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P07320

- CRGD_HUMAN

UniProt

P07320 - CRGD_HUMAN

Protein

Gamma-crystallin D

Gene

CRYGD

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

    Crystallins are the dominant structural components of the vertebrate eye lens.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei46 – 461Susceptible to oxidation

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. structural constituent of eye lens Source: UniProtKB

    GO - Biological processi

    1. cellular response to reactive oxygen species Source: UniProtKB
    2. lens development in camera-type eye Source: UniProtKB
    3. lens fiber cell differentiation Source: UniProtKB
    4. visual perception Source: UniProtKB

    Keywords - Molecular functioni

    Eye lens protein

    Keywords - Biological processi

    Sensory transduction, Vision

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gamma-crystallin D
    Alternative name(s):
    Gamma-D-crystallin
    Gamma-crystallin 4
    Gene namesi
    Name:CRYGD
    Synonyms:CRYG4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:2411. CRYGD.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProtKB

    Pathology & Biotechi

    Involvement in diseasei

    Cataract 4, multiple types (CTRCT4) [MIM:115700]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. CTRCT4 includes crystalline aculeiform, congenital cerulean and non-nuclear polymorphic cataracts, among others. Crystalline aculeiform cataract is characterized by fiberglass-like or needle-like crystals projecting in different directions, through or close to the axial region of the lens. Non-nuclear polymorphic cataract is a partial opacity with variable location between the fetal nucleus of the lens and the equator. The fetal nucleus is normal. The opacities are irregular and look similar to a bunch of grapes and may be present simultaneously in different lens layers. Congenital cerulean cataract is characterized by peripheral bluish and white opacifications organized in concentric layers with occasional central lesions arranged radially. The opacities are observed in the superficial layers of the fetal nucleus as well as the adult nucleus of the lens. Involvement is usually bilateral. Visual acuity is only mildly reduced in childhood. In adulthood, the opacifications may progress, making lens extraction necessary. Histologically the lesions are described as fusiform cavities between lens fibers which contain a deeply staining granular material. Although the lesions may take on various colors, a dull blue is the most common appearance and is responsible for the designation cerulean cataract.8 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti15 – 151R → C in CTRCT4; progressive punctate cataract with early onset; causes disulfide-linked oligomers formation with consequent protein aggregation and precipitation. 1 Publication
    VAR_010733
    Natural varianti24 – 241P → S in CTRCT4; lowered solubility. 1 Publication
    Corresponds to variant rs28931605 [ dbSNP | Ensembl ].
    VAR_034955
    Natural varianti24 – 241P → T in CTRCT4; lowered solubility. 2 Publications
    VAR_021145
    Natural varianti37 – 371R → S in CTRCT4; very low solubility; crystallizes spontaneously. 1 Publication
    VAR_010734
    Natural varianti43 – 431W → R in CTRCT4; much less stable than the wild-type protein; more prone to aggregate when subjected to environmental stresses such as heat and UV irradiation. 1 Publication
    VAR_064829
    Natural varianti59 – 591R → H in CTRCT4; lowered solubility; crystallizes easily. 1 Publication
    VAR_010735
    Natural varianti107 – 1071E → A in CTRCT4. 1 Publication
    VAR_034956

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi24 – 252PN → TK: Wild-type solubility. 1 Publication
    Mutagenesisi24 – 241P → TP: Wild-type solubility. 1 Publication
    Mutagenesisi24 – 241P → V: Slightly lowered solubility. 1 Publication

    Keywords - Diseasei

    Cataract, Disease mutation

    Organism-specific databases

    MIMi115700. phenotype.
    Orphaneti1377. Cataract-microcornea syndrome.
    98989. Cerulean cataract.
    98986. Coppock-like cataract.
    98990. Coralliform cataract.
    98991. Nuclear cataract.
    98995. Zonular cataract.
    PharmGKBiPA26918.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 174173Gamma-crystallin DPRO_0000057588Add
    BLAST

    Keywords - PTMi

    Oxidation

    Proteomic databases

    MaxQBiP07320.
    PaxDbiP07320.
    PeptideAtlasiP07320.
    PRIDEiP07320.

    PTM databases

    PhosphoSiteiP07320.

    Expressioni

    Gene expression databases

    BgeeiP07320.
    CleanExiHS_CRYGD.
    GenevestigatoriP07320.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CryaaP246232EBI-7673124,EBI-7673244From a different organism.
    CryabP239272EBI-7673124,EBI-299046From a different organism.

    Protein-protein interaction databases

    BioGridi107811. 4 interactions.
    DIPiDIP-46208N.
    IntActiP07320. 2 interactions.
    MINTiMINT-8303016.
    STRINGi9606.ENSP00000264376.

    Structurei

    Secondary structure

    1
    174
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 97
    Helixi10 – 123
    Beta strandi13 – 219
    Turni27 – 293
    Beta strandi34 – 4815
    Turni49 – 513
    Beta strandi52 – 587
    Beta strandi60 – 656
    Helixi66 – 694
    Beta strandi72 – 743
    Beta strandi78 – 825
    Beta strandi89 – 957
    Helixi96 – 983
    Beta strandi99 – 1079
    Helixi112 – 1143
    Beta strandi118 – 1203
    Beta strandi123 – 1297
    Beta strandi131 – 1366
    Turni137 – 1393
    Beta strandi140 – 1467
    Beta strandi148 – 1514
    Helixi154 – 1574
    Beta strandi166 – 1694

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1H4AX-ray1.15X2-174[»]
    1HK0X-ray1.25X2-174[»]
    1LD0model-A1-174[»]
    2G98X-ray2.20A/B2-174[»]
    2KFBNMR-A2-174[»]
    2KLJOther-A2-174[»]
    4GR7X-ray1.70A/X2-174[»]
    4JGFX-ray2.50A/B2-172[»]
    ProteinModelPortaliP07320.
    SMRiP07320. Positions 2-174.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07320.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 4039Beta/gamma crystallin 'Greek key' 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini41 – 8343Beta/gamma crystallin 'Greek key' 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini88 – 12841Beta/gamma crystallin 'Greek key' 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini129 – 17143Beta/gamma crystallin 'Greek key' 4PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni84 – 874Connecting peptide

    Domaini

    Has a two-domain beta-structure, folded into four very similar Greek key motifs.

    Sequence similaritiesi

    Belongs to the beta/gamma-crystallin family.Curated
    Contains 4 beta/gamma crystallin 'Greek key' domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG309484.
    HOGENOMiHOG000234389.
    HOVERGENiHBG003364.
    InParanoidiP07320.
    OMAiRGQMMEF.
    OrthoDBiEOG70CR7Z.
    PhylomeDBiP07320.

    Family and domain databases

    InterProiIPR001064. Beta/gamma_crystallin.
    IPR011024. G_crystallin-rel.
    [Graphical view]
    PfamiPF00030. Crystall. 2 hits.
    [Graphical view]
    PRINTSiPR01367. BGCRYSTALLIN.
    SMARTiSM00247. XTALbg. 2 hits.
    [Graphical view]
    SUPFAMiSSF49695. SSF49695. 1 hit.
    PROSITEiPS50915. CRYSTALLIN_BETA_GAMMA. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P07320-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGKITLYEDR GFQGRHYECS SDHPNLQPYL SRCNSARVDS GCWMLYEQPN    50
    YSGLQYFLRR GDYADHQQWM GLSDSVRSCR LIPHSGSHRI RLYEREDYRG 100
    QMIEFTEDCS CLQDRFRFNE IHSLNVLEGS WVLYELSNYR GRQYLLMPGD 150
    YRRYQDWGAT NARVGSLRRV IDFS 174
    Length:174
    Mass (Da):20,738
    Last modified:January 23, 2007 - v3
    Checksum:i437EC83FD79F12E4
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti15 – 151R → C in CTRCT4; progressive punctate cataract with early onset; causes disulfide-linked oligomers formation with consequent protein aggregation and precipitation. 1 Publication
    VAR_010733
    Natural varianti24 – 241P → S in CTRCT4; lowered solubility. 1 Publication
    Corresponds to variant rs28931605 [ dbSNP | Ensembl ].
    VAR_034955
    Natural varianti24 – 241P → T in CTRCT4; lowered solubility. 2 Publications
    VAR_021145
    Natural varianti37 – 371R → S in CTRCT4; very low solubility; crystallizes spontaneously. 1 Publication
    VAR_010734
    Natural varianti43 – 431W → R in CTRCT4; much less stable than the wild-type protein; more prone to aggregate when subjected to environmental stresses such as heat and UV irradiation. 1 Publication
    VAR_064829
    Natural varianti59 – 591R → H in CTRCT4; lowered solubility; crystallizes easily. 1 Publication
    VAR_010735
    Natural varianti102 – 1021M → V.2 Publications
    VAR_021146
    Natural varianti107 – 1071E → A in CTRCT4. 1 Publication
    VAR_034956

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K03006, K03005 Genomic DNA. Translation: AAA52112.1.
    U66583 mRNA. Translation: AAB38686.1.
    AC093698 Genomic DNA. Translation: AAY24041.1.
    BC117338 mRNA. Translation: AAI17339.1.
    BC117340 mRNA. Translation: AAI17341.1.
    CCDSiCCDS2378.1.
    PIRiI77413.
    RefSeqiNP_008822.2. NM_006891.3.
    UniGeneiHs.546247.

