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P01834 (IGKC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ig kappa chain C region
Gene names
Name:IGKC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length106 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Involvement in disease

Immunoglobulin kappa light chain deficiency (IGKCD) [MIM:614102]: A disease characterized by the complete absence of immunoglobulin kappa chains.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11

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.

Sequence similarities

Contains 1 Ig-like (immunoglobulin-like) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 106›106Ig kappa chain C region
PRO_0000153596

Regions

Domain5 – 10298Ig-like

Amino acid modifications

Disulfide bond26 ↔ 86 Ref.2
Disulfide bond106Interchain (with a heavy chain) Ref.2

Natural variations

Natural variant401W → R in IGKCD. Ref.11
VAR_066403
Natural variant831V → L in INV(1,2) marker.
VAR_003897

Experimental info

Sequence conflict141D → N AA sequence Ref.7
Sequence conflict141D → N AA sequence Ref.8
Sequence conflict571E → Q AA sequence Ref.5
Sequence conflict571E → Q AA sequence Ref.6
Non-terminal residue11

Secondary structure

........................ 106
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01834 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 51984D1FDD372CE8

FASTA10611,609
        10         20         30         40         50         60 
TVAAPSVFIF PPSDEQLKSG TASVVCLLNN FYPREAKVQW KVDNALQSGN SQESVTEQDS 

        70         80         90        100 
KDSTYSLSST LTLSKADYEK HKVYACEVTH QGLSSPVTKS FNRGEC 

« Hide

References

« Hide 'large scale' references
[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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J00241 Genomic DNA. Translation: AAA58989.1.
PIRK3HU. B90562.
UniGeneHs.449609.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
4D9RX-ray2.42D/L2-106[»]
4HIXX-ray2.20L1-106[»]
4NM4X-ray2.65L/M1-106[»]
4NM8X-ray4.00L/M/N1-106[»]
ProteinModelPortalP01834.
SMRP01834. Positions 1-103.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP01834. 36 interactions.
MINTMINT-159227.
STRING9606.ENSP00000374777.

Protein family/group databases

IMGTSearch...

PTM databases

PhosphoSiteP01834.

Polymorphism databases

DMDM125145.

2D gel databases

UCD-2DPAGEP01834.

Proteomic databases

MaxQBP01834.
PaxDbP01834.
PRIDEP01834.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GeneCardsGC02M089156.
H-InvDBHIX0161619.
HGNCHGNC:5716. IGKC.
MIM147200. gene.
614102. phenotype.
neXtProtNX_P01834.
Orphanet183675. Recurrent infections associated with rare immunoglobulin isotypes deficiency.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG116969.
HOGENOMHOG000059537.
HOVERGENHBG039526.
InParanoidP01834.
OMAWATDSSP.
PhylomeDBP01834.

Enzyme and pathway databases

ReactomeREACT_160300. Binding and Uptake of Ligands by Scavenger Receptors.
REACT_6900. Immune System.

Gene expression databases

BgeeP01834.
CleanExHS_IGKC.
GenevestigatorP01834.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
[Graphical view]
PfamPF07654. C1-set. 1 hit.
[Graphical view]
SMARTSM00407. IGc1. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP01834.
PROP01834.
SOURCESearch...

Entry information

Entry nameIGKC_HUMAN
AccessionPrimary (citable) accession number: P01834
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM