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Protein

Immunoglobulin heavy variable 3-23

Gene

IGHV3-23

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 heavy 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:22158414, PubMed:20176268). 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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Adaptive immunity, Immunity

Enzyme and pathway databases

BioCyciZFISH:ENSG00000170716-MONOMER.
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 heavy variable 3-232 Publications
Alternative name(s):
Ig heavy chain V-III region LAY1 Publication
Ig heavy chain V-III region POM1 Publication
Ig heavy chain V-III region TEI1 Publication
Ig heavy chain V-III region TIL1 Publication
Ig heavy chain V-III region TUR1 Publication
Ig heavy chain V-III region VH261 Publication
Ig heavy chain V-III region WAS1 Publication
Ig heavy chain V-III region ZAP1 Publication
Gene namesi
Name:IGHV3-232 Publications
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:5588. IGHV3-23.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • external side of plasma membrane Source: GO_Central
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: UniProtKB
  • immunoglobulin complex, circulating Source: GO_Central
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

OpenTargetsiENSG00000211949.
ENSG00000281962.

Polymorphism and mutation databases

DMDMi123843.
123844.
123854.
123855.
123856.
123857.
123858.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 193 PublicationsAdd BLAST19
ChainiPRO_000001524920 – 117Immunoglobulin heavy variable 3-233 PublicationsAdd BLAST98

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi41 ↔ 115PROSITE-ProRule annotationCombined sources2 Publications

Keywords - PTMi

Disulfide bond

Proteomic databases

PeptideAtlasiP01764.
PRIDEiP01764.

Interactioni

Subunit structurei

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

GO - Molecular functioni

Protein-protein interaction databases

IntActiP01764. 1 interactor.

Structurei

Secondary structure

1117
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi22 – 26Combined sources5
Beta strandi29 – 31Combined sources3
Beta strandi37 – 46Combined sources10
Helixi48 – 50Combined sources3
Beta strandi53 – 58Combined sources6
Turni60 – 62Combined sources3
Beta strandi65 – 70Combined sources6
Beta strandi74 – 79Combined sources6
Turni81 – 86Combined sources6
Beta strandi87 – 92Combined sources6
Turni93 – 96Combined sources4
Beta strandi97 – 102Combined sources6
Helixi107 – 109Combined sources3
Beta strandi111 – 116Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HOUmodel-H20-117[»]
1OHQX-ray2.00A/B20-116[»]
3BN9X-ray2.17D/F21-116[»]
3UPCX-ray2.80A/B/C/D/E/F/G/H/I/J22-117[»]
3ZHDX-ray1.96A/B20-116[»]
3ZHKX-ray1.96A/B20-116[»]
3ZHLX-ray2.47A20-116[»]
4KFZX-ray2.80C/D20-116[»]
ProteinModelPortaliP01764.
SMRiP01764.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01764.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – ›117Ig-likeAdd BLAST›98

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Immunoglobulin V region, Signal

Phylogenomic databases

GeneTreeiENSGT00760000118963.
HOVERGENiHBG018013.
InParanoidiP01764.
OMAiFMFISRI.

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.