    Genome annotation databases

    EnsembliENST00000264376; ENSP00000264376; ENSG00000118231.
    GeneIDi1421.
    KEGGihsa:1421.
    UCSCiuc002vcn.4. human.

    Polymorphism databases

    DMDMi2506321.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Eye disease Crystallin, gamma-D (CRYGD)

    Leiden Open Variation Database (LOVD)

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K03006 , K03005 Genomic DNA. Translation: AAA52112.1 .
    U66583 mRNA. Translation: AAB38686.1 .
    AC093698 Genomic DNA. Translation: AAY24041.1 .
    BC117338 mRNA. Translation: AAI17339.1 .
    BC117340 mRNA. Translation: AAI17341.1 .
    CCDSi CCDS2378.1.
    PIRi I77413.
    RefSeqi NP_008822.2. NM_006891.3.
    UniGenei Hs.546247.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1H4A X-ray 1.15 X 2-174 [» ]
    1HK0 X-ray 1.25 X 2-174 [» ]
    1LD0 model - A 1-174 [» ]
    2G98 X-ray 2.20 A/B 2-174 [» ]
    2KFB NMR - A 2-174 [» ]
    2KLJ Other - A 2-174 [» ]
    4GR7 X-ray 1.70 A/X 2-174 [» ]
    4JGF X-ray 2.50 A/B 2-172 [» ]
    ProteinModelPortali P07320.
    SMRi P07320. Positions 2-174.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107811. 4 interactions.
    DIPi DIP-46208N.
    IntActi P07320. 2 interactions.
    MINTi MINT-8303016.
    STRINGi 9606.ENSP00000264376.

    PTM databases

    PhosphoSitei P07320.

    Polymorphism databases

    DMDMi 2506321.

    Proteomic databases

    MaxQBi P07320.
    PaxDbi P07320.
    PeptideAtlasi P07320.
    PRIDEi P07320.

    Protocols and materials databases

    DNASUi 1421.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264376 ; ENSP00000264376 ; ENSG00000118231 .
    GeneIDi 1421.
    KEGGi hsa:1421.
    UCSCi uc002vcn.4. human.

    Organism-specific databases

    CTDi 1421.
    GeneCardsi GC02M208986.
    HGNCi HGNC:2411. CRYGD.
    MIMi 115700. phenotype.
    123690. gene.
    neXtProti NX_P07320.
    Orphaneti 1377. Cataract-microcornea syndrome.
    98989. Cerulean cataract.
    98986. Coppock-like cataract.
    98990. Coralliform cataract.
    98991. Nuclear cataract.
    98995. Zonular cataract.
    PharmGKBi PA26918.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG309484.
    HOGENOMi HOG000234389.
    HOVERGENi HBG003364.
    InParanoidi P07320.
    OMAi RGQMMEF.
    OrthoDBi EOG70CR7Z.
    PhylomeDBi P07320.

    Miscellaneous databases

    EvolutionaryTracei P07320.
    GeneWikii Crystallin,_gamma_D.
    GenomeRNAii 1421.
    NextBioi 5811.
    PROi P07320.
    SOURCEi Search...

    Gene expression databases

    Bgeei P07320.
    CleanExi HS_CRYGD.
    Genevestigatori P07320.

