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P01833

- PIGR_HUMAN

UniProt

P01833 - PIGR_HUMAN

Protein

Polymeric immunoglobulin receptor

Gene

PIGR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 4 (26 Jun 2007)
      Previous versions | rss
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    Functioni

    This receptor binds polymeric IgA and IgM at the basolateral surface of epithelial cells. The complex is then transported across the cell to be secreted at the apical surface. During this process a cleavage occurs that separates the extracellular (known as the secretory component) from the transmembrane segment.

    GO - Molecular functioni

    1. polymeric immunoglobulin receptor activity Source: UniProt

    GO - Biological processi

    1. detection of chemical stimulus involved in sensory perception of bitter taste Source: UniProt
    2. epidermal growth factor receptor signaling pathway Source: UniProt
    3. Fc receptor signaling pathway Source: UniProt
    4. immunoglobulin transcytosis in epithelial cells mediated by polymeric immunoglobulin receptor Source: UniProt
    5. receptor clustering Source: UniProt
    6. retina homeostasis Source: UniProt

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polymeric immunoglobulin receptor
    Short name:
    PIgR
    Short name:
    Poly-Ig receptor
    Alternative name(s):
    Hepatocellular carcinoma-associated protein TB6
    Cleaved into the following chain:
    Gene namesi
    Name:PIGR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:8968. PIGR.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: UniProt
    2. extracellular vesicular exosome Source: UniProt
    3. integral component of plasma membrane Source: ProtInc
    4. plasma membrane Source: UniProt
    5. receptor complex Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33300.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 18182 PublicationsAdd
    BLAST
    Chaini19 – 764746Polymeric immunoglobulin receptorPRO_0000014900Add
    BLAST
    Chaini19 – 603585Secretory componentPRO_0000014901Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi40 ↔ 1101 PublicationPROSITE-ProRule annotation
    Disulfide bondi56 ↔ 641 PublicationPROSITE-ProRule annotation
    Glycosylationi83 – 831N-linked (GlcNAc...)4 Publications
    Glycosylationi90 – 901N-linked (GlcNAc...)5 Publications
    Glycosylationi135 – 1351N-linked (GlcNAc...)2 Publications
    Disulfide bondi152 ↔ 2201 PublicationPROSITE-ProRule annotation
    Glycosylationi186 – 1861N-linked (GlcNAc...)3 Publications
    Disulfide bondi257 ↔ 3251 PublicationPROSITE-ProRule annotation
    Disulfide bondi271 ↔ 2791 PublicationPROSITE-ProRule annotation
    Disulfide bondi371 ↔ 4411 PublicationPROSITE-ProRule annotation
    Disulfide bondi385 ↔ 3951 PublicationPROSITE-ProRule annotation
    Glycosylationi421 – 4211N-linked (GlcNAc...)6 Publications
    Glycosylationi469 – 4691N-linked (GlcNAc...) (complex)7 Publications
    Disulfide bondi482 ↔ 5441 PublicationPROSITE-ProRule annotation
    Disulfide bondi486 ↔ 5201 PublicationPROSITE-ProRule annotation
    Disulfide bondi496 ↔ 5031 PublicationPROSITE-ProRule annotation
    Glycosylationi499 – 4991N-linked (GlcNAc...)3 Publications
    Modified residuei682 – 6821PhosphoserineBy similarity
    Modified residuei735 – 7351PhosphoserineBy similarity

    Post-translational modificationi

    N-glycosylation is not necessary for Ig binding.7 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP01833.
    PeptideAtlasiP01833.
    PRIDEiP01833.

    PTM databases

    PhosphoSiteiP01833.
    UniCarbKBiP01833.

    Expressioni

    Gene expression databases

    BgeeiP01833.
    CleanExiHS_PIGR.
    GenevestigatoriP01833.

    Organism-specific databases

    HPAiCAB009454.
    HPA006154.
    HPA012012.

    Interactioni

    Protein-protein interaction databases

    BioGridi111302. 8 interactions.
    IntActiP01833. 4 interactions.
    STRINGi9606.ENSP00000348888.

