UniProtKB - P01834 (IGKC_HUMAN)
Immunoglobulin kappa constant
IGKC
Functioni
Constant region of immunoglobulin light chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:22158414, PubMed:20176268).
The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268).
3 PublicationsCaution
GO - Molecular functioni
- antigen binding Source: GO_Central
- immunoglobulin receptor binding Source: GO_Central
GO - Biological processi
- adaptive immune response Source: ComplexPortal
- B cell receptor signaling pathway Source: GO_Central
- complement activation, classical pathway Source: GO_Central
- defense response to bacterium Source: GO_Central
- immune response Source: UniProtKB
- innate immune response Source: GO_Central
- phagocytosis, engulfment Source: GO_Central
- phagocytosis, recognition Source: GO_Central
- positive regulation of B cell activation Source: GO_Central
- retina homeostasis Source: UniProtKB
Keywordsi
Biological process | Adaptive immunity, Immunity |
Enzyme and pathway databases
PathwayCommonsi | P01834 |
Reactomei | R-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-202733, Cell surface interactions at the vascular wall 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-9664323, FCGR3A-mediated IL10 synthesis R-HSA-9664422, FCGR3A-mediated phagocytosis R-HSA-977606, Regulation of Complement cascade R-HSA-983695, Antigen activates B Cell Receptor (BCR) leading to generation of second messengers |
SignaLinki | P01834 |
Protein family/group databases
IMGT/GENE-DB | IGKC |
Names & Taxonomyi
Protein namesi | Recommended name: Immunoglobulin kappa constant2 PublicationsAlternative name(s): Ig kappa chain C regionCurated Ig kappa chain C region AG1 Publication Ig kappa chain C region CUM1 Publication Ig kappa chain C region EU1 Publication Ig kappa chain C region OU1 Publication Ig kappa chain C region ROY1 Publication Ig kappa chain C region TI1 Publication |
Gene namesi | Name:IGKC2 Publications |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:5716, IGKC |
MIMi | 147200, gene |
neXtProti | NX_P01834 |
Subcellular locationi
Plasma membrane
- Cell membrane 2 Publications
Extracellular region or secreted
- Secreted 2 Publications
Extracellular region or secreted
- blood microparticle Source: UniProtKB
- extracellular exosome Source: UniProtKB
- extracellular region Source: Reactome
- extracellular space Source: UniProtKB
- immunoglobulin complex, circulating Source: GO_Central
Plasma Membrane
- external side of plasma membrane Source: GO_Central
- plasma membrane Source: Reactome
Other locations
- IgA immunoglobulin complex Source: ComplexPortal
- IgD immunoglobulin complex Source: ComplexPortal
- IgE immunoglobulin complex Source: ComplexPortal
- IgG immunoglobulin complex Source: ComplexPortal
- IgM immunoglobulin complex Source: ComplexPortal
Keywords - Cellular componenti
Cell membrane, Immunoglobulin, Membrane, SecretedPathology & Biotechi
Involvement in diseasei
Immunoglobulin kappa light chain deficiency (IGKCD)1 Publication
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_066403 | 41 | W → R in IGKCD. 1 Publication | 1 |
Keywords - Diseasei
Disease variantOrganism-specific databases
MalaCardsi | IGKC |
MIMi | 614102, phenotype |
Orphaneti | 183675, Recurrent infections associated with rare immunoglobulin isotypes deficiency |
Miscellaneous databases