    Family and domain databases

    InterProi IPR001064. Beta/gamma_crystallin.
    IPR011024. G_crystallin-rel.
    [Graphical view ]
    Pfami PF00030. Crystall. 2 hits.
    [Graphical view ]
    PRINTSi PR01367. BGCRYSTALLIN.
    SMARTi SM00247. XTALbg. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49695. SSF49695. 1 hit.
    PROSITEi PS50915. CRYSTALLIN_BETA_GAMMA. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structural and evolutionary relationships among five members of the human gamma-crystallin gene family."
      Meakin S.O., Breitman M.L., Tsui L.-C.
      Mol. Cell. Biol. 5:1408-1414(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-102.
    2. "Cloning and expression of human lens crystallins."
      Petrash J.M., Mathur S., Manoharan M., Andley U.P.
      Invest. Ophthalmol. Vis. Sci. 36:S882-S882(1995)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lens.
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.
    5. "Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the identification of the major proteins in young human lens."
      Lampi K.J., Ma Z., Shih M., Shearer T.R., Smith J.B., Smith D.L., David L.L.
      J. Biol. Chem. 272:2268-2275(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-11.
    6. "Decrease in protein solubility and cataract formation caused by the Pro23 to Thr mutation in human gamma D-crystallin."
      Pande A., Annunziata O., Asherie N., Ogun O., Benedek G.B., Pande J.
      Biochemistry 44:2491-2500(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF PRO-24, CHARACTERIZATION OF VARIANTS CTRCT4 THR-24 AND SER-24.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "High-resolution X-ray crystal structures of human gammaD crystallin (1.25 A) and the R58H mutant (1.15 A) associated with aculeiform cataract."
      Basak A., Bateman O., Slingsby C., Pande A., Asherie N., Ogun O., Benedek G.B., Pande J.
      J. Mol. Biol. 328:1137-1147(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS), X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF VARIANT HIS-59.
    9. "Homology models of human gamma-crystallins: structural study of the extensive charge network in gamma-crystallins."
      Salim A., Zaidi Z.H.
      Biochem. Biophys. Res. Commun. 300:624-630(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING.
    10. Cited for: VARIANT CTRCT4 HIS-59.
    11. Cited for: VARIANT CTRCT4 CYS-15.
    12. "Link between a novel human gamma-D-crystallin allele and a unique cataract phenotype explained by protein crystallography."
      Kmoch S., Brynda J., Asfaw B., Bezouska K., Novak P., Rezacova P., Ondrova L., Filipec M., Sedlacek J., Elleder M.
      Hum. Mol. Genet. 9:1779-1786(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CTRCT4 SER-37.
    13. Cited for: SUBUNIT, CHARACTERIZATION OF VARIANT CTRCT4 CYS-15.
    14. "Crystal cataracts: human genetic cataract caused by protein crystallization."
      Pande A., Pande J., Asherie N., Lomakin A., Ogun O., King J., Benedek G.B.
      Proc. Natl. Acad. Sci. U.S.A. 98:6116-6120(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS CTRCT4 SER-37 AND HIS-59.
    15. "Novel mutations in the gamma-crystallin genes cause autosomal dominant congenital cataracts."
      Santhiya S.T., Shyam Manohar M., Rawlley D., Vijayalakshmi P., Namperumalsamy P., Gopinath P.M., Loester J., Graw J.
      J. Med. Genet. 39:352-358(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CTRCT4 THR-24, VARIANT VAL-102.
    16. "Gamma-D crystallin gene (CRYGD) mutation causes autosomal dominant congenital cerulean cataracts."
      Nandrot E., Slingsby C., Basak A., Cherif-Chefchaouni M., Benazzouz B., Hajaji Y., Boutayeb S., Gribouval O., Arbogast L., Berraho A., Abitbol M., Hilal L.
      J. Med. Genet. 40:262-267(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CTRCT4 THR-24.
    17. "Two affected siblings with nuclear cataract associated with a novel missense mutation in the CRYGD gene."
      Messina-Baas O.M., Gonzalez-Huerta L.M., Cuevas-Covarrubias S.A.
      Mol. Vis. 12:995-1000(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CTRCT4 ALA-107.
    18. "Conversion and compensatory evolution of the gamma-crystallin genes and identification of a cataractogenic mutation that reverses the sequence of the human CRYGD gene to an ancestral state."
      Plotnikova O.V., Kondrashov F.A., Vlasov P.K., Grigorenko A.P., Ginter E.K., Rogaev E.I.
      Am. J. Hum. Genet. 81:32-43(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CTRCT4 SER-24.
    19. "A novel CRYGD mutation (p.Trp43Arg) causing autosomal dominant congenital cataract in a Chinese family."
      Wang B., Yu C., Xi Y.B., Cai H.C., Wang J., Zhou S., Zhou S., Wu Y., Yan Y.B., Ma X., Xie L.
      Hum. Mutat. 32:E1939-E1947(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CTRCT4 ARG-43, CHARACTERIZATION OF VARIANT CTRCT4 ARG-43.

    Entry informationi

    Entry nameiCRGD_HUMAN
    AccessioniPrimary (citable) accession number: P07320
    Secondary accession number(s): Q17RF7, Q53R51, Q99681
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 161 of the entry and version 3 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 2
      Human chromosome 2: 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
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3