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Protein

Gamma-crystallin A

Gene

CRYGA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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

GO - Molecular functioni

  • structural constituent of eye lens Source: UniProtKB

GO - Biological processi

  • lens development in camera-type eye Source: Ensembl
  • visual perception Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Eye lens protein

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-crystallin A
Alternative name(s):
Gamma-A-crystallin
Gamma-crystallin 5
Gene namesi
Name:CRYGA
Synonyms:CRYG1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:2408. CRYGA.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26915.

Polymorphism and mutation databases

BioMutaiCRYGA.
DMDMi148887193.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 174173Gamma-crystallin APRO_0000057585Add
BLAST

Proteomic databases

PaxDbiP11844.
PRIDEiP11844.

PTM databases

PhosphoSiteiP11844.

Expressioni

Gene expression databases

BgeeiP11844.
CleanExiHS_CRYGA.
GenevisibleiP11844. HS.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi107808. 1 interaction.
STRINGi9606.ENSP00000302105.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LERmodel-A1-174[»]
ProteinModelPortaliP11844.
SMRiP11844. Positions 2-174.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiNOG321245.
GeneTreeiENSGT00760000118812.
HOGENOMiHOG000234389.
HOVERGENiHBG003364.
InParanoidiP11844.
OMAiSCRAIPY.
OrthoDBiEOG70CR7Z.
PhylomeDBiP11844.

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.

P11844-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKITFYEDR DFQGRCYNCI SDCPNLRVYF SRCNSIRVDS GCWMLYERPN
60 70 80 90 100
YQGHQYFLRR GKYPDYQHWM GLSDSVQSCR IIPHTSSHKL RLYERDDYRG
110 120 130 140 150
LMSELTDDCA CVPELFRLPE IYSLHVLEGC WVLYEMPNYR GRQYLLRPGD
160 170
YRRYHDWGGA DAKVGSLRRV TDLY
Length:174
Mass (Da):20,877
Last modified:May 29, 2007 - v3
Checksum:i99889A7641728090
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti148 – 1481P → L.2 Publications
VAR_021139

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17316, M17315 Genomic DNA. Translation: AAA52108.1.
EF426311 mRNA. Translation: ABO14696.1.
AC016697 Genomic DNA. Translation: AAX93220.1.
CCDSiCCDS33367.1.
PIRiA26912.
RefSeqiNP_055432.2. NM_014617.3.
UniGeneiHs.122566.

Genome annotation databases

EnsembliENST00000304502; ENSP00000302105; ENSG00000168582.
GeneIDi1418.
KEGGihsa:1418.
UCSCiuc002vcq.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17316, M17315 Genomic DNA. Translation: AAA52108.1.
EF426311 mRNA. Translation: ABO14696.1.
AC016697 Genomic DNA. Translation: AAX93220.1.
CCDSiCCDS33367.1.
PIRiA26912.
RefSeqiNP_055432.2. NM_014617.3.
UniGeneiHs.122566.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LERmodel-A1-174[»]
ProteinModelPortaliP11844.
SMRiP11844. Positions 2-174.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107808. 1 interaction.
STRINGi9606.ENSP00000302105.

PTM databases

PhosphoSiteiP11844.

Polymorphism and mutation databases

BioMutaiCRYGA.
DMDMi148887193.

Proteomic databases

PaxDbiP11844.
PRIDEiP11844.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000304502; ENSP00000302105; ENSG00000168582.
GeneIDi1418.
KEGGihsa:1418.
UCSCiuc002vcq.4. human.

Organism-specific databases

CTDi1418.
GeneCardsiGC02M209025.
HGNCiHGNC:2408. CRYGA.
MIMi123660. gene.
neXtProtiNX_P11844.
PharmGKBiPA26915.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG321245.
GeneTreeiENSGT00760000118812.
HOGENOMiHOG000234389.
HOVERGENiHBG003364.
InParanoidiP11844.
OMAiSCRAIPY.
OrthoDBiEOG70CR7Z.
PhylomeDBiP11844.

Miscellaneous databases

GeneWikiiCRYGA.
GenomeRNAii1418.
NextBioi5799.
PROiP11844.
SOURCEiSearch...

Gene expression databases

BgeeiP11844.
CleanExiHS_CRYGA.
GenevisibleiP11844. HS.

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. "Gamma-crystallins of the human eye lens: expression analysis of five members of the gene family."
    Meakin S.O., Du R.P., Tsui L.-C., Breitman M.L.
    Mol. Cell. Biol. 7:2671-2679(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-148.
  2. "Human gammaA-crystallin."
    Wistow G.
    Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
    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. "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.
  5. "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 LEU-148.

Entry informationi

Entry nameiCRGA_HUMAN
AccessioniPrimary (citable) accession number: P11844
Secondary accession number(s): Q53ST5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: May 29, 2007
Last modified: June 24, 2015
This is version 135 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, 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.