    Structurei

    Secondary structure

    1
    764
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi26 – 316
    Beta strandi36 – 416
    Helixi46 – 505
    Beta strandi53 – 575
    Beta strandi65 – 728
    Turni76 – 816
    Beta strandi82 – 876
    Turni88 – 914
    Beta strandi92 – 976
    Helixi102 – 1043
    Beta strandi106 – 1138
    Helixi115 – 1173
    Beta strandi120 – 1278

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XEDX-ray1.90A/B/C/D/E/F19-127[»]
    2OCWX-ray-A19-603[»]
    3CHNOther1.00J353-458[»]
    S19-603[»]
    3CM9Other1.00J353-458[»]
    S19-603[»]
    ProteinModelPortaliP01833.
    SMRiP01833. Positions 20-241, 247-327, 356-441.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01833.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini19 – 638620ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini662 – 764103CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei639 – 66123HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini19 – 120102Ig-like V-type 1Add
    BLAST
    Domaini145 – 23793Ig-like V-type 2Add
    BLAST
    Domaini250 – 352103Ig-like V-type 3Add
    BLAST
    Domaini364 – 45895Ig-like V-type 4Add
    BLAST
    Domaini462 – 561100Ig-like V-type 5Add
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG46873.
    HOGENOMiHOG000115545.
    HOVERGENiHBG008199.
    InParanoidiP01833.
    KOiK13073.
    OMAiYWCGVKQ.
    OrthoDBiEOG7PCJG8.
    PhylomeDBiP01833.
    TreeFamiTF334441.

    Family and domain databases

    Gene3Di2.60.40.10. 5 hits.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR013106. Ig_V-set.
    [Graphical view]
    PfamiPF07686. V-set. 5 hits.
    [Graphical view]
    SMARTiSM00409. IG. 5 hits.
    [Graphical view]
    PROSITEiPS50835. IG_LIKE. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P01833-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLLFVLTCLL AVFPAISTKS PIFGPEEVNS VEGNSVSITC YYPPTSVNRH    50
    TRKYWCRQGA RGGCITLISS EGYVSSKYAG RANLTNFPEN GTFVVNIAQL 100
    SQDDSGRYKC GLGINSRGLS FDVSLEVSQG PGLLNDTKVY TVDLGRTVTI 150
    NCPFKTENAQ KRKSLYKQIG LYPVLVIDSS GYVNPNYTGR IRLDIQGTGQ 200
    LLFSVVINQL RLSDAGQYLC QAGDDSNSNK KNADLQVLKP EPELVYEDLR 250
    GSVTFHCALG PEVANVAKFL CRQSSGENCD VVVNTLGKRA PAFEGRILLN 300
    PQDKDGSFSV VITGLRKEDA GRYLCGAHSD GQLQEGSPIQ AWQLFVNEES 350
    TIPRSPTVVK GVAGGSVAVL CPYNRKESKS IKYWCLWEGA QNGRCPLLVD 400
    SEGWVKAQYE GRLSLLEEPG NGTFTVILNQ LTSRDAGFYW CLTNGDTLWR 450
    TTVEIKIIEG EPNLKVPGNV TAVLGETLKV PCHFPCKFSS YEKYWCKWNN 500
    TGCQALPSQD EGPSKAFVNC DENSRLVSLT LNLVTRADEG WYWCGVKQGH 550
    FYGETAAVYV AVEERKAAGS RDVSLAKADA APDEKVLDSG FREIENKAIQ 600
    DPRLFAEEKA VADTRDQADG SRASVDSGSS EEQGGSSRAL VSTLVPLGLV 650
    LAVGAVAVGV ARARHRKNVD RVSIRSYRTD ISMSDFENSR EFGANDNMGA 700
    SSITQETSLG GKEEFVATTE STTETKEPKK AKRSSKEEAE MAYKDFLLQS 750
    STVAAEAQDG PQEA 764
    Length:764
    Mass (Da):83,284
    Last modified:June 26, 2007 - v4
    Checksum:i927461F4EB3B05C7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti136 – 1361D → Q AA sequence (PubMed:6526384)Curated
    Sequence conflicti136 – 1361D → Q AA sequence (PubMed:1859628)Curated
    Sequence conflicti158 – 1581N → D AA sequence (PubMed:6526384)Curated
    Sequence conflicti158 – 1581N → D AA sequence (PubMed:1859628)Curated
    Sequence conflicti208 – 2092NQ → DE AA sequence (PubMed:6526384)Curated
    Sequence conflicti208 – 2092NQ → DE AA sequence (PubMed:1859628)Curated
    Sequence conflicti229 – 2291Missing AA sequence (PubMed:6526384)Curated
    Sequence conflicti229 – 2291Missing AA sequence (PubMed:1859628)Curated
    Sequence conflicti234 – 2341D → N AA sequence (PubMed:6526384)Curated
    Sequence conflicti234 – 2341D → N AA sequence (PubMed:1859628)Curated
    Sequence conflicti241 – 2411E → Q AA sequence (PubMed:6526384)Curated
    Sequence conflicti241 – 2411E → Q AA sequence (PubMed:1859628)Curated
    Sequence conflicti262 – 2621E → Q AA sequence (PubMed:6526384)Curated
    Sequence conflicti262 – 2621E → Q AA sequence (PubMed:1859628)Curated
    Sequence conflicti280 – 2801D → N AA sequence (PubMed:6526384)Curated
    Sequence conflicti280 – 2801D → N AA sequence (PubMed:1859628)Curated
    Sequence conflicti392 – 3921N → D AA sequence (PubMed:6526384)Curated
    Sequence conflicti392 – 3921N → D AA sequence (PubMed:1859628)Curated
    Sequence conflicti500 – 5001N → D AA sequence (PubMed:6526384)Curated
    Sequence conflicti500 – 5001N → D AA sequence (PubMed:1859628)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti365 – 3651G → S.6 Publications
    Corresponds to variant rs2275531 [ dbSNP | Ensembl ].
    VAR_025283
    Natural varianti555 – 5551T → I.
    Corresponds to variant rs7542760 [ dbSNP | Ensembl ].
    VAR_032822
    Natural varianti580 – 5801A → V.
    Corresponds to variant rs291102 [ dbSNP | Ensembl ].
    VAR_003920

