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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

  • antigen binding Source: UniProtKB
  • immunoglobulin receptor binding Source: GO_Central
  • serine-type endopeptidase activity Source: Reactome

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-HSA-166663. Initial triggering of complement.
R-HSA-173623. Classical antibody-mediated complement activation.
R-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
R-HSA-2029481. FCGR activation.
R-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-2029485. Role of phospholipids in phagocytosis.
R-HSA-2168880. Scavenging of heme from plasma.
R-HSA-2454202. Fc epsilon receptor (FCERI) signaling.
R-HSA-2730905. Role of LAT2/NTAL/LAB on calcium mobilization.
R-HSA-2871796. FCERI mediated MAPK activation.
R-HSA-2871809. FCERI mediated Ca+2 mobilization.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-5690714. CD22 mediated BCR regulation.
R-HSA-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Names & Taxonomyi

Protein namesi
Recommended name:
Ig kappa chain C region
Gene namesi
Name:IGKC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:5716. IGKC.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • external side of plasma membrane Source: GO_Central
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • immunoglobulin complex, circulating Source: GO_Central
  • 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)DescriptionActionsGraphical viewLength
Natural variantiVAR_06640340W → R in IGKCD. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi3514.
MalaCardsiIGKC.
MIMi614102. phenotype.
Orphaneti183675. Recurrent infections associated with rare immunoglobulin isotypes deficiency.

Polymorphism and mutation databases

DMDMi125145.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000153596‹1 – 106Ig kappa chain C regionAdd BLAST›106

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi26 ↔ 86PROSITE-ProRule annotation1 Publication
Disulfide bondi106Interchain (with a heavy chain)PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiP01834.
MaxQBiP01834.
PeptideAtlasiP01834.
PRIDEiP01834.

2D gel databases

UCD-2DPAGEP01834.

PTM databases

iPTMnetiP01834.
PhosphoSitePlusiP01834.
SwissPalmiP01834.

Expressioni

Gene expression databases

BgeeiENSG00000211592.
CleanExiHS_IGKC.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

IntActiP01834. 38 interactors.
MINTiMINT-159227.

Structurei

Secondary structure

1106
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 10Combined sources5
Helixi14 – 17Combined sources4
Turni18 – 20Combined sources3
Beta strandi21 – 34Combined sources14
Beta strandi36 – 44Combined sources9
Beta strandi45 – 47Combined sources3
Beta strandi49 – 55Combined sources7
Turni60 – 62Combined sources3
Beta strandi65 – 74Combined sources10
Helixi75 – 78Combined sources4
Beta strandi82 – 90Combined sources9
Beta strandi93 – 95Combined sources3
Beta strandi97 – 102Combined sources6
Turni103 – 105Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4D3CX-ray2.62L1-106[»]
4D9RX-ray2.42D/L2-106[»]
4HIXX-ray2.20L1-106[»]
4NM4X-ray2.65L/M1-106[»]
4NM8X-ray4.00L/M/N1-106[»]
4XMPX-ray1.78L1-106[»]
4XNYX-ray2.30L1-106[»]
4XNZX-ray3.39C/F/L1-106[»]
4XXDX-ray2.41A/D1-106[»]
4YDVX-ray2.70A/L1-106[»]
5B38X-ray2.30C93-101[»]
5B39X-ray2.50C93-101[»]
5ESVX-ray3.10B/D/L1-106[»]
5ESZX-ray4.19B/L1-106[»]
ProteinModelPortaliP01834.
SMRiP01834.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01834.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 102Ig-likeAdd BLAST98

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin C region, Immunoglobulin domain

Phylogenomic databases

HOGENOMiHOG000059537.
HOVERGENiHBG039526.
InParanoidiP01834.
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]
SUPFAMiSSF48726. SSF48726. 1 hit.
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)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Sequence conflicti14D → N AA sequence (PubMed:4893682).Curated1
Sequence conflicti14D → N AA sequence (PubMed:5447531).Curated1
Sequence conflicti57E → Q AA sequence (Ref. 5) Curated1
Sequence conflicti57E → Q AA sequence (PubMed:5586923).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06640340W → R in IGKCD. 1 Publication1
Natural variantiVAR_00389783V → L in INV(1,2) marker. 1

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
PDB 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[»]
4D3CX-ray2.62L1-106[»]
4D9RX-ray2.42D/L2-106[»]
4HIXX-ray2.20L1-106[»]
4NM4X-ray2.65L/M1-106[»]
4NM8X-ray4.00L/M/N1-106[»]
4XMPX-ray1.78L1-106[»]
4XNYX-ray2.30L1-106[»]
4XNZX-ray3.39C/F/L1-106[»]
4XXDX-ray2.41A/D1-106[»]
4YDVX-ray2.70A/L1-106[»]
5B38X-ray2.30C93-101[»]
5B39X-ray2.50C93-101[»]
5ESVX-ray3.10B/D/L1-106[»]
5ESZX-ray4.19B/L1-106[»]
ProteinModelPortaliP01834.
SMRiP01834.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP01834. 38 interactors.
MINTiMINT-159227.

Protein family/group databases

IMGTiSearch...

PTM databases

iPTMnetiP01834.
PhosphoSitePlusiP01834.
SwissPalmiP01834.

Polymorphism and mutation databases

DMDMi125145.

2D gel databases

UCD-2DPAGEP01834.

Proteomic databases

EPDiP01834.
MaxQBiP01834.
PeptideAtlasiP01834.
PRIDEiP01834.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

DisGeNETi3514.
GeneCardsiIGKC.
IGKV1-8.
IGKV3-11.
H-InvDBHIX0161619.
HGNCiHGNC:5716. IGKC.
MalaCardsiIGKC.
MIMi147200. gene.
614102. phenotype.
neXtProtiNX_P01834.
Orphaneti183675. Recurrent infections associated with rare immunoglobulin isotypes deficiency.
GenAtlasiSearch...

Phylogenomic databases

HOGENOMiHOG000059537.
HOVERGENiHBG039526.
InParanoidiP01834.
PhylomeDBiP01834.

Enzyme and pathway databases

ReactomeiR-HSA-166663. Initial triggering of complement.
R-HSA-173623. Classical antibody-mediated complement activation.
R-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
R-HSA-2029481. FCGR activation.
R-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-2029485. Role of phospholipids in phagocytosis.
R-HSA-2168880. Scavenging of heme from plasma.
R-HSA-2454202. Fc epsilon receptor (FCERI) signaling.
R-HSA-2730905. Role of LAT2/NTAL/LAB on calcium mobilization.
R-HSA-2871796. FCERI mediated MAPK activation.
R-HSA-2871809. FCERI mediated Ca+2 mobilization.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-5690714. CD22 mediated BCR regulation.
R-HSA-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Miscellaneous databases

EvolutionaryTraceiP01834.
PROiP01834.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000211592.
CleanExiHS_IGKC.

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]
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 165 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

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 one 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.