Pharosi | P01834, Tdark |
Chemistry databases
DrugBanki | DB07909, (1S,2S,5S)2-(4-GLUTARIDYLBENZYL)-5-PHENYL-1-CYCLOHEXANOL DB07416, (2S)-2-(BUTYRYLOXY)-3-HYDROXYPROPYL NONANOATE DB07716, (4Z)-2,8:7,12:11,15:14,18:17,22-PENTAANHYDRO-4,5,6,9,10,13,19,20,21-NONADEOXY-D-ARABINO-D-ALLO-D-ALLO-DOCOSA-4,9,20-TRIENITOL DB07441, 3-{[(9-CYANO-9,10-DIHYDRO-10-METHYLACRIDIN-9-YL)CARBONYL]AMINO}PROPANOIC ACID DB08562, 4-(4-STYRYL-PHENYLCARBAMOYL)-BUTYRIC ACID DB07882, 4-{4-[2-(1A,7A-DIMETHYL-4-OXY-OCTAHYDRO-1-OXA-4-AZA-CYCLOPROPA[A]NAPHTHALEN-4-YL) -ACETYLAMINO]-PHENYLCARBAMOYL}-BUTYRIC ACID DB07784, [4-(4-ACETYLAMINO-PHENYL)-3,5-DIOXO-4-AZA-TRICYCLO[5.2.2.0 2,6]UNDEC-1-YLCARBAMOYLOXY]-ACETIC ACID DB07375, Etiocholanedione DB08413, METHYL-PHOSPHONIC ACID MONO-(4-NITRO-PHENYL) ESTER DB04688, Methylecgonine DB08289, N-(PARA-GLUTARAMIDOPHENYL-ETHYL)-PIPERIDINIUM-N-OXIDE DB07893, PHENYL[1-(N-SUCCINYLAMINO)PENTYL]PHOSPHONATE DB01851, Tetrabutylammonium Ion DB08647, Trazeolide |
Genetic variation databases
BioMutai | IGKC |
DMDMi | 125145 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000153596 | ‹1 – 107 | Immunoglobulin kappa constantAdd BLAST | ›107 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 27 ↔ 87 | PROSITE-ProRule annotation1 Publication | ||
Disulfide bondi | 107 | Interchain (with a heavy chain)1 Publication |
Keywords - PTMi
Disulfide bondProteomic databases
EPDi | P01834 |
jPOSTi | P01834 |
MassIVEi | P01834 |
PeptideAtlasi | P01834 |
PRIDEi | P01834 |
ProteomicsDBi | 51490 |
2D gel databases
UCD-2DPAGEi | P01834 |
PTM databases
CarbonylDBi | P01834 |
iPTMneti | P01834 |
PhosphoSitePlusi | P01834 |
SwissPalmi | P01834 |
Expressioni
Gene expression databases
Bgeei | ENSG00000211592, Expressed in lymph node and 115 other tissues |
Interactioni
Subunit structurei
Immunoglobulins are composed of two identical heavy chains and two identical light chains; disulfide-linked.
1 PublicationGO - Molecular functioni
- immunoglobulin receptor binding Source: GO_Central
Protein-protein interaction databases
ComplexPortali | CPX-6744, IgD - Ig kappa immunoglobulin complex, constant regions CPX-6911, IgM - Ig kappa immunoglobulin complex, constant regions CPX-6929, IgG1 - Ig kappa immunoglobulin complex, constant regions CPX-6936, IgG2 - Ig kappa immunoglobulin complex, constant regions CPX-6943, IgG3 - Ig kappa immunoglobulin complex, constant regions CPX-6949, IgG4 - Ig kappa immunoglobulin complex, constant regions CPX-6955, IgA1 - Ig kappa immunoglobulin complex, constant regions CPX-6962, IgA2 - Ig kappa immunoglobulin complex, constant regions CPX-6969, IgE - Ig kappa immunoglobulin complex, constant regions |
IntActi | P01834, 69 interactors |
MINTi | P01834 |
Miscellaneous databases
RNActi | P01834, protein |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P01834 |
SMRi | P01834 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P01834 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 6 – 103 | Ig-likePROSITE-ProRule annotationAdd BLAST | 98 |
Keywords - Domaini
Immunoglobulin domainPhylogenomic databases
InParanoidi | P01834 |
PhylomeDBi | P01834 |
Family and domain databases
Gene3Di | 2.60.40.10, 1 hit |
InterProi | View protein in InterPro IPR007110, Ig-like_dom IPR036179, Ig-like_dom_sf IPR013783, Ig-like_fold IPR003006, Ig/MHC_CS IPR003597, Ig_C1-set |
