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P07477 (TRY1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. Alpha-trypsin chain 1
  2. Alpha-trypsin chain 2
Gene names
Name:PRSS1
Synonyms:TRP1, TRY1, TRYP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length247 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9

Catalytic activity

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

Cofactor

Binds 1 calcium ion per subunit.

Subcellular location

Secretedextracellular space.

Post-translational modification

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

Involvement in disease

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. Ref.8 Ref.11 Ref.12 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Caution

Tyr-154 was proposed to be phosphorylated (Ref.15) but it has been shown (Ref.14) to be sulfated instead. Phosphate and sulfate groups are similar in mass and size, and this can lead to erroneous interpretation of the results.

Mass spectrometry

Molecular mass is 24348±2 Da from positions 24 - 247. Determined by ESI. Ref.15

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515 Ref.9 Ref.10
Propeptide16 – 238Activation peptide
PRO_0000028197
Chain24 – 247224Trypsin-1
PRO_0000028198
Chain24 – 12299Alpha-trypsin chain 1
PRO_0000313570
Chain123 – 247125Alpha-trypsin chain 2
PRO_0000313571

Regions

Domain24 – 244221Peptidase S1

Sites

Active site631Charge relay system
Active site1071Charge relay system
Active site2001Charge relay system
Metal binding751Calcium
Metal binding771Calcium; via carbonyl oxygen
Metal binding801Calcium; via carbonyl oxygen
Metal binding851Calcium
Site1941Required for specificity By similarity

Amino acid modifications

Modified residue1541Sulfotyrosine Ref.14
Disulfide bond30 ↔ 160
Disulfide bond48 ↔ 64
Disulfide bond139 ↔ 206
Disulfide bond171 ↔ 185
Disulfide bond196 ↔ 220

Natural variations

Natural variant161A → V in PCTT; disrupts signal sequence cleavage site. Ref.18
VAR_011693
Natural variant221D → G in PCTT; increased rate of activation. Ref.8
VAR_011652
Natural variant231K → R in PCTT; increased rate of activation. Ref.19
VAR_011653
Natural variant291N → I in PCTT. Ref.12 Ref.16 Ref.17 Ref.23
VAR_006720
Natural variant291N → T in PCTT. Ref.21
VAR_012712
Natural variant541N → S in PCTT; associated with Ile-29; the double mutant shows increased autocatalytic activation which is solely due to the Ile-29 mutation. Ref.23
VAR_037908
Natural variant791E → 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. Ref.22
Corresponds to variant rs28934902 [ dbSNP | Ensembl ].
VAR_037909
Natural variant1041L → P in PCTT. Ref.12
VAR_011654
Natural variant1161R → C in PCTT. Ref.12
VAR_011655
Natural variant1221R → C in PCTT; suppresses an autocleavage site. Ref.21
VAR_012713
Natural variant1221R → 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. Ref.11 Ref.12 Ref.16 Ref.18 Ref.20
VAR_006721
Natural variant1371T → M in a colorectal cancer sample; somatic mutation. Ref.24
VAR_036299
Natural variant1391C → F in PCTT. Ref.12
VAR_011656

Experimental info

Mutagenesis1541Y → F: Lack of sulfation. Ref.14
Sequence conflict41L → F in AAI28227. Ref.7

Secondary structure

........................................... 247
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07477 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: DD49A487B8062813

FASTA24726,558
        10         20         30         40         50         60 
MNPLLILTFV AAALAAPFDD DDKIVGGYNC EENSVPYQVS LNSGYHFCGG SLINEQWVVS 

        70         80         90        100        110        120 
AGHCYKSRIQ VRLGEHNIEV LEGNEQFINA AKIIRHPQYD RKTLNNDIML IKLSSRAVIN 

       130        140        150        160        170        180 
ARVSTISLPT APPATGTKCL ISGWGNTASS GADYPDELQC LDAPVLSQAK CEASYPGKIT 

       190        200        210        220        230        240 
SNMFCVGFLE GGKDSCQGDS GGPVVCNGQL QGVVSWGDGC AQKNKPGVYT KVYNYVKWIK 


NTIAANS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Hereditary pancreatitis is caused by a mutation in the cationic trypsinogen gene."
Whitcomb D.C., Gorry M.C., Preston R.A., Furey W., Sossenheimer M.J., Ulrich C.D., Martin S.P., Gates L.K. Jr., Amann S.T., Toskes P.P., Liddle R., McGrath K., Uomo G., Post J.C., Ehrlich G.D.
Nat. Genet. 14:141-145(1996) [PubMed] [Europe PMC] [Abstract]
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-137.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS5872.1.
PIRA25852.
S50020.
S50021.
RefSeqNP_002760.1. NM_002769.4.
UniGeneHs.449281.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FXYX-ray2.15A127-247[»]
1TRNX-ray2.20A/B24-247[»]
2RA3X-ray1.46A/B24-247[»]
ProteinModelPortalP07477.
SMRP07477. Positions 24-247.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111626. 10 interactions.
IntActP07477. 4 interactions.

Chemistry

BindingDBP07477.
ChEMBLCHEMBL209.
GuidetoPHARMACOLOGY2397.

Protein family/group databases

MEROPSS01.127.

PTM databases

PhosphoSiteP07477.

Polymorphism databases

DMDM136408.

Proteomic databases

MaxQBP07477.
PaxDbP07477.
PeptideAtlasP07477.
PRIDEP07477.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000311737; ENSP00000308720; ENSG00000204983.
ENST00000561535; ENSP00000455361; ENSG00000261473.
GeneID5644.
KEGGhsa:5644.
UCSCuc003wak.2. human.

Organism-specific databases

CTD5644.
GeneCardsGC07P142711.
GeneReviewsPRSS1.
HGNCHGNC:9475. PRSS1.
HPACAB025487.
CAB025538.
MIM167800. phenotype.
276000. gene.
neXtProtNX_P07477.
Orphanet676. Hereditary chronic pancreatitis.
PharmGKBPA33828.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5640.
HOVERGENHBG013304.
InParanoidP07477.
KOK01312.
PhylomeDBP07477.
TreeFamTF331065.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP07477.
BgeeP07477.
GenevestigatorP07477.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07477.
GeneWikiTrypsin_1.
GenomeRNAi5644.
NextBio21926.
PMAP-CutDBP07477.
PROP07477.
SOURCESearch...

Entry information

Entry nameTRY1_HUMAN
AccessionPrimary (citable) accession number: P07477
Secondary accession number(s): A1A509 expand/collapse secondary AC list , A6NJ71, B2R5I5, Q5NV57, Q7M4N3, Q7M4N4, Q92955, Q9HAN4, Q9HAN5, Q9HAN6, Q9HAN7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: July 9, 2014
This is version 164 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM