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Protein

Immunoglobulin kappa variable 2D-28

Gene

IGKV2D-28

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

Functioni

V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. 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:20176268, PubMed:22158414). 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:20176268, PubMed:17576170).3 Publications

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Adaptive immunity, Immunity

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:
Immunoglobulin kappa variable 2D-282 Publications
Alternative name(s):
Ig kappa chain V-II region FR1 Publication
Ig kappa chain V-II region GM6071 Publication
Ig kappa chain V-II region MIL1 Publication
Ig kappa chain V-II region TEW2 Publications
Gene namesi
Name:IGKV2D-282 Publications
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:5799. IGKV2D-28.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

OpenTargetsiENSG00000242534.
ENSG00000244116.
ENSG00000282025.

Polymorphism and mutation databases

DMDMi125784.
125786.
125788.
125790.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 194 PublicationsAdd BLAST19
ChainiPRO_000005975920 – 120Immunoglobulin kappa variable 2D-283 PublicationsAdd BLAST101

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi43 ↔ 113PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PeptideAtlasiP01615.
PRIDEiP01615.

Interactioni

Subunit structurei

Immunoglobulins are composed of two identical heavy chains and two identical light chains, linked by disulfide bonds.1 Publication

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DH4model-L21-120[»]
ProteinModelPortaliP01615.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – ›120Ig-likePROSITE-ProRule annotationAdd BLAST›101

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni21 – 43Framework-11 PublicationAdd BLAST23
Regioni44 – 59Complementarity-determining-11 PublicationAdd BLAST16
Regioni60 – 74Framework-21 PublicationAdd BLAST15
Regioni75 – 81Complementarity-determining-21 Publication7
Regioni82 – 113Framework-31 PublicationAdd BLAST32
Regioni114 – ›120Complementarity-determining-31 Publication›7

Sequence similaritiesi

Contains 1 Ig-like (immunoglobulin-like) domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Immunoglobulin V region, Signal

Phylogenomic databases

GeneTreeiENSGT00860000133683.
HOVERGENiHBG018013.
PhylomeDBiP01615.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00406. IGv. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01615-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLPAQLLGL LMLWVSGSSG DIVMTQSPLS LPVTPGEPAS ISCRSSQSLL
60 70 80 90 100
HSNGYNYLDW YLQKPGQSPQ LLIYLGSNRA SGVPDRFSGS GSGTDFTLKI
110 120
SRVEAEDVGV YYCMQALQTP
Length:120
Mass (Da):12,957
Last modified:November 2, 2016 - v2
Checksum:i0B78BEF46FFB1F97
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti22I → V AA sequence (PubMed:821524).Curated1
Sequence conflicti24M → L AA sequence (Ref. 3) Curated1
Sequence conflicti30S → F AA sequence (PubMed:821524).Curated1
Sequence conflicti35P → L AA sequence (PubMed:821524).Curated1
Sequence conflicti42S → Q AA sequence (PubMed:821524).Curated1
Sequence conflicti48S → N AA sequence (Ref. 3) Curated1
Sequence conflicti50 – 52LHS → VYR AA sequence (PubMed:821524).Curated3
Sequence conflicti51H → Z AA sequence (Ref. 3) Curated1
Sequence conflicti53 – 56NGYN → DGFD AA sequence (PubMed:4596149).Curated4
Sequence conflicti55 – 56YN → BT AA sequence (PubMed:821524).Curated2
Sequence conflicti55Missing AA sequence (Ref. 3) Curated1
Sequence conflicti59D → N AA sequence (PubMed:4596149).Curated1
Sequence conflicti66G → Q in Z00009 (PubMed:6325927).Curated1
Sequence conflicti70Q → E AA sequence (PubMed:821524).Curated1
Sequence conflicti75 – 76LG → AL AA sequence (PubMed:4596149).Curated2
Sequence conflicti76 – 80GSNRA → SSYRD AA sequence (PubMed:821524).Curated5
Sequence conflicti85D → N AA sequence (Ref. 3) Curated1
Sequence conflicti89G → D AA sequence (PubMed:821524).Curated1
Sequence conflicti101S → T AA sequence (PubMed:821524).Curated1
Sequence conflicti104E → Q AA sequence (PubMed:821524).Curated1
Sequence conflicti116A → G in Z00009 (PubMed:6325927).Curated1
Sequence conflicti117 – 119LQT → TZS AA sequence (PubMed:821524).Curated3
Sequence conflicti119T → A AA sequence (PubMed:4596149).Curated1
Non-terminal residuei1201

Polymorphismi

There are several alleles. The sequence shown is that of IMGT allele IGKV2D-28*01.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC233264 Genomic DNA. No translation available.
Z00009 Genomic DNA. No translation available.
PIRiA01886. K2HUFR.
A01887. K2HUML.
A01889. K2HUGM.
A90370. K2HUTW.
UniGeneiHs.449609.

Genome annotation databases

EnsembliENST00000453166; ENSP00000393492; ENSG00000242534.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

IMGT/GENE-DB

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC233264 Genomic DNA. No translation available.
Z00009 Genomic DNA. No translation available.
PIRiA01886. K2HUFR.
A01887. K2HUML.
A01889. K2HUGM.
A90370. K2HUTW.
UniGeneiHs.449609.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DH4model-L21-120[»]
ProteinModelPortaliP01615.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

IMGTiSearch...
Search...

Polymorphism and mutation databases

DMDMi125784.
125786.
125788.
125790.

Proteomic databases

PeptideAtlasiP01615.
PRIDEiP01615.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000453166; ENSP00000393492; ENSG00000242534.

Organism-specific databases

H-InvDBHIX0161623.
HIX0197200.
HGNCiHGNC:5799. IGKV2D-28.
OpenTargetsiENSG00000242534.
ENSG00000244116.
ENSG00000282025.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00860000133683.
HOVERGENiHBG018013.
PhylomeDBiP01615.

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.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00406. IGv. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKVD28_HUMAN
AccessioniPrimary (citable) accession number: P01615
Secondary accession number(s): A0A0A0MTQ6
, P01616, P01617, P06309
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 2, 2016
Last modified: November 30, 2016
This is version 89 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

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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.