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Protein

Ig gamma-2 chain C region

Gene

IGHG2

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

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei156 – 1561At or near the complement-binding site

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-HSA-166663. Initial triggering of complement.
R-HSA-173623. Classical antibody-mediated complement activation.
R-HSA-2029481. FCGR activation.
R-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-2029485. Role of phospholipids in phagocytosis.

Names & Taxonomyi

Protein namesi
Recommended name:
Ig gamma-2 chain C region
Gene namesi
Name:IGHG2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:5526. IGHG2.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • external side of plasma membrane Source: GO_Central
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • immunoglobulin complex, circulating Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

Orphaneti183675. Recurrent infections associated with rare immunoglobulin isotypes deficiency.

Polymorphism and mutation databases

DMDMi218512079.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 326›326Ig gamma-2 chain C regionPRO_0000153579Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi14 – 14Interchain (with a light chain)
Disulfide bondi27 ↔ 83PROSITE-ProRule annotation1 Publication
Disulfide bondi102 – 102Interchain (with a heavy chain)
Disulfide bondi103 – 103Interchain (with a heavy chain)
Disulfide bondi106 – 106Interchain (with a heavy chain)
Disulfide bondi109 – 109Interchain (with a heavy chain)
Disulfide bondi140 ↔ 200PROSITE-ProRule annotation1 Publication
Glycosylationi176 – 1761N-linked (GlcNAc...) (complex)3 Publications
Disulfide bondi246 ↔ 304PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP01859.

2D gel databases

UCD-2DPAGEP01859.

PTM databases

iPTMnetiP01859.
PhosphoSiteiP01859.
UniCarbKBiP01859.

Expressioni

Gene expression databases

BgeeiP01859.
GenevisibleiP01859. HS.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
Q281093EBI-1044662,EBI-8061363From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

IntActiP01859. 4 interactions.
MINTiMINT-1782619.

Structurei

Secondary structure

1
326
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi118 – 1225Combined sources
Helixi126 – 1305Combined sources
Beta strandi137 – 1459Combined sources
Beta strandi147 – 1493Combined sources
Beta strandi152 – 1587Combined sources
Beta strandi161 – 1633Combined sources
Beta strandi179 – 1868Combined sources
Helixi189 – 1935Combined sources
Beta strandi198 – 2047Combined sources
Beta strandi207 – 2093Combined sources
Beta strandi210 – 2156Combined sources
Beta strandi226 – 2305Combined sources
Helixi234 – 2385Combined sources
Beta strandi239 – 25416Combined sources
Beta strandi257 – 2626Combined sources
Beta strandi265 – 2673Combined sources
Beta strandi270 – 2723Combined sources
Beta strandi283 – 29210Combined sources
Helixi293 – 2975Combined sources
Beta strandi302 – 3076Combined sources
Helixi312 – 3143Combined sources
Beta strandi316 – 3205Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QSCX-ray2.80H1-99[»]
4HAFX-ray2.04A/B104-326[»]
4HAGX-ray3.40A104-326[»]
4L4JX-ray1.92A/B106-326[»]
ProteinModelPortaliP01859.
SMRiP01859. Positions 1-326.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01859.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 9898CH1Add
BLAST
Regioni99 – 11012HingeAdd
BLAST
Regioni111 – 219109CH2Add
BLAST
Regioni220 – 326107CH3Add
BLAST

Keywords - Domaini

Immunoglobulin C region, Immunoglobulin domain

Phylogenomic databases

GeneTreeiENSGT00530000063726.
HOVERGENiHBG005814.
InParanoidiP01859.
OMAiASISVEW.
PhylomeDBiP01859.
TreeFamiTF334176.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
[Graphical view]
PfamiPF07654. C1-set. 3 hits.
[Graphical view]
SMARTiSM00407. IGc1. 3 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
PROSITEiPS50835. IG_LIKE. 3 hits.
PS00290. IG_MHC. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P01859-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ASTKGPSVFP LAPCSRSTSE STAALGCLVK DYFPEPVTVS WNSGALTSGV
60 70 80 90 100
HTFPAVLQSS GLYSLSSVVT VPSSNFGTQT YTCNVDHKPS NTKVDKTVER
110 120 130 140 150
KCCVECPPCP APPVAGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP
160 170 180 190 200
EVQFNWYVDG VEVHNAKTKP REEQFNSTFR VVSVLTVVHQ DWLNGKEYKC
210 220 230 240 250
KVSNKGLPAP IEKTISKTKG QPREPQVYTL PPSREEMTKN QVSLTCLVKG
260 270 280 290 300
FYPSDISVEW ESNGQPENNY KTTPPMLDSD GSFFLYSKLT VDKSRWQQGN
310 320
VFSCSVMHEA LHNHYTQKSL SLSPGK
Length:326
Mass (Da):35,901
Last modified:December 16, 2008 - v2
Checksum:i95DC5D8C6860B7FC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Sequence conflicti109 – 1091C → S (PubMed:6811139).Curated
Sequence conflicti257 – 2571S → A in AAB59393 (PubMed:6804948).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti60 – 601S → A in myeloma proteins TIL and ZIE.
VAR_003889

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL928742 Genomic DNA. No translation available.
J00230 Genomic DNA. Translation: AAB59393.1.
PIRiA93906. G2HU.
UniGeneiHs.510635.

