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Protein

Beta-crystallin B2

Gene

Crybb2

Organism
Mus musculus (Mouse)
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

  • identical protein binding Source: MGI
  • protein homodimerization activity Source: MGI
  • structural constituent of eye lens Source: MGI

GO - Biological processi

  • camera-type eye development Source: MGI
  • visual perception Source: MGI
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:88519. Crybb2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 205204Beta-crystallin B2PRO_0000057555Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP62696.
PaxDbiP62696.
PRIDEiP62696.

PTM databases

PhosphoSiteiP62696.

Expressioni

Gene expression databases

BgeeiP62696.
CleanExiMM_CRYBB2.
GenevisibleiP62696. MM.

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

GO - Molecular functioni

  • identical protein binding Source: MGI
  • protein homodimerization activity Source: MGI

Protein-protein interaction databases

BioGridi198914. 1 interaction.
STRINGi10090.ENSMUSP00000031295.

Structurei

Secondary structure

1
205
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 247
Helixi25 – 273
Beta strandi28 – 369
Helixi41 – 444
Beta strandi51 – 566
Beta strandi59 – 646
Turni65 – 673
Beta strandi68 – 747
Beta strandi76 – 794
Beta strandi96 – 994

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E7NX-ray2.35A/B2-104[»]
ProteinModelPortaliP62696.
SMRiP62696. Positions 15-195.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62696.

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.
InParanoidiP62696.
OMAiHELTGPC.
OrthoDBiEOG754HNK.
PhylomeDBiP62696.
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.

P62696-1 [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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60559 mRNA. Translation: AAA21181.1.
AK020891 mRNA. Translation: BAB32243.1.
BC085185 mRNA. Translation: AAH85185.1.
CCDSiCCDS19546.1.
PIRiA39757.
RefSeqiNP_031799.1. NM_007773.4.
XP_006534821.1. XM_006534758.2.
XP_006534822.1. XM_006534759.1.
XP_006534823.1. XM_006534760.1.
UniGeneiMm.1215.

Genome annotation databases

EnsembliENSMUST00000031295; ENSMUSP00000031295; ENSMUSG00000042240.
ENSMUST00000112336; ENSMUSP00000107955; ENSMUSG00000042240.
GeneIDi12961.
KEGGimmu:12961.
UCSCiuc008ytx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60559 mRNA. Translation: AAA21181.1.
AK020891 mRNA. Translation: BAB32243.1.
BC085185 mRNA. Translation: AAH85185.1.
CCDSiCCDS19546.1.
PIRiA39757.
RefSeqiNP_031799.1. NM_007773.4.
XP_006534821.1. XM_006534758.2.
XP_006534822.1. XM_006534759.1.
XP_006534823.1. XM_006534760.1.
UniGeneiMm.1215.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E7NX-ray2.35A/B2-104[»]
ProteinModelPortaliP62696.
SMRiP62696. Positions 15-195.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198914. 1 interaction.
STRINGi10090.ENSMUSP00000031295.

PTM databases

PhosphoSiteiP62696.

Proteomic databases

MaxQBiP62696.
PaxDbiP62696.
PRIDEiP62696.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031295; ENSMUSP00000031295; ENSMUSG00000042240.
ENSMUST00000112336; ENSMUSP00000107955; ENSMUSG00000042240.
GeneIDi12961.
KEGGimmu:12961.
UCSCiuc008ytx.2. mouse.

Organism-specific databases

CTDi1415.
MGIiMGI:88519. Crybb2.

Phylogenomic databases

eggNOGiENOG410IJYD. Eukaryota.
ENOG410Y7P1. LUCA.
GeneTreeiENSGT00760000118812.
HOGENOMiHOG000234388.
HOVERGENiHBG003364.
InParanoidiP62696.
OMAiHELTGPC.
OrthoDBiEOG754HNK.
PhylomeDBiP62696.
TreeFamiTF331401.

Miscellaneous databases

EvolutionaryTraceiP62696.
PROiP62696.
SOURCEiSearch...

Gene expression databases

BgeeiP62696.
CleanExiMM_CRYBB2.
GenevisibleiP62696. MM.

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

« Hide 'large scale' publications
  1. "Deletion mutation in an eye lens beta-crystallin. An animal model for inherited cataracts."
    Chambers C., Russell P.
    J. Biol. Chem. 266:6742-6746(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Swiss Webster.
    Tissue: Lens.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Retina.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Eye.

Entry informationi

Entry nameiCRBB2_MOUSE
AccessioniPrimary (citable) accession number: P62696
Secondary accession number(s): P19942, P26775, Q0VGT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 93 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, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.