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P07477

- TRY1_HUMAN

UniProt

P07477 - TRY1_HUMAN

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Protein
Trypsin-1
Gene
PRSS1, TRP1, TRY1, TRYP1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 specificity By 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
Complete GO annotation...

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
Complete GO annotation...

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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.11 Publications
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 Publications
Add
BLAST
Propeptidei16 – 238Activation peptide
PRO_0000028197
Chaini24 – 247224Trypsin-1
PRO_0000028198Add
BLAST
Chaini24 – 12299Alpha-trypsin chain 1
PRO_0000313570Add
BLAST
Chaini123 – 247125Alpha-trypsin chain 2
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiP07477.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 244221Peptidase S1
Add
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41L → F in AAI28227. 1 Publication

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.
ENST00000561535; ENSP00000455361; ENSG00000261473.
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 .
ENST00000561535 ; ENSP00000455361 ; ENSG00000261473 .
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 165 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 (1 Publication) but it has been shown (1 Publication) to be sulfated instead. Phosphate and sulfate groups are similar in mass and size, and this can lead to erroneous interpretation of the results.

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

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