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Protein

Immunoglobulin heavy constant alpha 1

Gene

IGHA1

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

Functioni

Constant region of immunoglobulin heavy chains. 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:17576170, PubMed:20176268). Ig alpha is the major immunoglobulin class in body secretions (PubMed:2241915).4 Publications

Caution

For an example of a full-length immunoglobulin alpha heavy chain see AC P0DOX2.Curated

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei352Multimeric 3-hydroxykynurenine chromophore (covalent); in form alpha-1-microglobulin complex1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processAdaptive immunity, Immunity
LigandChromophore

Enzyme and pathway databases

ReactomeiR-HSA-202733 Cell surface interactions at the vascular wall
R-HSA-2168880 Scavenging of heme from plasma

Protein family/group databases

IMGT/GENE-DBIGHA1

Names & Taxonomyi

Protein namesi
Recommended name:
Immunoglobulin heavy constant alpha 12 Publications
Alternative name(s):
Ig alpha-1 chain C regionCurated
Ig alpha-1 chain C region BUR1 Publication
Ig alpha-1 chain C region TRO1 Publication
Gene namesi
Name:IGHA12 Publications
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

EuPathDBiHostDB:ENSG00000211895.4
HGNCiHGNC:5478 IGHA1
MIMi146900 gene
neXtProtiNX_P01876

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

Involvement in diseasei

A chromosomal aberration involving IGHA1 is found in multiple myeloma (MM) cell lines. Translocation t(1;14)(q21;q32) that forms a FCRL4-IGHA1 fusion protein.1 Publication

Organism-specific databases

DisGeNETi3493
OpenTargetsiENSG00000211895

Polymorphism and mutation databases

DMDMi113584

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000153566‹1 – 353Immunoglobulin heavy constant alpha 1Add BLAST›353

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi14Interchain (with light chain)1 Publication
Disulfide bondi26 ↔ 85PROSITE-ProRule annotation
Disulfide bondi77 ↔ 101
Glycosylationi105O-linked (GalNAc...) serine1
Glycosylationi111O-linked (GalNAc...) serine1
Glycosylationi113O-linked (GalNAc...) serine1
Glycosylationi119O-linked (GalNAc...) serine1
Glycosylationi121O-linked (GalNAc...) serine1
Disulfide bondi122Interchain (with heavy chain)1 Publication
Disulfide bondi123 ↔ 180Or C-123 with C-1821 Publication
Glycosylationi144N-linked (GlcNAc...) (complex) asparagine4 Publications1
Disulfide bondi147 ↔ 204PROSITE-ProRule annotation
Disulfide bondi182Interchain (with heavy chain) (or with C-180)1 Publication
Disulfide bondi192Interchain (with heavy chain of another subunit)1 Publication
Disulfide bondi250 ↔ 313PROSITE-ProRule annotation
Glycosylationi340N-linked (GlcNAc...) (complex) asparagine1 Publication1
Disulfide bondi352Interchain (with J chain); in oligomeric form1 Publication

Post-translational modificationi

3-Hydroxykynurenine, an oxidized tryptophan metabolite that is common in biological fluids, reacts with alpha-1-microglobulin to form heterogeneous polycyclic chromophores including hydroxanthommatin. The chromophore reacts with accessible cysteines forming non-reducible thioether cross-links with Ig alpha-1 chain C region Cys-352.1 Publication
N- and O-glycosylated. N-glycan at Asn-144: Hex5HexNAc4.4 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiP01876
PeptideAtlasiP01876
PRIDEiP01876
ProteomicsDBi51500

PTM databases

CarbonylDBiP01876
GlyConnecti820
iPTMnetiP01876
PhosphoSitePlusiP01876
UniCarbKBiP01876

Expressioni

Gene expression databases

BgeeiENSG00000211895 Expressed in 88 organ(s), highest expression level in lung
GenevisibleiP01876 HS