Pfami | View protein in Pfam PF07654, C1-set, 1 hit |
SMARTi | View protein in SMART SM00407, IGc1, 1 hit |
SUPFAMi | SSF48726, SSF48726, 1 hit |
PROSITEi | View protein in PROSITE PS50835, IG_LIKE, 1 hit PS00290, IG_MHC, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All
10 20 30 40 50
RTVAAPSVFI FPPSDEQLKS GTASVVCLLN NFYPREAKVQ WKVDNALQSG
60 70 80 90 100
NSQESVTEQD SKDSTYSLSS TLTLSKADYE KHKVYACEVT HQGLSSPVTK
SFNRGEC
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketA0A5H1ZRQ3 | A0A5H1ZRQ3_HUMAN | Immunoglobulin kappa constant | IGKC | 107 | Annotation score: |
Sequence cautioni
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Non-terminal residuei | 1 | 1 | ||
Sequence conflicti | 15 | D → N AA sequence (PubMed:4893682).Curated | 1 | |
Sequence conflicti | 15 | D → N AA sequence (PubMed:5447531).Curated | 1 | |
Sequence conflicti | 58 | E → Q AA sequence (Ref. 3) Curated | 1 | |
Sequence conflicti | 58 | E → Q AA sequence (PubMed:5586923).Curated | 1 |
Polymorphismi
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_066403 | 41 | W → R in IGKCD. 1 Publication | 1 | |
Natural variantiVAR_003897 | 84 | V → L1 Publication | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J00241 Genomic DNA Translation: AAA58989.1 Different initiation. AC244205 Genomic DNA No translation available. |
PIRi | B90562, K3HU |
Genome annotation databases
UCSCi | uc061lpw.1, human uc061lpy.1, human |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J00241 Genomic DNA Translation: AAA58989.1 Different initiation. AC244205 Genomic DNA No translation available. |
PIRi | B90562, K3HU |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1A4J | X-ray | 2.10 | A/L | 2-105 | [»] | |
1A4K | X-ray | 2.40 | A/L | 2-105 | [»] | |
1CLY | X-ray | 2.50 | L | 2-107 | [»] | |
1D5B | X-ray | 2.80 | A/L | 2-104 | [»] | |
1D5I | X-ray | 2.00 | L | 2-104 | [»] | |
1D6V | X-ray | 2.00 | L | 2-104 | [»] | |
1DFB | X-ray | 2.70 | L | 2-107 | [»] | |
1GAF | X-ray | 1.95 | L | 2-107 | [»] | |
1HEZ | X-ray | 2.70 | A/C | 2-107 | [»] | |
1HKL | X-ray | 2.68 | L | 2-107 | [»] | |
1HZH | X-ray | 2.70 | L/M | 2-107 | [»] | |
1I7Z | X-ray | 2.30 | A/C | 2-107 | [»] | |
1MIM | X-ray | 2.60 | L | 2-106 | [»] | |
1N0X | X-ray | 1.80 | L/M | 2-107 | [»] | |
1UCB | X-ray | 2.50 | L | 2-107 | [»] | |
2NY7 | X-ray | 2.30 | L | 2-107 | [»] | |
2O5X | X-ray | 2.05 | L | 2-107 | [»] | |
2O5Y | X-ray | 2.85 | L | 2-107 | [»] | |
2O5Z | X-ray | 2.40 | L | 2-107 | [»] | |
2QQK | X-ray | 2.75 | L | 2-107 | [»] | |
2QQL | X-ray | 3.10 | L | 2-107 | [»] | |
2QQN | X-ray | 2.20 | L | 2-107 | [»] | |
2QSC | X-ray | 2.80 | L | 2-107 | [»] | |
2R56 | X-ray | 2.80 | L/M | 2-104 | [»] | |
2RFX | X-ray | 2.50 | C | 94-102 | [»] | |
2VXQ | X-ray | 1.90 | L | 2-107 | [»] | |
3B2U | X-ray | 2.58 | D/G/K/L/O/R/U/X | 2-105 | [»] | |
3B2V | X-ray | 3.30 | L | 2-105 | [»] | |
3BDY | X-ray | 2.60 | L | 2-107 | [»] | |
3BE1 | X-ray | 2.90 | L | 2-107 | [»] | |
3BKY | X-ray | 2.61 | L | 2-107 | [»] | |
3BN9 | X-ray | 2.17 | C/E | 2-107 | [»] | |
3BQU | X-ray | 3.00 | A | 2-107 | [»] | |
3C08 | X-ray | 2.15 | L | 2-106 | [»] | |
3C09 | X-ray | 3.20 | B/L | 2-106 | [»] | |
3CFJ | X-ray | 2.60 | A/C/E/L | 2-107 | [»] | |
3CFK | X-ray | 2.60 | A/C/E/G/J/L/M/O | 2-107 | [»] | |
3CSY | X-ray | 3.40 | B/D/F/H | 2-104 | [»] | |
3D0L | X-ray | 2.35 | A | 2-106 | [»] | |
