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Protein

Beta-crystallin B2

Gene

CRYBB2

Organism
Bos taurus (Bovine)
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

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-crystallin B2
Alternative name(s):
Beta-B2 crystallin
Beta-crystallin Bp
Gene namesi
Name:CRYBB2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 17

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000575522 – 205Beta-crystallin B2Add BLAST204

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Glycosylationi11N-linked (Glc) (glycation); in vitro1
Glycosylationi48N-linked (Glc) (glycation); in vitro1
Glycosylationi68N-linked (Glc) (glycation); in vitro1
Glycosylationi76N-linked (Glc) (glycation); in vitro1
Glycosylationi101N-linked (Glc) (glycation); in vitro1
Glycosylationi108N-linked (Glc) (glycation); in vitro1
Glycosylationi120N-linked (Glc) (glycation); in vitro1
Glycosylationi121N-linked (Glc) (glycation); in vitro1
Glycosylationi140N-linked (Glc) (glycation); in vitro1
Glycosylationi168N-linked (Glc) (glycation); in vitro1
Glycosylationi172N-linked (Glc) (glycation); in vitro1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei18Not glycated1
Sitei42Not glycated1

Keywords - PTMi

Acetylation, Glycation, Glycoprotein

Proteomic databases

PaxDbiP02522.

PTM databases

iPTMnetiP02522.

Expressioni

Gene expression databases

BgeeiENSBTAG00000004088.

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

IntActiP02522. 1 interactor.
STRINGi9913.ENSBTAP00000005341.

Structurei

Secondary structure

1205
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi18 – 24Combined sources7
Turni25 – 27Combined sources3
Beta strandi28 – 36Combined sources9
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 – 99Combined sources4
Beta strandi108 – 114Combined sources7
Turni115 – 117Combined sources3
Beta strandi118 – 127Combined sources10
Helixi133 – 135Combined sources3
Beta strandi143 – 146Combined sources4
Beta strandi151 – 156Combined sources6
Turni157 – 159Combined sources3
Beta strandi160 – 166Combined sources7
Beta strandi168 – 173Combined sources6
Helixi174 – 177Combined sources4
Beta strandi180 – 182Combined sources3
Beta strandi186 – 189Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BLBX-ray3.30A/B/C/D2-205[»]
2BB2X-ray2.10A15-195[»]
ProteinModelPortaliP02522.
SMRiP02522.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02522.

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.
HOGENOMiHOG000234388.
HOVERGENiHBG003364.
InParanoidiP02522.
OMAiHELTGPC.
OrthoDBiEOG091G0KRX.
TreeFamiTF331401.

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.

P02522-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASDHQTQAG KPQPLNPKII IFEQENFQGH SHELNGPCPN LKETGVEKAG
60 70 80 90 100
SVLVQAGPWV GYEQANCKGE QFVFEKGEYP RWDSWTSSRR TDSLSSLRPI
110 120 130 140 150
KVDSQEHKIT LYENPNFTGK KMEVIDDDVP SFHAHGYQEK VSSVRVQSGT
160 170 180 190 200
WVGYQYPGYR GLQYLLEKGD YKDSGDFGAP QPQVQSVRRI RDMQWHQRGA

FHPSS
Length:205
Mass (Da):23,298
Last modified:January 23, 2007 - v3
Checksum:i9613C228491E3C8C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti4D → N AA sequence (PubMed:7035168).Curated1
Sequence conflicti6Q → E AA sequence (PubMed:7035168).Curated1
Sequence conflicti28Q → H AA sequence (PubMed:7035168).Curated1
Sequence conflicti32H → Q AA sequence (PubMed:7035168).Curated1
Sequence conflicti36 – 37GP → PG AA sequence (PubMed:7035168).Curated2
Sequence conflicti40N → C AA sequence (PubMed:7035168).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22466 mRNA. Translation: AAA30472.1.
PIRiA54730. CYBOB.
RefSeqiNP_777232.1. NM_174807.1.
UniGeneiBt.398.

Genome annotation databases

EnsembliENSBTAT00000005341; ENSBTAP00000005341; ENSBTAG00000004088.
GeneIDi287011.
KEGGibta:287011.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22466 mRNA. Translation: AAA30472.1.
PIRiA54730. CYBOB.
RefSeqiNP_777232.1. NM_174807.1.
UniGeneiBt.398.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BLBX-ray3.30A/B/C/D2-205[»]
2BB2X-ray2.10A15-195[»]
ProteinModelPortaliP02522.
SMRiP02522.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP02522. 1 interactor.
STRINGi9913.ENSBTAP00000005341.

PTM databases

iPTMnetiP02522.

Proteomic databases

PaxDbiP02522.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000005341; ENSBTAP00000005341; ENSBTAG00000004088.
GeneIDi287011.
KEGGibta:287011.

Organism-specific databases

CTDi1415.

Phylogenomic databases

eggNOGiENOG410IJYD. Eukaryota.
ENOG410Y7P1. LUCA.
GeneTreeiENSGT00760000118812.
HOGENOMiHOG000234388.
HOVERGENiHBG003364.
InParanoidiP02522.
OMAiHELTGPC.
OrthoDBiEOG091G0KRX.
TreeFamiTF331401.

Miscellaneous databases

EvolutionaryTraceiP02522.

Gene expression databases

BgeeiENSBTAG00000004088.

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_BOVIN
AccessioniPrimary (citable) accession number: P02522
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 138 of the entry and version 3 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.