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Protein

Beta-crystallin S

Gene

CRYGS

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Eye lens protein

Enzyme and pathway databases

BioCyciZFISH:G66-31975-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-crystallin S
Alternative name(s):
Gamma-S-crystallin
Gamma-crystallin S
Gene namesi
Name:CRYGS
Synonyms:CRYG8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:2417. CRYGS.

Pathology & Biotechi

Involvement in diseasei

Cataract 20, multiple types (CTRCT20)1 Publication
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. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. CTRCT20 includes progressive polymorphic anterior, posterior, or peripheral cortical.
See also OMIM:116100
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06979718G → V in CTRCT20. 1 PublicationCorresponds to variant rs104893736dbSNPEnsembl.1

Keywords - Diseasei

Cataract, Disease mutation

Organism-specific databases

DisGeNETi1427.
MalaCardsiCRYGS.
MIMi116100. phenotype.
OpenTargetsiENSG00000213139.
Orphaneti306561. Autosomal dominant childhood-onset cortical cataract.
PharmGKBiPA26922.

Polymorphism and mutation databases

BioMutaiCRYGS.
DMDMi4033688.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000575652 – 178Beta-crystallin SAdd BLAST177

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP22914.
PeptideAtlasiP22914.
PRIDEiP22914.

PTM databases

iPTMnetiP22914.
PhosphoSitePlusiP22914.

Expressioni

Gene expression databases

BgeeiENSG00000213139.
CleanExiHS_CRYGS.
ExpressionAtlasiP22914. baseline and differential.
GenevisibleiP22914. HS.

Organism-specific databases

HPAiHPA035103.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi107814. 3 interactors.
DIPiDIP-60585N.
IntActiP22914. 3 interactors.
STRINGi9606.ENSP00000312099.

Structurei

Secondary structure

1178
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 14Combined sources7
Beta strandi18 – 25Combined sources8
Turni31 – 33Combined sources3
Beta strandi38 – 41Combined sources4
Beta strandi43 – 45Combined sources3
Beta strandi47 – 52Combined sources6
Turni53 – 55Combined sources3
Beta strandi56 – 62Combined sources7
Beta strandi64 – 69Combined sources6
Helixi70 – 73Combined sources4
Beta strandi76 – 78Combined sources3
Beta strandi83 – 85Combined sources3
Beta strandi95 – 101Combined sources7
Turni102 – 104Combined sources3
Beta strandi105 – 113Combined sources9
Helixi118 – 122Combined sources5
Beta strandi129 – 135Combined sources7
Beta strandi137 – 142Combined sources6
Turni143 – 145Combined sources3
Beta strandi146 – 152Combined sources7
Beta strandi154 – 159Combined sources6
Helixi160 – 163Combined sources4
Beta strandi166 – 169Combined sources4
Beta strandi172 – 175Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HA4X-ray2.40A/B92-178[»]
2M3TNMR-A2-178[»]
2M3UNMR-A2-178[»]
ProteinModelPortaliP22914.
SMRiP22914.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22914.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 44Beta/gamma crystallin 'Greek key' 1PROSITE-ProRule annotationAdd BLAST39
Domaini45 – 87Beta/gamma crystallin 'Greek key' 2PROSITE-ProRule annotationAdd BLAST43
Domaini94 – 134Beta/gamma crystallin 'Greek key' 3PROSITE-ProRule annotationAdd BLAST41
Domaini135 – 177Beta/gamma crystallin 'Greek key' 4PROSITE-ProRule annotationAdd BLAST43

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 5N-terminal arm4
Regioni88 – 93Connecting peptide6

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

eggNOGiENOG410IEJ7. Eukaryota.
ENOG4111EVU. LUCA.
GeneTreeiENSGT00760000118812.
HOGENOMiHOG000234389.
HOVERGENiHBG003364.
InParanoidiP22914.
OMAiQSFRRIM.
OrthoDBiEOG091G0L2P.
PhylomeDBiP22914.

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.