Genome annotation databases

EnsembliENST00000390545; ENSP00000374987; ENSG00000211893.
ENST00000621803; ENSP00000480351; ENSG00000274497.
UCSCiuc059gct.1. human.

Cross-referencesi

Web resourcesi

IGHG2base

IGHG2 mutation db

IMGT/GENE-DB

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL928742 Genomic DNA. No translation available.
J00230 Genomic DNA. Translation: AAB59393.1.
PIRiA93906. G2HU.
UniGeneiHs.510635.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QSCX-ray2.80H1-99[»]
4HAFX-ray2.04A/B104-326[»]
4HAGX-ray3.40A104-326[»]
4L4JX-ray1.92A/B106-326[»]
ProteinModelPortaliP01859.
SMRiP01859. Positions 1-326.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP01859. 4 interactions.
MINTiMINT-1782619.

Protein family/group databases

IMGTiSearch...
Search...

PTM databases

iPTMnetiP01859.
PhosphoSiteiP01859.
UniCarbKBiP01859.

Polymorphism and mutation databases

DMDMi218512079.

2D gel databases

UCD-2DPAGEP01859.

Proteomic databases

PRIDEiP01859.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000390545; ENSP00000374987; ENSG00000211893.
ENST00000621803; ENSP00000480351; ENSG00000274497.
UCSCiuc059gct.1. human.

Organism-specific databases

GeneCardsiIGHG2.
HGNCiHGNC:5526. IGHG2.
MIMi147110. gene.
neXtProtiNX_P01859.
Orphaneti183675. Recurrent infections associated with rare immunoglobulin isotypes deficiency.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00530000063726.
HOVERGENiHBG005814.
InParanoidiP01859.
OMAiASISVEW.
PhylomeDBiP01859.
TreeFamiTF334176.

Enzyme and pathway databases

ReactomeiR-HSA-166663. Initial triggering of complement.
R-HSA-173623. Classical antibody-mediated complement activation.
R-HSA-2029481. FCGR activation.
R-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-2029485. Role of phospholipids in phagocytosis.

Miscellaneous databases

EvolutionaryTraceiP01859.
PROiP01859.
SOURCEiSearch...

Gene expression databases

BgeeiP01859.
GenevisibleiP01859. HS.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
[Graphical view]
PfamiPF07654. C1-set. 3 hits.
[Graphical view]
SMARTiSM00407. IGc1. 3 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
PROSITEiPS50835. IG_LIKE. 3 hits.
PS00290. IG_MHC. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "Linkage and sequence homology of two human immunoglobulin gamma heavy chain constant region genes."
    Ellison J.W., Hood L.E.
    Proc. Natl. Acad. Sci. U.S.A. 79:1984-1988(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-326.
  3. "Structure of human immunoglobulin gamma genes: implications for evolution of a gene family."
    Takahashi N., Ueda S., Obata M., Nikaido T., Nakai S., Honjo T.
    Cell 29:671-679(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 88-115.
    Tissue: Fetal liver.
  4. "Comparison of the hinge-coding segments in human immunoglobulin gamma heavy chain genes and the linkage of the gamma 2 and gamma 4 subclass genes."
    Krawinkel U., Rabbitts T.H.
    EMBO J. 1:403-407(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 99-177 AND 310-326.
    Tissue: Fetal liver.
  5. "The primary structure of a human IgG2 heavy chain: genetic, evolutionary, and functional implications."
    Wang A.-C., Tung E., Fudenberg H.H.
    J. Immunol. 125:1048-1054(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-325 (MYELOMA PROTEIN TIL).
  6. "The amino acid sequences of the three heavy chain constant region domains of a human IgG2 myeloma protein."
    Connell G.E., Parr D.M., Hofmann T.
    Can. J. Biochem. 57:758-767(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-85 AND 132-325 (MYELOMA PROTEIN ZIE).
  7. "A note of the amino acid sequence of residues 381-391 of human immunoglobulins gamma chains."
    Hofmann T., Parr D.M.
    Mol. Immunol. 16:923-925(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 238-275 (ZIE).
  8. Hofmann T., Parr D.M.
    Submitted (MAR-1980) to the PIR data bank
    Cited for: SEQUENCE REVISION TO 25; 59; 60 AND 264-268 (ZIE).
  9. "Characterization of the two unique human anti-flavin monoclonal immunoglobulins."
    Stoppini M., Bellotti V., Negri A., Merlini G., Garver F., Ferri G.
    Eur. J. Biochem. 228:886-893(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-121 (DOT).
  10. "Disulphide bridges of the heavy chain of human immunoglobulin G2."
    Milstein C., Frangione B.
    Biochem. J. 121:217-225(1971) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  11. Cited for: DISULFIDE BONDS.
  12. Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-176.
    Tissue: Bile.
  13. "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-176.
    Tissue: Liver.
  14. Cited for: GLYCOSYLATION AT ASN-176.

Entry informationi

Entry nameiIGHG2_HUMAN
AccessioniPrimary (citable) accession number: P01859
Secondary accession number(s): A6NE66
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 16, 2008
Last modified: May 11, 2016
This is version 146 of the entry and version 2 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.