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Reviewed, UniProtKB/Swiss-Prot P01857 (IGHG1_HUMAN)

Last modified November 25, 2008. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Ig gamma-1 chain C region
Gene names
Name: IGHG1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Subcellular location

Secreted.

Involvement in disease

Chromosomal aberrations involving IGHG1 may be a cause of multiple myeloma [MIM:254500]. 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 G1M(17) allotypic marker, 97-K, and the G1M(1) markers, 239-D and 241-L. KOL and EU sequences have the G1M(3) marker and the G1M (non-1) markers.

Nie also differs in the amidation states of 35, 116, 198, 269 and 272.

EU also differs in the amidation states of residues 155, 166, 177, 195, 198, 269, and 272 and in the order of residues 268-272.

KOL also differs in the amidation states of residues 198, 267 and 272.

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Ontologies

Keywords

   Cellular componentSecreted
   Coding sequence diversityChromosomal rearrangement
   DomainImmunoglobulin C region
Immunoglobulin domain
   PTMGlycoprotein
   Technical term3D-structure
Direct protein sequencing

Gene Ontology (GO)

   Biological processimmune response

Non-traceable author statement. Source: UniProtKB

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

membrane fraction

Non-traceable author statement. Source: UniProtKB

   Molecular functionantigen binding Ref.1

Traceable author statement. Source: UniProtKB

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

FCGR2BP319942EBI-356114,EBI-724784

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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...)
Disulfide bond27 ↔ 83
Disulfide bond103Interchain (with light chain)
Disulfide bond109Interchain (with heavy chain)
Disulfide bond112Interchain (with heavy chain)
Disulfide bond144 ↔ 204
Disulfide bond250 ↔ 308

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

1 .................................................... 330
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P01857-1 [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

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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: 6287432] [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: 5489771] [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: 5530842] [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: 826475] [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: 6884994] [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: 4923144] [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: 1002129] [Abstract]
Cited for: DISULFIDE BONDS.
[8]"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: 7236608] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
[9]"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: 8943038] [Abstract]
Cited for: INVOLVEMENT IN MULTIPLE MYELOMA.
[10]"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: 11972529] [Abstract]
Cited for: INVOLVEMENT IN MULTIPLE MYELOMA.
+Additional computationally mapped references.

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Cross-references

Sequence databases

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

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1AJ7X-ray2.10H1-103[»]
1AQKX-ray1.84H1-103[»]
1D5BX-ray2.80B/H1-101[»]
1D5IX-ray2.00H1-101[»]
1D6VX-ray2.00H1-101[»]
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[»]
1HKLX-ray2.68H1-103[»]
1HZHX-ray2.70H/K1-330[»]
1I7ZX-ray2.30B/D1-103[»]
1L6XX-ray1.65A120-326[»]
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[»]
2DTQX-ray2.00A/B108-330[»]
2DTSX-ray2.20A/B108-330[»]
2GJ7X-ray5.00A/B105-330[»]
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[»]
2RCSX-ray2.10H1-103[»]
3B2UX-ray2.58C/F/H/J/N/Q/T/W1-102[»]
3B2VX-ray3.30H1-102[»]
3BKYX-ray2.61H1-104[»]
3BN9X-ray2.17D/F1-107[»]
3C08X-ray2.15H1-102[»]
3C09X-ray3.20C/H1-102[»]
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[»]
3D0VX-ray2.05B2-105[»]
3D85X-ray1.90B1-108[»]
3DJ9X-ray1.75A119-225[»]
3DROX-ray3.90B2-103[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:29187N.
IntActP01857.

Protein family/group databases

IMGTSearch...

2-D gel databases

Cornea-2DPAGEP01857.
DOSAC-COBS-2DPAGEP01857.
REPRODUCTION-2DPAGEP01857.

Genome annotation databases

EnsemblENSG00000211896. Homo sapiens. [Contig view]

Organism-specific databases

H-InvDBHIX0012029.
HGNCHGNC:5525. IGHG1.
HPACAB008642.
MIM147100. gene.
254500. phenotype.
Orphanet69. Amyloidosis.