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P01857

- IGHG1_HUMAN

UniProt

P01857 - IGHG1_HUMAN

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
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. antigen binding Source: UniProtKB
    2. protein binding Source: IntAct

    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

    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: UniProt

    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

    ArrayExpressiP01857.
    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 strandi3 – 64
    Beta strandi7 – 148
    Beta strandi16 – 183
    Beta strandi22 – 3514
    Beta strandi38 – 414
    Helixi42 – 443
    Beta strandi45 – 484
    Beta strandi50 – 523
    Beta strandi53 – 586
    Beta strandi63 – 7210
    Helixi73 – 753
    Turni76 – 783
    Beta strandi82 – 876
    Helixi88 – 903
    Beta strandi92 – 976
    Beta strandi101 – 1033
    Helixi107 – 1093
    Beta strandi111 – 1188
    Beta strandi122 – 1265
    Helixi130 – 1345
    Beta strandi136 – 1405
    Beta strandi141 – 1499
    Beta strandi151 – 1533
    Beta strandi157 – 1626
    Beta strandi165 – 1673
    Beta strandi171 – 1733
    Beta strandi176 – 1783
    Beta strandi179 – 1813
    Beta strandi183 – 1908
    Helixi193 – 1975
    Beta strandi202 – 2076
    Beta strandi211 – 2133
    Beta strandi215 – 2195
    Beta strandi223 – 2297
    Beta strandi230 – 2345
    Helixi238 – 2425
    Beta strandi243 – 25816
    Beta strandi261 – 2666
    Beta strandi269 – 2713
    Beta strandi274 – 2763
    Beta strandi283 – 2853
    Beta strandi287 – 29610
    Helixi297 – 3015
    Beta strandi306 – 3116
    Beta strandi313 – 3153
    Helixi316 – 3183
    Beta strandi320 – 3245

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    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.
    HOVERGENiHBG005814.
    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

    ASTKGPSVFP LAPSSKSTSG GTAALGCLVK DYFPEPVTVS WNSGALTSGV    50
    HTFPAVLQSS GLYSLSSVVT VPSSSLGTQT YICNVNHKPS NTKVDKKVEP 100
    KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS 150
    HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK 200
    EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC 250
    LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW 300
    QQGNVFSCSV MHEALHNHYT QKSLSLSPGK 330
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J00228 Genomic DNA. Translation: AAC82527.1 . Different initiation.
    PIRi A93433. GHHU.
    UniGenei Hs.510635.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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 [» ]
    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.

    Chemistry

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

    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.
    HOVERGENi HBG005814.
    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

    ArrayExpressi P01857.
    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

    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: October 1, 2014
    This is version 158 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