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Protein

Carboxypeptidase M

Gene

CPM

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Zn2+Note: 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

    • carboxypeptidase activity Source: ProtInc
    • metallocarboxypeptidase activity Source: ProtInc
    • zinc ion binding Source: InterPro

    GO - Biological processi

    • anatomical structure morphogenesis Source: ProtInc
    Complete GO annotation...

    Keywords - Molecular functioni

    Carboxypeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi3.4.17.12. 2681.
    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 Componenti: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:2311. CPM.

    Subcellular locationi

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

    GO - Cellular componenti

    • anchored component of membrane Source: UniProtKB-KW
    • cell surface Source: UniProtKB
    • extracellular exosome Source: UniProtKB
    • plasma membrane Source: ProtInc
    Complete GO annotation...

    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.

    Polymorphism and mutation databases

    BioMutaiCPM.
    DMDMi14916957.

    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

    BgeeiP14384.
    CleanExiHS_CPM.
    ExpressionAtlasiP14384. baseline and differential.
    GenevisibleiP14384. HS.

    Organism-specific databases

    HPAiHPA002657.

    Interactioni

    Protein-protein interaction databases

    BioGridi107760. 6 interactions.
    IntActiP14384. 3 interactions.
    STRINGi9606.ENSP00000339157.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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.
    GeneTreeiENSGT00760000119124.
    HOGENOMiHOG000232185.
    HOVERGENiHBG003410.
    InParanoidiP14384.
    KOiK01296.
    OMAiFYSNGRE.
    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

            10         20         30         40         50
    MDFPCLWLGL LLPLVAALDF NYHRQEGMEA FLKTVAQNYS SVTHLHSIGK
    60 70 80 90 100
    SVKGRNLWVL VVGRFPKEHR IGIPEFKYVA NMHGDETVGR ELLLHLIDYL
    110 120 130 140 150
    VTSDGKDPEI TNLINSTRIH IMPSMNPDGF EAVKKPDCYY SIGRENYNQY
    160 170 180 190 200
    DLNRNFPDAF EYNNVSRQPE TVAVMKWLKT ETFVLSANLH GGALVASYPF
    210 220 230 240 250
    DNGVQATGAL YSRSLTPDDD VFQYLAHTYA SRNPNMKKGD ECKNKMNFPN
    260 270 280 290 300
    GVTNGYSWYP LQGGMQDYNY IWAQCFEITL ELSCCKYPRE EKLPSFWNNN
    310 320 330 340 350
    KASLIEYIKQ VHLGVKGQVF DQNGNPLPNV IVEVQDRKHI CPYRTNKYGE
    360 370 380 390 400
    YYLLLLPGSY IINVTVPGHD PHITKVIIPE KSQNFSALKK DILLPFQGQL
    410 420 430 440
    DSIPVSNPSC PMIPLYRNLP DHSAATKPSL FLFLVSLLHI FFK
    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:
    EMBLi
    GenBanki
    DDBJi
    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.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

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

    Protein-protein interaction databases

    BioGridi107760. 6 interactions.
    IntActiP14384. 3 interactions.
    STRINGi9606.ENSP00000339157.

    Chemistry

    BindingDBiP14384.
    ChEMBLiCHEMBL3038.

    Protein family/group databases

    MEROPSiM14.006.

    PTM databases

    PhosphoSiteiP14384.

    Polymorphism and mutation databases

    BioMutaiCPM.
    DMDMi14916957.

    Proteomic databases

    MaxQBiP14384.
    PaxDbiP14384.
    PRIDEiP14384.

    Protocols and materials databases

    DNASUi1368.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CTDi1368.
    GeneCardsiGC12M069244.
    HGNCiHGNC:2311. CPM.
    HPAiHPA002657.
    MIMi114860. gene.
    neXtProtiNX_P14384.
    PharmGKBiPA26828.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG2866.
    GeneTreeiENSGT00760000119124.
    HOGENOMiHOG000232185.
    HOVERGENiHBG003410.
    InParanoidiP14384.
    KOiK01296.
    OMAiFYSNGRE.
    PhylomeDBiP14384.
    TreeFamiTF315592.

    Enzyme and pathway databases

    BRENDAi3.4.17.12. 2681.
    SABIO-RKP14384.

    Miscellaneous databases

    ChiTaRSiCPM. human.
    EvolutionaryTraceiP14384.
    GeneWikiiCPM_(gene).
    GenomeRNAii1368.
    NextBioi5541.
    PROiP14384.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP14384.
    CleanExiHS_CPM.
    ExpressionAtlasiP14384. baseline and differential.
    GenevisibleiP14384. HS.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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: July 22, 2015
    This is version 158 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.