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Protein

Ig kappa chain C region

Gene

IGKC

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

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. receptor-mediated endocytosis Source: Reactome
  8. regulation of immune response Source: Reactome
  9. retina homeostasis Source: UniProtKB
Complete GO annotation...

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 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:5716. IGKC.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: UniProtKB
  2. extracellular region Source: Reactome
  3. extracellular space Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProtKB
  5. plasma membrane Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Immunoglobulin kappa light chain deficiency (IGKCD)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disease characterized by the complete absence of immunoglobulin kappa chains.

See also OMIM:614102
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.

Polymorphism and mutation databases

DMDMi125145.

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 ↔ 86PROSITE-ProRule annotation1 Publication
Disulfide bondi106 – 106Interchain (with a heavy chain)PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP01834.
PaxDbiP01834.
PRIDEiP01834.

2D gel databases

UCD-2DPAGEP01834.

PTM databases

PhosphoSiteiP01834.

Expressioni

Gene expression databases

BgeeiP01834.
CleanExiHS_IGKC.
ExpressionAtlasiP01834. baseline.
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 – 105Combined sources
Helixi14 – 174Combined sources
Turni18 – 203Combined sources
Beta strandi21 – 3414Combined sources
Beta strandi36 – 449Combined sources
Beta strandi45 – 473Combined sources
Beta strandi49 – 557Combined sources
Turni60 – 623Combined sources
Beta strandi65 – 7410Combined sources
Helixi75 – 784Combined sources
Beta strandi82 – 909Combined sources
Beta strandi93 – 953Combined sources
Beta strandi97 – 1026Combined sources
Turni103 – 1053Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
3X11X-ray2.15C93-101[»]
3X12X-ray1.80C93-101[»]
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.
OMAiKSFNRNE.
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

        10         20         30         40         50
TVAAPSVFIF PPSDEQLKSG TASVVCLLNN FYPREAKVQW KVDNALQSGN
60 70 80 90 100
SQESVTEQDS KDSTYSLSST LTLSKADYEK HKVYACEVTH QGLSSPVTKS

FNRGEC
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 (Ref. 5) Curated
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:
EMBLi
GenBanki
DDBJi
Links Updated
J00241 Genomic DNA. Translation: AAA58989.1.
PIRiB90562. K3HU.
UniGeneiHs.449609.

Cross-referencesi

Web resourcesi

IMGT/GENE-DB

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00241 Genomic DNA. Translation: AAA58989.1.
PIRiB90562. K3HU.
UniGeneiHs.449609.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
3X11X-ray2.15C93-101[»]
3X12X-ray1.80C93-101[»]
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...

Protein-protein interaction databases

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

Protein family/group databases

IMGTiSearch...

PTM databases

PhosphoSiteiP01834.

Polymorphism and mutation databases

DMDMi125145.

2D gel databases

UCD-2DPAGEP01834.

Proteomic databases

MaxQBiP01834.
PaxDbiP01834.
PRIDEiP01834.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

GeneCardsiGC02M089156.
H-InvDBHIX0161619.
HGNCiHGNC:5716. IGKC.
MIMi147200. gene.
614102. phenotype.
neXtProtiNX_P01834.
Orphaneti183675. Recurrent infections associated with rare immunoglobulin isotypes deficiency.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG116969.
HOGENOMiHOG000059537.
HOVERGENiHBG039526.
InParanoidiP01834.
OMAiKSFNRNE.
PhylomeDBiP01834.

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.

Miscellaneous databases

EvolutionaryTraceiP01834.
PROiP01834.
SOURCEiSearch...

Gene expression databases

BgeeiP01834.
CleanExiHS_IGKC.
ExpressionAtlasiP01834. baseline.
GenevestigatoriP01834.

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]
ProtoNetiSearch...

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. "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: March 4, 2015
This is version 148 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

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.