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Protein

Gamma-crystallin D

Gene

CRYGD

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

Functioni

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

GO - Molecular functioni

  1. 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
Complete GO annotation...

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 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:2411. CRYGD.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Cataract 4, multiple types (CTRCT4)8 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn 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.

See also OMIM:115700
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. 2 Publications
VAR_010733
Natural varianti24 – 241P → S in CTRCT4; lowered solubility. 2 Publications
Corresponds to variant rs28931605 [ dbSNP | Ensembl ].
VAR_034955
Natural varianti24 – 241P → T in CTRCT4; lowered solubility. 3 Publications
VAR_021145
Natural varianti37 – 371R → S in CTRCT4; very low solubility; crystallizes spontaneously. 2 Publications
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. 3 Publications
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.
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.

Polymorphism and mutation databases

BioMutaiCRYGD.
DMDMi2506321.

PTM / Processingi

Molecule processing

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

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 – 97Combined sources
Helixi10 – 123Combined sources
Beta strandi13 – 219Combined sources
Turni27 – 293Combined sources
Beta strandi34 – 4815Combined sources
Turni49 – 513Combined sources
Beta strandi52 – 587Combined sources
Beta strandi60 – 656Combined sources
Helixi66 – 694Combined sources
Beta strandi72 – 743Combined sources
Beta strandi78 – 825Combined sources
Beta strandi89 – 957Combined sources
Helixi96 – 983Combined sources
Beta strandi99 – 1079Combined sources
Helixi112 – 1143Combined sources
Beta strandi118 – 1203Combined sources
Beta strandi123 – 1297Combined sources
Beta strandi131 – 1366Combined sources
Turni137 – 1393Combined sources
Beta strandi140 – 1467Combined sources
Beta strandi148 – 1514Combined sources
Helixi154 – 1574Combined sources
Beta strandi166 – 1694Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118812.
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

        10         20         30         40         50
MGKITLYEDR GFQGRHYECS SDHPNLQPYL SRCNSARVDS GCWMLYEQPN
60 70 80 90 100
YSGLQYFLRR GDYADHQQWM GLSDSVRSCR LIPHSGSHRI RLYEREDYRG
110 120 130 140 150
QMIEFTEDCS CLQDRFRFNE IHSLNVLEGS WVLYELSNYR GRQYLLMPGD
160 170
YRRYQDWGAT NARVGSLRRV IDFS
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. 2 Publications
VAR_010733
Natural varianti24 – 241P → S in CTRCT4; lowered solubility. 2 Publications
Corresponds to variant rs28931605 [ dbSNP | Ensembl ].
VAR_034955
Natural varianti24 – 241P → T in CTRCT4; lowered solubility. 3 Publications
VAR_021145
Natural varianti37 – 371R → S in CTRCT4; very low solubility; crystallizes spontaneously. 2 Publications
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. 3 Publications
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:
EMBLi
GenBanki
DDBJi
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 and mutation databases

BioMutaiCRYGD.

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiP07320.

Polymorphism and mutation databases

BioMutaiCRYGD.
DMDMi2506321.

Proteomic databases

MaxQBiP07320.
PaxDbiP07320.
PeptideAtlasiP07320.
PRIDEiP07320.

Protocols and materials databases

DNASUi1421.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1421.
GeneCardsiGC02M208986.
HGNCiHGNC:2411. CRYGD.
MIMi115700. phenotype.
123690. gene.
neXtProtiNX_P07320.
Orphaneti1377. Cataract-microcornea syndrome.
98989. Cerulean cataract.
98986. Coppock-like cataract.
98990. Coralliform cataract.
98991. Nuclear cataract.
98995. Zonular cataract.
PharmGKBiPA26918.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG309484.
GeneTreeiENSGT00760000118812.
HOGENOMiHOG000234389.
HOVERGENiHBG003364.
InParanoidiP07320.
OMAiRGQMMEF.
OrthoDBiEOG70CR7Z.
PhylomeDBiP07320.

Miscellaneous databases

EvolutionaryTraceiP07320.
GeneWikiiCrystallin,_gamma_D.
GenomeRNAii1421.
NextBioi5811.
PROiP07320.
SOURCEiSearch...

Gene expression databases

BgeeiP07320.
CleanExiHS_CRYGD.
GenevestigatoriP07320.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 166 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

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 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.