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S62403 mRNA. Translation: AAB20203.1.
    S43449
    , S43437, S43441, S43442, S43443, S43444, S43445, S43446, S43447, S43448 Genomic DNA. Translation: AAB23176.1.
    AF272149 mRNA. Translation: AAN65630.1.
    CR749533 mRNA. Translation: CAH18339.1.
    M24559 mRNA. Translation: AAA36102.1.
    CCDSiCCDS1474.1.
    PIRiA46537. QRHUGS.
    RefSeqiNP_002635.2. NM_002644.3.
    UniGeneiHs.497589.

    Genome annotation databases

    EnsembliENST00000356495; ENSP00000348888; ENSG00000162896.
    GeneIDi5284.
    KEGGihsa:5284.
    UCSCiuc001hez.3. human.

    Polymorphism databases

    DMDMi150421625.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S62403 mRNA. Translation: AAB20203.1 .
    S43449
    , S43437 , S43441 , S43442 , S43443 , S43444 , S43445 , S43446 , S43447 , S43448 Genomic DNA. Translation: AAB23176.1 .
    AF272149 mRNA. Translation: AAN65630.1 .
    CR749533 mRNA. Translation: CAH18339.1 .
    M24559 mRNA. Translation: AAA36102.1 .
    CCDSi CCDS1474.1.
    PIRi A46537. QRHUGS.
    RefSeqi NP_002635.2. NM_002644.3.
    UniGenei Hs.497589.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XED X-ray 1.90 A/B/C/D/E/F 19-127 [» ]
    2OCW X-ray - A 19-603 [» ]
    3CHN Other 1.00 J 353-458 [» ]
    S 19-603 [» ]
    3CM9 Other 1.00 J 353-458 [» ]
    S 19-603 [» ]
    ProteinModelPortali P01833.
    SMRi P01833. Positions 20-241, 247-327, 356-441.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111302. 8 interactions.
    IntActi P01833. 4 interactions.
    STRINGi 9606.ENSP00000348888.

    PTM databases

    PhosphoSitei P01833.
    UniCarbKBi P01833.

    Polymorphism databases

    DMDMi 150421625.

    Proteomic databases

    PaxDbi P01833.
    PeptideAtlasi P01833.
    PRIDEi P01833.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356495 ; ENSP00000348888 ; ENSG00000162896 .
    GeneIDi 5284.
    KEGGi hsa:5284.
    UCSCi uc001hez.3. human.

    Organism-specific databases

    CTDi 5284.
    GeneCardsi GC01M207101.
    H-InvDB HIX0028583.
    HGNCi HGNC:8968. PIGR.
    HPAi CAB009454.
    HPA006154.
    HPA012012.
    MIMi 173880. gene.
    neXtProti NX_P01833.
    PharmGKBi PA33300.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG46873.
    HOGENOMi HOG000115545.
    HOVERGENi HBG008199.
    InParanoidi P01833.
    KOi K13073.
    OMAi YWCGVKQ.
    OrthoDBi EOG7PCJG8.
    PhylomeDBi P01833.
    TreeFami TF334441.

