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Protein

Beta-crystallin B2

Gene

Crybb2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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

  • camera-type eye development Source: RGD
  • visual perception Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Eye lens protein

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-crystallin B2
Alternative name(s):
Beta-B2 crystallin
Beta-crystallin Bp
Gene namesi
Name:Crybb2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 12

Organism-specific databases

RGDi2417. Crybb2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 205204Beta-crystallin B2PRO_0000057556Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP62697.
PRIDEiP62697.

PTM databases

PhosphoSiteiP62697.

Expressioni

Gene expression databases

GenevisibleiP62697. RN.

Interactioni

Subunit structurei

Homo/heterodimer, or complexes of higher-order. The structure of beta-crystallin oligomers seems to be stabilized through interactions between the N-terminal arms (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000067708.

Structurei

Secondary structure

1
205
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 247Combined sources
Helixi25 – 273Combined sources
Beta strandi31 – 366Combined sources
Helixi41 – 444Combined sources
Beta strandi51 – 566Combined sources
Beta strandi59 – 646Combined sources
Turni65 – 673Combined sources
Beta strandi68 – 747Combined sources
Beta strandi76 – 794Combined sources
Helixi82 – 843Combined sources
Beta strandi96 – 983Combined sources
Beta strandi108 – 1147Combined sources
Turni115 – 1173Combined sources
Beta strandi118 – 1269Combined sources
Helixi133 – 1353Combined sources
Beta strandi143 – 1464Combined sources
Beta strandi148 – 1569Combined sources
Helixi157 – 1593Combined sources
Beta strandi160 – 1667Combined sources
Beta strandi168 – 1736Combined sources
Helixi174 – 1774Combined sources
Beta strandi180 – 1823Combined sources
Beta strandi186 – 1905Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BD7X-ray2.78A/B15-192[»]
ProteinModelPortaliP62697.
SMRiP62697. Positions 15-195.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62697.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 5640Beta/gamma crystallin 'Greek key' 1PROSITE-ProRule annotationAdd
BLAST
Domaini57 – 10145Beta/gamma crystallin 'Greek key' 2PROSITE-ProRule annotationAdd
BLAST
Domaini107 – 14842Beta/gamma crystallin 'Greek key' 3PROSITE-ProRule annotationAdd
BLAST
Domaini149 – 19143Beta/gamma crystallin 'Greek key' 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 1615N-terminal armAdd
BLAST
Regioni102 – 1065Connecting peptide
Regioni193 – 20513C-terminal armAdd
BLAST

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

eggNOGiENOG410IJYD. Eukaryota.
ENOG410Y7P1. LUCA.
GeneTreeiENSGT00760000118812.
HOVERGENiHBG003364.
InParanoidiP62697.
OMAiHELTGPC.
OrthoDBiEOG754HNK.
PhylomeDBiP62697.

Family and domain databases

InterProiIPR001064. Beta/gamma_crystallin.
IPR033058. CRYBB2.
IPR011024. G_crystallin-rel.
[Graphical view]
PANTHERiPTHR11818:SF11. PTHR11818:SF11. 1 hit.
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.

P62697-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASDHQTQAG KPQPLNPKII IFEQENFQGH SHELSGPCPN LKETGMEKAG
60 70 80 90 100
SVLVQAGPWV GYEQANCKGE QFVFEKGEYP RWDSWTSSRR TDSLSSLRPI
110 120 130 140 150
KVDSQEHKII LYENPNFTGK KMEIVDDDVP SFHAHGYQEK VSSVRVQSGT
160 170 180 190 200
WVGYQYPGYR GLQYLLEKGD YKDNSDFGAP HPQVQSVRRI RDMQWHQRGA

FHPSS
Length:205
Mass (Da):23,381
Last modified:January 23, 2007 - v2
Checksum:i73B4C4789D79B9FA
GO

Mass spectrometryi

Molecular mass is 23292.0 Da from positions 2 - 205. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16072 mRNA. Translation: CAA34204.1.
PIRiS05015.
RefSeqiNP_037069.1. NM_012937.1.
UniGeneiRn.10350.

Genome annotation databases

EnsembliENSRNOT00000072683; ENSRNOP00000067708; ENSRNOG00000050023.
GeneIDi25422.
KEGGirno:25422.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16072 mRNA. Translation: CAA34204.1.
PIRiS05015.
RefSeqiNP_037069.1. NM_012937.1.
UniGeneiRn.10350.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BD7X-ray2.78A/B15-192[»]
ProteinModelPortaliP62697.
SMRiP62697. Positions 15-195.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000067708.

PTM databases

PhosphoSiteiP62697.

Proteomic databases

PaxDbiP62697.
PRIDEiP62697.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000072683; ENSRNOP00000067708; ENSRNOG00000050023.
GeneIDi25422.
KEGGirno:25422.

Organism-specific databases

CTDi1415.
RGDi2417. Crybb2.

Phylogenomic databases

eggNOGiENOG410IJYD. Eukaryota.
ENOG410Y7P1. LUCA.
GeneTreeiENSGT00760000118812.
HOVERGENiHBG003364.
InParanoidiP62697.
OMAiHELTGPC.
OrthoDBiEOG754HNK.
PhylomeDBiP62697.

Miscellaneous databases

EvolutionaryTraceiP62697.
NextBioi606587.
PROiP62697.

Gene expression databases

GenevisibleiP62697. RN.

Family and domain databases

InterProiIPR001064. Beta/gamma_crystallin.
IPR033058. CRYBB2.
IPR011024. G_crystallin-rel.
[Graphical view]
PANTHERiPTHR11818:SF11. PTHR11818:SF11. 1 hit.
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

  1. "Crystallin gene expression during rat lens development."
    Aarts H.J.M., Lubsen N.H., Schoenmakers J.G.G.
    Eur. J. Biochem. 183:31-36(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Lubsen N.H.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Beta-crystallins insolubilized by calpain II in vitro contain cleavage sites similar to beta-crystallins insolubilized during cataract."
    David L.L., Shearer T.R.
    FEBS Lett. 324:265-270(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 9-14.
  4. "Lens proteomics: analysis of rat crystallin sequences and two-dimensional electrophoresis map."
    Lampi K.J., Shih M., Ueda Y., Shearer T.R., David L.L.
    Invest. Ophthalmol. Vis. Sci. 43:216-224(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Lens.
  5. "Circular permutation of betaB2-crystallin changes the hierarchy of domain assembly."
    Wright G., Basak A.K., Wieligmann K., Mayr E.M., Slingsby C.
    Protein Sci. 7:1280-1285(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.78 ANGSTROMS).

Entry informationi

Entry nameiCRBB2_RAT
AccessioniPrimary (citable) accession number: P62697
Secondary accession number(s): P19942, P26775
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.