Interactioni

Subunit structurei

Immunoglobulins are composed of two identical heavy chains and two identical light chains; disulfide-linked (PubMed:20176268). Monomeric or polymeric (PubMed:2241915).2 Publications

Protein-protein interaction databases

IntActiP01876, 48 interactors
MINTiP01876

Structurei

Secondary structure

1353
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP01876
SMRiP01876
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01876

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 98Ig-like 1PROSITE-ProRule annotationAdd BLAST93
Domaini125 – 220Ig-like 2PROSITE-ProRule annotationAdd BLAST96
Domaini228 – 330Ig-like 3PROSITE-ProRule annotationAdd BLAST103

Keywords - Domaini

Immunoglobulin C region, Immunoglobulin domain

Phylogenomic databases

GeneTreeiENSGT00530000063726
HOVERGENiHBG005814
InParanoidiP01876
OMAiYTNPSQD
PhylomeDBiP01876
TreeFamiTF334176

Family and domain databases

Gene3Di2.60.40.10, 3 hits
InterProiView protein in InterPro
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR003006 Ig/MHC_CS
IPR003597 Ig_C1-set
PfamiView protein in Pfam
PF07654 C1-set, 2 hits
SMARTiView protein in SMART
SM00407 IGc1, 2 hits
SUPFAMiSSF48726 SSF48726, 3 hits
PROSITEiView protein in PROSITE
PS50835 IG_LIKE, 3 hits
PS00290 IG_MHC, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.iShow all

P01876-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
ASPTSPKVFP LSLCSTQPDG NVVIACLVQG FFPQEPLSVT WSESGQGVTA
60 70 80 90 100
RNFPPSQDAS GDLYTTSSQL TLPATQCLAG KSVTCHVKHY TNPSQDVTVP
110 120 130 140 150
CPVPSTPPTP SPSTPPTPSP SCCHPRLSLH RPALEDLLLG SEANLTCTLT
160 170 180 190 200
GLRDASGVTF TWTPSSGKSA VQGPPERDLC GCYSVSSVLP GCAEPWNHGK
210 220 230 240 250
TFTCTAAYPE SKTPLTATLS KSGNTFRPEV HLLPPPSEEL ALNELVTLTC
260 270 280 290 300
LARGFSPKDV LVRWLQGSQE LPREKYLTWA SRQEPSQGTT TFAVTSILRV
310 320 330 340 350
AAEDWKKGDT FSCMVGHEAL PLAFTQKTID RLAGKPTHVN VSVVMAEVDG

TCY
Length:353
Mass (Da):37,655
Last modified:February 1, 1991 - v2
Checksum:iEBA11ECB7E85DB21
GO

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A286YEY1A0A286YEY1_HUMAN
Immunoglobulin heavy constant alpha...
IGHA1
398Annotation score:

Sequence cautioni

The sequence AAC82528 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Sequence conflicti163 – 165TPS → PST AA sequence (PubMed:107164).Curated3
Sequence conflicti176E → B AA sequence (PubMed:809331).Curated1
Sequence conflicti190P → S AA sequence (PubMed:809331).Curated1
Sequence conflicti227R → H AA sequence (PubMed:809331).Curated1
Sequence conflicti231H → R AA sequence (PubMed:809331).Curated1
Sequence conflicti290T → E AA sequence (PubMed:809331).Curated1

Polymorphismi

There are several alleles. The sequence shown is that of IMGT allele IGHA1*02.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_014602176E → D. Corresponds to variant dbSNP:rs1407Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00220 Genomic DNA Translation: AAC82528.1 Different initiation.
AL901608 Genomic DNA No translation available.
AL928768 Genomic DNA No translation available.
PIRiA22360 A1HU
UniGeneiHs.699841

Genome annotation databases

EnsembliENST00000390547; ENSP00000374989; ENSG00000211895
ENST00000633714; ENSP00000488021; ENSG00000282633
UCSCiuc059gcy.1 human

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiIGHA1_HUMAN
AccessioniPrimary (citable) accession number: P01876
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1991
Last modified: September 12, 2018
This is version 184 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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