Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Immunoglobulin heavy variable 1-46

Gene

IGHV1-46

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 (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

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-DBIGHV1-46.

Names & Taxonomyi

Protein namesi
Recommended name:
Immunoglobulin heavy variable 1-462 Publications
Alternative name(s):
Ig heavy chain V-I region DOT1 Publication
Ig heavy chain V-I region HG31 Publication
Ig heavy chain V-I region Mot1 Publication
Gene namesi
Name:IGHV1-462 Publications
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

EuPathDBiHostDB:ENSG00000211962.2.
HGNCiHGNC:5554. IGHV1-46.

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

OpenTargetsiENSG00000211962.

Polymorphism and mutation databases

DMDMi123799.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 192 PublicationsAdd BLAST19
ChainiPRO_000001524420 – 117Immunoglobulin heavy variable 1-462 PublicationsAdd BLAST98

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi41 ↔ 115PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PeptideAtlasiP01743.
PRIDEiP01743.

PTM databases

iPTMnetiP01743.
PhosphoSitePlusiP01743.

Expressioni

Gene expression databases

BgeeiENSG00000211962.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP01743.
SMRiP01743.
ModBaseiSearch...
MobiDBiSearch...

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.
OMAiEWMGIIN.
PhylomeDBiP01743.

Family and domain databases

InterProiView protein in InterPro
IPR007110. Ig-like_dom.
IPR036179. Ig-like_dom_sf.
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.

P01743-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDWTWRVFCL LAVAPGAHSQ VQLVQSGAEV KKPGASVKVS CKASGYTFTS
60 70 80 90 100
YYMHWVRQAP GQGLEWMGII NPSGGSTSYA QKFQGRVTMT RDTSTSTVYM
110
ELSSLRSEDT AVYYCAR
Length:117
Mass (Da):12,933
Last modified:October 5, 2016 - v2
Checksum:iB3CD92FC7538FFF2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti20Q → A AA sequence (PubMed:7737190).Curated1
Sequence conflicti28 – 32AEVKK → VERKV AA sequence (PubMed:7737190).Curated5
Sequence conflicti35A → S AA sequence (PubMed:3084950).Curated1
Sequence conflicti37 – 39VKV → ARL AA sequence (PubMed:3084950).Curated3
Sequence conflicti38 – 39KV → RI AA sequence (PubMed:7737190).Curated2
Sequence conflicti43A → V AA sequence (PubMed:3084950).Curated1
Sequence conflicti46 – 47YT → DD AA sequence (PubMed:3084950).Curated2
Sequence conflicti47 – 50TFTS → AFEN AA sequence (PubMed:7737190).Curated4
Sequence conflicti50S → T AA sequence (PubMed:3084950).Curated1
Sequence conflicti52 – 53YM → DI AA sequence (PubMed:3084950).Curated2
Sequence conflicti53M → I AA sequence (PubMed:7737190).Curated1
Sequence conflicti62Q → L AA sequence (PubMed:7737190).Curated1
Sequence conflicti62Q → R AA sequence (PubMed:3084950).Curated1
Sequence conflicti68 – 71GIIN → AVVH AA sequence (PubMed:3084950).Curated4
Sequence conflicti70I → F AA sequence (PubMed:7737190).Curated1
Sequence conflicti73 – 81SGGSTSYAQ → VAGAVSSE AA sequence (PubMed:7737190).Curated9
Sequence conflicti74 – 76GGS → DDR AA sequence (PubMed:3084950).Curated3
Sequence conflicti78S → T AA sequence (PubMed:3084950).Curated1
Sequence conflicti80 – 83AQKF → GPRS AA sequence (PubMed:3084950).Curated4
Sequence conflicti84 – 91QGRVTMTR → RDRLVMSS AA sequence (PubMed:7737190).Curated8
Sequence conflicti85G → A AA sequence (PubMed:3084950).Curated1
Sequence conflicti87V → F AA sequence (PubMed:3084950).Curated1
Sequence conflicti89M → V AA sequence (PubMed:3084950).Curated1
Sequence conflicti93T → S AA sequence (PubMed:3084950).Curated1
Sequence conflicti95 – 96TS → AN AA sequence (PubMed:7737190).Curated2
Sequence conflicti96S → T AA sequence (PubMed:3084950).Curated1
Sequence conflicti99 – 104YMELSS → SMQLRN AA sequence (PubMed:7737190).Curated6
Sequence conflicti103 – 104SS → TA AA sequence (PubMed:3084950).Curated2
Sequence conflicti106R → I AA sequence (PubMed:3084950).Curated1
Sequence conflicti108E → A AA sequence (PubMed:3084950).Curated1
Sequence conflicti108E → D AA sequence (PubMed:7737190).Curated1
Sequence conflicti111 – 114AVYY → GRYF AA sequence (PubMed:7737190).Curated4
Sequence conflicti112V → I AA sequence (PubMed:3084950).Curated1
Non-terminal residuei1171

Polymorphismi

There are several alleles. The sequence shown is that of IMGT allele IGHV1-46*01.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07671249T → N in IMGT allele IGHV1-46*02. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00240 Genomic DNA. Translation: AAA52988.1.
AC244452 Genomic DNA. No translation available.
PIRiA02024. HVHUHG.
A02025. HVHUMO.

Genome annotation databases

EnsembliENST00000390622; ENSP00000375031; ENSG00000211962.
ENST00000632105; ENSP00000488713; ENSG00000282131.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiHV146_HUMAN
AccessioniPrimary (citable) accession number: P01743
Secondary accession number(s): A0A0B4J1V4, P06326, P80421
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 5, 2016
Last modified: October 25, 2017
This is version 120 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

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

Keywords - Technical termi

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