Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000575562 – 205Beta-crystallin B2Add BLAST204

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP62697.

PTM databases

PhosphoSitePlusiP62697.

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

1205
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi18 – 24Combined sources7
Helixi25 – 27Combined sources3
Beta strandi31 – 36Combined sources6
Helixi41 – 44Combined sources4
Beta strandi51 – 56Combined sources6
Beta strandi59 – 64Combined sources6
Turni65 – 67Combined sources3
Beta strandi68 – 74Combined sources7
Beta strandi76 – 79Combined sources4
Helixi82 – 84Combined sources3
Beta strandi96 – 98Combined sources3
Beta strandi108 – 114Combined sources7
Turni115 – 117Combined sources3
Beta strandi118 – 126Combined sources9
Helixi133 – 135Combined sources3
Beta strandi143 – 146Combined sources4
Beta strandi148 – 156Combined sources9
Helixi157 – 159Combined sources3
Beta strandi160 – 166Combined sources7
Beta strandi168 – 173Combined sources6
Helixi174 – 177Combined sources4
Beta strandi180 – 182Combined sources3
Beta strandi186 – 190Combined sources5

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP62697.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini17 – 56Beta/gamma crystallin 'Greek key' 1PROSITE-ProRule annotationAdd BLAST40
Domaini57 – 101Beta/gamma crystallin 'Greek key' 2PROSITE-ProRule annotationAdd BLAST45
Domaini107 – 148Beta/gamma crystallin 'Greek key' 3PROSITE-ProRule annotationAdd BLAST42
Domaini149 – 191Beta/gamma crystallin 'Greek key' 4PROSITE-ProRule annotationAdd BLAST43

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 16N-terminal armAdd BLAST15
Regioni102 – 106Connecting peptide5
Regioni193 – 205C-terminal armAdd BLAST13

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.
OrthoDBiEOG091G0KRX.
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.
XP_017453762.1. XM_017598273.1.
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.
XP_017453762.1. XM_017598273.1.
UniGeneiRn.10350.

3D structure databases

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000067708.

PTM databases

PhosphoSitePlusiP62697.

Proteomic databases

PaxDbiP62697.

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.
OrthoDBiEOG091G0KRX.
PhylomeDBiP62697.

Miscellaneous databases

EvolutionaryTraceiP62697.
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...

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: November 30, 2016
This is version 87 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.