P01857 (IGHG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ig gamma-1 chain C region

Gene names

Name:

IGHG1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	330 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Chromosomal rearrangement
Domain	Immunoglobulin C region Immunoglobulin domain
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Fc-gamma receptor signaling pathway involved in phagocytosis Traceable author statement. Source: Reactome complement activation, classical pathway Traceable author statement. Source: Reactome innate immune response Traceable author statement. Source: Reactome
Cellular_component	extracellular region Traceable author statement. Source: Reactome membrane Non-traceable author statement. Source: UniProtKB
Molecular_function	antigen binding Traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FCGR2B	P31994	31	EBI-356114,EBI-724784

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

‹1 – 330

›330

Ig gamma-1 chain C region

PRO_0000153578

Regions

Region

1 – 98

98

CH1

Region

99 – 110

12

Hinge

Region

111 – 223

113

CH2

Region

224 – 330

107

CH3

Amino acid modifications

Glycosylation

180

1

N-linked (GlcNAc...) Ref.8

Disulfide bond

27 ↔ 83

Ref.5 Ref.6 Ref.7

Disulfide bond

103

Interchain (with light chain) Ref.5 Ref.6 Ref.7

Disulfide bond

109

Interchain (with heavy chain) Ref.5 Ref.6 Ref.7

Disulfide bond

112

Interchain (with heavy chain) Ref.5 Ref.6 Ref.7

Disulfide bond

144 ↔ 204

Ref.5 Ref.6 Ref.7

Disulfide bond

250 ↔ 308

Ref.5 Ref.6 Ref.7

Natural variations

Natural variant

97

1

K → R in G1M(3) marker.

VAR_003886

Natural variant

239

1

D → E in G1M(non-1) marker.

VAR_003887

Natural variant

241

1

L → M in G1M(non-1) marker.

VAR_003888

Experimental info

Non-terminal residue

1

1

Secondary structure

1

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330

Helix Strand Turn

Details...

Beta strand

7 – 11

5

Helix

15 – 17

3

Beta strand

20 – 35

16

Beta strand

38 – 41

4

Helix

42 – 44

3

Beta strand

50 – 52

3

Beta strand

63 – 72

10

Helix

73 – 75

3

Turn

76 – 78

3

Beta strand

81 – 87

7

Helix

88 – 90

3

Beta strand

92 – 98

7

Helix

115 – 117

3

Beta strand

122 – 126

5

Helix

130 – 134

5

Beta strand

135 – 138

4

Beta strand

141 – 149

9

Beta strand

151 – 153

3

Beta strand

157 – 162

6

Beta strand

165 – 167

3

Beta strand

171 – 173

3

Beta strand

176 – 178

3

Beta strand

179 – 181

3

Beta strand

183 – 190

8

Helix

193 – 197

5

Beta strand

202 – 207

6

Beta strand

211 – 213

3

Beta strand

215 – 219

5

Beta strand

230 – 234

5

Helix

238 – 242

5

Beta strand

243 – 258

16

Beta strand

261 – 266

6

Beta strand

269 – 271

3

Beta strand

274 – 276

3

Beta strand

283 – 285

3

Beta strand

287 – 296

10

Helix

297 – 301

5

Beta strand

306 – 311

6

Beta strand

313 – 315

3

Helix

316 – 318

3

Beta strand

320 – 324

5

Sequences

	Sequence		Length	Mass (Da)
	P01857 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 3770EE106C2FA33D	FASTA	330	36,106
	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

References

	« Hide 'large scale' referencesShow '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]	"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, MASS SPECTROMETRY. Tissue: Liver.
[9]	"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].
[10]	"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).
[11]	"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.
[12]	"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

IMGT/GENE-DB

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J00228 Genomic DNA. Translation: AAC82527.1. Different initiation.

IPI

IPI00423463.

PIR

GHHU. A93433.

