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P01857 (IGHG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 156. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ig gamma-1 chain C region
Gene names
Name:IGHG1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Subcellular location

Secreted.

Involvement in disease

Multiple myeloma (MM) [MIM:254500]: A malignant tumor of plasma cells usually arising in the bone marrow and characterized by diffuse involvement of the skeletal system, hyperglobulinemia, Bence-Jones proteinuria and anemia. Complications of multiple myeloma are bone pain, hypercalcemia, renal failure and spinal cord compression. The aberrant antibodies that are produced lead to impaired humoral immunity and patients have a high prevalence of infection. Amyloidosis may develop in some patients. Multiple myeloma is part of a spectrum of diseases ranging from monoclonal gammopathy of unknown significance (MGUS) to plasma cell leukemia.
Note: The disease is caused by mutations affecting the gene represented in this entry. A chromosomal aberration involving IGHG1 is found in multiple myeloma. Translocation t(11;14)(q13;q32) with the IgH locus. Translocation t(11;14)(q13;q32) with CCND1; translocation t(4;14)(p16.3;q32.3) with FGFR3; translocation t(6;14)(p25;q32) with IRF4.

Miscellaneous

Nie has the G1M17 allotypic marker, 97-K, and the G1M1 markers, 239-D and 241-L. KOL and EU sequences have the G1M3 marker and the G1M (non-1) markers.

Sequence caution

The sequence AAC82527.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FCGR2BP3199431EBI-356114,EBI-724784

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 330›330Ig gamma-1 chain C region
PRO_0000153578

Regions

Region1 – 9898CH1
Region99 – 11012Hinge
Region111 – 223113CH2
Region224 – 330107CH3

Amino acid modifications

Glycosylation1801N-linked (GlcNAc...) (complex) Ref.8 Ref.9 Ref.10
Disulfide bond27 ↔ 83 Ref.5 Ref.6 Ref.7
Disulfide bond103Interchain (with light chain) Ref.5 Ref.6 Ref.7
Disulfide bond109Interchain (with heavy chain) Ref.5 Ref.6 Ref.7
Disulfide bond112Interchain (with heavy chain) Ref.5 Ref.6 Ref.7
Disulfide bond144 ↔ 204 Ref.5 Ref.6 Ref.7
Disulfide bond250 ↔ 308 Ref.5 Ref.6 Ref.7

Natural variations

Natural variant971K → R in G1M(3) marker.
VAR_003886
Natural variant2391D → E in G1M(non-1) marker.
VAR_003887
Natural variant2411L → M in G1M(non-1) marker.
VAR_003888

Experimental info

Non-terminal residue11

Secondary structure

.................................................................................. 330
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01857 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 3770EE106C2FA33D

FASTA33036,106
        10         20         30         40         50         60 
ASTKGPSVFP LAPSSKSTSG GTAALGCLVK DYFPEPVTVS WNSGALTSGV HTFPAVLQSS 

        70         80         90        100        110        120 
GLYSLSSVVT VPSSSLGTQT YICNVNHKPS NTKVDKKVEP KSCDKTHTCP PCPAPELLGG 

       130        140        150        160        170        180 
PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN 

       190        200        210        220        230        240 
STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE 

       250        260        270        280        290        300 
LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW 

