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P14384

- CBPM_HUMAN

UniProt

P14384 - CBPM_HUMAN

Protein

Carboxypeptidase M

Gene

CPM

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 2 (11 Jul 2001)
      Previous versions | rss
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    Functioni

    Specifically removes C-terminal basic residues (Arg or Lys) from peptides and proteins. It is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins.1 Publication

    Catalytic activityi

    Cleavage of C-terminal arginine or lysine residues from polypeptides.

    Cofactori

    Binds 1 zinc ion per subunit.

    Enzyme regulationi

    Inhibited by O-phenanthroline and MGTA and activated by cobalt.

    Kineticsi

    1. KM=59 µM for synthetic dansyl-Ala-Arg1 Publication
    2. KM=57 µM for placental peptide hormones1 Publication

    pH dependencei

    Optimum pH is 7.0.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi83 – 831Zinc
    Metal bindingi86 – 861Zinc
    Metal bindingi190 – 1901Zinc
    Sitei277 – 2771Probable structural role
    Active sitei281 – 2811Nucleophile

    GO - Molecular functioni

    1. carboxypeptidase activity Source: ProtInc
    2. metallocarboxypeptidase activity Source: ProtInc
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. anatomical structure morphogenesis Source: ProtInc

    Keywords - Molecular functioni

    Carboxypeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    SABIO-RKP14384.

    Protein family/group databases

    MEROPSiM14.006.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carboxypeptidase M (EC:3.4.17.12)
    Short name:
    CPM
    Gene namesi
    Name:CPM
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:2311. CPM.

    Subcellular locationi

    Cell membrane 1 Publication; Lipid-anchorGPI-anchor 1 Publication

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. extracellular vesicular exosome Source: UniProt
    3. plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi277 – 2771E → A: 5-fold decrease in substrate affinity. 22-fold decrease in specific affinity. 104-fold decrease in catalytic efficiency. Greatly reduced heat stability. 1 Publication
    Mutagenesisi277 – 2771E → Q: 2-fold decrease in substrate affinity. Small increase in specific affinity. Reduced heat stability by 50%. 1 Publication
    Mutagenesisi281 – 2811E → Q: Abolishes enzyme activity. 1 Publication
    Mutagenesisi423 – 4231S → A or T: Expressed on cell membrane. Released from membrane by PI-PLC. 1 Publication
    Mutagenesisi423 – 4231S → P: Little expression on cell membrane. Perinuclear localization. Not released from membrane by PI-PLC. 1 Publication

    Organism-specific databases

    PharmGKBiPA26828.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 17172 PublicationsAdd
    BLAST
    Chaini18 – 423406Carboxypeptidase MPRO_0000004391Add
    BLAST
    Propeptidei424 – 44320Removed in mature formCuratedPRO_0000251910Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi38 – 381N-linked (GlcNAc...)1 Publication
    Glycosylationi115 – 1151N-linked (GlcNAc...)2 Publications
    Disulfide bondi138 ↔ 2851 Publication
    Glycosylationi164 – 1641N-linked (GlcNAc...)1 Publication
    Disulfide bondi242 ↔ 2841 Publication
    Disulfide bondi341 ↔ 4101 Publication
    Glycosylationi363 – 3631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi384 – 3841N-linked (GlcNAc...)Sequence Analysis
    Lipidationi423 – 4231GPI-anchor amidated serine1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    MaxQBiP14384.
    PaxDbiP14384.
    PRIDEiP14384.

    PTM databases

    PhosphoSiteiP14384.

    Expressioni

    Gene expression databases

    ArrayExpressiP14384.
    BgeeiP14384.
    CleanExiHS_CPM.
    GenevestigatoriP14384.

    Organism-specific databases

    HPAiHPA002657.

    Interactioni

    Protein-protein interaction databases

    BioGridi107760. 2 interactions.
    IntActiP14384. 3 interactions.
    STRINGi9606.ENSP00000339157.

    Structurei

    Secondary structure

    1
    443
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi25 – 3814
    Turni39 – 413
    Beta strandi42 – 509
    Beta strandi56 – 6510
    Beta strandi75 – 806
    Helixi88 – 10316
    Turni104 – 1063
    Helixi108 – 1169
    Beta strandi118 – 1236
    Helixi127 – 1326
    Beta strandi159 – 1613
    Helixi169 – 18012
    Beta strandi183 – 1853
    Beta strandi188 – 1903
    Beta strandi192 – 1998
    Helixi205 – 2073
    Helixi209 – 2113
    Helixi219 – 23113
    Turni234 – 2385
    Beta strandi243 – 2453
    Beta strandi252 – 2554
    Turni256 – 2583
    Helixi265 – 2717
    Beta strandi279 – 2879
    Helixi290 – 2923
    Helixi293 – 2986
    Helixi301 – 3088
    Helixi309 – 3124
    Beta strandi314 – 3207
    Beta strandi331 – 3344
    Beta strandi350 – 3534
    Beta strandi357 – 3659
    Beta strandi367 – 3693
    Beta strandi372 – 3787
    Beta strandi383 – 3864
    Turni415 – 4184

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UWYX-ray3.00A18-443[»]
    ProteinModelPortaliP14384.
    SMRiP14384. Positions 18-419.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14384.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M14 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2866.
    HOGENOMiHOG000232185.
    HOVERGENiHBG003410.
    InParanoidiP14384.
    KOiK01296.
    OMAiITNGYSW.
    PhylomeDBiP14384.
    TreeFamiTF315592.

