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P01834

- IGKC_HUMAN

UniProt

P01834 - IGKC_HUMAN

Protein

Ig kappa chain C region

Gene

IGKC

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

    GO - Molecular functioni

    1. antigen binding Source: UniProtKB

    GO - Biological processi

    1. complement activation Source: Reactome
    2. complement activation, classical pathway Source: Reactome
    3. Fc-epsilon receptor signaling pathway Source: Reactome
    4. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    5. immune response Source: UniProtKB
    6. innate immune response Source: Reactome
    7. regulation of immune response Source: Reactome
    8. retina homeostasis Source: UniProt

    Enzyme and pathway databases

    ReactomeiREACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
    REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_160158. Role of phospholipids in phagocytosis.
    REACT_160163. Scavenging of heme from plasma.
    REACT_160274. FCGR activation.
    REACT_163701. FCERI mediated MAPK activation.
    REACT_163769. Role of LAT2/NTAL/LAB on calcium mobilization.
    REACT_163834. FCERI mediated Ca+2 mobilization.
    REACT_163936. Fc epsilon receptor (FCERI) signaling.
    REACT_163994. FCERI mediated NF-kB activation.
    REACT_7956. Classical antibody-mediated complement activation.
    REACT_8024. Initial triggering of complement.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ig kappa chain C region
    Gene namesi
    Name:IGKC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Unplaced

    Organism-specific databases

    HGNCiHGNC:5716. IGKC.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. extracellular region Source: Reactome
    3. extracellular space Source: UniProt
    4. extracellular vesicular exosome Source: UniProt
    5. plasma membrane Source: Reactome

    Pathology & Biotechi

    Involvement in diseasei

    Immunoglobulin kappa light chain deficiency (IGKCD) [MIM:614102]: A disease characterized by the complete absence of immunoglobulin kappa chains.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti40 – 401W → R in IGKCD. 1 Publication
    VAR_066403

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi614102. phenotype.
    Orphaneti183675. Recurrent infections associated with rare immunoglobulin isotypes deficiency.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – 106›106Ig kappa chain C regionPRO_0000153596Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi26 ↔ 861 PublicationPROSITE-ProRule annotation
    Disulfide bondi106 – 106Interchain (with a heavy chain)1 PublicationPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiP01834.
    PaxDbiP01834.
    PRIDEiP01834.

    2D gel databases

    UCD-2DPAGEP01834.

    PTM databases

    PhosphoSiteiP01834.

    Expressioni

    Gene expression databases

    BgeeiP01834.
    CleanExiHS_IGKC.
    GenevestigatoriP01834.

    Interactioni

    Protein-protein interaction databases

    IntActiP01834. 37 interactions.
    MINTiMINT-159227.
    STRINGi9606.ENSP00000374777.

    Structurei

    Secondary structure

    1
    106
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 105
    Helixi14 – 174
    Turni18 – 203
    Beta strandi21 – 3414
    Beta strandi36 – 449
    Beta strandi45 – 473
    Beta strandi49 – 557
    Turni60 – 623
    Beta strandi65 – 7410
    Helixi75 – 784
    Beta strandi82 – 909
    Beta strandi93 – 953
    Beta strandi97 – 1026
    Turni103 – 1053