3D85 | X-ray | 1.90 | A | 2-107 | [»] | |
3DVG | X-ray | 2.60 | A | 2-107 | [»] | |
3DVN | X-ray | 2.70 | A/L | 2-107 | [»] | |
3EYF | X-ray | 2.30 | A/C | 2-107 | [»] | |
3EYO | X-ray | 2.50 | A/C | 2-107 | [»] | |
3EYQ | X-ray | 2.40 | C | 2-107 | [»] | |
3IU3 | X-ray | 2.90 | B/D/L | 2-106 | [»] | |
3O11 | X-ray | 2.80 | A/L | 2-107 | [»] | |
3QCT | X-ray | 2.15 | L | 3-106 | [»] | |
3QCU | X-ray | 1.98 | L/M | 3-106 | [»] | |
3QCV | X-ray | 2.51 | L/M | 3-106 | [»] | |
3RU8 | X-ray | 2.07 | L | 2-107 | [»] | |
3U0W | X-ray | 2.00 | L | 2-107 | [»] | |
3U7W | X-ray | 2.60 | L | 2-107 | [»] | |
3U7Y | X-ray | 2.45 | L | 2-107 | [»] | |
3VH8 | X-ray | 1.80 | C/F | 94-102 | [»] | |
3WUW | X-ray | 2.00 | C | 94-102 | [»] | |
3X11 | X-ray | 2.15 | C | 94-102 | [»] | |
3X12 | X-ray | 1.80 | C | 94-102 | [»] | |
4D3C | X-ray | 2.62 | L | 2-107 | [»] | |
4D9R | X-ray | 2.42 | D/L | 3-107 | [»] | |
4HIX | X-ray | 2.20 | L | 2-107 | [»] | |
4NM4 | X-ray | 2.65 | L/M | 2-107 | [»] | |
4NM8 | X-ray | 4.00 | L/M/N | 2-107 | [»] | |
4XMP | X-ray | 1.78 | L | 2-107 | [»] | |
4XNY | X-ray | 2.30 | L | 2-107 | [»] | |
4XNZ | X-ray | 3.39 | C/F/L | 2-107 | [»] | |
4XXD | X-ray | 2.41 | A/D | 2-107 | [»] | |
4YDV | X-ray | 2.70 | A/L | 2-107 | [»] | |
5B38 | X-ray | 2.30 | C | 94-102 | [»] | |
5B39 | X-ray | 2.50 | C | 94-102 | [»] | |
5C7K | X-ray | 4.60 | F | 1-107 | [»] | |
5ESV | X-ray | 3.10 | B/D/L | 2-107 | [»] | |
5ESZ | X-ray | 4.19 | B/L | 2-107 | [»] | |
5EWI | X-ray | 1.60 | L | 1-107 | [»] | |
5VEB | X-ray | 2.34 | B/L | 1-107 | [»] | |
5VIY | electron microscopy | 6.20 | G/I | 1-107 | [»] | |
6AU5 | X-ray | 2.48 | A/C | 1-106 | [»] | |
6AXP | X-ray | 2.48 | A/C | 1-106 | [»] | |
6AYN | X-ray | 2.48 | A/C | 1-106 | [»] | |
6AZK | X-ray | 2.48 | A/C | 1-106 | [»] | |
6AZL | X-ray | 2.48 | A/C | 1-106 | [»] | |
6B9Y | X-ray | 2.14 | A | 1-107 | [»] | |
6B9Z | X-ray | 1.82 | A | 1-107 | [»] | |
6BAE | X-ray | 2.14 | A | 1-107 | [»] | |
6BAH | X-ray | 1.90 | A | 1-107 | [»] | |
6DCV | X-ray | 1.90 | A/L | 1-107 | [»] | |
6DCW | X-ray | 2.00 | L | 1-107 | [»] | |
6N2X | X-ray | 3.00 | K/L | 2-106 | [»] | |
6N32 | X-ray | 2.20 | L/M | 2-106 | [»] | |
6N35 | X-ray | 1.75 | K/L | 2-106 | [»] | |
6OGE | electron microscopy | 4.36 | B/D | 1-107 | [»] | |
6OKP | electron microscopy | 3.28 | N/P/R | 1-107 | [»] | |
7CZY | electron microscopy | 3.30 | K/N | 1-107 | [»] | |
7CZZ | electron microscopy | 3.20 | K/M/N | 1-107 | [»] | |
AlphaFoldDBi | P01834 | |||||
SMRi | P01834 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
ComplexPortali | CPX-6744, IgD - Ig kappa immunoglobulin complex, constant regions CPX-6911, IgM - Ig kappa immunoglobulin complex, constant regions CPX-6929, IgG1 - Ig kappa immunoglobulin complex, constant regions CPX-6936, IgG2 - Ig kappa immunoglobulin complex, constant regions CPX-6943, IgG3 - Ig kappa immunoglobulin complex, constant regions CPX-6949, IgG4 - Ig kappa immunoglobulin complex, constant regions CPX-6955, IgA1 - Ig kappa immunoglobulin complex, constant regions CPX-6962, IgA2 - Ig kappa immunoglobulin complex, constant regions CPX-6969, IgE - Ig kappa immunoglobulin complex, constant regions |
IntActi | P01834, 69 interactors |
MINTi | P01834 |
Chemistry databases
DrugBanki | DB07909, (1S,2S,5S)2-(4-GLUTARIDYLBENZYL)-5-PHENYL-1-CYCLOHEXANOL DB07416, (2S)-2-(BUTYRYLOXY)-3-HYDROXYPROPYL NONANOATE DB07716, (4Z)-2,8:7,12:11,15:14,18:17,22-PENTAANHYDRO-4,5,6,9,10,13,19,20,21-NONADEOXY-D-ARABINO-D-ALLO-D-ALLO-DOCOSA-4,9,20-TRIENITOL DB07441, 3-{[(9-CYANO-9,10-DIHYDRO-10-METHYLACRIDIN-9-YL)CARBONYL]AMINO}PROPANOIC ACID DB08562, 4-(4-STYRYL-PHENYLCARBAMOYL)-BUTYRIC ACID DB07882, 4-{4-[2-(1A,7A-DIMETHYL-4-OXY-OCTAHYDRO-1-OXA-4-AZA-CYCLOPROPA[A]NAPHTHALEN-4-YL) -ACETYLAMINO]-PHENYLCARBAMOYL}-BUTYRIC ACID DB07784, [4-(4-ACETYLAMINO-PHENYL)-3,5-DIOXO-4-AZA-TRICYCLO[5.2.2.0 2,6]UNDEC-1-YLCARBAMOYLOXY]-ACETIC ACID DB07375, Etiocholanedione DB08413, METHYL-PHOSPHONIC ACID MONO-(4-NITRO-PHENYL) ESTER DB04688, Methylecgonine DB08289, N-(PARA-GLUTARAMIDOPHENYL-ETHYL)-PIPERIDINIUM-N-OXIDE DB07893, PHENYL[1-(N-SUCCINYLAMINO)PENTYL]PHOSPHONATE DB01851, Tetrabutylammonium Ion DB08647, Trazeolide |
Protein family/group databases
IMGT/GENE-DB | IGKC |
PTM databases
CarbonylDBi | P01834 |
iPTMneti | P01834 |
PhosphoSitePlusi | P01834 |
SwissPalmi | P01834 |
Genetic variation databases
BioMutai | IGKC |
DMDMi | 125145 |
2D gel databases
UCD-2DPAGEi | P01834 |
Proteomic databases
EPDi | P01834 |
jPOSTi | P01834 |
MassIVEi | P01834 |
PeptideAtlasi | P01834 |
PRIDEi | P01834 |
ProteomicsDBi | 51490 |
Protocols and materials databases
ABCDi | P01834, 1 sequenced antibody |
Genome annotation databases
UCSCi | uc061lpw.1, human uc061lpy.1, human |
Organism-specific databases
GeneCardsi | IGKC |
HGNCi | HGNC:5716, IGKC |
MalaCardsi | IGKC |
MIMi | 147200, gene 614102, phenotype |
neXtProti | NX_P01834 |
Orphaneti | 183675, Recurrent infections associated with rare immunoglobulin isotypes deficiency |
GenAtlasi | Search... |
Phylogenomic databases
InParanoidi | P01834 |
PhylomeDBi | P01834 |
Enzyme and pathway databases
PathwayCommonsi | P01834 |
Reactomei | R-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-202733, Cell surface interactions at the vascular wall 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-9664323, FCGR3A-mediated IL10 synthesis R-HSA-9664422, FCGR3A-mediated phagocytosis R-HSA-977606, Regulation of Complement cascade R-HSA-983695, Antigen activates B Cell Receptor (BCR) leading to generation of second messengers |
SignaLinki | P01834 |
Miscellaneous databases
ChiTaRSi | IGKC, human |
EvolutionaryTracei | P01834 |
Pharosi | P01834, Tdark |
PROi | PR:P01834 |
RNActi | P01834, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000211592, Expressed in lymph node and 115 other tissues |
Family and domain databases
Gene3Di | 2.60.40.10, 1 hit |
InterProi | View protein in InterPro IPR007110, Ig-like_dom IPR036179, Ig-like_dom_sf IPR013783, Ig-like_fold IPR003006, Ig/MHC_CS IPR003597, Ig_C1-set |
Pfami | View protein in Pfam PF07654, C1-set, 1 hit |
SMARTi | View protein in SMART SM00407, IGc1, 1 hit |
SUPFAMi | SSF48726, SSF48726, 1 hit |
PROSITEi | View protein in PROSITE PS50835, IG_LIKE, 1 hit PS00290, IG_MHC, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | IGKC_HUMAN | |
Accessioni | P01834Primary (citable) accession number: P01834 Secondary accession number(s): A0A075B6H6, A0A087X130 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | March 15, 2017 | |
Last modified: | May 25, 2022 | |
This is version 201 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 2
Human chromosome 2: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references