    Family and domain databases

    Gene3Di2.60.40.1120. 1 hit.
    InterProiIPR008969. CarboxyPept-like_regulatory.
    IPR014766. CarboxyPept_regulatory_dom.
    IPR027062. CPM.
    IPR000834. Peptidase_M14.
    [Graphical view]
    PANTHERiPTHR11532:SF53. PTHR11532:SF53. 1 hit.
    PfamiPF00246. Peptidase_M14. 1 hit.
    [Graphical view]
    PRINTSiPR00765. CRBOXYPTASEA.
    SMARTiSM00631. Zn_pept. 1 hit.
    [Graphical view]
    SUPFAMiSSF49464. SSF49464. 1 hit.
    PROSITEiPS00132. CARBOXYPEPT_ZN_1. 1 hit.
    PS00133. CARBOXYPEPT_ZN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P14384-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDFPCLWLGL LLPLVAALDF NYHRQEGMEA FLKTVAQNYS SVTHLHSIGK    50
    SVKGRNLWVL VVGRFPKEHR IGIPEFKYVA NMHGDETVGR ELLLHLIDYL 100
    VTSDGKDPEI TNLINSTRIH IMPSMNPDGF EAVKKPDCYY SIGRENYNQY 150
    DLNRNFPDAF EYNNVSRQPE TVAVMKWLKT ETFVLSANLH GGALVASYPF 200
    DNGVQATGAL YSRSLTPDDD VFQYLAHTYA SRNPNMKKGD ECKNKMNFPN 250
    GVTNGYSWYP LQGGMQDYNY IWAQCFEITL ELSCCKYPRE EKLPSFWNNN 300
    KASLIEYIKQ VHLGVKGQVF DQNGNPLPNV IVEVQDRKHI CPYRTNKYGE 350
    YYLLLLPGSY IINVTVPGHD PHITKVIIPE KSQNFSALKK DILLPFQGQL 400
    DSIPVSNPSC PMIPLYRNLP DHSAATKPSL FLFLVSLLHI FFK 443
    Length:443
    Mass (Da):50,514
    Last modified:July 11, 2001 - v2
    Checksum:i98EB0C94E201B901
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti24 – 241R → H.
    Corresponds to variant rs7978197 [ dbSNP | Ensembl ].
    VAR_048600
    Natural varianti133 – 1331V → I.
    Corresponds to variant rs7309831 [ dbSNP | Ensembl ].
    VAR_048601

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04970 mRNA. Translation: AAA35651.2.
    AF262947
    , AF262940, AF262941, AF262942, AF262943, AF262944, AF262945, AF262946 Genomic DNA. Translation: AAG47641.1.
    AF368463 mRNA. Translation: AAK69717.1.
    AK313180 mRNA. Translation: BAG35997.1.
    BC022276 mRNA. Translation: AAH22276.1.
    CCDSiCCDS8987.1.
    PIRiA32619.
    RefSeqiNP_001005502.1. NM_001005502.2.
    NP_001865.1. NM_001874.4.
    NP_938079.1. NM_198320.3.
    UniGeneiHs.654387.

    Genome annotation databases

    EnsembliENST00000338356; ENSP00000339157; ENSG00000135678.
    ENST00000546373; ENSP00000447255; ENSG00000135678.
    ENST00000551568; ENSP00000448517; ENSG00000135678.
    GeneIDi1368.
    KEGGihsa:1368.
    UCSCiuc001sup.3. human.

    Polymorphism databases

    DMDMi14916957.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04970 mRNA. Translation: AAA35651.2 .
    AF262947
    , AF262940 , AF262941 , AF262942 , AF262943 , AF262944 , AF262945 , AF262946 Genomic DNA. Translation: AAG47641.1 .
    AF368463 mRNA. Translation: AAK69717.1 .
    AK313180 mRNA. Translation: BAG35997.1 .
    BC022276 mRNA. Translation: AAH22276.1 .
    CCDSi CCDS8987.1.
    PIRi A32619.
    RefSeqi NP_001005502.1. NM_001005502.2.
    NP_001865.1. NM_001874.4.
    NP_938079.1. NM_198320.3.
    UniGenei Hs.654387.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UWY X-ray 3.00 A 18-443 [» ]
    ProteinModelPortali P14384.
    SMRi P14384. Positions 18-419.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107760. 2 interactions.
    IntActi P14384. 3 interactions.
    STRINGi 9606.ENSP00000339157.