       310        320        330 
QQGNVFSCSV MHEALHNHYT QKSLSLSPGK 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of a human immunoglobulin C gamma1 gene."
Ellison J.W., Berson B.J., Hood L.E.
Nucleic Acids Res. 10:4071-4079(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The covalent structure of a human gamma G-immunoglobulin. VII. Amino acid sequence of heavy-chain cyanogen bromide fragments H1-H4."
Cunningham B.A., Rutishauser U., Gall W.E., Gottlieb P.D., Waxdal M.J., Edelman G.M.
Biochemistry 9:3161-3170(1970) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-135 (MYELOMA PROTEIN EU).
[3]"The covalent structure of a human gamma G-immunoglobulin. 8. Amino acid sequence of heavy-chain cyanogen bromide fragments H5-H7."
Rutishauser U., Cunningham B.A., Bennett C., Konigsberg W.H., Edelman G.M.
Biochemistry 9:3171-3181(1970) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 136-329 (EU).
[4]"The rule of antibody structure. The primary structure of a monoclonal IgG1 immunoglobulin (myeloma protein Nie). III. The chymotryptic peptides of the H-chain, alignment of the tryptic peptides and discussion of the complete structure."
Ponstingl H., Hilschmann N.
Hoppe-Seyler's Z. Physiol. Chem. 357:1571-1604(1976) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE (MYELOMA PROTEIN NIE).
[5]"Three-dimensional structure determination of antibodies. Primary structure of crystallized monoclonal immunoglobulin IgG1 KOL, I."
Schmidt W.E., Jung H.-D., Palm W., Hilschmann N.
Hoppe-Seyler's Z. Physiol. Chem. 364:713-747(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE (MYELOMA PROTEIN KOL), DISULFIDE BONDS.
[6]"The covalent structure of a human gamma G-immunoglobulin. X. Intrachain disulfide bonds."
Gall W.E., Edelman G.M.
Biochemistry 9:3188-3196(1970) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
[7]"Rule of antibody structure. The primary structure of a monoclonal IgG1 immunoglobulin (myeloma protein Nie), I: purification and characterization of the protein, the L- and H-chains, the cyanogen bromide cleavage products, and the disulfide bridges."
Dreker L., Schwarz J., Reichel W., Hilschmann N.
Hoppe-Seyler's Z. Physiol. Chem. 357:1515-1540(1976) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
[8]"Site-specific glycoprofiling of N-linked glycopeptides using MALDI-TOF MS: strong correlation between signal strength and glycoform quantities."
Thaysen-Andersen M., Mysling S., Hojrup P.
Anal. Chem. 81:3933-3943(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-180.
[9]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-180.
Tissue: Liver.
[10]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-180.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution."
Deisenhofer J.
Biochemistry 20:2361-2370(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
[13]"Promiscuous translocations into immunoglobulin heavy chain switch regions in multiple myeloma."
Bergsagel P.L., Chesi M., Nardini E., Brents L.A., Kirby S.L., Kuehl W.M.
Proc. Natl. Acad. Sci. U.S.A. 93:13931-13936(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MULTIPLE MYELOMA.
[14]"Translocations of 14q32 and deletions of 13q14 are common chromosomal abnormalities in systemic amyloidosis."
Harrison C.J., Mazzullo H., Ross F.M., Cheung K.L., Gerrard G., Harewood L., Mehta A., Lachmann H.J., Hawkins P.N., Orchard K.H.
Br. J. Haematol. 117:427-435(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MULTIPLE MYELOMA.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J00228 Genomic DNA. Translation: AAC82527.1. Different initiation.
PIRGHHU. A93433.
UniGeneHs.510635.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AJ7X-ray2.10H1-103[»]
1AQKX-ray1.84H1-103[»]
1BEYX-ray3.25H1-98[»]
1D5BX-ray2.80B/H1-101[»]
1D5IX-ray2.00H1-101[»]
1D6VX-ray2.00H1-101[»]
1DFBX-ray2.70H1-103[»]
1DN2X-ray2.70A/B120-326[»]
1E4KX-ray3.20A/B106-330[»]
1FC1X-ray2.90A/B106-329[»]
1FC2X-ray2.80D106-329[»]
1FCCX-ray3.20A/B121-326[»]
1GAFX-ray1.95H1-103[»]
1H3TX-ray2.40A/B108-330[»]
1H3UX-ray2.40A/B108-330[»]
1H3VX-ray3.10A/B108-330[»]
1H3WX-ray2.85M108-330[»]
1H3XX-ray2.44A/B108-330[»]
1H3YX-ray4.10A/B108-330[»]
1HKLX-ray2.68H1-103[»]
1HZHX-ray2.70H/K1-330[»]
1I7ZX-ray2.30B/D1-103[»]
1L6XX-ray1.65A120-326[»]
1N7MX-ray1.80L2-102[»]
1OP3X-ray1.75H/M1-102[»]
1OQOX-ray2.30A/B119-330[»]
1OQXX-ray2.60A/B119-330[»]
1T83X-ray3.00A/B107-330[»]
1T89X-ray3.50A/B107-330[»]
1VGEX-ray2.00H1-103[»]
2DTSX-ray2.20A/B108-330[»]
2GJ7X-ray5.00A/B106-330[»]
2I5YX-ray2.20H1-101[»]
2IWGX-ray2.35A/D120-326[»]
2J6EX-ray3.00A/B99-330[»]
2JB5X-ray2.80H1-102[»]
2JB6X-ray2.85B/H1-102[»]
2O5XX-ray2.05H1-108[»]
2O5YX-ray2.85H1-108[»]
2O5ZX-ray2.40H1-108[»]
2OSLX-ray2.60A/H1-103[»]
2QADX-ray3.30D/H1-101[»]
2QL1X-ray2.53A106-330[»]
2QQKX-ray2.75H1-107[»]
2QQLX-ray3.10H1-107[»]
2QQNX-ray2.20H1-107[»]
2QR0X-ray3.50B/F/H/L/N/R/T/X1-103[»]
2R56X-ray2.80H/I1-100[»]
2RCJX-ray-C/D/G/H/K/L/O/P/S/T1-326[»]
2RCSX-ray2.10H1-103[»]
2VXQX-ray1.90H1-100[»]
2WAHX-ray2.51A/B120-328[»]
3AGVX-ray2.15A/B120-330[»]
3AVEX-ray2.00A/B108-330[»]
3AY4X-ray2.20A/B108-330[»]
3B2UX-ray2.58C/F/H/J/N/Q/T/W1-102[»]
3B2VX-ray3.30H1-102[»]
3BDYX-ray2.60H1-107[»]
3BE1X-ray2.90H1-107[»]
3BKYX-ray2.61H1-104[»]
3BN9X-ray2.17D/F1-107[»]
3BQUX-ray3.00B2-103[»]
3C08X-ray2.15H1-102[»]
3C09X-ray3.20C/H1-102[»]
3C2SX-ray2.30A106-330[»]
3CFJX-ray2.60B/D/F/H1-104[»]
3CFKX-ray2.60B/D/F/H/I/K/N/P1-104[»]
3CSYX-ray3.40A/C/E/G1-101[»]
3D0LX-ray2.35B2-105[»]
3D0VX-ray2.05B2-105[»]
3D6GX-ray2.30A/B119-328[»]
3D85X-ray1.90B1-108[»]
3DJ9X-ray1.75A119-225[»]
3DNKX-ray2.84A/B119-330[»]
3DO3X-ray2.50A/B119-330[»]
3DROX-ray3.90B2-103[»]
3DRQX-ray2.00B2-103[»]
3DVGX-ray2.60B1-107[»]
3DVNX-ray2.70B/H1-107[»]
3EYFX-ray2.30B/D1-108[»]
3EYOX-ray2.50B/D1-108[»]
3EYQX-ray2.40D1-108[»]
3FJTX-ray2.50A/B119-327[»]
3O11X-ray2.80B/H1-103[»]
3RY6X-ray3.80A/B114-327[»]
3S7GX-ray3.13A/B/C/D104-330[»]
3SGJX-ray2.20A/B106-330[»]
3SGKX-ray2.40A/B106-330[»]
3TV3X-ray1.29H1-104[»]
3TWCX-ray1.65H1-104[»]
3TYGX-ray3.25H1-104[»]
3U0WX-ray2.00H1-103[»]
3U7WX-ray2.60H1-104[»]
3U7YX-ray2.45H1-104[»]
3V7MX-ray2.02A119-327[»]
3V8CX-ray2.77A/B119-330[»]
3V95X-ray2.70A/B119-330[»]
3WJJX-ray2.60A/B99-328[»]
3WJLX-ray2.86A/B99-328[»]
4ACPX-ray2.49A/B101-329[»]
4B7IX-ray2.36A/B120-329[»]
4BM7X-ray1.95A/B106-329[»]
4BSVX-ray1.75A/B106-330[»]
4BSWX-ray2.15A/B106-330[»]
4BYHX-ray2.30A/B106-329[»]
4D9QX-ray2.28E/H2-102[»]
4D9RX-ray2.42E/H2-103[»]
4DAGX-ray3.39H2-98[»]
4DZ8X-ray1.91A/B108-330[»]
4EOWX-ray1.97H1-101[»]
4J12X-ray1.90A119-327[»]
4KU1X-ray1.90A/B120-327[»]
4LLDX-ray1.19A1-103[»]
4LLMX-ray1.75A1-103[»]
4LLQX-ray1.42A1-103[»]
4N0UX-ray3.80E119-327[»]
4NQSX-ray2.64A/B/G/H118-330[»]
4NQTX-ray2.10A118-330[»]
4NQUX-ray2.50A118-330[»]
4O4YX-ray1.85A106-119[»]
4O51X-ray2.20M/N/O/P106-119[»]
ProteinModelPortalP01857.
SMRP01857. Positions 1-330.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29187N.
IntActP01857. 78 interactions.
MINTMINT-120799.
STRING9606.ENSP00000374990.

