strongly associated with chronic pancreatitis."
      Witt H., Luck W., Becker M.
      Gastroenterology 117:7-10(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PCTT VAL-16 AND HIS-122.
    19. "Mutations in the cationic trypsinogen gene and evidence for genetic heterogeneity in hereditary pancreatitis."
      Ferec C., Raguenes O., Salomon R., Roche C., Bernard J.P., Guillot M., Quere I., Faure C., Mercier B., Audrezet M.-P., Guillausseau P.J., Dupont C., Munnich A., Bignon J.D., Le Bodic L.
      J. Med. Genet. 36:228-232(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PCTT ARG-23.
    20. "A CGC>CAT gene conversion-like event resulting in the R122H mutation in the cationic trypsinogen gene and its implication in the genotyping of pancreatitis."
      Chen J.-M., Raguenes O., Ferec C., Deprez P.H., Verellen-Dumoulin C.
      J. Med. Genet. 37:E36-E36(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PCTT HIS-122.
    21. "Novel cationic trypsinogen (PRSS1) N29T and R122C mutations cause autosomal dominant hereditary pancreatitis."
      Pfutzer R., Myers E., Applebaum-Shapiro S., Finch R., Ellis I., Neoptolemos J., Kant J.A., Whitcomb D.C.
      Gut 50:271-272(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PCTT THR-29 AND CYS-122.
    22. "Interaction between trypsinogen isoforms in genetically determined pancreatitis: mutation E79K in cationic trypsin (PRSS1) causes increased transactivation of anionic trypsinogen (PRSS2)."
      Teich N., Le Marechal C., Kukor Z., Caca K., Witzigmann H., Chen J.-M., Toth M., Moessner J., Keim V., Ferec C., Sahin-Toth M.
      Hum. Mutat. 23:22-31(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PCTT LYS-79, CHARACTERIZATION OF VARIANT PCTT LYS-79.
    23. "Gene conversion between functional trypsinogen genes PRSS1 and PRSS2 associated with chronic pancreatitis in a six-year-old girl."
      Teich N., Nemoda Z., Koehler H., Heinritz W., Moessner J., Keim V., Sahin-Toth M.
      Hum. Mutat. 25:343-347(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PCTT ILE-29 AND SER-54, CHARACTERIZATION OF VARIANTS PCTT ILE-29 AND SER-54.
    24. Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-137.

    Entry informationi

    Entry nameiTRY1_HUMAN
    AccessioniPrimary (citable) accession number: P07477
    Secondary accession number(s): A1A509
    , A6NJ71, B2R5I5, Q5NV57, Q7M4N3, Q7M4N4, Q92955, Q9HAN4, Q9HAN5, Q9HAN6, Q9HAN7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: April 1, 1988
    Last modified: October 1, 2014
    This is version 166 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

    Caution

    Tyr-154 was proposed to be phosphorylated (PubMed:8683601) but it has been shown (PubMed:17087724) to be sulfated instead. Phosphate and sulfate groups are similar in mass and size, and this can lead to erroneous interpretation of the results.2 Publications

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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

    External Data

    Dasty 3