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O43847

- NRDC_HUMAN

UniProt

O43847 - NRDC_HUMAN

Protein

Nardilysin

Gene

NRD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 2 (11 Apr 2003)
      Previous versions | rss
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    Functioni

    Cleaves peptide substrates on the N-terminus of arginine residues in dibasic pairs.

    Catalytic activityi

    Hydrolysis of polypeptides, preferably at -Xaa-|-Arg-Lys-, and less commonly at -Arg-|-Arg-Xaa-, in which Xaa is not Arg or Lys.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi232 – 2321ZincPROSITE-ProRule annotation
    Active sitei235 – 2351Proton acceptorPROSITE-ProRule annotation
    Metal bindingi236 – 2361ZincPROSITE-ProRule annotation
    Metal bindingi313 – 3131ZincPROSITE-ProRule annotation

    GO - Molecular functioni

    1. epidermal growth factor binding Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. metalloendopeptidase activity Source: UniProtKB
    4. protein binding Source: IntAct

    GO - Biological processi

    1. cell migration Source: UniProtKB
    2. cell proliferation Source: UniProtKB
    3. neuromuscular junction development Source: ProtInc
    4. positive regulation of membrane protein ectodomain proteolysis Source: BHF-UCL
    5. proteolysis Source: UniProtKB
    6. regulation of endopeptidase activity Source: BHF-UCL

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi3.4.24.61. 2681.
    SignaLinkiO43847.

    Protein family/group databases

    MEROPSiM16.005.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nardilysin (EC:3.4.24.61)
    Alternative name(s):
    N-arginine dibasic convertase
    Short name:
    NRD convertase
    Short name:
    NRD-C
    Gene namesi
    Name:NRD1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:7995. NRD1.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: UniProtKB
    2. cytosol Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31774.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 11501130NardilysinPRO_0000026755Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei86 – 861PhosphoserineBy similarity
    Modified residuei94 – 941Phosphoserine4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO43847.
    PaxDbiO43847.
    PRIDEiO43847.

    PTM databases

    PhosphoSiteiO43847.

    Expressioni

    Tissue specificityi

    Primarily in adult heart, skeletal muscle, and testis and at much lower levels in other tissues.

    Gene expression databases

    ArrayExpressiO43847.
    BgeeiO43847.
    CleanExiHS_NRD1.
    GenevestigatoriO43847.

    Organism-specific databases

    HPAiHPA023679.
    HPA053661.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TP53P046376EBI-2371631,EBI-366083

    Protein-protein interaction databases

    BioGridi110954. 38 interactions.
    IntActiO43847. 7 interactions.
    STRINGi9606.ENSP00000346890.

    Structurei

    3D structure databases

    ProteinModelPortaliO43847.
    SMRiO43847. Positions 206-1088.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi142 – 20059Asp/Glu-rich (highly acidic)Add
    BLAST
    Compositional biasi144 – 15310Poly-Glu

    Sequence similaritiesi

    Belongs to the peptidase M16 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1025.
    HOVERGENiHBG006530.
    KOiK01411.
    OrthoDBiEOG7HHWRD.
    PhylomeDBiO43847.

    Family and domain databases

    Gene3Di3.30.830.10. 5 hits.
    InterProiIPR011249. Metalloenz_LuxS/M16.
    IPR011237. Pept_M16_dom.
    IPR011765. Pept_M16_N.
    IPR001431. Pept_M16_Zn_BS.
    IPR007863. Peptidase_M16_C.
    [Graphical view]
    PfamiPF00675. Peptidase_M16. 1 hit.
    PF05193. Peptidase_M16_C. 2 hits.
    [Graphical view]
    SUPFAMiSSF63411. SSF63411. 5 hits.
    PROSITEiPS00143. INSULINASE. 1 hit.
    [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: O43847-1) [UniParc]FASTAAdd to Basket