    Chemistry

    BindingDBi P14384.
    ChEMBLi CHEMBL3038.

    Protein family/group databases

    MEROPSi M14.006.

    PTM databases

    PhosphoSitei P14384.

    Polymorphism databases

    DMDMi 14916957.

    Proteomic databases

    MaxQBi P14384.
    PaxDbi P14384.
    PRIDEi P14384.

    Protocols and materials databases

    DNASUi 1368.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000338356 ; ENSP00000339157 ; ENSG00000135678 .
    ENST00000546373 ; ENSP00000447255 ; ENSG00000135678 .
    ENST00000551568 ; ENSP00000448517 ; ENSG00000135678 .
    GeneIDi 1368.
    KEGGi hsa:1368.
    UCSCi uc001sup.3. human.

    Organism-specific databases

    CTDi 1368.
    GeneCardsi GC12M069244.
    HGNCi HGNC:2311. CPM.
    HPAi HPA002657.
    MIMi 114860. gene.
    neXtProti NX_P14384.
    PharmGKBi PA26828.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2866.
    HOGENOMi HOG000232185.
    HOVERGENi HBG003410.
    InParanoidi P14384.
    KOi K01296.
    OMAi ITNGYSW.
    PhylomeDBi P14384.
    TreeFami TF315592.

    Enzyme and pathway databases

    SABIO-RK P14384.

    Miscellaneous databases

    ChiTaRSi CPM. human.
    EvolutionaryTracei P14384.
    GeneWikii CPM_(gene).
    GenomeRNAii 1368.
    NextBioi 5541.
    PROi P14384.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P14384.
    Bgeei P14384.
    CleanExi HS_CPM.
    Genevestigatori P14384.

    Family and domain databases

    Gene3Di 2.60.40.1120. 1 hit.
    InterProi IPR008969. CarboxyPept-like_regulatory.
    IPR014766. CarboxyPept_regulatory_dom.
    IPR027062. CPM.
    IPR000834. Peptidase_M14.
    [Graphical view ]
    PANTHERi PTHR11532:SF53. PTHR11532:SF53. 1 hit.
    Pfami PF00246. Peptidase_M14. 1 hit.
    [Graphical view ]
    PRINTSi PR00765. CRBOXYPTASEA.
    SMARTi SM00631. Zn_pept. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49464. SSF49464. 1 hit.
    PROSITEi PS00132. CARBOXYPEPT_ZN_1. 1 hit.
    PS00133. CARBOXYPEPT_ZN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and sequencing of the cDNA for human membrane-bound carboxypeptidase M. Comparison with carboxypeptidases A, B, H, and N."
      Tan F., Chan S.J., Steiner D.F., Schilling J.W., Skidgel R.A.
      J. Biol. Chem. 264:13165-13170(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-48.
      Tissue: Placenta.
    2. Skidgel R.A.
      Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Type 2 diabetes locus on 12q15: further mapping and mutation screening of two candidate genes."
      Bektas A., Hughes J.N., Warram J.H., Krolewski A.S., Doria A.
      Diabetes 50:204-208(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Molecular structure and alternative splicing of the human carboxypeptidase M gene."
      Pessoa L.G., Guerreiro da S.I., Baptista H.A., Pesquero J.L., Paiva A.C.M., Bader M., Pesquero J.B.
      Biol. Chem. 383:263-269(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "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: Lung.
    6. "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].
      Tissue: Placenta.
    7. "Effect of mutation of two critical glutamic acid residues on the activity and stability of human carboxypeptidase M and characterization of its signal for glycosylphosphatidylinositol anchoring."
      Tan F., Balsitis S., Black J.K., Bloechl A., Mao J.-F., Becker R.P., Schacht D., Skidgel R.A.
      Biochem. J. 370:567-578(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 18-21, GPI-ANCHOR AT SER-423, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF GLU-277; GLU-281 AND SER-423.
    8. "Proteomic analysis of glycosylphosphatidylinositol-anchored membrane proteins."
      Elortza F., Nuehse T.S., Foster L.J., Stensballe A., Peck S.C., Jensen O.N.
      Mol. Cell. Proteomics 2:1261-1270(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment."
      Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S., Brodbeck U., Peck S.C., Jensen O.N.
      J. Proteome Res. 5:935-943(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-115 AND ASN-164.
      Tissue: Liver.
    11. "Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity."
      Reverter D., Maskos K., Tan F., Skidgel R.A., Bode W.
      J. Mol. Biol. 338:257-269(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 18-443, DISULFIDE BONDS, GLYCOSYLATION AT ASN-38 AND ASN-115.

    Entry informationi

    Entry nameiCBPM_HUMAN
    AccessioniPrimary (citable) accession number: P14384
    Secondary accession number(s): B2R800, Q9H2K9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: July 11, 2001
    Last modified: October 1, 2014
    This is version 150 of the entry and version 2 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 12
      Human chromosome 12: 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