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P20142

- PEPC_HUMAN

UniProt

P20142 - PEPC_HUMAN

Protein

Gastricsin

Gene

PGC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
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    Functioni

    Hydrolyzes a variety of proteins.

    Catalytic activityi

    More restricted specificity than pepsin A, but shows preferential cleavage at Tyr-|-Xaa bonds. High activity on hemoglobin.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei91 – 911
    Active sitei276 – 2761

    GO - Molecular functioni

    1. aspartic-type endopeptidase activity Source: ProtInc

    GO - Biological processi

    1. digestion Source: ProtInc
    2. proteolysis Source: ProtInc

    Keywords - Molecular functioni

    Aspartyl protease, Hydrolase, Protease

    Keywords - Biological processi

    Digestion

    Protein family/group databases

    MEROPSiA01.003.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gastricsin (EC:3.4.23.3)
    Alternative name(s):
    Pepsinogen C
    Gene namesi
    Name:PGC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:8890. PGC.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: ProtInc
    2. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33228.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 16162 PublicationsAdd
    BLAST
    Propeptidei17 – 5943Activation peptidePRO_0000026056Add
    BLAST
    Chaini60 – 388329GastricsinPRO_0000026057Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi104 ↔ 109
    Disulfide bondi267 ↔ 271
    Disulfide bondi310 ↔ 343

    Keywords - PTMi

    Disulfide bond, Zymogen

    Proteomic databases

    MaxQBiP20142.
    PaxDbiP20142.
    PRIDEiP20142.

    PTM databases

    PhosphoSiteiP20142.

    Miscellaneous databases

    PMAP-CutDBP20142.

    Expressioni

    Gene expression databases

    ArrayExpressiP20142.
    BgeeiP20142.
    CleanExiHS_PGC.
    GenevestigatoriP20142.

    Organism-specific databases

    HPAiHPA031717.
    HPA031718.

    Interactioni

    Protein-protein interaction databases

    BioGridi111246. 4 interactions.
    STRINGi9606.ENSP00000362116.

    Structurei

    Secondary structure

    1
    388
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi19 – 257
    Helixi29 – 357
    Helixi39 – 435
    Helixi50 – 545
    Helixi65 – 684
    Beta strandi73 – 797
    Turni80 – 834
    Beta strandi84 – 918
    Beta strandi97 – 1015
    Helixi107 – 1104
    Helixi117 – 1193
    Beta strandi124 – 13411
    Beta strandi137 – 15014
    Beta strandi153 – 16513
    Helixi169 – 1735
    Beta strandi178 – 1814
    Helixi185 – 1873
    Helixi189 – 1913
    Helixi195 – 2017
    Beta strandi205 – 21410
    Beta strandi219 – 22911
    Helixi232 – 2343
    Beta strandi235 – 24410
    Beta strandi246 – 2494
    Beta strandi251 – 2544
    Beta strandi256 – 2594
    Turni266 – 2694
    Beta strandi271 – 2755
    Beta strandi281 – 2855
    Helixi286 – 2883
    Helixi289 – 2968
    Beta strandi306 – 3083
    Helixi310 – 3156
    Beta strandi319 – 3235
    Beta strandi326 – 3305
    Helixi332 – 3354
    Beta strandi336 – 3383
    Beta strandi343 – 3508
    Beta strandi360 – 3634
    Helixi365 – 3684
    Beta strandi371 – 3766
    Turni377 – 3804
    Beta strandi381 – 3877

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AVFX-ray2.36A/J60-388[»]
    P/Q17-42[»]
    1HTRX-ray1.62B60-388[»]
    P17-59[»]
    ProteinModelPortaliP20142.
    SMRiP20142. Positions 17-388.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20142.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase A1 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG248684.
    HOGENOMiHOG000197681.
    HOVERGENiHBG000482.
    InParanoidiP20142.
    KOiK01377.
    OMAiASGWCSE.
    OrthoDBiEOG7HQN88.
    PhylomeDBiP20142.
    TreeFamiTF314990.

    Family and domain databases

    Gene3Di2.40.70.10. 2 hits.
    InterProiIPR001461. Aspartic_peptidase.
    IPR001969. Aspartic_peptidase_AS.
    IPR012848. Aspartic_peptidase_N.
    IPR021109. Peptidase_aspartic_dom.
    [Graphical view]
    PANTHERiPTHR13683. PTHR13683. 1 hit.
    PfamiPF07966. A1_Propeptide. 1 hit.
    PF00026. Asp. 1 hit.
    [Graphical view]
    PRINTSiPR00792. PEPSIN.
    SUPFAMiSSF50630. SSF50630. 1 hit.
    PROSITEiPS00141. ASP_PROTEASE. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P20142-1) [UniParc]FASTAAdd to Basket

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

    « Hide

    MKWMVVVLVC LQLLEAAVVK VPLKKFKSIR ETMKEKGLLG EFLRTHKYDP    50
    AWKYRFGDLS VTYEPMAYMD AAYFGEISIG TPPQNFLVLF DTGSSNLWVP 100
    SVYCQSQACT SHSRFNPSES STYSTNGQTF SLQYGSGSLT GFFGYDTLTV 150
    QSIQVPNQEF GLSENEPGTN FVYAQFDGIM GLAYPALSVD EATTAMQGMV 200
    QEGALTSPVF SVYLSNQQGS SGGAVVFGGV DSSLYTGQIY WAPVTQELYW 250
    QIGIEEFLIG GQASGWCSEG CQAIVDTGTS LLTVPQQYMS ALLQATGAQE 300
    DEYGQFLVNC NSIQNLPSLT FIINGVEFPL PPSSYILSNN GYCTVGVEPT 350
    YLSSQNGQPL WILGDVFLRS YYSVYDLGNN RVGFATAA 388
    Length:388
    Mass (Da):42,426
    Last modified:February 1, 1991 - v1
    Checksum:iF862DFDC1438BB92
    GO
    Isoform 2 (identifier: P20142-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         217-388: QQGSSGGAVV...NNRVGFATAA → LVLESSGLGP...PPRSQHHSGA

    Show »
    Length:315
    Mass (Da):34,208
    Checksum:i79BD7C79ABDF8879
    GO

    Sequence cautioni

    The sequence AAA60062.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti40 – 412GE → ED AA sequence (PubMed:6816595)Curated
    Sequence conflicti52 – 521W → S AA sequence (PubMed:6816595)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei217 – 388172QQGSS…FATAA → LVLESSGLGPLLTPSRAAPP SSTLQLPEKPLEQTWNILTP FTKTLPVSNLSRKVTSWAGV GIPVTCLPEAGSGGERRAEC GLGVPTTRGPPRSQHHSGA in isoform 2. 1 PublicationVSP_042312Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M18667
    , M18659, M18660, M18661, M18662, M18663, M18664, M18665, M18666 Genomic DNA. Translation: AAA60062.1. Different initiation.
    J04443 mRNA. Translation: AAA60074.1.
    M23077
    , M23069, M23070, M23071, M23072, M23073, M23074, M23075 Genomic DNA. Translation: AAA60063.1.
    U75272 mRNA. Translation: AAB18273.1.
    AK301298 mRNA. Translation: BAG62855.1.
    AL365205 Genomic DNA. Translation: CAI13181.1.
    BC073740 mRNA. Translation: AAH73740.1.
    CCDSiCCDS4859.1. [P20142-1]
    CCDS55000.1. [P20142-2]
    PIRiA29937.
    RefSeqiNP_001159896.1. NM_001166424.1. [P20142-2]
    NP_002621.1. NM_002630.3. [P20142-1]
    UniGeneiHs.1867.

    Genome annotation databases

    EnsembliENST00000373025; ENSP00000362116; ENSG00000096088. [P20142-1]
    ENST00000425343; ENSP00000405094; ENSG00000096088. [P20142-2]
    GeneIDi5225.
    KEGGihsa:5225.
    UCSCiuc003ora.2. human. [P20142-1]
    uc021yzm.1. human. [P20142-2]

    Polymorphism databases

    DMDMi129796.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M18667
    , M18659 , M18660 , M18661 , M18662 , M18663 , M18664 , M18665 , M18666 Genomic DNA. Translation: AAA60062.1 . Different initiation.
    J04443 mRNA. Translation: AAA60074.1 .
    M23077
    , M23069 , M23070 , M23071 , M23072 , M23073 , M23074 , M23075 Genomic DNA. Translation: AAA60063.1 .
    U75272 mRNA. Translation: AAB18273.1 .
    AK301298 mRNA. Translation: BAG62855.1 .
    AL365205 Genomic DNA. Translation: CAI13181.1 .
    BC073740 mRNA. Translation: AAH73740.1 .
    CCDSi CCDS4859.1. [P20142-1 ]
    CCDS55000.1. [P20142-2 ]
    PIRi A29937.
    RefSeqi NP_001159896.1. NM_001166424.1. [P20142-2 ]
    NP_002621.1. NM_002630.3. [P20142-1 ]
    UniGenei Hs.1867.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AVF X-ray 2.36 A/J 60-388 [» ]
    P/Q 17-42 [» ]
    1HTR X-ray 1.62 B 60-388 [» ]
    P 17-59 [» ]
    ProteinModelPortali P20142.
    SMRi P20142. Positions 17-388.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111246. 4 interactions.
    STRINGi 9606.ENSP00000362116.

    Chemistry

    BindingDBi P20142.
    ChEMBLi CHEMBL2136.

    Protein family/group databases

    MEROPSi A01.003.

