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Protein

Beta-crystallin B1

Gene

Crybb1

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Eye lens protein

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-crystallin B1
Alternative name(s):
Beta-B1 crystallin
Cleaved into the following chain:
Gene namesi
Name:Crybb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:104992. Crybb1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 250249Beta-crystallin B1PRO_0000006337Add
BLAST
Chaini12 – 250239Beta-crystallin B1BPRO_0000006338Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei228 – 2281Omega-N-methylated arginineBy similarity
Modified residuei229 – 2291Omega-N-methylated arginineBy similarity

Post-translational modificationi

Specific cleavages in the N-terminal arm occur during lens maturation and give rise to truncated forms, leading to impaired oligomerization and protein insolubilization. The protease responsible for this partial degradation could be calpain II.

Keywords - PTMi

Acetylation, Methylation

Proteomic databases

MaxQBiQ9WVJ5.
PaxDbiQ9WVJ5.
PRIDEiQ9WVJ5.

PTM databases

PhosphoSiteiQ9WVJ5.

Miscellaneous databases

PMAP-CutDBQ9WVJ5.

Expressioni

Gene expression databases

BgeeiQ9WVJ5.
CleanExiMM_CRYBB1.
ExpressionAtlasiQ9WVJ5. baseline and differential.
GenevisibleiQ9WVJ5. 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.

Binary interactionsi

WithEntry#Exp.IntActNotes
CryabP239282EBI-8520354,EBI-916888From a different organism.

Protein-protein interaction databases

IntActiQ9WVJ5. 1 interaction.
STRINGi10090.ENSMUSP00000031286.

Structurei

3D structure databases

ProteinModelPortaliQ9WVJ5.
SMRiQ9WVJ5. Positions 53-235.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini57 – 9640Beta/gamma crystallin 'Greek key' 1PROSITE-ProRule annotationAdd
BLAST
Domaini97 – 14145Beta/gamma crystallin 'Greek key' 2PROSITE-ProRule annotationAdd
BLAST
Domaini147 – 18842Beta/gamma crystallin 'Greek key' 3PROSITE-ProRule annotationAdd
BLAST
Domaini189 – 23143Beta/gamma crystallin 'Greek key' 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 5655N-terminal armAdd
BLAST
Regioni142 – 1465Connecting peptide
Regioni233 – 25018C-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

eggNOGiENOG410IJ9M. Eukaryota.
ENOG410ZYKU. LUCA.
GeneTreeiENSGT00760000118812.
HOVERGENiHBG003364.
InParanoidiQ9WVJ5.
OMAiMSFRPIK.
OrthoDBiEOG754HNK.
TreeFamiTF331401.

Family and domain databases

InterProiIPR001064. Beta/gamma_crystallin.
IPR033059. CRYBB1.
IPR011024. G_crystallin-rel.
[Graphical view]
PANTHERiPTHR11818:SF12. PTHR11818:SF12. 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.

Q9WVJ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQAAKASAT TAVNPGPDGK GKGAPSTGPA PAPGPTPVPA SVPRPAAKVG
60 70 80 90 100
DLPPGSYRLI VFEQENFQGR RVEFSGECLN LGDRGFDRVR SLIVVSGPWV
110 120 130 140 150
AFEQSAFRGE MFVLEKGEYP RWDTWTSSYR SDRLMSFRPI RMDSQEHKIC
160 170 180 190 200
LFEGANFKGN TMEIQEDDVP SLWVYGFCDR VGSITVSGGT WVGYQYPGYR
210 220 230 240 250
GYQYLLEPGD FRHWNEWGAF QPQMQAVRRL RDRQWHQEGC FPVLTAEPPK
Length:250
Mass (Da):28,003
Last modified:January 23, 2007 - v3
Checksum:iCCF26E7D2F6B92EF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF106853 mRNA. Translation: AAD42048.1.
AK014012 mRNA. Translation: BAB29113.1.
AK053869 mRNA. Translation: BAC35565.1.
CCDSiCCDS19537.1.
RefSeqiNP_001299822.1. NM_001312893.1.
NP_001299823.1. NM_001312894.1.
NP_001299824.1. NM_001312895.1.
NP_076184.1. NM_023695.3.
XP_006534818.1. XM_006534755.2.
XP_006534819.1. XM_006534756.1.
XP_006534820.1. XM_006534757.1.
UniGeneiMm.29488.

Genome annotation databases

EnsembliENSMUST00000031286; ENSMUSP00000031286; ENSMUSG00000029343.
ENSMUST00000112375; ENSMUSP00000107994; ENSMUSG00000029343.
GeneIDi12960.
KEGGimmu:12960.
UCSCiuc008ysv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF106853 mRNA. Translation: AAD42048.1.
AK014012 mRNA. Translation: BAB29113.1.
AK053869 mRNA. Translation: BAC35565.1.
CCDSiCCDS19537.1.
RefSeqiNP_001299822.1. NM_001312893.1.
NP_001299823.1. NM_001312894.1.
NP_001299824.1. NM_001312895.1.
NP_076184.1. NM_023695.3.
XP_006534818.1. XM_006534755.2.
XP_006534819.1. XM_006534756.1.
XP_006534820.1. XM_006534757.1.
UniGeneiMm.29488.

3D structure databases

ProteinModelPortaliQ9WVJ5.
SMRiQ9WVJ5. Positions 53-235.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9WVJ5. 1 interaction.
STRINGi10090.ENSMUSP00000031286.

PTM databases

PhosphoSiteiQ9WVJ5.

Proteomic databases

MaxQBiQ9WVJ5.
PaxDbiQ9WVJ5.
PRIDEiQ9WVJ5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031286; ENSMUSP00000031286; ENSMUSG00000029343.
ENSMUST00000112375; ENSMUSP00000107994; ENSMUSG00000029343.
GeneIDi12960.
KEGGimmu:12960.
UCSCiuc008ysv.1. mouse.

Organism-specific databases

CTDi1414.
MGIiMGI:104992. Crybb1.

Phylogenomic databases

eggNOGiENOG410IJ9M. Eukaryota.
ENOG410ZYKU. LUCA.
GeneTreeiENSGT00760000118812.
HOVERGENiHBG003364.
InParanoidiQ9WVJ5.
OMAiMSFRPIK.
OrthoDBiEOG754HNK.
TreeFamiTF331401.

Miscellaneous databases

ChiTaRSiCrybb1. mouse.
PMAP-CutDBQ9WVJ5.
PROiQ9WVJ5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WVJ5.
CleanExiMM_CRYBB1.
ExpressionAtlasiQ9WVJ5. baseline and differential.
GenevisibleiQ9WVJ5. MM.

Family and domain databases

InterProiIPR001064. Beta/gamma_crystallin.
IPR033059. CRYBB1.
IPR011024. G_crystallin-rel.
[Graphical view]
PANTHERiPTHR11818:SF12. PTHR11818:SF12. 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. "Beta-B1 crystallin: evidence for changes in gene regulation during evolution."
    Duncan M.K., Hejtmancik J.F., Piatigorsky J.
    Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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: Eye and Head.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiCRBB1_MOUSE
AccessioniPrimary (citable) accession number: Q9WVJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 92 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.