Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ig kappa chain V-IV region Len

Gene
N/A
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Bence-Jones protein

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 V-IV region Len
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • extracellular region Source: UniProtKB
  • plasma membrane Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Chemistry

DrugBankiDB02325. Isopropyl Alcohol.

Polymorphism and mutation databases

DMDMi1730075.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›114›114Ig kappa chain V-IV region LenPRO_0000059768Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi23 ↔ 94PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP01625.

Structurei

Secondary structure

1
114
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74Combined sources
Beta strandi9 – 135Combined sources
Beta strandi19 – 279Combined sources
Turni32 – 354Combined sources
Beta strandi39 – 446Combined sources
Beta strandi51 – 555Combined sources
Turni56 – 583Combined sources
Beta strandi68 – 736Combined sources
Beta strandi76 – 838Combined sources
Helixi86 – 883Combined sources
Beta strandi90 – 967Combined sources
Beta strandi98 – 1014Combined sources
Beta strandi108 – 1125Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DH6model-L1-114[»]
1EEQX-ray1.50A/B1-114[»]
1EEUX-ray1.60A/B1-114[»]
1EFQX-ray1.60A1-114[»]
1EK3X-ray1.90A/B1-114[»]
1LVEX-ray1.95A1-114[»]
1QACX-ray1.80A/B1-114[»]
2LVEX-ray2.70A1-114[»]
3LVEX-ray2.00A1-114[»]
4LVEX-ray2.30A/B1-114[»]
5LVEX-ray2.00A1-114[»]
ProteinModelPortaliP01625.
SMRiP01625. Positions 1-114.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01625.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 2323Framework-1Add
BLAST
Regioni24 – 4017Complementarity-determining-1Add
BLAST
Regioni41 – 5515Framework-2Add
BLAST
Regioni56 – 627Complementarity-determining-2
Regioni63 – 9432Framework-3Add
BLAST
Regioni95 – 1017Complementarity-determining-3
Regioni102 – 11312Framework-4Add
BLAST

Keywords - Domaini

Immunoglobulin domain, Immunoglobulin V region

Phylogenomic databases

HOVERGENiHBG018013.
PhylomeDBiP01625.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00406. IGv. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P01625-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
DIVMTQSPDS LAVSLGERAT INCKSSQSVL YSSNSKNYLA WYQQKPGQPP
60 70 80 90 100
KLLIYWASTR ESGVPDRFSG SGSGTDFTLT ISSLQAEDVA VYYCQQYYST
110
PYSFGQGTKL EIKR
Length:114
Mass (Da):12,640
Last modified:October 1, 1996 - v2
Checksum:i0647F1D17F236485
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei114 – 1141

Sequence databases

PIRiA01903. K4HULN.
PH0869.

Cross-referencesi

Sequence databases

PIRiA01903. K4HULN.
PH0869.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DH6model-L1-114[»]
1EEQX-ray1.50A/B1-114[»]
1EEUX-ray1.60A/B1-114[»]
1EFQX-ray1.60A1-114[»]
1EK3X-ray1.90A/B1-114[»]
1LVEX-ray1.95A1-114[»]
1QACX-ray1.80A/B1-114[»]
2LVEX-ray2.70A1-114[»]
3LVEX-ray2.00A1-114[»]
4LVEX-ray2.30A/B1-114[»]
5LVEX-ray2.00A1-114[»]
ProteinModelPortaliP01625.
SMRiP01625. Positions 1-114.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

DrugBankiDB02325. Isopropyl Alcohol.

Polymorphism and mutation databases

DMDMi1730075.

Proteomic databases

PRIDEiP01625.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG018013.
PhylomeDBiP01625.

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

EvolutionaryTraceiP01625.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00406. IGv. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The primary structure of a monoclonic immunoglobulin-L-chain of subgroup IV of the kappa type (Bence-Jones protein Len)."
    Schneider M., Hilschmann N.
    Hoppe-Seyler's Z. Physiol. Chem. 356:507-557(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  2. Salomon A.
    Submitted (AUG-1996) to UniProtKB
    Cited for: SEQUENCE REVISION TO 9.

Entry informationi

Entry nameiKV402_HUMAN
AccessioniPrimary (citable) accession number: P01625
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 103 of the entry and version 2 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 C region of this chain has the INV (3) marker.
This is a Bence-Jones protein.

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.