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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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	Defects in IGHG1 are a cause of multiple myeloma (MM) [MIM:254500]. MM is 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=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 G1M(17) 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	immune response Non-traceable author statement. Source: UniProtKB
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell membrane fraction Non-traceable author statement. Source: UniProtKB
Molecular function	antigen binding Traceable author statement Ref.1. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
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

Beta strand

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 – 73

11

Turn

74 – 78

5

Beta strand

82 – 87

6

Helix

88 – 90

3

Beta strand

92 – 97

6

Beta strand

122 – 126

5

Helix

130 – 134

5

Beta strand

141 – 153

13

Beta strand

157 – 162

6

Beta strand

180 – 190

11

Helix

193 – 197

5

Beta strand

202 – 207

6

Beta strand

215 – 219

5

Beta strand

230 – 234

5

Turn

238 – 242

5

Beta strand

243 – 258

16

Beta strand

261 – 270

10

Beta strand

274 – 276

3

Beta strand

287 – 296

10

Helix

297 – 301

5

Beta strand

306 – 311

6

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: 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]	"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: 19159218] [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: 21269460] [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: 7236608] [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: 8943038] [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: 11972529] [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	[»]
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	[»]
3U7W	X-ray	2.60	H	1-104	[»]
3U7Y	X-ray	2.45	H	1-104	[»]

ProteinModelPortal

P01857.

SMR

P01857. Positions 1-330.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29187N.

IntAct

P01857. 75 interactions.

MINT

MINT-120799.

STRING

P01857.

Protein family/group databases

IMGT

Search...

PTM databases

PhosphoSite

P01857.

Polymorphism databases

DMDM

121039.

2D gel databases

Cornea-2DPAGE

P01857.

DOSAC-COBS-2DPAGE

P01857.

REPRODUCTION-2DPAGE

P01857.

UCD-2DPAGE

P01857.

Proteomic databases

PRIDE

P01857.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000390549; ENSP00000374991; ENSG00000211896.

UCSC

uc001yse.2. human.

Organism-specific databases

GeneCards

GC14M106204.

H-InvDB

HIX0175858.

HGNC

HGNC:5525. IGHG1.

MIM

147100. gene.
254500. phenotype.

neXtProt

NX_P01857.

Orphanet

67038. Chronic B-cell lymphocytic leukemia.
85443. Primary amyloidosis.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG10023.

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

Bgee

P01857.

CleanEx

HS_IGHG1.

Genevestigator

P01857.

GermOnline

ENSG00000130076. Homo sapiens.

Family and domain databases

InterPro

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

Gene3D

G3DSA:2.60.40.10. Ig-like_fold. 3 hits.

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.

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:	January 25, 2012
This is version 129 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.