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A4JX-ray2.10A/L1-104[»]
    1A4KX-ray2.40A/L1-104[»]
    1CLYX-ray2.50L1-106[»]
    1D5BX-ray2.80A/L1-103[»]
    1D5IX-ray2.00L1-103[»]
    1D6VX-ray2.00L1-103[»]
    1DFBX-ray2.70L1-106[»]
    1GAFX-ray1.95L1-106[»]
    1HEZX-ray2.70A/C1-106[»]
    1HKLX-ray2.68L1-106[»]
    1HZHX-ray2.70L/M1-106[»]
    1I7ZX-ray2.30A/C1-106[»]
    1MIMX-ray2.60L1-105[»]
    1N0XX-ray1.80L/M1-106[»]
    1OM3X-ray2.20L/M1-105[»]
    1OP3X-ray1.75K/L1-105[»]
    1OP5X-ray3.00K/L1-105[»]
    1UCBX-ray2.50L1-106[»]
    2NY7X-ray2.30L1-106[»]
    2O5XX-ray2.05L1-106[»]
    2O5YX-ray2.85L1-106[»]
    2O5ZX-ray2.40L1-106[»]
    2QQKX-ray2.75L1-106[»]
    2QQLX-ray3.10L1-106[»]
    2QQNX-ray2.20L1-106[»]
    2QSCX-ray2.80L1-106[»]
    2R56X-ray2.80L/M1-103[»]
    2RFXX-ray2.50C93-101[»]
    2VXQX-ray1.90L1-106[»]
    3B2UX-ray2.58D/G/K/L/O/R/U/X1-104[»]
    3B2VX-ray3.30L1-104[»]
    3BDYX-ray2.60L1-106[»]
    3BE1X-ray2.90L1-106[»]
    3BKYX-ray2.61L1-106[»]
    3BN9X-ray2.17C/E1-106[»]
    3BQUX-ray3.00A1-106[»]
    3C08X-ray2.15L1-105[»]
    3C09X-ray3.20B/L1-105[»]
    3CFJX-ray2.60A/C/E/L1-106[»]
    3CFKX-ray2.60A/C/E/G/J/L/M/O1-106[»]
    3CSYX-ray3.40B/D/F/H1-103[»]
    3D0LX-ray2.35A1-105[»]
    3D85X-ray1.90A1-106[»]
    3DVGX-ray2.60A1-106[»]
    3DVNX-ray2.70A/L1-106[»]
    3EYFX-ray2.30A/C1-106[»]
    3EYOX-ray2.50A/C1-106[»]
    3EYQX-ray2.40C1-106[»]
    3IU3X-ray2.90B/D/L1-105[»]
    3O11X-ray2.80A/L1-106[»]
    3QCTX-ray2.15L2-105[»]
    3QCUX-ray1.98L/M2-105[»]
    3QCVX-ray2.51L/M2-105[»]
    3RU8X-ray2.07L1-106[»]
    3U0WX-ray2.00L1-106[»]
    3U7WX-ray2.60L1-106[»]
    3U7YX-ray2.45L1-106[»]
    3VH8X-ray1.80C/F93-101[»]
    3WUWX-ray2.00C93-101[»]
    4D9RX-ray2.42D/L2-106[»]
    4HIXX-ray2.20L1-106[»]
    4NM4X-ray2.65L/M1-106[»]
    4NM8X-ray4.00L/M/N1-106[»]
    ProteinModelPortaliP01834.
    SMRiP01834. Positions 1-103.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01834.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 10298Ig-likeAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Immunoglobulin C region, Immunoglobulin domain

    Phylogenomic databases

    eggNOGiNOG116969.
    HOGENOMiHOG000059537.
    HOVERGENiHBG039526.
    InParanoidiP01834.
    OMAiWATDSSP.
    PhylomeDBiP01834.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003006. Ig/MHC_CS.
    IPR003597. Ig_C1-set.
    [Graphical view]
    PfamiPF07654. C1-set. 1 hit.
    [Graphical view]
    SMARTiSM00407. IGc1. 1 hit.
    [Graphical view]
    PROSITEiPS50835. IG_LIKE. 1 hit.
    PS00290. IG_MHC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P01834-1 [UniParc]FASTAAdd to Basket

    « Hide

    TVAAPSVFIF PPSDEQLKSG TASVVCLLNN FYPREAKVQW KVDNALQSGN    50
    SQESVTEQDS KDSTYSLSST LTLSKADYEK HKVYACEVTH QGLSSPVTKS 100
    FNRGEC 106
    Length:106
    Mass (Da):11,609
    Last modified:July 21, 1986 - v1
    Checksum:i51984D1FDD372CE8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11
    Sequence conflicti14 – 141D → N AA sequence (PubMed:4893682)Curated
    Sequence conflicti14 – 141D → N AA sequence (PubMed:5447531)Curated
    Sequence conflicti57 – 571E → Q AA sequence 1 PublicationCurated
    Sequence conflicti57 – 571E → Q AA sequence (PubMed:5586923)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti40 – 401W → R in IGKCD. 1 Publication
    VAR_066403
    Natural varianti83 – 831V → L in INV(1,2) marker.
    VAR_003897

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J00241 Genomic DNA. Translation: AAA58989.1.
    PIRiB90562. K3HU.
    UniGeneiHs.449609.

    Polymorphism databases

    DMDMi125145.

