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Protein

Ig mu chain C region

Gene

IGHM

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

Functioni

IgM antibodies play an important role in primary defense mechanisms. They have been shown to be involved in early recognition of external invaders like bacteria and viruses, cellular waste and modified self, as well as in recognition and elimination of precancerous and cancerous lesions. The membrane-bound form is found in the majority of normal B-cells alongside with IgD. Membrane-bound IgM induces the phosphorylation of CD79A and CD79B by the Src family of protein tyrosine kinases. It may cause death of cells by apoptosis. It is also found in soluble form, which represents about 30% of the total serum immunoglobulins where it is found almost exclusively as a homopentamer. After the antigen binds to the B-cell receptor, the secreted form is secreted in large amounts.1 Publication

GO - Molecular functioni

GO - Biological processi

  • adaptive immune response Source: UniProtKB
  • antibacterial humoral response Source: UniProtKB
  • B cell receptor signaling pathway Source: GO_Central
  • complement activation, classical pathway Source: GO_Central
  • defense response to Gram-negative bacterium Source: UniProtKB
  • innate immune response Source: UniProtKB
  • phagocytosis, engulfment Source: GO_Central
  • phagocytosis, recognition Source: GO_Central
  • positive regulation of B cell activation Source: GO_Central
Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:ENSG00000130076-MONOMER.
ReactomeiR-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:
Ig mu chain C region
Gene namesi
Name:IGHM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:5541. IGHM.

Subcellular locationi

Isoform 1 :
  • Secreted

  • Note: During differentiation, B-lymphocytes switch from expression of membrane-bound IgM to secretion of IgM.

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • cell surface Source: UniProtKB
  • external side of plasma membrane Source: GO_Central
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • hexameric IgM immunoglobulin complex Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • pentameric IgM immunoglobulin complex Source: UniProtKB
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

Agammaglobulinemia 1, autosomal recessive (AGM1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA primary immunodeficiency characterized by profoundly low or absent serum antibodies and low or absent circulating B cells due to an early block of B-cell development. Affected individuals develop severe infections in the first years of life.
See also OMIM:601495

Organism-specific databases

DisGeNETi3507.
MalaCardsiIGHM.
MIMi601495. phenotype.
Orphaneti33110. Autosomal agammaglobulinemia.

Polymorphism and mutation databases

DMDMi193806374.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000153619‹1 – 452Ig mu chain C regionAdd BLAST›452

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi14Interchain (with light chain)PROSITE-ProRule annotation1 Publication
Disulfide bondi28 ↔ 88PROSITE-ProRule annotation1 Publication
Glycosylationi46N-linked (GlcNAc...) (complex)3 Publications1
Disulfide bondi134 ↔ 197PROSITE-ProRule annotation1 Publication
Glycosylationi209N-linked (GlcNAc...) (complex)1 Publication1
Disulfide bondi214Interchain (with heavy chain)PROSITE-ProRule annotation1 Publication
Disulfide bondi244 ↔ 303PROSITE-ProRule annotation1 Publication
Glycosylationi272N-linked (GlcNAc...)1 Publication1
Glycosylationi279N-linked (GlcNAc...)1 Publication1
Disulfide bondi291Interchain (with heavy chain of another subunit)PROSITE-ProRule annotation1 Publication
Disulfide bondi351 ↔ 413PROSITE-ProRule annotation1 Publication
GlycosylationiCAR_000219439N-linked (GlcNAc...)1 Publication1
Disulfide bondi451Interchain (with heavy chain)PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PeptideAtlasiP01871.
PRIDEiP01871.

2D gel databases

UCD-2DPAGEP01871.

PTM databases

iPTMnetiP01871.
PhosphoSitePlusiP01871.
UniCarbKBiP01871.

Interactioni

Subunit structurei

Immunoglobulin (Ig) molecules consist of two chains, one heavy chain (which can be alpha, delta, epsilon, gamma or mu) and one light chain (which can be kappa or lambda) each consisting of a variable and a constant region. An IgM molecule contains thus a mu heavy chain combined with either a kappa or a lambda light chains. It is found almost exclusively as a homopentamer in the serum. Membrane-bound IgM molecules are non-covalently associated with heterodimer of CD79A and CD79B.

