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P01876

- IGHA1_HUMAN

UniProt

P01876 - IGHA1_HUMAN

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Protein

Ig alpha-1 chain C region

Gene

IGHA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Ig alpha is the major immunoglobulin class in body secretions. It may serve both to defend against local infection and to prevent access of foreign antigens to the general immunologic system.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei352 – 3521Multimeric 3-hydroxykynurenine chromophore (covalent); in form alpha-1-microglobulin complex

GO - Molecular functioni

  1. antigen binding Source: UniProtKB

GO - Biological processi

  1. antibacterial humoral response Source: UniProt
  2. glomerular filtration Source: UniProt
  3. immune response Source: UniProtKB
  4. positive regulation of respiratory burst Source: UniProt
  5. protein-chromophore linkage Source: UniProtKB-KW
  6. retina homeostasis Source: UniProt
Complete GO annotation...

Keywords - Ligandi

Chromophore

Enzyme and pathway databases

ReactomeiREACT_160163. Scavenging of heme from plasma.

Protein family/group databases

MEROPSiI43.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Ig alpha-1 chain C region
Gene namesi
Name:IGHA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:5478. IGHA1.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. extracellular region Source: Reactome
  3. extracellular space Source: UniProt
  4. extracellular vesicular exosome Source: UniProtKB
  5. monomeric IgA immunoglobulin complex Source: UniProt
  6. secretory dimeric IgA immunoglobulin complex Source: UniProt
  7. secretory IgA immunoglobulin complex Source: UniProt
Complete GO annotation...

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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 353›353Ig alpha-1 chain C regionPRO_0000153566Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi14 – 14Interchain (with light chain)
Disulfide bondi26 ↔ 85
Disulfide bondi77 ↔ 101
Glycosylationi105 – 1051O-linked (GalNAc...)
Glycosylationi111 – 1111O-linked (GalNAc...)
Glycosylationi113 – 1131O-linked (GalNAc...)
Glycosylationi119 – 1191O-linked (GalNAc...)
Glycosylationi121 – 1211O-linked (GalNAc...)
Disulfide bondi122 – 122Interchain (with heavy chain)
Disulfide bondi123 ↔ 180Or C-123 with C-182
Glycosylationi144 – 1441N-linked (GlcNAc...) (complex)4 Publications
Disulfide bondi147 ↔ 204
Disulfide bondi182 – 182Interchain (with heavy chain) (or with C-180)
Disulfide bondi192 – 192Interchain (with heavy chain of another subunit)Curated
Disulfide bondi250 ↔ 313
Glycosylationi340 – 3401N-linked (GlcNAc...) (complex)1 Publication
Disulfide bondi352 – 352Interchain (with J chain); in oligomeric form

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.
N- and O-glycosylated. N-glycan at Asn-144: Hex5HexNAc4.4 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP01876.
PRIDEiP01876.

PTM databases

PhosphoSiteiP01876.

Expressioni

Gene expression databases

BgeeiP01876.
ExpressionAtlasiP01876. baseline.
GenevestigatoriP01876.

Interactioni

Subunit structurei

Monomeric or polymeric.

Protein-protein interaction databases

IntActiP01876. 44 interactions.
STRINGi9606.ENSP00000374989.

Structurei

Secondary structure

1
353
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi128 – 1303Combined sources
Helixi134 – 1396Combined sources
Beta strandi146 – 1494Combined sources
Beta strandi162 – 1643Combined sources
Beta strandi185 – 1884Combined sources
Turni190 – 1923Combined sources
Helixi193 – 1986Combined sources
Beta strandi201 – 2066Combined sources
Beta strandi215 – 2206Combined sources
Beta strandi229 – 2335Combined sources
Turni237 – 2415Combined sources
Beta strandi242 – 25817Combined sources
Beta strandi261 – 2666Combined sources
Helixi273 – 2753Combined sources
Beta strandi276 – 2783Combined sources
Beta strandi287 – 2893Combined sources
Beta strandi292 – 30110Combined sources
Helixi302 – 3076Combined sources
Beta strandi311 – 3166Combined sources
Beta strandi323 – 3253Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IGAX-ray-A/B1-353[»]
1OW0X-ray3.10A/B122-335[»]
2QEJX-ray3.20A/B123-336[»]
3CHNX-ray-A/B/C/D2-353[»]
ProteinModelPortaliP01876.
SMRiP01876. Positions 1-102, 123-331.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01876.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 9893Ig-like 1Add
BLAST
Domaini125 – 22096Ig-like 2Add
BLAST
Domaini228 – 330103Ig-like 3Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin C region, Immunoglobulin domain, Repeat

Phylogenomic databases

eggNOGiNOG27314.
GeneTreeiENSGT00530000063726.
HOVERGENiHBG005814.
InParanoidiP01876.
OMAiEVDGTCY.
PhylomeDBiP01876.
TreeFamiTF334176.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
[Graphical view]
PfamiPF07654. C1-set. 2 hits.
[Graphical view]
SMARTiSM00407. IGc1. 2 hits.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 3 hits.
PS00290. IG_MHC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Sequence cautioni

The sequence AAC82528.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Sequence conflicti163 – 1653TPS → PST AA sequence (PubMed:107164)Curated
Sequence conflicti176 – 1761E → B AA sequence (PubMed:809331)Curated
Sequence conflicti190 – 1901P → S AA sequence (PubMed:809331)Curated
Sequence conflicti227 – 2271R → H AA sequence (PubMed:809331)Curated
Sequence conflicti231 – 2311H → R AA sequence (PubMed:809331)Curated
Sequence conflicti290 – 2901T → E AA sequence (PubMed:809331)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti176 – 1761E → D.
Corresponds to variant rs1407 [ dbSNP | Ensembl ].
VAR_014602

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00220 Genomic DNA. Translation: AAC82528.1. Different initiation.
PIRiA22360. A1HU.
UniGeneiHs.699841.