    Cross-referencesi

    Web resourcesi

    IMGT/GENE-DB

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J00241 Genomic DNA. Translation: AAA58989.1 .
    PIRi B90562. K3HU.
    UniGenei Hs.449609.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A4J X-ray 2.10 A/L 1-104 [» ]
    1A4K X-ray 2.40 A/L 1-104 [» ]
    1CLY X-ray 2.50 L 1-106 [» ]
    1D5B X-ray 2.80 A/L 1-103 [» ]
    1D5I X-ray 2.00 L 1-103 [» ]
    1D6V X-ray 2.00 L 1-103 [» ]
    1DFB X-ray 2.70 L 1-106 [» ]
    1GAF X-ray 1.95 L 1-106 [» ]
    1HEZ X-ray 2.70 A/C 1-106 [» ]
    1HKL X-ray 2.68 L 1-106 [» ]
    1HZH X-ray 2.70 L/M 1-106 [» ]
    1I7Z X-ray 2.30 A/C 1-106 [» ]
    1MIM X-ray 2.60 L 1-105 [» ]
    1N0X X-ray 1.80 L/M 1-106 [» ]
    1OM3 X-ray 2.20 L/M 1-105 [» ]
    1OP3 X-ray 1.75 K/L 1-105 [» ]
    1OP5 X-ray 3.00 K/L 1-105 [» ]
    1UCB X-ray 2.50 L 1-106 [» ]
    2NY7 X-ray 2.30 L 1-106 [» ]
    2O5X X-ray 2.05 L 1-106 [» ]
    2O5Y X-ray 2.85 L 1-106 [» ]
    2O5Z X-ray 2.40 L 1-106 [» ]
    2QQK X-ray 2.75 L 1-106 [» ]
    2QQL X-ray 3.10 L 1-106 [» ]
    2QQN X-ray 2.20 L 1-106 [» ]
    2QSC X-ray 2.80 L 1-106 [» ]
    2R56 X-ray 2.80 L/M 1-103 [» ]
    2RFX X-ray 2.50 C 93-101 [» ]
    2VXQ X-ray 1.90 L 1-106 [» ]
    3B2U X-ray 2.58 D/G/K/L/O/R/U/X 1-104 [» ]
    3B2V X-ray 3.30 L 1-104 [» ]
    3BDY X-ray 2.60 L 1-106 [» ]
    3BE1 X-ray 2.90 L 1-106 [» ]
    3BKY X-ray 2.61 L 1-106 [» ]
    3BN9 X-ray 2.17 C/E 1-106 [» ]
    3BQU X-ray 3.00 A 1-106 [» ]
    3C08 X-ray 2.15 L 1-105 [» ]
    3C09 X-ray 3.20 B/L 1-105 [» ]
    3CFJ X-ray 2.60 A/C/E/L 1-106 [» ]
    3CFK X-ray 2.60 A/C/E/G/J/L/M/O 1-106 [» ]
    3CSY X-ray 3.40 B/D/F/H 1-103 [» ]
    3D0L X-ray 2.35 A 1-105 [» ]
    3D85 X-ray 1.90 A 1-106 [» ]
    3DVG X-ray 2.60 A 1-106 [» ]
    3DVN X-ray 2.70 A/L 1-106 [» ]
    3EYF X-ray 2.30 A/C 1-106 [» ]
    3EYO X-ray 2.50 A/C 1-106 [» ]
    3EYQ X-ray 2.40 C 1-106 [» ]
    3IU3 X-ray 2.90 B/D/L 1-105 [» ]
    3O11 X-ray 2.80 A/L 1-106 [» ]
    3QCT X-ray 2.15 L 2-105 [» ]
    3QCU X-ray 1.98 L/M 2-105 [» ]
    3QCV X-ray 2.51 L/M 2-105 [» ]
    3RU8 X-ray 2.07 L 1-106 [» ]
    3U0W X-ray 2.00 L 1-106 [» ]
    3U7W X-ray 2.60 L 1-106 [» ]
    3U7Y X-ray 2.45 L 1-106 [» ]
    3VH8 X-ray 1.80 C/F 93-101 [» ]
    3WUW X-ray 2.00 C 93-101 [» ]
    4D9R X-ray 2.42 D/L 2-106 [» ]
    4HIX X-ray 2.20 L 1-106 [» ]
    4NM4 X-ray 2.65 L/M 1-106 [» ]
    4NM8 X-ray 4.00 L/M/N 1-106 [» ]
    ProteinModelPortali P01834.
    SMRi P01834. Positions 1-103.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P01834. 37 interactions.
    MINTi MINT-159227.
    STRINGi 9606.ENSP00000374777.

    Protein family/group databases

    IMGTi Search...

    PTM databases

    PhosphoSitei P01834.

    Polymorphism databases

    DMDMi 125145.

    2D gel databases

    UCD-2DPAGE P01834.

    Proteomic databases

    MaxQBi P01834.
    PaxDbi P01834.
    PRIDEi P01834.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    GeneCardsi GC02M089156.
    H-InvDB HIX0161619.
    HGNCi HGNC:5716. IGKC.
    MIMi 147200. gene.
    614102. phenotype.
    neXtProti NX_P01834.
    Orphaneti 183675. Recurrent infections associated with rare immunoglobulin isotypes deficiency.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG116969.
    HOGENOMi HOG000059537.
    HOVERGENi HBG039526.
    InParanoidi P01834.
    OMAi WATDSSP.
    PhylomeDBi P01834.