Binary interactionsi

WithEntry#Exp.IntActNotes
CD19P153912EBI-953797,EBI-79902

Protein-protein interaction databases

IntActiP01871. 61 interactors.
MINTiMINT-2860005.

Structurei

Secondary structure

1452
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi178 – 184Combined sources7
Beta strandi196 – 201Combined sources6
Beta strandi206 – 208Combined sources3
Beta strandi210 – 216Combined sources7
Beta strandi223 – 227Combined sources5
Helixi236 – 238Combined sources3
Beta strandi240 – 242Combined sources3
Helixi249 – 251Combined sources3
Beta strandi253 – 258Combined sources6
Turni261 – 264Combined sources4
Beta strandi265 – 272Combined sources8
Helixi275 – 277Combined sources3
Beta strandi279 – 285Combined sources7
Beta strandi287 – 290Combined sources4
Beta strandi300 – 302Combined sources3
Beta strandi316 – 318Combined sources3
Beta strandi345 – 351Combined sources7
Beta strandi354 – 359Combined sources6
Beta strandi363 – 366Combined sources4
Beta strandi386 – 388Combined sources3
Beta strandi391 – 393Combined sources3
Beta strandi396 – 401Combined sources6
Helixi402 – 405Combined sources4
Beta strandi406 – 409Combined sources4
Beta strandi412 – 417Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AGJX-ray2.60H169-428[»]
ProteinModelPortaliP01871.
SMRiP01871.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01871.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 105CH1Add BLAST105
Regioni106 – 217CH2Add BLAST112
Regioni218 – 323CH3Add BLAST106
Regioni324 – 452CH4Add BLAST129

Keywords - Domaini

Immunoglobulin C region, Immunoglobulin domain, Transmembrane

Phylogenomic databases

HOGENOMiHOG000202819.
HOVERGENiHBG005814.
InParanoidiP01871.
PhylomeDBiP01871.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
[Graphical view]
PfamiPF07654. C1-set. 4 hits.
[Graphical view]
SMARTiSM00407. IGc1. 4 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
PROSITEiPS50835. IG_LIKE. 4 hits.
PS00290. IG_MHC. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P01871-1) [UniParc]FASTAAdd to basket
Also known as: Secreted

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
GSASAPTLFP LVSCENSPSD TSSVAVGCLA QDFLPDSITL SWKYKNNSDI
60 70 80 90 100
SSTRGFPSVL RGGKYAATSQ VLLPSKDVMQ GTDEHVVCKV QHPNGNKEKN
110 120 130 140 150
VPLPVIAELP PKVSVFVPPR DGFFGNPRKS KLICQATGFS PRQIQVSWLR
160 170 180 190 200
EGKQVGSGVT TDQVQAEAKE SGPTTYKVTS TLTIKESDWL GQSMFTCRVD
210 220 230 240 250
HRGLTFQQNA SSMCVPDQDT AIRVFAIPPS FASIFLTKST KLTCLVTDLT
260 270 280 290 300
TYDSVTISWT RQNGEAVKTH TNISESHPNA TFSAVGEASI CEDDWNSGER
310 320 330 340 350
FTCTVTHTDL PSPLKQTISR PKGVALHRPD VYLLPPAREQ LNLRESATIT
360 370 380 390 400
CLVTGFSPAD VFVQWMQRGQ PLSPEKYVTS APMPEPQAPG RYFAHSILTV
410 420 430 440 450
SEEEWNTGET YTCVAHEALP NRVTERTVDK STGKPTLYNV SLVMSDTAGT

CY
Length:452
Mass (Da):49,307
Last modified:July 1, 2008 - v3
Checksum:i83E7603C8526CB7A
GO
Isoform 2 (identifier: P01871-2) [UniParc]FASTAAdd to basket
Also known as: Membrane-bound

The sequence of this isoform differs from the canonical sequence as follows:
     433-452: GKPTLYNVSLVMSDTAGTCY → EGEVSADEEGFENLWATASTFIVLFLLSLFYSTTVTLFKVK