UniGene

Hs.510635.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AJ7	X-ray	2.10	H	1-103	[»]
1AQK	X-ray	1.84	H	1-103	[»]
1BEY	X-ray	3.25	H	1-98	[»]
1D5B	X-ray	2.80	B/H	1-101	[»]
1D5I	X-ray	2.00	H	1-101	[»]
1D6V	X-ray	2.00	H	1-101	[»]
1DFB	X-ray	2.70	H	1-103	[»]
1DN2	X-ray	2.70	A/B	120-326	[»]
1E4K	X-ray	3.20	A/B	106-330	[»]
1FC1	X-ray	2.90	A/B	106-329	[»]
1FC2	X-ray	2.80	D	106-329	[»]
1FCC	X-ray	3.20	A/B	121-326	[»]
1GAF	X-ray	1.95	H	1-103	[»]
1H3T	X-ray	2.40	A/B	108-330	[»]
1H3U	X-ray	2.40	A/B	108-330	[»]
1H3V	X-ray	3.10	A/B	108-330	[»]
1H3W	X-ray	2.85	M	108-330	[»]
1H3Y	X-ray	4.10	A/B	108-330	[»]
1HKL	X-ray	2.68	H	1-103	[»]
1HZH	X-ray	2.70	H/K	1-330	[»]
1I7Z	X-ray	2.30	B/D	1-103	[»]
1L6X	X-ray	1.65	A	120-326	[»]
1OP3	X-ray	1.75	H/M	1-102	[»]
1OQO	X-ray	2.30	A/B	119-330	[»]
1OQX	X-ray	2.60	A/B	119-330	[»]
1T83	X-ray	3.00	A/B	107-330	[»]
1T89	X-ray	3.50	A/B	107-330	[»]
1VGE	X-ray	2.00	H	1-103	[»]
2DTS	X-ray	2.20	A/B	108-330	[»]
2GJ7	X-ray	5.00	A/B	106-330	[»]
2I5Y	X-ray	2.20	H	1-101	[»]
2IWG	X-ray	2.35	A/D	120-326	[»]
2J6E	X-ray	3.00	A/B	99-330	[»]
2JB5	X-ray	2.80	H	1-102	[»]
2JB6	X-ray	2.85	B/H	1-102	[»]
2O5X	X-ray	2.05	H	1-108	[»]
2O5Y	X-ray	2.85	H	1-108	[»]
2O5Z	X-ray	2.40	H	1-108	[»]
2OSL	X-ray	2.60	A/H	1-103	[»]
2QAD	X-ray	3.30	D/H	1-101	[»]
2QL1	X-ray	2.53	A	106-330	[»]
2QQK	X-ray	2.75	H	1-107	[»]
2QQL	X-ray	3.10	H	1-107	[»]
2QQN	X-ray	2.20	H	1-107	[»]
2QR0	X-ray	3.50	B/F/H/L/N/R/T/X	1-103	[»]
2R56	X-ray	2.80	H/I	1-100	[»]
2RCS	X-ray	2.10	H	1-103	[»]
2VXQ	X-ray	1.90	H	1-100	[»]
3AGV	X-ray	2.15	A/B	120-330	[»]
3AVE	X-ray	2.00	A/B	108-330	[»]
3AY4	X-ray	2.20	A/B	108-330	[»]
3B2U	X-ray	2.58	C/F/H/J/N/Q/T/W	1-102	[»]
3B2V	X-ray	3.30	H	1-102	[»]
3BDY	X-ray	2.60	H	1-107	[»]
3BE1	X-ray	2.90	H	1-107	[»]
3BKY	X-ray	2.61	H	1-104	[»]
3BN9	X-ray	2.17	D/F	1-107	[»]
3BQU	X-ray	3.00	B	2-103	[»]
3C08	X-ray	2.15	H	1-102	[»]
3C09	X-ray	3.20	C/H	1-102	[»]
3C2S	X-ray	2.30	A	106-330	[»]
3CFJ	X-ray	2.60	B/D/F/H	1-104	[»]
3CFK	X-ray	2.60	B/D/F/H/I/K/N/P	1-104	[»]
3CSY	X-ray	3.40	A/C/E/G	1-101	[»]
3D0L	X-ray	2.35	B	2-105	[»]
3D0V	X-ray	2.05	B	2-105	[»]
3D6G	X-ray	2.30	A/B	119-328	[»]
3D85	X-ray	1.90	B	1-108	[»]
3DJ9	X-ray	1.75	A	119-225	[»]
3DNK	X-ray	2.84	A/B	119-330	[»]
3DO3	X-ray	2.50	A/B	119-330	[»]
3DRO	X-ray	3.90	B	2-103	[»]
3DRQ	X-ray	2.00	B	2-103	[»]
3DVG	X-ray	2.60	B	1-107	[»]
3DVN	X-ray	2.70	B/H	1-107	[»]
3EYF	X-ray	2.30	B/D	1-108	[»]
3EYO	X-ray	2.50	B/D	1-108	[»]
3EYQ	X-ray	2.40	D	1-108	[»]
3RY6	X-ray	3.80	A/B	114-327	[»]
3S7G	X-ray	3.13	A/B/C/D	104-330	[»]
3SGJ	X-ray	2.20	A/B	106-330	[»]
3SGK	X-ray	2.40	A/B	106-330	[»]
3TV3	X-ray	1.29	H	1-104	[»]
3TWC	X-ray	1.65	H	1-104	[»]
3TYG	X-ray	3.25	H	1-104	[»]
3U0W	X-ray	2.00	H	1-103	[»]
3U7W	X-ray	2.60	H	1-104	[»]
3U7Y	X-ray	2.45	H	1-104	[»]
3V7M	X-ray	2.02	A	119-327	[»]
3V8C	X-ray	2.77	A/B	119-330	[»]
3V95	X-ray	2.70	A/B	119-330	[»]
4ACP	X-ray	2.49	A/B	101-329	[»]
4B7I	X-ray	2.36	A/B	120-329	[»]
4DZ8	X-ray	1.91	A/B	108-330	[»]
4EOW	X-ray	1.97	H	1-101	[»]