    Also known as: NRD1

    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

    MLRRVTVAAV CATRRKLCEA GRELAALWGI ETRGRCEDSA AARPFPILAM     50
    PGRNKAKSTC SCPDLQPNGQ DLGENSRVAR LGADESEEEG RRGSLSNAGD 100
    PEIVKSPSDP KQYRYIKLQN GLQALLISDL SNMEGKTGNT TDDEEEEEVE 150
    EEEDDDEDSG AEIEDDDEEG FDDEDEFDDE HDDDLDTEDN ELEELEERAE 200
    ARKKTTEKQS AAALCVGVGS FADPDDLPGL AHFLEHMVFM GSLKYPDENG 250
    FDAFLKKHGG SDNASTDCER TVFQFDVQRK YFKEALDRWA QFFIHPLMIR 300
    DAIDREVEAV DSEYQLARPS DANRKEMLFG SLARPGHPMG KFFWGNAETL 350
    KHEPRKNNID THARLREFWM RYYSSHYMTL VVQSKETLDT LEKWVTEIFS 400
    QIPNNGLPRP NFGHLTDPFD TPAFNKLYRV VPIRKIHALT ITWALPPQQQ 450
    HYRVKPLHYI SWLVGHEGKG SILSFLRKKC WALALFGGNG ETGFEQNSTY 500
    SVFSISITLT DEGYEHFYEV AYTVFQYLKM LQKLGPEKRI FEEIRKIEDN 550
    EFHYQEQTDP VEYVENMCEN MQLYPLQDIL TGDQLLFEYK PEVIGEALNQ 600
    LVPQKANLVL LSGANEGKCD LKEKWFGTQY SIEDIENSWA ELWNSNFELN 650
    PDLHLPAENK YIATDFTLKA FDCPETEYPV KIVNTPQGCL WYKKDNKFKI 700
    PKAYIRFHLI SPLIQKSAAN VVLFDIFVNI LTHNLAEPAY EADVAQLEYK 750
    LVAGEHGLII RVKGFNHKLP LLFQLIIDYL AEFNSTPAVF TMITEQLKKT 800
    YFNILIKPET LAKDVRLLIL EYARWSMIDK YQALMDGLSL ESLLSFVKEF 850
    KSQLFVEGLV QGNVTSTESM DFLKYVVDKL NFKPLEQEMP VQFQVVELPS 900
    GHHLCKVKAL NKGDANSEVT VYYQSGTRSL REYTLMELLV MHMEEPCFDF 950
    LRTKQTLGYH VYPTCRNTSG ILGFSVTVGT QATKYNSEVV DKKIEEFLSS 1000
    FEEKIENLTE EAFNTQVTAL IKLKECEDTH LGEEVDRNWN EVVTQQYLFD 1050
    RLAHEIEALK SFSKSDLVNW FKAHRGPGSK MLSVHVVGYG KYELEEDGTP 1100
    SSEDSNSSCE VMQLTYLPTS PLLADCIIPI TDIRAFTTTL NLLPYHKIVK 1150
    Length:1,150
    Mass (Da):131,572
    Last modified:April 11, 2003 - v2
    Checksum:i3B46DADB898E038B
    GO
    Isoform 2 (identifier: O43847-2) [UniParc]FASTAAdd to Basket

    Also known as: NRD2

    The sequence of this isoform differs from the canonical sequence as follows:
         209-209: Q → QQLQSLFLLWSKLTDRLWFKSTYSKMSSTLLVETRNLYGVVGAESRSAPVQHLAGWQAEEQQGETDTVL

    Show »
    Length:1,218
    Mass (Da):139,284
    Checksum:i071971B4E83016AF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti23 – 242EL → DV in CAA63698. (PubMed:9581555)Curated
    Sequence conflicti23 – 242EL → DV in CAA63694. (PubMed:9581555)Curated
    Sequence conflicti526 – 5261Q → L in CAA63698. (PubMed:9581555)Curated
    Sequence conflicti526 – 5261Q → L in CAA63694. (PubMed:9581555)Curated
    Sequence conflicti640 – 6401A → G in AAC39597. (PubMed:9479496)Curated
    Sequence conflicti752 – 7521V → A in CAA63698. (PubMed:9581555)Curated
    Sequence conflicti752 – 7521V → A in CAA63694. (PubMed:9581555)Curated
    Sequence conflicti1086 – 10861V → A in AAC39597. (PubMed:9479496)Curated
    Sequence conflicti1099 – 10991T → S in CAA63698. (PubMed:9581555)Curated
    Sequence conflicti1099 – 10991T → S in CAA63694. (PubMed:9581555)Curated
    Sequence conflicti1125 – 115026DCIIP…HKIVK → SVSSPLLISGLSQQHSTFSP TIK(PubMed:9479496)CuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti153 – 1531E → EE.3 Publications
    VAR_021221
    Natural varianti831 – 8311Y → S.
    Corresponds to variant rs34957144 [ dbSNP | Ensembl ].
    VAR_057058

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei209 – 2091Q → QQLQSLFLLWSKLTDRLWFK STYSKMSSTLLVETRNLYGV VGAESRSAPVQHLAGWQAEE QQGETDTVL in isoform 2. 1 PublicationVSP_007114

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U64898 mRNA. Translation: AAC39597.1.
    X93209 mRNA. Translation: CAA63698.1.
    X93207 mRNA. Translation: CAA63694.1.
    AL589663, AL050343 Genomic DNA. Translation: CAH74100.1.
    AL050343, AL589663 Genomic DNA. Translation: CAI22216.1.
    CH471059 Genomic DNA. Translation: EAX06809.1.
    BC008775 mRNA. Translation: AAH08775.1.
    AJ000350 Genomic DNA. Translation: CAA04025.1.
    RefSeqiNP_001095132.1. NM_001101662.1.
    NP_001229290.1. NM_001242361.1.
    NP_002516.2. NM_002525.2.
    UniGeneiHs.584782.

    Genome annotation databases

    EnsembliENST00000352171; ENSP00000262679; ENSG00000078618.
    GeneIDi4898.
    KEGGihsa:4898.
    UCSCiuc009vzb.3. human. [O43847-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U64898 mRNA. Translation: AAC39597.1 .
    X93209 mRNA. Translation: CAA63698.1 .
    X93207 mRNA. Translation: CAA63694.1 .
    AL589663 , AL050343 Genomic DNA. Translation: CAH74100.1 .
    AL050343 , AL589663 Genomic DNA. Translation: CAI22216.1 .
    CH471059 Genomic DNA. Translation: EAX06809.1 .
    BC008775 mRNA. Translation: AAH08775.1 .
    AJ000350 Genomic DNA. Translation: CAA04025.1 .
    RefSeqi NP_001095132.1. NM_001101662.1.
    NP_001229290.1. NM_001242361.1.
    NP_002516.2. NM_002525.2.
    UniGenei Hs.584782.

    3D structure databases

    ProteinModelPortali O43847.
    SMRi O43847. Positions 206-1088.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110954. 38 interactions.
    IntActi O43847. 7 interactions.
    STRINGi 9606.ENSP00000346890.

    Protein family/group databases

    MEROPSi M16.005.

    PTM databases

    PhosphoSitei O43847.

    Proteomic databases

    MaxQBi O43847.
    PaxDbi O43847.
    PRIDEi O43847.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000352171 ; ENSP00000262679 ; ENSG00000078618 .
    GeneIDi 4898.
    KEGGi hsa:4898.
    UCSCi uc009vzb.3. human. [O43847-1 ]

    Organism-specific databases

    CTDi 4898.
    GeneCardsi GC01M052254.
    H-InvDB HIX0000576.
    HGNCi HGNC:7995. NRD1.
    HPAi HPA023679.
    HPA053661.
    MIMi 602651. gene.
    neXtProti NX_O43847.
    PharmGKBi PA31774.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1025.
    HOVERGENi HBG006530.
    KOi K01411.
    OrthoDBi EOG7HHWRD.
    PhylomeDBi O43847.

    Enzyme and pathway databases

    BRENDAi 3.4.24.61. 2681.
    SignaLinki O43847.

    Miscellaneous databases

    ChiTaRSi NRD1. human.
    GeneWikii NRD1.
    GenomeRNAii 4898.
    NextBioi 18847.
    PROi O43847.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43847.
    Bgeei O43847.
    CleanExi HS_NRD1.
    Genevestigatori O43847.

    Family and domain databases

    Gene3Di 3.30.830.10. 5 hits.
    InterProi IPR011249. Metalloenz_LuxS/M16.
    IPR011237. Pept_M16_dom.
    IPR011765. Pept_M16_N.
    IPR001431. Pept_M16_Zn_BS.
    IPR007863. Peptidase_M16_C.
    [Graphical view ]
    Pfami PF00675. Peptidase_M16. 1 hit.
    PF05193. Peptidase_M16_C. 2 hits.
    [Graphical view ]
    SUPFAMi SSF63411. SSF63411. 5 hits.
    PROSITEi PS00143. INSULINASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human NRD convertase: a highly conserved metalloendopeptidase expressed at specific sites during development and in adult tissues."
      Fumagalli P., Accarino M., Egeo A., Scartezzini P., Rappazzo G., Pizzuti A., Avvantaggiato V., Simeone A., Arrigo G., Zuffardi O., Ottolenghi S., Taramelli R.
      Genomics 47:238-245(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Heart.
    2. "Human and rat testis express two mRNA species encoding variants of NRD convertase, a metalloendopeptidase of the insulinase family."
      Hospital V., Prat A., Joulie C., Cherif D., Day R., Cohen P.
      Biochem. J. 327:773-779(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT GLU-153 INS.
      Tissue: Testis.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-153 INS.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-153 INS.
    5. "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: Placenta.
    6. "Gene expression of the dibasic-pair cleaving enzyme NRD convertase (N-arginine dibasic convertase) is differentially regulated in the GH3 pituitary and Mat-Lu prostate cell lines."
      Winter A.G., Pierotti A.R.
      Biochem. J. 351:755-764(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-107.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiNRDC_HUMAN
    AccessioniPrimary (citable) accession number: O43847
    Secondary accession number(s): A6NI41
    , O15241, O15242, Q5VUL0, Q96HB2, Q9NU57
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: April 11, 2003
    Last modified: October 1, 2014
    This is version 128 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3