Chemistry

DrugBankDB00051. Adalimumab.
DB00074. Basiliximab.
DB00111. Daclizumab.
DB00065. Infliximab.
DB00043. Omalizumab.
DB00073. Rituximab.
DB00081. Tositumomab.
DB00072. Trastuzumab.

Protein family/group databases

IMGTSearch...

PTM databases

PhosphoSiteP01857.

Polymorphism databases

DMDM121039.

2D gel databases

DOSAC-COBS-2DPAGEP01857.
REPRODUCTION-2DPAGEP01857.
UCD-2DPAGEP01857.

Proteomic databases

MaxQBP01857.
PaxDbP01857.
PRIDEP01857.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000390549; ENSP00000374991; ENSG00000211896.
ENST00000605583; ENSP00000474225; ENSG00000271292.
UCSCuc001yse.3. human.

Organism-specific databases

GeneCardsGC14M106204.
HGNCHGNC:5525. IGHG1.
MIM147100. gene.
254500. phenotype.
neXtProtNX_P01857.
Orphanet67038. B-cell chronic lymphocytic leukemia.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG313034.
HOVERGENHBG005814.
PhylomeDBP01857.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressP01857.
BgeeP01857.
CleanExHS_IGHG1.
GenevestigatorP01857.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
[Graphical view]
PfamPF07654. C1-set. 3 hits.
[Graphical view]
SMARTSM00407. IGc1. 2 hits.
[Graphical view]
PROSITEPS50835. IG_LIKE. 3 hits.
PS00290. IG_MHC. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP01857.
PROP01857.
SOURCESearch...

Entry information

Entry nameIGHG1_HUMAN
AccessionPrimary (citable) accession number: P01857
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM