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P01857

- IGHG1_HUMAN

UniProt

P01857 - IGHG1_HUMAN

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Protein

Ig gamma-1 chain C region

Gene

IGHG1

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

Functioni

GO - Molecular functioni

  1. antigen binding Source: UniProtKB

GO - Biological processi

  1. complement activation Source: Reactome
  2. complement activation, classical pathway Source: Reactome
  3. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  4. innate immune response Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_160158. Role of phospholipids in phagocytosis.
REACT_160274. FCGR activation.
REACT_7956. Classical antibody-mediated complement activation.
REACT_8024. Initial triggering of complement.

Names & Taxonomyi

Protein namesi
Recommended name:
Ig gamma-1 chain C region
Gene namesi
Name:IGHG1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:5525. IGHG1.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. extracellular region Source: Reactome
  3. extracellular space Source: UniProt
  4. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

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.2 Publications
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.

Organism-specific databases

MIMi254500. phenotype.
Orphaneti67038. B-cell chronic lymphocytic leukemia.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 330›330Ig gamma-1 chain C regionPRO_0000153578Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 83
Disulfide bondi103 – 103Interchain (with light chain)
Disulfide bondi109 – 109Interchain (with heavy chain)
Disulfide bondi112 – 112Interchain (with heavy chain)
Disulfide bondi144 ↔ 204
Glycosylationi180 – 1801N-linked (GlcNAc...) (complex)3 Publications
Disulfide bondi250 ↔ 308

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP01857.
PaxDbiP01857.
PRIDEiP01857.

2D gel databases

DOSAC-COBS-2DPAGEP01857.
REPRODUCTION-2DPAGEP01857.
UCD-2DPAGEP01857.

PTM databases

PhosphoSiteiP01857.

Expressioni

Gene expression databases

BgeeiP01857.
CleanExiHS_IGHG1.
GenevestigatoriP01857.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

DIPiDIP-29187N.
IntActiP01857. 78 interactions.
MINTiMINT-120799.
STRINGi9606.ENSP00000374990.

Structurei

Secondary structure

1
330
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 148Combined sources
Beta strandi16 – 183Combined sources
Beta strandi22 – 3514Combined sources
Beta strandi38 – 414Combined sources
Helixi42 – 443Combined sources
Beta strandi45 – 484Combined sources
Beta strandi50 – 523Combined sources
Beta strandi53 – 586Combined sources
Beta strandi63 – 7210Combined sources
Helixi73 – 753Combined sources
Turni76 – 783Combined sources
Beta strandi82 – 876Combined sources
Helixi88 – 903Combined sources
Beta strandi92 – 976Combined sources
Beta strandi101 – 1033Combined sources
Helixi107 – 1093Combined sources
Beta strandi111 – 1188Combined sources
Beta strandi122 – 1265Combined sources
Helixi130 – 1345Combined sources
Beta strandi136 – 1405Combined sources
Beta strandi141 – 1499Combined sources
Beta strandi151 – 1533Combined sources
Beta strandi157 – 1626Combined sources
Beta strandi165 – 1673Combined sources
Beta strandi171 – 1733Combined sources
Beta strandi176 – 1783Combined sources
Beta strandi179 – 1813Combined sources
Beta strandi183 – 1908Combined sources
Helixi193 – 1975Combined sources
Beta strandi202 – 2076Combined sources
Beta strandi211 – 2133Combined sources
Beta strandi215 – 2195Combined sources
Beta strandi223 – 2297Combined sources
Beta strandi230 – 2345Combined sources
Helixi238 – 2425Combined sources
Beta strandi243 – 25816Combined sources
Beta strandi261 – 2666Combined sources
Beta strandi269 – 2713Combined sources
Beta strandi274 – 2763Combined sources
Beta strandi283 – 2853Combined sources
Beta strandi287 – 29610Combined sources
Helixi297 – 3015Combined sources
Beta strandi306 – 3116Combined sources
Beta strandi313 – 3153Combined sources
Helixi316 – 3183Combined sources
Beta strandi320 – 3245Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AJ7X-ray2.10H1-103[»]
1AQKX-ray1.84H21-245[»]
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[»]
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[»]
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[»]
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[»]
4D9QX-ray2.28E/H2-102[»]
4D9RX-ray2.42E/H2-103[»]
4DAGX-ray3.39H2-98[»]
4DZ8X-ray1.91A/B108-330[»]
4EOWX-ray1.97H1-101[»]
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[»]
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[»]
ProteinModelPortaliP01857.
SMRiP01857. Positions 1-330.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01857.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 9898CH1Add
BLAST
Regioni99 – 11012HingeAdd
BLAST
Regioni111 – 223113CH2Add
BLAST
Regioni224 – 330107CH3Add
BLAST

Keywords - Domaini

Immunoglobulin C region, Immunoglobulin domain

Phylogenomic databases

eggNOGiNOG313034.
GeneTreeiENSGT00530000063726.
HOVERGENiHBG005814.
InParanoidiP01857.
PhylomeDBiP01857.

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. 2 hits.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 3 hits.
PS00290. IG_MHC. 2 hits.
[Graphical view]

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 AAC82527.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti97 – 971K → R in G1M(3) marker.
VAR_003886
Natural varianti239 – 2391D → E in G1M(non-1) marker.
VAR_003887
Natural varianti241 – 2411L → M in G1M(non-1) marker.
VAR_003888

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00228 Genomic DNA. Translation: AAC82527.1. Different initiation.
PIRiA93433. GHHU.
UniGeneiHs.510635.

Genome annotation databases

EnsembliENST00000390549; ENSP00000374991; ENSG00000211896.
UCSCiuc001yse.3. human.

Polymorphism databases

DMDMi121039.

Keywords - Coding sequence diversityi

Chromosomal rearrangement

Cross-referencesi

Web resourcesi

IMGT/GENE-DB

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00228 Genomic DNA. Translation: AAC82527.1 . Different initiation.
PIRi A93433. GHHU.
UniGenei Hs.510635.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AJ7 X-ray 2.10 H 1-103 [» ]
1AQK X-ray 1.84 H 21-245 [» ]
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 [» ]
1H3X X-ray 2.44 A/B 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 [» ]
1N7M X-ray 1.80 L 2-102 [» ]
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 [» ]
2RCJ X-ray - C/D/G/H/K/L/O/P/S/T 1-326 [» ]
2RCS X-ray 2.10 H 1-103 [» ]
2VXQ X-ray 1.90 H 1-100 [» ]
2WAH X-ray 2.51 A/B 120-328 [» ]
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 [» ]
3FJT X-ray 2.50 A/B 119-327 [» ]
3O11 X-ray 2.80 B/H 1-103 [» ]
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 [» ]
3WJJ X-ray 2.60 A/B 99-328 [» ]
3WJL X-ray 2.86 A/B 99-328 [» ]
4ACP X-ray 2.49 A/B 101-329 [» ]
4B7I X-ray 2.36 A/B 120-329 [» ]
4BM7 X-ray 1.95 A/B 106-329 [» ]
4BSV X-ray 1.75 A/B 106-330 [» ]
4BSW X-ray 2.15 A/B 106-330 [» ]
4BYH X-ray 2.30 A/B 106-329 [» ]
4D9Q X-ray 2.28 E/H 2-102 [» ]
4D9R X-ray 2.42 E/H 2-103 [» ]
4DAG X-ray 3.39 H 2-98 [» ]
4DZ8 X-ray 1.91 A/B 108-330 [» ]
4EOW X-ray 1.97 H 1-101 [» ]
4J12 X-ray 1.90 A 119-327 [» ]
4KU1 X-ray 1.90 A/B 120-327 [» ]
4LLD X-ray 1.19 A 1-103 [» ]
4LLM X-ray 1.75 A 1-103 [» ]
4LLQ X-ray 1.42 A 1-103 [» ]
4N0U X-ray 3.80 E 119-327 [» ]
4NQS X-ray 2.64 A/B/G/H 118-330 [» ]
4NQT X-ray 2.10 A 118-330 [» ]
4NQU X-ray 2.50 A 118-330 [» ]
4O4Y X-ray 1.85 A 106-119 [» ]
4O51 X-ray 2.20 M/N/O/P 106-119 [» ]
4Q6Y X-ray 3.00 A/B/C/D 109-329 [» ]
4Q74 X-ray 2.19 A/B 108-329 [» ]
4Q7D X-ray 2.35 A/B 109-329 [» ]
ProteinModelPortali P01857.
SMRi P01857. Positions 1-330.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-29187N.
IntActi P01857. 78 interactions.
MINTi MINT-120799.
STRINGi 9606.ENSP00000374990.

Protein family/group databases

IMGTi Search...

PTM databases

PhosphoSitei P01857.

Polymorphism databases

DMDMi 121039.

2D gel databases

DOSAC-COBS-2DPAGE P01857.
REPRODUCTION-2DPAGE P01857.
UCD-2DPAGE P01857.

Proteomic databases

MaxQBi P01857.
PaxDbi P01857.
PRIDEi P01857.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000390549 ; ENSP00000374991 ; ENSG00000211896 .
UCSCi uc001yse.3. human.

Organism-specific databases

GeneCardsi GC14M106204.
HGNCi HGNC:5525. IGHG1.
MIMi 147100. gene.
254500. phenotype.
neXtProti NX_P01857.
Orphaneti 67038. B-cell chronic lymphocytic leukemia.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG313034.
GeneTreei ENSGT00530000063726.
HOVERGENi HBG005814.
InParanoidi P01857.
PhylomeDBi P01857.

Enzyme and pathway databases

Reactomei REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_160158. Role of phospholipids in phagocytosis.
REACT_160274. FCGR activation.
REACT_7956. Classical antibody-mediated complement activation.
REACT_8024. Initial triggering of complement.

Miscellaneous databases

EvolutionaryTracei P01857.
PROi P01857.
SOURCEi Search...

Gene expression databases

Bgeei P01857.
CleanExi HS_IGHG1.
Genevestigatori P01857.

Family and domain databases

Gene3Di 2.60.40.10. 3 hits.
InterProi IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
[Graphical view ]
Pfami PF07654. C1-set. 3 hits.
[Graphical view ]
SMARTi SM00407. IGc1. 2 hits.
[Graphical view ]
PROSITEi PS50835. IG_LIKE. 3 hits.
PS00290. IG_MHC. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. "Site-specific glycoprofiling of N-linked glycopeptides using MALDI-TOF MS: strong correlation between signal strength and glycoform quantities."
    Thaysen-Andersen M., Mysling S., Hojrup P.
    Anal. Chem. 81:3933-3943(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-180.
  9. "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.
    Tissue: Liver.
  10. Cited for: GLYCOSYLATION AT ASN-180.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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).
  13. "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.
  14. "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.

Entry informationi

Entry nameiIGHG1_HUMAN
AccessioniPrimary (citable) accession number: P01857
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 26, 2014
This is version 160 of the entry and version 1 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

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.

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

External Data

Dasty 3