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Protein

Immunoglobulin kappa variable 2D-28

Gene

IGKV2D-28

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

Functioni

V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). 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).4 Publications

Caution

For an example of a full-length immunoglobulin kappa light chain see AC P0DOX7.Curated

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

Biological processAdaptive 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-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-977606 Regulation of Complement cascade
R-HSA-983695 Antigen activates B Cell Receptor (BCR) leading to generation of second messengers

Protein family/group databases

IMGT/GENE-DBIGKV2D-28

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

EuPathDBiHostDB:ENSG00000242534.2
HGNCiHGNC:5799 IGKV2D-28
neXtProtiNX_P01615

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

OpenTargetsiENSG00000244116

Chemistry databases

DrugBankiDB08562 4-(4-STYRYL-PHENYLCARBAMOYL)-BUTYRIC ACID

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

PTM databases

iPTMnetiP01615
PhosphoSitePlusiP01615

Expressioni

Gene expression databases

BgeeiENSG00000242534

Interactioni

Subunit structurei

Immunoglobulins are composed of two identical heavy chains and two identical light chains; disulfide-linked.1 Publication

Protein-protein interaction databases

IntActiP01615 2 interactors.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DH4model-L21-120[»]
ProteinModelPortaliP01615
SMRiP01615
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

Keywords - Domaini

Immunoglobulin domain, Immunoglobulin V region, Signal

Phylogenomic databases

GeneTreeiENSGT00860000133683
HOVERGENiHBG018013
PhylomeDBiP01615

Family and domain databases

Gene3Di2.60.40.101 hit
InterProiView protein in InterPro
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR013106 Ig_V-set
PfamiView protein in Pfam
PF07686 V-set, 1 hit
SMARTiView protein in SMART
SM00406 IGv, 1 hit
SUPFAMiSSF48726 SSF48726, 1 hit
PROSITEiView protein in PROSITE
PS50835 IG_LIKE, 1 hit

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

Genome annotation databases

EnsembliENST00000453166; ENSP00000393492; ENSG00000242534

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiKVD28_HUMAN
AccessioniPrimary (citable) accession number: P01615
Secondary accession number(s): A0A0A0MTQ6
, P01616, P01617, P06309
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 2, 2016
Last modified: March 28, 2018
This is version 99 of the entry and version 2 of the sequence. See 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