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-I region AU

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-I region AU
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

Polymorphism and mutation databases

DMDMi125758.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›108›108Ig kappa chain V-I region AUPRO_0000059738Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi23 ↔ 88PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PeptideAtlasiP01594.
PRIDEiP01594.

Interactioni

Protein-protein interaction databases

DIPiDIP-58572N.

Structurei

Secondary structure

1
108
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74Combined sources
Beta strandi9 – 135Combined sources
Beta strandi19 – 279Combined sources
Beta strandi33 – 386Combined sources
Beta strandi44 – 496Combined sources
Turni50 – 523Combined sources
Beta strandi62 – 676Combined sources
Beta strandi70 – 778Combined sources
Helixi80 – 823Combined sources
Beta strandi84 – 907Combined sources
Beta strandi92 – 954Combined sources
Beta strandi102 – 1065Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B0WX-ray1.80A/B/C1-108[»]
1JV5X-ray2.20A1-107[»]
1QP1X-ray2.06A/B/C1-107[»]
2Q20X-ray1.30A/B1-107[»]
3CDCX-ray1.53A/B1-107[»]
3CDFX-ray1.53A/B/C/D/E/F1-107[»]
3CDYX-ray2.43A/B1-107[»]
4K07X-ray2.83A/B/C/D/E/F/G/H/I/J1-107[»]
ProteinModelPortaliP01594.
SMRiP01594. Positions 1-107.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01594.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 2323Framework-1Add
BLAST
Regioni24 – 3411Complementarity-determining-1Add
BLAST
Regioni35 – 4915Framework-2Add
BLAST
Regioni50 – 567Complementarity-determining-2
Regioni57 – 8832Framework-3Add
BLAST
Regioni89 – 979Complementarity-determining-3
Regioni98 – 10710Framework-4

Keywords - Domaini

Immunoglobulin domain, Immunoglobulin V region

Phylogenomic databases

HOVERGENiHBG018013.
PhylomeDBiP01594.

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.

P01594-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
DIQMTQSPSS LSASVGDRVT ITCQASQDIS DYLNWYQQKP GKAPKLLIYD
60 70 80 90 100
ASNLESGVPS RFSGGGSGAH FTFTISSLQP EDIATYYCQQ YDYLPWTFGQ

GTKVEIKR
Length:108
Mass (Da):11,939
Last modified:July 21, 1986 - v1
Checksum:iE8011187EE6F6FB9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei108 – 1081

Sequence databases

PIRiA91653. K1HUAU.
S42265.

Cross-referencesi

Sequence databases

PIRiA91653. K1HUAU.
S42265.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B0WX-ray1.80A/B/C1-108[»]
1JV5X-ray2.20A1-107[»]
1QP1X-ray2.06A/B/C1-107[»]
2Q20X-ray1.30A/B1-107[»]
3CDCX-ray1.53A/B1-107[»]
3CDFX-ray1.53A/B/C/D/E/F1-107[»]
3CDYX-ray2.43A/B1-107[»]
4K07X-ray2.83A/B/C/D/E/F/G/H/I/J1-107[»]
ProteinModelPortaliP01594.
SMRiP01594. Positions 1-107.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-58572N.

Polymorphism and mutation databases

DMDMi125758.

Proteomic databases

PeptideAtlasiP01594.
PRIDEiP01594.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

H-InvDBHIX0161621.

Phylogenomic databases

HOVERGENiHBG018013.
PhylomeDBiP01594.

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

EvolutionaryTraceiP01594.

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...

Entry informationi

Entry nameiKV102_HUMAN
AccessioniPrimary (citable) accession number: P01594
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 6, 2016
This is version 106 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 structure of the V region was determined by molecular replacement methods using the known structure of the V region of the kappa chain REI.
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.