    Miscellaneous databases

    ChiTaRSi PIGR. human.
    EvolutionaryTracei P01833.
    GeneWikii Polymeric_immunoglobulin_receptor.
    GenomeRNAii 5284.
    NextBioi 20420.
    PROi P01833.
    SOURCEi Search...

    Gene expression databases

    Bgeei P01833.
    CleanExi HS_PIGR.
    Genevestigatori P01833.

    Family and domain databases

    Gene3Di 2.60.40.10. 5 hits.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR013106. Ig_V-set.
    [Graphical view ]
    Pfami PF07686. V-set. 5 hits.
    [Graphical view ]
    SMARTi SM00409. IG. 5 hits.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The human transmembrane secretory component (poly-Ig receptor): molecular cloning, restriction fragment length polymorphism and chromosomal sublocalization."
      Krajci P., Grzeschik K.H., Geurts van Kessel A.H., Olaisen B., Brandtzaeg P.
      Hum. Genet. 87:642-648(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-365.
    2. "Molecular cloning and exon-intron mapping of the gene encoding human transmembrane secretory component (the poly-Ig receptor)."
      Krajci P., Kvale D., Tasken K., Brandtzaeg P.
      Eur. J. Immunol. 22:2309-2315(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-365.
    3. "Cloning and characterization of hepatocellular carcinoma associated-genes."
      Dong X., Pang X., Cheng W.
      Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-365.
      Tissue: Small intestine.
    5. "Molecular cloning of the human transmembrane secretory component (poly-Ig receptor) and its mRNA expression in human tissues."
      Krajci P., Solberg R., Sandberg M., Oyen O., Jahnsen T., Brandtzaeg P.
      Biochem. Biophys. Res. Commun. 158:783-789(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 72-764, VARIANT SER-365.
    6. "The primary structure of human free secretory component and the arrangement of disulfide bonds."
      Eiffert H., Quentin E., Decker J., Hillemeir S., Hufschmidt M., Klingmueller D., Weber M.H., Hilschmann N.
      Hoppe-Seyler's Z. Physiol. Chem. 365:1489-1495(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-577, VARIANT SER-365, DISULFIDE BONDS, GLYCOSYLATION AT ASN-83; ASN-90; ASN-135; ASN-186; ASN-421; ASN-469 AND ASN-499.
    7. "Determination of the molecular structure of the human free secretory component."
      Eiffert H., Quentin E., Wiederhold M., Hillemeir S., Decker J., Weber M., Hilschmann N.
      Biol. Chem. Hoppe-Seyler 372:119-128(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-577, VARIANT SER-365.
    8. "Human free secretory component is composed of the first 585 amino acid residues of the polymeric immunoglobulin receptor."
      Hughes G.J., Frutiger S., Savoy L.-A., Reason A.J., Morris H.R., Jaton J.-C.
      FEBS Lett. 410:443-446(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 118-138; 212-230; 232-268; 273-288 AND 578-603.
    9. Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-83; ASN-90; ASN-421 AND ASN-469.
      Tissue: Bile.
    10. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-90; ASN-421 AND ASN-469.
      Tissue: Plasma.
    11. "Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry."
      Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.
      J. Proteome Res. 5:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-83; ASN-90; ASN-186; ASN-421; ASN-469 AND ASN-499.
      Tissue: Saliva.
    12. "Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry."
      Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.
      Proteomics 8:3833-3847(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-83; ASN-90; ASN-135; ASN-186; ASN-421; ASN-469 AND ASN-499.
      Tissue: Milk.
    13. "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-421 AND ASN-469.
      Tissue: Liver.
    14. Cited for: GLYCOSYLATION AT ASN-469.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Crystal structure of a polymeric immunoglobulin binding fragment of the human polymeric immunoglobulin receptor."
      Hamburger A.E., West A.P. Jr., Bjorkman P.J.
      Structure 12:1925-1935(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 19-127.

    Entry informationi

    Entry nameiPIGR_HUMAN
    AccessioniPrimary (citable) accession number: P01833
    Secondary accession number(s): Q68D81, Q8IZY7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: June 26, 2007
    Last modified: October 1, 2014
    This is version 153 of the entry and version 4 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 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3