    Enzyme and pathway databases

    Reactomei REACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
    REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_160158. Role of phospholipids in phagocytosis.
    REACT_160163. Scavenging of heme from plasma.
    REACT_160274. FCGR activation.
    REACT_163701. FCERI mediated MAPK activation.
    REACT_163769. Role of LAT2/NTAL/LAB on calcium mobilization.
    REACT_163834. FCERI mediated Ca+2 mobilization.
    REACT_163936. Fc epsilon receptor (FCERI) signaling.
    REACT_163994. FCERI mediated NF-kB activation.
    REACT_7956. Classical antibody-mediated complement activation.
    REACT_8024. Initial triggering of complement.

    Miscellaneous databases

    EvolutionaryTracei P01834.
    PROi P01834.
    SOURCEi Search...

    Gene expression databases

    Bgeei P01834.
    CleanExi HS_IGKC.
    Genevestigatori P01834.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003006. Ig/MHC_CS.
    IPR003597. Ig_C1-set.
    [Graphical view ]
    Pfami PF07654. C1-set. 1 hit.
    [Graphical view ]
    SMARTi SM00407. IGc1. 1 hit.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 1 hit.
    PS00290. IG_MHC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The covalent structure of a human gamma G-immunoglobulin. VI. Amino acid sequence of the light chain."
      Gottlieb P.D., Cunningham B.A., Rutishauser U., Edelman G.M.
      Biochemistry 9:3155-3161(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE (MYELOMA PROTEIN EU).
    2. "The covalent structure of a human gamma G-immunoglobulin. X. Intrachain disulfide bonds."
      Gall W.E., Edelman G.M.
      Biochemistry 9:3188-3196(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS.
    3. "Rule of antibody structure. The primary structure of a monoclonal immunoglobulin L-chain of kappa-type, subgroup 3 (Bence-Jones protein Ti). IV. The complete amino acid sequence and its significance for the mechanism of antibody production."
      Suter L., Barnikol H.U., Watanabe S., Hilschmann N.
      Hoppe-Seyler's Z. Physiol. Chem. 353:189-208(1972) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE (BENCE-JONES PROTEIN TI).
    4. "Cloned human and mouse kappa immunoglobulin constant and J region genes conserve homology in functional segments."
      Hieter P.A., Max E.E., Seidman J.G., Maizel J.V. Jr., Leder P.
      Cell 22:197-207(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. Hilschmann N., Barnikol H.U., Hess M., Langer B., Ponstingl H., Steinmetz-Kayne M., Suter L., Watanabe S.
      (In) Franek F., Shugar D. (eds.); Gamma globulins: structure and function, pp.57-74, Academic Press, New York (1969)
      Cited for: PROTEIN SEQUENCE (BENCE-JONES PROTEIN ROY).
    6. "The complete amino acid sequence of Bence Jones protein Cum (kappa-type)."
      Hilschmann N.
      Hoppe-Seyler's Z. Physiol. Chem. 348:1718-1722(1967) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE (BENCE-JONES PROTEIN CUM).
    7. "The amino acid sequence of a kappa type Bence-Jones protein. 3. The complete sequence and the location of the disulfide bridges."
      Titani K., Shinoda T., Putnam F.W.
      J. Biol. Chem. 244:3550-3560(1969) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE (BENCE-JONES PROTEIN AG).
    8. "Macroglobulin structure: variable sequence of light and heavy chains."
      Kohler H., Shimizu A., Paul C., Putnam F.W.
      Science 169:56-59(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE (WALDENSTROM'S MACROGLOBULIN OU).
    9. "Extended analysis of AL-amyloid protein from abdominal wall subcutaneous fat biopsy: kappa IV immunoglobulin light chain."
      Olsen K.E., Sletten K., Westermark P.
      Biochem. Biophys. Res. Commun. 245:713-716(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-33; 38-41 AND 62-80.
      Tissue: Abdominal adipose tissue.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Molecular defects in a human immunoglobulin kappa chain deficiency."
      Stavnezer-Nordgren J., Kekish O., Zegers B.J.
      Science 230:458-461(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT IGKCD ARG-40.

    Entry informationi

    Entry nameiIGKC_HUMAN
    AccessioniPrimary (citable) accession number: P01834
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 144 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

    Miscellaneous

    The EU sequence has the INV (3) allotypic marker, Ala-45 and Val-83. The ROY sequence has the INV (1,2) allotypic marker, Ala-45 and Leu-83.

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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