ProteinModelPortal

P01857.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29187N.

IntAct

P01857. 77 interactions.

MINT

MINT-120799.

STRING

9606.ENSP00000374990.

Protein family/group databases

IMGT

Search...

PTM databases

PhosphoSite

P01857.

Polymorphism databases

DMDM

121039.

2D gel databases

DOSAC-COBS-2DPAGE

P01857.

REPRODUCTION-2DPAGE

P01857.

UCD-2DPAGE

P01857.

Proteomic databases

PaxDb

P01857.

PRIDE

P01857.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000390549; ENSP00000374991; ENSG00000211896.

UCSC

uc001yse.3. human.

Organism-specific databases

GeneCards

GC14M106204.

HGNC

HGNC:5525. IGHG1.

MIM

147100. gene.
254500. phenotype.

neXtProt

NX_P01857.

Orphanet

67038. B-cell chronic lymphocytic leukemia.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG313034.

HOVERGEN

HBG005814.

OrthoDB

EOG4RR6HW.

Enzyme and pathway databases

Pathway_Interaction_DB

il4_2pathway. IL4-mediated signaling events.

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P01857.

Bgee

P01857.

CleanEx

HS_IGHG1.

Genevestigator

P01857.

GermOnline

ENSG00000130076. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 3 hits.

InterPro

IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
[Graphical view]

Pfam

PF07654. C1-set. 3 hits.
[Graphical view]

SMART

SM00407. IGc1. 2 hits.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 3 hits.
PS00290. IG_MHC. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00051. Adalimumab.
DB00074. Basiliximab.
DB00111. Daclizumab.
DB00065. Infliximab.
DB00043. Omalizumab.
DB00073. Rituximab.
DB00081. Tositumomab.
DB00072. Trastuzumab.

EvolutionaryTrace

P01857.

SOURCE

Search...

Entry information

Entry name

IGHG1_HUMAN

Accession

Primary (citable) accession number: P01857

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 29, 2013
This is version 143 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.