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Protein

Ig heavy chain V-III region 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 segment of the variable region of immunoglobulins heavy chain that participates to the antigen recognition. Immunoglobulins (Igs), also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound Igs serve as receptors which, upon binding of a specific antigen (Ag), trigger the clonal expansion and differentiation of B lymphocytes into Ig-secreting plasma cells. Secreted Igs 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 region of one heavy chain, together with that of its associated light chain. Thus, each Ig has two antigen binding sites with remarkable affinity for a particular antigen. The variable regions are assembled by a process called V(D)J recombination and can then be subjected to somatic hypermutation after exposure to antigen to allow affinity maturation for a particular Ag (PubMed:20176268, PubMed:17576170).3 Publications

GO - Molecular functioni

  • antigen binding Source: UniProtKB
  • immunoglobulin receptor binding Source: GO_Central
  • 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:
Ig heavy chain V-III region 23Curated
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
Immunoglobulin heavy variable 3-23Imported
Gene namesi
Name:IGHV3-23Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componentsi: Chromosome 14, Unplaced

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
  • immunoglobulin complex, circulating Source: GO_Central
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Polymorphism and mutation databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19193 PublicationsAdd
BLAST
Chaini20 – 11798Ig heavy chain V-III region 23PRO_0000015249Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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 interaction.

Structurei

Secondary structure

1
117
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 265Combined sources
Beta strandi29 – 313Combined sources
Beta strandi37 – 4610Combined sources
Helixi48 – 503Combined sources
Beta strandi53 – 586Combined sources
Turni60 – 623Combined sources
Beta strandi65 – 706Combined sources
Beta strandi74 – 796Combined sources
Turni81 – 866Combined sources
Beta strandi87 – 926Combined sources
Turni93 – 964Combined sources
Beta strandi97 – 1026Combined sources
Helixi107 – 1093Combined sources
Beta strandi111 – 1166Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 20-117.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01764.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – ›117›98Ig-likeAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201E → A AA sequence (PubMed:4139708).Curated
Sequence conflicti29 – 291G → A AA sequence (PubMed:4522793).Curated
Sequence conflicti37 – 371L → G AA sequence (PubMed:4522793).Curated
Sequence conflicti47 – 548TFSSYAMS → SFSTDAMY AA sequence (PubMed:4522793).Curated
Sequence conflicti50 – 534SYAM → RVLS AA sequence (PubMed:4522793).Curated
Sequence conflicti50 – 523SYA → TYV AA sequence (PubMed:409716).Curated
Sequence conflicti50 – 501S → A AA sequence (PubMed:4139708).Curated
Sequence conflicti50 – 501S → T AA sequence (PubMed:4522793).Curated
Sequence conflicti51 – 544YAMS → TSAVY AA sequence (PubMed:4522793).Curated
Sequence conflicti51 – 544YAMS → TTSRF AA sequence (PubMed:4522793).Curated
Sequence conflicti51 – 511Y → S AA sequence (PubMed:4139708).Curated
Sequence conflicti68 – 8417SAISG…ADSVK → AWKYQEASNSHFADTVN AA sequence (PubMed:4522793).CuratedAdd
BLAST
Sequence conflicti68 – 8417SAISG…ADSVK → GWRYEGSSLTHYAVSVQ AA sequence (PubMed:4522793).CuratedAdd
BLAST
Sequence conflicti68 – 7811SAISGSGGSTY → AWKYENGNDKH AA sequence (PubMed:4139708).CuratedAdd
BLAST
Sequence conflicti68 – 7811SAISGSGGSTY → EFRVQGSAISH AA sequence (PubMed:4522793).CuratedAdd
BLAST
Sequence conflicti68 – 7811SAISGSGGSTY → GAIZGLSVSZS AA sequence (PubMed:409716).CuratedAdd
BLAST
Sequence conflicti69 – 8416AISGS…ADSVK → GRLNASSNLHFAVSAQ AA sequence (PubMed:4522793).CuratedAdd
BLAST
Sequence conflicti84 – 852KG → QA AA sequence (PubMed:4522793).Curated
Sequence conflicti84 – 841K → N AA sequence (PubMed:4139708).Curated
Sequence conflicti92 – 932DN → ND AA sequence (PubMed:4139708).Curated
Sequence conflicti92 – 932DN → ND AA sequence (PubMed:4522793).Curated
Sequence conflicti93 – 1019NSKNTLYLQ → DSKNT AA sequence (PubMed:409716).Curated
Sequence conflicti101 – 1011Q → L AA sequence (PubMed:4139708).Curated
Sequence conflicti103 – 1075NSLRA → LSLEP AA sequence (PubMed:4522793).Curated
Sequence conflicti103 – 1064NSLR → LSLQ AA sequence (PubMed:4522793).Curated
Sequence conflicti104 – 1129SLRAEDTAV → GLQAZVSAI AA sequence (PubMed:4139708).Curated
Sequence conflicti104 – 1063SLR → RLE AA sequence (PubMed:4522793).Curated
Sequence conflicti104 – 1063SLR → TGE AA sequence (PubMed:4522793).Curated
Sequence conflicti106 – 1127RAEDTAV → QAZBTAL AA sequence (PubMed:4139708).Curated
Sequence conflicti112 – 1121V → L AA sequence (PubMed:4522793).Curated
Sequence conflicti117 – 1171K → R AA sequence (PubMed:4139708).Curated
Sequence conflicti117 – 1171K → R AA sequence (PubMed:4522793).Curated
Non-terminal residuei117 – 1171

Polymorphismi

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti24 – 241V → L in allele IGHV3-23*02. 1 Publication
VAR_073326
Natural varianti80 – 801A → G in allele IGHV3-23*02. 1 Publication
VAR_073327

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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

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
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. Positions 20-117.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP01764. 1 interaction.

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.

Organism-specific databases

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

Phylogenomic databases

GeneTreeiENSGT00760000118963.
HOVERGENiHBG018013.
InParanoidiP01764.
OMAiFMFISRI.

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

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: September 7, 2016
This is version 134 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.