P01764-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEFGLSWLFL VAILKGVQCE VQLVESGGGL VQPGGSLRLS CAASGFTFSS
60 70 80 90 100
YAMSWVRQAP GKGLEWVSAI SGSGGSTYYA DSVKGRFTIS RDNSKNTLYL
110
QMNSLRAEDT AVYYCAK
Length:117
Mass (Da):12,582
Last modified:May 27, 2015 - v2
Checksum:iE96D8794FA22F0B5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti20E → A AA sequence (PubMed:4139708).Curated1
Sequence conflicti29G → A AA sequence (PubMed:4522793).Curated1
Sequence conflicti37L → G AA sequence (PubMed:4522793).Curated1
Sequence conflicti47 – 54TFSSYAMS → SFSTDAMY AA sequence (PubMed:4522793).Curated8
Sequence conflicti50 – 53SYAM → RVLS AA sequence (PubMed:4522793).Curated4
Sequence conflicti50 – 52SYA → TYV AA sequence (PubMed:409716).Curated3
Sequence conflicti50S → A AA sequence (PubMed:4139708).Curated1
Sequence conflicti50S → T AA sequence (PubMed:4522793).Curated1
Sequence conflicti51 – 54YAMS → TSAVY AA sequence (PubMed:4522793).Curated4
Sequence conflicti51 – 54YAMS → TTSRF AA sequence (PubMed:4522793).Curated4
Sequence conflicti51Y → S AA sequence (PubMed:4139708).Curated1
Sequence conflicti68 – 84SAISG…ADSVK → AWKYQEASNSHFADTVN AA sequence (PubMed:4522793).CuratedAdd BLAST17
Sequence conflicti68 – 84SAISG…ADSVK → GWRYEGSSLTHYAVSVQ AA sequence (PubMed:4522793).CuratedAdd BLAST17
Sequence conflicti68 – 78SAISGSGGSTY → AWKYENGNDKH AA sequence (PubMed:4139708).CuratedAdd BLAST11
Sequence conflicti68 – 78SAISGSGGSTY → EFRVQGSAISH AA sequence (PubMed:4522793).CuratedAdd BLAST11
Sequence conflicti68S → G AA sequence (PubMed:409716).Curated1
Sequence conflicti69 – 84AISGS…ADSVK → GRLNASSNLHFAVSAQ AA sequence (PubMed:4522793).CuratedAdd BLAST16
Sequence conflicti71 – 78SGSGGSTY → ZGLSVSZS AA sequence (PubMed:409716).Curated8
Sequence conflicti84 – 85KG → QA AA sequence (PubMed:4522793).Curated2
Sequence conflicti84K → N AA sequence (PubMed:4139708).Curated1
Sequence conflicti92 – 93DN → ND AA sequence (PubMed:4139708).Curated2
Sequence conflicti92 – 93DN → ND AA sequence (PubMed:4522793).Curated2
Sequence conflicti93 – 101NSKNTLYLQ → DSKNT AA sequence (PubMed:409716).Curated9
Sequence conflicti101Q → L AA sequence (PubMed:4139708).Curated1
Sequence conflicti103 – 107NSLRA → LSLEP AA sequence (PubMed:4522793).Curated5
Sequence conflicti103 – 106NSLR → LSLQ AA sequence (PubMed:4522793).Curated4
Sequence conflicti104 – 105SL → TG AA sequence (PubMed:4522793).Curated2
Sequence conflicti104S → G AA sequence (PubMed:4139708).Curated1
Sequence conflicti104S → R AA sequence (PubMed:4522793).Curated1
Sequence conflicti106R → E AA sequence (PubMed:4522793).Curated1
Sequence conflicti106R → Q AA sequence (PubMed:4139708).Curated1
Sequence conflicti109 – 112DTAV → VSAI AA sequence (PubMed:4139708).Curated4
Sequence conflicti112V → L AA sequence (PubMed:4522793).Curated1
Sequence conflicti112V → L AA sequence (PubMed:4139708).Curated1
Sequence conflicti117K → R AA sequence (PubMed:4139708).Curated1
Sequence conflicti117K → R AA sequence (PubMed:4522793).Curated1
Non-terminal residuei1171

Polymorphismi

There are several alleles. The sequence shown is that of IMGT allele IGHV3-23*04.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07332624V → L in IMGT allele IGHV3-23*02. 1 Publication1
Natural variantiVAR_07332780A → G in IMGT allele IGHV3-23*02. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35415 Genomic DNA. Translation: AAA58735.1.
AC245166 Genomic DNA. No translation available.
PIRiA02047. H3HU26.
A02048. H3HUTL.
A02057. M3HUPM.
A02058. M3HULY.
A02059. G1HUWS.
A02060. G1HUTE.
A02061. A1HUZP.
A02062. A1HUTU.
UniGeneiHs.719895.

Genome annotation databases

EnsembliENST00000390609; ENSP00000375018; ENSG00000211949.
ENST00000632630; ENSP00000487761; ENSG00000281962.
UCSCiuc059gga.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

IMGT/GENE-DB

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35415 Genomic DNA. Translation: AAA58735.1.
AC245166 Genomic DNA. No translation available.
PIRiA02047. H3HU26.
A02048. H3HUTL.
A02057. M3HUPM.
A02058. M3HULY.
A02059. G1HUWS.
A02060. G1HUTE.
A02061. A1HUZP.
A02062. A1HUTU.
UniGeneiHs.719895.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HOUmodel-H20-117[»]
1OHQX-ray2.00A/B20-116[»]
3BN9X-ray2.17D/F21-116[»]
3UPCX-ray2.80A/B/C/D/E/F/G/H/I/J22-117[»]
3ZHDX-ray1.96A/B20-116[»]
3ZHKX-ray1.96A/B20-116[»]
3ZHLX-ray2.47A20-116[»]
4KFZX-ray2.80C/D20-116[»]
ProteinModelPortaliP01764.
SMRiP01764.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP01764. 1 interactor.

Protein family/group databases

IMGTiSearch...
Search...

Polymorphism and mutation databases

DMDMi123843.
123844.
123854.
123855.
123856.
123857.
123858.

Proteomic databases

PeptideAtlasiP01764.
PRIDEiP01764.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000390609; ENSP00000375018; ENSG00000211949.
ENST00000632630; ENSP00000487761; ENSG00000281962.
UCSCiuc059gga.1. human.

Organism-specific databases

HGNCiHGNC:5588. IGHV3-23.
OpenTargetsiENSG00000211949.
ENSG00000281962.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00760000118963.
HOVERGENiHBG018013.
InParanoidiP01764.
OMAiFMFISRI.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000170716-MONOMER.
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

EvolutionaryTraceiP01764.
PROiP01764.

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 nameiHV323_HUMAN
AccessioniPrimary (citable) accession number: P01764
Secondary accession number(s): A0A087WSX3
, P01765, P01774, P01775, P01776, P01777, P01778, P01779
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 27, 2015
Last modified: November 2, 2016
This is version 136 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 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.