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Protein

Immunoglobulin heavy constant gamma 1

Gene

IGHG1

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

Functioni

Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:22158414, PubMed:20176268). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268).3 Publications

GO - Molecular functioni

  • antigen binding Source: UniProtKB
  • immunoglobulin receptor binding Source: GO_Central
  • serine-type endopeptidase activity Source: Reactome

GO - Biological processi

Keywordsi

Biological processAdaptive immunity, Immunity

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.
R-HSA-6785807. Interleukin-4 and 13 signaling.
R-HSA-977606. Regulation of Complement cascade.

Protein family/group databases

IMGT/GENE-DBIGHG1.

Names & Taxonomyi

Protein namesi
Recommended name:
Immunoglobulin heavy constant gamma 12 Publications
Alternative name(s):
Ig gamma-1 chain C regionCurated
Ig gamma-1 chain C region EU2 Publications
Ig gamma-1 chain C region KOL1 Publication
Ig gamma-1 chain C region NIE1 Publication
Gene namesi
Name:IGHG12 Publications
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:5525. IGHG1.

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

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

Multiple myeloma (MM)2 Publications
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.
Disease descriptionA 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.
See also OMIM:254500

Organism-specific databases

DisGeNETi3500.
MalaCardsiIGHG1.
MIMi254500. phenotype.
OpenTargetsiENSG00000211896.
Orphaneti67038. B-cell chronic lymphocytic leukemia.

Chemistry databases

DrugBankiDB07883. (2-AMINO-3-PHENYL-BICYCLO[2.2.1]HEPT-2-YL)-PHENYL-METHANONE.
DB08294. 2-(4-HYDROXY-3-NITROPHENYL)ACETIC ACID.
DB07371. 3-(10-METHYL-ANTHRACEN-9-YL)-PROPIONIC ACID.
DB08562. 4-(4-STYRYL-PHENYLCARBAMOYL)-BUTYRIC ACID.
DB08409. 4-NITRO-BENZYLPHOSPHONOBUTANOYL-GLYCINE.
DB08296. 5-(PARA-NITROPHENYL PHOSPHONATE)-PENTANOIC ACID.
DB08412. 6-{4-[HYDROXY-(4-NITRO-PHENOXY)-PHOSPHORYL]-BUTYRYLAMINO}-HEXANOIC ACID.
DB08332. [2'-CARBOXYLETHYL]-10-METHYL-ANTHRACENE ENDOPEROXIDE.
DB04473. Alpha-L-Fucose.
DB04639. Biphenylalanine.
DB07764. FLUORESCIN.
DB01631. Methyl Nonanoate (Ester).
DB07816. N-(P-CYANOPHENYL)-N'-DIPHENYLMETHYL-GUANIDINE-ACETIC ACID.
DB03740. N-acetyl-alpha-D-glucosamine.
DB07881. N-{[2-({[1-(4-CARBOXYBUTANOYL)AMINO]-2-PHENYLETHYL}-HYDROXYPHOSPHINYL)OXY]ACETYL}-2-PHENYLETHYLAMINE.
DB08410. PARA-NITROBENZYL GLUTARYL GLYCINIC ACID.
DB08377. PARA-NITROPHENYL PHOSPHONOBUTANOYL D-ALANINE.
DB08411. PARA-NITROPHENYL PHOSPHONOBUTANOYL L-ALANINE.
DB08394. PARA-NITROPHENYLPHOSPHONOBUTANOYL-GLYCINE.
DB07672. TRANS-2-(DIMETHYLPHENYLSILYL)-PIPERIDINE-N-OXIDE.

Polymorphism and mutation databases

DMDMi121039.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000153578‹1 – 330Immunoglobulin heavy constant gamma 1Add BLAST›330

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi27 ↔ 83PROSITE-ProRule annotation
Disulfide bondi103Interchain (with light chain)
Disulfide bondi109Interchain (with heavy chain)
Disulfide bondi112Interchain (with heavy chain)
Disulfide bondi144 ↔ 204PROSITE-ProRule annotation
Glycosylationi180N-linked (GlcNAc...) (complex) asparagine3 Publications1
Disulfide bondi250 ↔ 308PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiP01857.
MaxQBiP01857.
PeptideAtlasiP01857.
PRIDEiP01857.

2D gel databases

DOSAC-COBS-2DPAGEiP01857.
REPRODUCTION-2DPAGEiP01857.
UCD-2DPAGEiP01857.

PTM databases

iPTMnetiP01857.
PhosphoSitePlusiP01857.
SwissPalmiP01857.
UniCarbKBiP01857.

Expressioni

Gene expression databases

BgeeiENSG00000211896.
CleanExiHS_IGHG1.
ExpressionAtlasiP01857. baseline and differential.
GenevisibleiP01857. HS.

Interactioni

Subunit structurei

Immunoglobulins are composed of two identical heavy chains and two identical light chains; disulfide-linked.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
FCGR2BP3199431EBI-356114,EBI-724784

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-29187N.
IntActiP01857. 85 interactors.
MINTiMINT-120799.

Structurei

Secondary structure

1330
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 14Combined sources8
Beta strandi16 – 18Combined sources3
Beta strandi22 – 35Combined sources14
Beta strandi38 – 41Combined sources4
Helixi42 – 44Combined sources3
Beta strandi50 – 52Combined sources3
Beta strandi63 – 72Combined sources10
Helixi73 – 75Combined sources3
Turni76 – 78Combined sources3
Beta strandi82 – 87Combined sources6
Helixi88 – 90Combined sources3
Beta strandi92 – 97Combined sources6
Helixi115 – 117Combined sources3
Beta strandi118 – 120Combined sources3
Beta strandi122 – 126Combined sources5
Helixi130 – 134Combined sources5
Beta strandi136 – 138Combined sources3
Beta strandi141 – 149Combined sources9
Beta strandi151 – 153Combined sources3
Beta strandi157 – 162Combined sources6
Beta strandi165 – 167Combined sources3
Beta strandi170 – 172Combined sources3
Beta strandi173 – 175Combined sources3
Beta strandi176 – 178Combined sources3
Beta strandi179 – 181Combined sources3
Beta strandi183 – 190Combined sources8
Helixi193 – 197Combined sources5
Beta strandi202 – 207Combined sources6
Beta strandi211 – 213Combined sources3
Beta strandi215 – 219Combined sources5
Beta strandi230 – 234Combined sources5
Helixi240 – 242Combined sources3
Beta strandi243 – 258Combined sources16
Beta strandi261 – 266Combined sources6
Beta strandi269 – 271Combined sources3
Beta strandi272 – 276Combined sources5
Beta strandi283 – 285Combined sources3
Beta strandi287 – 296Combined sources10
Helixi297 – 301Combined sources5
Beta strandi306 – 311Combined sources6
Beta strandi313 – 315Combined sources3
Beta strandi318 – 324Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AJ7X-ray2.10H1-103[»]
1AQKX-ray1.84H21-245[»]
1AXSX-ray2.60B/H1-101[»]
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[»]
1PG7X-ray2.50H/I1-100[»]
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[»]
3MCLX-ray1.70H1-107[»]
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[»]
3WKNX-ray2.90A/B/C/D/I/J/M/N119-330[»]
3WN5X-ray2.78A/B/D/E99-328[»]
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[»]
4CDHX-ray2.30A/B101-330[»]
4D9QX-ray2.28E/H2-102[»]
4D9RX-ray2.42E/H2-103[»]
4DAGX-ray3.39H2-98[»]
4DZ8X-ray1.91A/B108-330[»]
4EOWX-ray1.97H1-101[»]
4HIXX-ray2.20H1-107[»]
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[»]
4NWTX-ray1.75H6-95[»]
4NWUX-ray1.60H6-105[»]
4O4YX-ray1.85A106-119[»]
4O51X-ray2.20M/N/O/P106-119[»]
4Q6YX-ray3.00A/B/C/D109-329[»]
4Q74X-ray2.19A/B108-329[»]
4Q7DX-ray2.35A/B109-329[»]
4W4NX-ray1.80A/B107-329[»]
4W4OX-ray1.80A/B107-330[»]
4WI2X-ray1.90A/B120-327[»]
4WI3X-ray2.70A/B120-327[»]
4WI4X-ray2.80A/B121-327[»]
4WI5X-ray2.80A/B120-327[»]
4WI6X-ray2.20A/B120-327[»]
4WI7X-ray1.90A/B120-327[»]
4WI8X-ray2.80A/B120-327[»]
4WI9X-ray2.65A/B120-327[»]
4X4MX-ray3.48A/B/C/D112-330[»]
4X98X-ray2.50A108-327[»]
B121-327[»]
4X99X-ray2.50A/B108-330[»]
4XMPX-ray1.78H1-103[»]
4XNYX-ray2.30H1-103[»]
4XNZX-ray3.39B/E/H1-103[»]
4XXDX-ray2.41B/E1-107[»]
4ZNEX-ray2.42E/J104-330[»]
5BW7X-ray3.00A/B108-330[»]
5D4QX-ray2.39A/B109-329[»]
5D6DX-ray3.13A/B108-329[»]
5DI8X-ray1.90A/B104-330[»]
5DJ0X-ray2.28A/B104-330[»]
5DJ2X-ray2.56A/B104-330[»]
5DJ6X-ray2.00A/B104-330[»]
5DJ8X-ray2.40A/B104-330[»]
5DJAX-ray2.90A/B104-330[»]
5DJCX-ray2.10A/B/D/E104-330[»]
5DJDX-ray2.30A/B104-330[»]
5DJXX-ray2.25A/B/D/E104-330[»]
5DJYX-ray2.15A/B104-330[»]
5DJZX-ray1.90A/B104-330[»]
5DK0X-ray2.30A/B104-330[»]
5DK2X-ray2.60A/B/D/E104-330[»]
5DVKX-ray2.60A104-330[»]
5DVLX-ray1.90A104-330[»]
5DVMX-ray2.95A104-330[»]
5DVNX-ray2.50A104-330[»]
5DVOX-ray2.50A/B104-330[»]
5HSFX-ray1.52A/B221-330[»]
5HY9X-ray2.70A/B104-330[»]
5HYEX-ray1.89A/C104-330[»]
5HYFX-ray1.80A104-330[»]
5HYIX-ray2.90A/B/C/D104-330[»]
5IQ7X-ray3.29H1-102[»]
5IQ9X-ray2.40A/H1-101[»]
5IW3X-ray2.05A119-326[»]
5IW6X-ray2.34A119-327[»]
B122-326[»]
5JIHX-ray1.66A/B108-329[»]
5JIIX-ray1.79A/B108-329[»]
5JIKX-ray1.82A/B108-329[»]
5K33X-ray3.30A108-329[»]
5K8DX-ray4.19B104-329[»]
5KWGX-ray4.30A108-330[»]
5M3VX-ray1.97A/B104-330[»]
5U52X-ray1.94A/B119-326[»]
5U66X-ray1.70A120-326[»]
5V43X-ray2.32A/B104-329[»]
5V4EX-ray3.22A/B/C/D/E/F/G/H104-329[»]
ProteinModelPortaliP01857.
SMRiP01857.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01857.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 99Ig-like 1PROSITE-ProRule annotationAdd BLAST94
Domaini121 – 220Ig-like 2PROSITE-ProRule annotationAdd BLAST100
Domaini229 – 325Ig-like 3PROSITE-ProRule annotationAdd BLAST97