Genome annotation databases

EnsembliENST00000390547; ENSP00000374989; ENSG00000211895.

Polymorphism databases

DMDMi113584.

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

IMGT/GENE-DB

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00220 Genomic DNA. Translation: AAC82528.1 . Different initiation.
PIRi A22360. A1HU.
UniGenei Hs.699841.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IGA X-ray - A/B 1-353 [» ]
1OW0 X-ray 3.10 A/B 122-335 [» ]
2QEJ X-ray 3.20 A/B 123-336 [» ]
3CHN X-ray - A/B/C/D 2-353 [» ]
ProteinModelPortali P01876.
SMRi P01876. Positions 1-102, 123-331.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P01876. 44 interactions.
STRINGi 9606.ENSP00000374989.

Protein family/group databases

MEROPSi I43.001.
IMGTi Search...

PTM databases

PhosphoSitei P01876.

Polymorphism databases

DMDMi 113584.

Proteomic databases

PaxDbi P01876.
PRIDEi P01876.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000390547 ; ENSP00000374989 ; ENSG00000211895 .

Organism-specific databases

GeneCardsi GC14M106171.
HGNCi HGNC:5478. IGHA1.
MIMi 146900. gene.
neXtProti NX_P01876.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG27314.
GeneTreei ENSGT00530000063726.
HOVERGENi HBG005814.
InParanoidi P01876.
OMAi EVDGTCY.
PhylomeDBi P01876.
TreeFami TF334176.

Enzyme and pathway databases

Reactomei REACT_160163. Scavenging of heme from plasma.

Miscellaneous databases

EvolutionaryTracei P01876.
PROi P01876.
SOURCEi Search...

Gene expression databases

Bgeei P01876.
ExpressionAtlasi P01876. baseline.
Genevestigatori P01876.

Family and domain databases

Gene3Di 2.60.40.10. 3 hits.
InterProi IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
[Graphical view ]
Pfami PF07654. C1-set. 2 hits.
[Graphical view ]
SMARTi SM00407. IGc1. 2 hits.
[Graphical view ]
PROSITEi PS50835. IG_LIKE. 3 hits.
PS00290. IG_MHC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mechanisms of divergence and convergence of the human immunoglobulin alpha 1 and alpha 2 constant region gene sequences."
    Flanagan J.G., Lefranc M.-P., Rabbitts T.H.
    Cell 36:681-688(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Primary structure of a human IgA1 immunoglobulin. IV. Streptococcal IgA1 protease, digestion, Fab and Fc fragments, and the complete amino acid sequence of the alpha 1 heavy chain."
    Putnam F.W., Liu Y.-S.V., Low T.L.K.
    J. Biol. Chem. 254:2865-2874(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE (MYELOMA PROTEIN BUR), DISULFIDE BONDS.
  3. "The primary structure of a monoclonal IgA-immunoglobulin (IgA Tro.), II. The amino acid sequence of the H-chain, alpha-type, subgroup III; structure of the complete IgA-molecule."
    Kratzin H., Altevogt P., Ruban E., Kortt A., Staroscik K., Hilschmann N.
    Hoppe-Seyler's Z. Physiol. Chem. 356:1337-1342(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE (MYELOMA PROTEIN TRO).
  4. "Rule of antibody structure. Primary structure of a human monoclonal IgA-immunoglobulin (myeloma protein Tro). VII. Purification and characterization of the disulfide bridges."
    Yang C.-Y., Kratzin H., Gotz H., Hilschmann N.
    Hoppe-Seyler's Z. Physiol. Chem. 360:1919-1940(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  5. "Location of a novel type of interpolypeptide chain linkage in the human protein HC-IgA complex (HC-IgA) and identification of a heterogeneous chromophore associated with the complex."
    Calero M., Escribano J., Grubb A., Mendez E.
    J. Biol. Chem. 269:384-389(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 345-353, BINDING TO CHROMOPHORE.
  6. "The structure and function of human IgA."
    Kerr M.A.
    Biochem. J. 271:285-296(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  7. "IRTA1 and IRTA2, novel immunoglobulin superfamily receptors expressed in B cells and involved in chromosome 1q21 abnormalities in B cell malignancy."
    Hatzivassiliou G., Miller I., Takizawa J., Palanisamy N., Rao P.H., Iida S., Tagawa S., Taniwaki M., Russo J., Neri A., Cattoretti G., Clynes R., Mendelsohn C., Chaganti R.S.K., Dalla-Favera R.
    Immunity 14:277-289(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL TRANSLOCATION WITH FCRL4.
  8. Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-144.
    Tissue: Bile.
  9. Cited for: GLYCOSYLATION AT ASN-144 AND ASN-340.
  10. "Enrichment of glycopeptides for glycan structure and attachment site identification."
    Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
    Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-144, STRUCTURE OF CARBOHYDRATES.
    Tissue: Cerebrospinal fluid.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
    Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
    Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-144, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiIGHA1_HUMAN
AccessioniPrimary (citable) accession number: P01876
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1991
Last modified: November 26, 2014
This is version 151 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3