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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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 205204Beta-crystallin B2PRO_0000057552Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Glycosylationi11 – 111N-linked (Glc) (glycation); in vitro
Glycosylationi48 – 481N-linked (Glc) (glycation); in vitro
Glycosylationi68 – 681N-linked (Glc) (glycation); in vitro
Glycosylationi76 – 761N-linked (Glc) (glycation); in vitro
Glycosylationi101 – 1011N-linked (Glc) (glycation); in vitro
Glycosylationi108 – 1081N-linked (Glc) (glycation); in vitro
Glycosylationi120 – 1201N-linked (Glc) (glycation); in vitro
Glycosylationi121 – 1211N-linked (Glc) (glycation); in vitro
Glycosylationi140 – 1401N-linked (Glc) (glycation); in vitro
Glycosylationi168 – 1681N-linked (Glc) (glycation); in vitro
Glycosylationi172 – 1721N-linked (Glc) (glycation); in vitro

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei18 – 181Not glycated
Sitei42 – 421Not glycated

Keywords - PTMi

Acetylation, Glycation, Glycoprotein

Proteomic databases

PaxDbiP02522.

PTM databases

iPTMnetiP02522.

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 interaction.
STRINGi9913.ENSBTAP00000005341.

Structurei

Secondary structure

1
205
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 247Combined sources
Turni25 – 273Combined sources
Beta strandi28 – 369Combined 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 – 994Combined sources
Beta strandi108 – 1147Combined sources
Turni115 – 1173Combined sources
Beta strandi118 – 12710Combined sources
Helixi133 – 1353Combined sources
Beta strandi143 – 1464Combined sources
Beta strandi151 – 1566Combined sources
Turni157 – 1593Combined sources
Beta strandi160 – 1667Combined sources
Beta strandi168 – 1736Combined sources
Helixi174 – 1774Combined sources
Beta strandi180 – 1823Combined sources
Beta strandi186 – 1894Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BLBX-ray3.30A/B/C/D2-205[»]
2BB2X-ray2.10A15-195[»]
ProteinModelPortaliP02522.
SMRiP02522. Positions 9-195.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02522.

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.
HOGENOMiHOG000234388.
HOVERGENiHBG003364.
InParanoidiP02522.
OMAiHELTGPC.
OrthoDBiEOG754HNK.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41D → N AA sequence (PubMed:7035168).Curated
Sequence conflicti6 – 61Q → E AA sequence (PubMed:7035168).Curated
Sequence conflicti28 – 281Q → H AA sequence (PubMed:7035168).Curated
Sequence conflicti32 – 321H → Q AA sequence (PubMed:7035168).Curated
Sequence conflicti36 – 372GP → PG AA sequence (PubMed:7035168).Curated
Sequence conflicti40 – 401N → C AA sequence (PubMed:7035168).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1BLBX-ray3.30A/B/C/D2-205[»]
2BB2X-ray2.10A15-195[»]
ProteinModelPortaliP02522.
SMRiP02522. Positions 9-195.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP02522. 1 interaction.
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.
OrthoDBiEOG754HNK.
TreeFamiTF331401.

Miscellaneous databases

EvolutionaryTraceiP02522.
NextBioi20806535.

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. "Primary structure of the bovine beta-crystallin Bp chain. Internal duplication and homology with gamma-crystallin."
    Driessen H.P.C., Herbrink P., Bloemendal H., de Jong W.W.
    Eur. J. Biochem. 121:83-91(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-205, ACETYLATION AT ALA-2.
  2. "Nucleotide sequence for the cDNA of the bovine beta B2 crystallin and assignment of the orthologous human locus to chromosome 22."
    Hogg D., Gorin M.B., Heinzmann C., Zollmann S., Mohandas T., Klisak I., Sparkes R.S., Breitman M., Tsui L.-C., Horwitz J.
    Curr. Eye Res. 6:1335-1342(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Sites of glycation of beta B2-crystallin by glucose and fructose."
    Zhao H.R., Smith J.B., Jiang X.Y., Abraham E.C.
    Biochem. Biophys. Res. Commun. 229:128-133(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCATION AT LYS-11; LYS-48; LYS-68; LYS-76; LYS-101; LYS-108; LYS-120; LYS-121; LYS-140; LYS-168 AND LYS-172, ABSENCE OF GLYCATION AT LYS-18 AND LYS-42, IDENTIFICATION BY MASS SPECTROMETRY.
  4. "X-ray analysis of beta B2-crystallin and evolution of oligomeric lens proteins."
    Bax B., Lapatto R., Nalini V., Driessen H.P.C., Lindley P.F., Mahadevan D., Blundell T.L., Slingsby C.
    Nature 347:776-780(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), SEQUENCE REVISION.
  5. "1H-NMR spectroscopy of beta B2-crystallin from bovine eye lens. Conformation of the N- and C-terminal extensions."
    Carver J.A., Cooper P.G., Truscott R.J.
    Eur. J. Biochem. 213:313-320(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

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: March 16, 2016
This is version 134 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.