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Protein

Immunoglobulin heavy variable 1-2

Gene

IGHV1-2

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

Functioni

V region of the variable domain of immunoglobulin heavy 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: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).4 Publications

Caution

For examples of full-length immunoglobulin heavy chains (of different isotypes) see AC P0DOX2, AC P0DOX3, AC P0DOX4, AC P0DOX5 and AC P0DOX6.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-DBIGHV1-2

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

EuPathDBiHostDB:ENSG00000211934.3
HGNCiHGNC:5550 IGHV1-2
neXtProtiNX_P23083

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

DisGeNETi28474
OpenTargetsiENSG00000211934

Chemistry databases

DrugBankiDB08294 2-(4-HYDROXY-3-NITROPHENYL)ACETIC ACID
DB08295 4-HYDROXY-3-NITROPHENYLACETYL-EPSILON-AMINOCAPROIC ACID ANION
DB08273 4-HYDROXY-5-IODO-3-NITROPHENYLACETYL-EPSILON-AMINOCAPROIC ACID ANION

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
ProteomicsDBi51458
54052

PTM databases

CarbonylDBiP23083

Expressioni

Gene expression databases

BgeeiENSG00000211934

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP23083
SMRiP23083
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23083

Family & Domainsi

Domains and Repeats

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

Keywords - Domaini

Immunoglobulin domain, Immunoglobulin V region, Signal

Phylogenomic databases

GeneTreeiENSGT00820000126987
HOGENOMiHOG000154831
HOVERGENiHBG018013
OMAiISTAYME

Family and domain databases

Gene3Di2.60.40.10, 1 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.

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

Similar proteinsi

Entry informationi

Entry nameiHV102_HUMAN
AccessioniPrimary (citable) accession number: P23083
Secondary accession number(s): A0A087WSX2, P01744
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: September 7, 2016
Last modified: June 20, 2018
This is version 122 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

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

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