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 98CH1Add BLAST98
Regioni99 – 110HingeAdd BLAST12
Regioni111 – 223CH2Add BLAST113
Regioni224 – 330CH3Add BLAST107

Keywords - Domaini

Immunoglobulin C region, Immunoglobulin domain

Phylogenomic databases

GeneTreeiENSGT00530000063726.
HOVERGENiHBG005814.
InParanoidiP01857.
PhylomeDBiP01857.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiView protein in InterPro
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
PfamiView protein in Pfam
PF07654. C1-set. 3 hits.
SMARTiView protein in SMART
SM00407. IGc1. 3 hits.
SUPFAMiSSF48726. SSF48726. 3 hits.
PROSITEiView protein in PROSITE
PS50835. IG_LIKE. 3 hits.
PS00290. IG_MHC. 2 hits.

Sequencei

Sequence statusi: Complete.

P01857-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ASTKGPSVFP LAPSSKSTSG GTAALGCLVK DYFPEPVTVS WNSGALTSGV
60 70 80 90 100
HTFPAVLQSS GLYSLSSVVT VPSSSLGTQT YICNVNHKPS NTKVDKKVEP
110 120 130 140 150
KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS
160 170 180 190 200
HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK
210 220 230 240 250
EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC
260 270 280 290 300
LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW
310 320 330
QQGNVFSCSV MHEALHNHYT QKSLSLSPGK
Length:330
Mass (Da):36,106
Last modified:July 21, 1986 - v1
Checksum:i3770EE106C2FA33D
GO

Sequence cautioni

The sequence AAC82527 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Polymorphismi

There are several alleles. The sequence shown is that of IMGT allele IGHG1*05.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00388697K → R in IMGT allele IGHG1*03. 1
Natural variantiVAR_003887239D → E in IMGT allele IGHG1*03. 1
Natural variantiVAR_003888241L → M in IMGT allele IGHG1*03. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00228 Genomic DNA. Translation: AAC82527.1. Different initiation.
AL122127 Genomic DNA. No translation available.
PIRiA93433. GHHU.
UniGeneiHs.510635.

Genome annotation databases

EnsembliENST00000390549; ENSP00000374991; ENSG00000211896.
ENST00000631466; ENSP00000488387; ENSG00000277633.
UCSCiuc059gdc.1. human.

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiIGHG1_HUMAN
AccessioniPrimary (citable) accession number: P01857
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: August 30, 2017
This is version 190 of the entry and version 1 of the sequence. See 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

Caution

For an example of a full length immunoglobulin gamma heavy chain see AC P0DOX5.Curated

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