    PTM databases

    PhosphoSitei P20142.

    Polymorphism databases

    DMDMi 129796.

    Proteomic databases

    MaxQBi P20142.
    PaxDbi P20142.
    PRIDEi P20142.

    Protocols and materials databases

    DNASUi 5225.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373025 ; ENSP00000362116 ; ENSG00000096088 . [P20142-1 ]
    ENST00000425343 ; ENSP00000405094 ; ENSG00000096088 . [P20142-2 ]
    GeneIDi 5225.
    KEGGi hsa:5225.
    UCSCi uc003ora.2. human. [P20142-1 ]
    uc021yzm.1. human. [P20142-2 ]

    Organism-specific databases

    CTDi 5225.
    GeneCardsi GC06M041704.
    HGNCi HGNC:8890. PGC.
    HPAi HPA031717.
    HPA031718.
    MIMi 169740. gene.
    neXtProti NX_P20142.
    PharmGKBi PA33228.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG248684.
    HOGENOMi HOG000197681.
    HOVERGENi HBG000482.
    InParanoidi P20142.
    KOi K01377.
    OMAi ASGWCSE.
    OrthoDBi EOG7HQN88.
    PhylomeDBi P20142.
    TreeFami TF314990.

    Miscellaneous databases

    ChiTaRSi PGC. human.
    EvolutionaryTracei P20142.
    GeneWikii Gastricsin.
    GenomeRNAii 5225.
    NextBioi 20200.
    PMAP-CutDB P20142.
    PROi P20142.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P20142.
    Bgeei P20142.
    CleanExi HS_PGC.
    Genevestigatori P20142.

    Family and domain databases

    Gene3Di 2.40.70.10. 2 hits.
    InterProi IPR001461. Aspartic_peptidase.
    IPR001969. Aspartic_peptidase_AS.
    IPR012848. Aspartic_peptidase_N.
    IPR021109. Peptidase_aspartic_dom.
    [Graphical view ]
    PANTHERi PTHR13683. PTHR13683. 1 hit.
    Pfami PF07966. A1_Propeptide. 1 hit.
    PF00026. Asp. 1 hit.
    [Graphical view ]
    PRINTSi PR00792. PEPSIN.
    SUPFAMi SSF50630. SSF50630. 1 hit.
    PROSITEi PS00141. ASP_PROTEASE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of human pepsinogen C gene."
      Hayano T., Sogawa K., Ichihara Y., Fujii-Kuriyama Y., Takahashi K.
      J. Biol. Chem. 263:1382-1385(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Erratum
      Hayano T., Sogawa K., Ichihara Y., Fujii-Kuriyama Y., Takahashi K.
      J. Biol. Chem. 263:14592-14592(1988)
    3. "Human pepsinogen C (progastricsin). Isolation of cDNA clones, localization to chromosome 6, and sequence homology with pepsinogen A."
      Taggart R.T., Cass L.G., Mohandas T.K., Derby P., Barr P.J., Pals G., Bell G.I.
      J. Biol. Chem. 264:375-379(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Human pepsinogen C (progastricsin) polymorphism: evidence for a single locus located at 6p21.1-pter."
      Pals G., Azuma T., Mohandas T.K., Bell G.I., Bacon J., Samloff I.M., Walz D.A., Barr P.J., Taggart R.T.
      Genomics 4:137-148(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Placenta.
    5. "cDNA sequence of human gastricsin."
      Wong R.N.S., Tang J.
      Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    6. "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] (ISOFORM 2).
      Tissue: Stomach.
    7. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Liver.
    9. "A comparative study on the NH2-terminal amino acid sequences and some other properties of six isozymic forms of human pepsinogens and pepsins."
      Athauda S.B.P., Tanji M., Kageyama T., Takahashi K.
      J. Biochem. 106:920-927(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 17-101.
    10. "Human progastricsin. Analysis of intermediates during activation into gastricsin and determination of the amino acid sequence of the propart."
      Foltmann B., Jensen A.L.
      Eur. J. Biochem. 128:63-70(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 17-64.
    11. "Crystal and molecular structures of human progastricsin at 1.62-A resolution."
      Moore S.A., Sielecki A.R., Chernaia M.M., Tarasova N.I., James M.N.G.
      J. Mol. Biol. 247:466-485(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS).
    12. "Structural characterization of activation 'intermediate 2' on the pathway to human gastricsin."
      Khan A.R., Cherney M.M., Tarasova N.I., James M.N.
      Nat. Struct. Biol. 4:1010-1015(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS).

    Entry informationi

    Entry nameiPEPC_HUMAN
    AccessioniPrimary (citable) accession number: P20142
    Secondary accession number(s): B4DVZ3, Q5T3D7, Q5T3D8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 147 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Peptidase families
      Classification of peptidase families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3