P22914-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKTGTKITF YEDKNFQGRR YDCDCDCADF HTYLSRCNSI KVEGGTWAVY
60 70 80 90 100
ERPNFAGYMY ILPQGEYPEY QRWMGLNDRL SSCRAVHLPS GGQYKIQIFE
110 120 130 140 150
KGDFSGQMYE TTEDCPSIME QFHMREIHSC KVLEGVWIFY ELPNYRGRQY
160 170
LLDKKEYRKP IDWGAASPAV QSFRRIVE
Length:178
Mass (Da):21,007
Last modified:January 23, 2007 - v4
Checksum:i29C46720A80EF6C2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti4T → A AA sequence (PubMed:1445197).Curated1
Sequence conflicti20R → H AA sequence (PubMed:1445197).Curated1
Sequence conflicti23C → S AA sequence (PubMed:1445197).Curated1
Sequence conflicti29D → E AA sequence (PubMed:1445197).Curated1
Sequence conflicti32T → M AA sequence (PubMed:1445197).Curated1
Sequence conflicti41K → R AA sequence (PubMed:1445197).Curated1
Sequence conflicti52R → T AA sequence (PubMed:1445197).Curated1
Sequence conflicti105S → N AA sequence (PubMed:1445197).Curated1
Sequence conflicti109Y → R AA sequence (PubMed:1445197).Curated1
Sequence conflicti114D → N AA sequence (PubMed:1445197).Curated1

Mass spectrometryi

Molecular mass is 20918±0.3 Da from positions 2 - 178. Determined by ESI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06979718G → V in CTRCT20. 1 PublicationCorresponds to variant rs104893736dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK314172 mRNA. Translation: BAG36855.1.
AF161703 mRNA. Translation: AAD45901.1.
AF242198, AF242197 Genomic DNA. Translation: AAF72490.1.
CH471052 Genomic DNA. Translation: EAW78195.1.
BC069478 mRNA. Translation: AAH69478.1.
BC070241 mRNA. Translation: AAH70241.1.
L36869 mRNA. Translation: AAA92870.1.
CCDSiCCDS3275.1.
PIRiS29111.
S55269.
RefSeqiNP_060011.1. NM_017541.3.
UniGeneiHs.376209.

Genome annotation databases

EnsembliENST00000307944; ENSP00000312099; ENSG00000213139.
ENST00000392499; ENSP00000376287; ENSG00000213139.
GeneIDi1427.
KEGGihsa:1427.
UCSCiuc003fqe.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK314172 mRNA. Translation: BAG36855.1.
AF161703 mRNA. Translation: AAD45901.1.
AF242198, AF242197 Genomic DNA. Translation: AAF72490.1.
CH471052 Genomic DNA. Translation: EAW78195.1.
BC069478 mRNA. Translation: AAH69478.1.
BC070241 mRNA. Translation: AAH70241.1.
L36869 mRNA. Translation: AAA92870.1.
CCDSiCCDS3275.1.
PIRiS29111.
S55269.
RefSeqiNP_060011.1. NM_017541.3.
UniGeneiHs.376209.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HA4X-ray2.40A/B92-178[»]
2M3TNMR-A2-178[»]
2M3UNMR-A2-178[»]
ProteinModelPortaliP22914.
SMRiP22914.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107814. 3 interactors.
DIPiDIP-60585N.
IntActiP22914. 3 interactors.
STRINGi9606.ENSP00000312099.

PTM databases

iPTMnetiP22914.
PhosphoSitePlusiP22914.

Polymorphism and mutation databases

BioMutaiCRYGS.
DMDMi4033688.

Proteomic databases

PaxDbiP22914.
PeptideAtlasiP22914.
PRIDEiP22914.

Protocols and materials databases

DNASUi1427.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000307944; ENSP00000312099; ENSG00000213139.
ENST00000392499; ENSP00000376287; ENSG00000213139.
GeneIDi1427.
KEGGihsa:1427.
UCSCiuc003fqe.4. human.

Organism-specific databases

CTDi1427.
DisGeNETi1427.
GeneCardsiCRYGS.
HGNCiHGNC:2417. CRYGS.
HPAiHPA035103.
MalaCardsiCRYGS.
MIMi116100. phenotype.
123730. gene.
neXtProtiNX_P22914.
OpenTargetsiENSG00000213139.
Orphaneti306561. Autosomal dominant childhood-onset cortical cataract.
PharmGKBiPA26922.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IEJ7. Eukaryota.
ENOG4111EVU. LUCA.
GeneTreeiENSGT00760000118812.
HOGENOMiHOG000234389.
HOVERGENiHBG003364.
InParanoidiP22914.
OMAiQSFRRIM.
OrthoDBiEOG091G0L2P.
PhylomeDBiP22914.

Enzyme and pathway databases

BioCyciZFISH:G66-31975-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP22914.
GeneWikiiCRYGS.
GenomeRNAii1427.
PROiP22914.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000213139.
CleanExiHS_CRYGS.
ExpressionAtlasiP22914. baseline and differential.
GenevisibleiP22914. 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...

Entry informationi

Entry nameiCRBS_HUMAN
AccessioniPrimary (citable) accession number: P22914
Secondary accession number(s): B2RAF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 163 of the entry and version 4 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 3
    Human chromosome 3: 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

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 one 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.