Show »
Length:473
Mass (Da):51,790
Checksum:i878EB62603593D37
GO

Sequence cautioni

The sequence CAA33071 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA34971 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Sequence conflicti40L → F in CAA34971 (PubMed:2115996).Curated1
Sequence conflicti40L → F in CAB37838 (Ref. 3) Curated1
Sequence conflicti128R → RS in CAA34971 (PubMed:2115996).Curated1
Sequence conflicti220T → I in CAB37838 (Ref. 3) Curated1
Sequence conflicti414V → VV in CAA34971 (PubMed:2115996).Curated1
Sequence conflicti414V → VV in CAB37838 (Ref. 3) Curated1
Sequence conflicti417E → D in AAB59422 (PubMed:6795593).Curated1
Isoform 2 (identifier: P01871-2)
Sequence conflicti437S → N in AAB59422 (PubMed:6795593).Curated1
Sequence conflicti439D → E in AAB59422 (PubMed:6795593).Curated1
Sequence conflicti448A → T in AAB59422 (PubMed:6795593).Curated1
Sequence conflicti471 – 473KVK → K in AAB59422 (PubMed:6795593).Curated3

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_003903191G → S.1 Publication1
Natural variantiVAR_003904215V → G.Corresponds to variant rs12365dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_034488433 – 452GKPTL…AGTCY → EGEVSADEEGFENLWATAST FIVLFLLSLFYSTTVTLFKV K in isoform 2. 1 PublicationAdd BLAST20

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14940 Genomic DNA. Translation: CAE82013.1.
X14940 Genomic DNA. Translation: CAE82014.1.
X14940 Genomic DNA. Translation: CAA33069.1.
X14940 Genomic DNA. Translation: CAA33070.1.
X14940 Genomic DNA. Translation: CAA33071.1. Different initiation.
X14939 Genomic DNA. Translation: CAA33065.1.
X17115 mRNA. Translation: CAA34971.1. Different initiation.
X57086 mRNA. Translation: CAB37838.1.
K01310 Genomic DNA. Translation: AAB59422.1.
PIRiS14683.
S16510. MHHUM.
UniGeneiHs.510635.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

IGHMbase

IGHM mutation db

IMGT/GENE-DB

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14940 Genomic DNA. Translation: CAE82013.1.
X14940 Genomic DNA. Translation: CAE82014.1.
X14940 Genomic DNA. Translation: CAA33069.1.
X14940 Genomic DNA. Translation: CAA33070.1.
X14940 Genomic DNA. Translation: CAA33071.1. Different initiation.
X14939 Genomic DNA. Translation: CAA33065.1.
X17115 mRNA. Translation: CAA34971.1. Different initiation.
X57086 mRNA. Translation: CAB37838.1.
K01310 Genomic DNA. Translation: AAB59422.1.
PIRiS14683.
S16510. MHHUM.
UniGeneiHs.510635.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AGJX-ray2.60H169-428[»]
ProteinModelPortaliP01871.
SMRiP01871.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP01871. 61 interactors.
MINTiMINT-2860005.

Protein family/group databases

IMGTiSearch...
Search...
Search...
Search...
Search...
Search...
Search...
Search...
Search...

PTM databases

iPTMnetiP01871.
PhosphoSitePlusiP01871.
UniCarbKBiP01871.

Polymorphism and mutation databases

DMDMi193806374.

2D gel databases

UCD-2DPAGEP01871.

Proteomic databases

PeptideAtlasiP01871.
PRIDEiP01871.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

DisGeNETi3507.
GeneCardsiIGHM.
HGNCiHGNC:5541. IGHM.
MalaCardsiIGHM.
MIMi147020. gene.
601495. phenotype.
neXtProtiNX_P01871.
Orphaneti33110. Autosomal agammaglobulinemia.
GenAtlasiSearch...

Phylogenomic databases

HOGENOMiHOG000202819.
HOVERGENiHBG005814.
InParanoidiP01871.
PhylomeDBiP01871.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000130076-MONOMER.
ReactomeiR-HSA-5690714. CD22 mediated BCR regulation.
R-HSA-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Miscellaneous databases

EvolutionaryTraceiP01871.
PROiP01871.
SOURCEiSearch...

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
[Graphical view]
PfamiPF07654. C1-set. 4 hits.
[Graphical view]
SMARTiSM00407. IGc1. 4 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
PROSITEiPS50835. IG_LIKE. 4 hits.
PS00290. IG_MHC. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIGHM_HUMAN
AccessioniPrimary (citable) accession number: P01871
Secondary accession number(s): P20769
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 2008
Last modified: November 2, 2016
This is version 168 of the entry and version 3 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

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.