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Protein

Immunoglobulin heavy variable 1-2

Gene

IGHV1-2

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

  • antigen binding Source: UniProtKB

GO - Biological processi

  • adaptive immune response Source: UniProtKB-KW
  • immune response Source: UniProtKB
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 heavy variable 1-22 Publications
Alternative name(s):
Ig heavy chain V-I region ND1 Publication
Ig heavy chain V-I region V351 Publication
Gene namesi
Name:IGHV1-22 Publications
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:5550. IGHV1-2.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

OpenTargetsiENSG00000211934.
ENSG00000282550.

Polymorphism and mutation databases

DMDMi11182433.
123808.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 191 PublicationAdd BLAST19
ChainiPRO_000001524520 – 117Immunoglobulin heavy variable 1-21 PublicationAdd BLAST98

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei20Pyrrolidone carboxylic acid1 Publication1
Disulfide bondi41 ↔ 115PROSITE-ProRule annotationCombined sources1 Publication

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Proteomic databases

PeptideAtlasiP23083.
PRIDEiP23083.

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
1WT5X-ray2.10A20-117[»]
ProteinModelPortaliP23083.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23083.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – ›117Ig-likePROSITE-ProRule annotationAdd BLAST›98

Sequence similaritiesi

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

Keywords - Domaini

Immunoglobulin domain, Immunoglobulin V region, Signal

Phylogenomic databases

GeneTreeiENSGT00820000126987.
HOGENOMiHOG000154831.
HOVERGENiHBG018013.

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.

P23083-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDWTWRILFL VAAATGAHSQ VQLVQSGAEV KKPGASVKVS CKASGYTFTG
60 70 80 90 100
YYMHWVRQAP GQGLEWMGWI NPNSGGTNYA QKFQGWVTMT RDTSISTAYM
110
ELSRLRSDDT AVYYCAR
Length:117
Mass (Da):13,085
Last modified:September 7, 2016 - v2
Checksum:iCFCC08BE572F76A8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti16 – 21GAHSQV → RVHSQT (PubMed:6815656).Curated6
Sequence conflicti31K → R (PubMed:6815656).Curated1
Sequence conflicti38K → R (PubMed:6815656).Curated1
Sequence conflicti49 – 56TGYYMHWV → IDSYIHWI AA sequence (Ref. 4) Curated8
Sequence conflicti53 – 54MH → HI AA sequence (Ref. 4) Curated2
Sequence conflicti62Q → H (PubMed:6815656).Curated1
Sequence conflicti67 – 68MG → GV AA sequence (Ref. 4) Curated2
Sequence conflicti67M → V (PubMed:6815656).Curated1
Sequence conflicti81 – 82QK → PR (PubMed:6815656).Curated2
Sequence conflicti93 – 95TSI → ASF (PubMed:6815656).Curated3
Sequence conflicti101 – 104ELSR → DLRS (PubMed:6815656).Curated4
Sequence conflicti110 – 117TAVYYCAR → SAVFYCAK (PubMed:6815656).Curated8
Non-terminal residuei1171

Polymorphismi

There are several alleles. The sequence shown is that of IMGT allele IGHV1-2*04.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07617369W → R in IMGT allele IGHV1-2*01. 2 Publications1
Natural variantiVAR_07617486W → R in IMGT allele IGHV1-2*01. 2 Publications1
Natural variantiVAR_07617589M → S in IMGT allele IGHV1-2*01, requires 2 nucleotide substitutions. 2 Publications1
Natural variantiVAR_076176111A → V in IMGT allele IGHV1-2*01. 2 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07448 Genomic DNA. No translation available.
AC246787 Genomic DNA. No translation available.
PIRiA93933. E1HUND.
S00476. HVHU35.
UniGeneiHs.458446.

Genome annotation databases

EnsembliENST00000390594; ENSP00000375003; ENSG00000211934.
ENST00000633350; ENSP00000488290; ENSG00000282550.
UCSCiuc059gfn.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
X07448 Genomic DNA. No translation available.
AC246787 Genomic DNA. No translation available.
PIRiA93933. E1HUND.
S00476. HVHU35.
UniGeneiHs.458446.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WT5X-ray2.10A20-117[»]
ProteinModelPortaliP23083.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

IMGTiSearch...
Search...

Polymorphism and mutation databases

DMDMi11182433.
123808.

Proteomic databases

PeptideAtlasiP23083.
PRIDEiP23083.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000390594; ENSP00000375003; ENSG00000211934.
ENST00000633350; ENSP00000488290; ENSG00000282550.
UCSCiuc059gfn.1. human.

Organism-specific databases

HGNCiHGNC:5550. IGHV1-2.
OpenTargetsiENSG00000211934.
ENSG00000282550.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00820000126987.
HOGENOMiHOG000154831.
HOVERGENiHBG018013.

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

EvolutionaryTraceiP23083.
PROiP23083.

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 nameiHV102_HUMAN
AccessioniPrimary (citable) accession number: P23083
Secondary accession number(s): A0A087WSX2, P01744
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: September 7, 2016
Last modified: November 30, 2016
This is version 110 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.