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P05813

- CRBA1_HUMAN

UniProt

P05813 - CRBA1_HUMAN

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Protein

Beta-crystallin A3

Gene

CRYBA1

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. structural constituent of eye lens Source: UniProtKB-KW

GO - Biological processi

  1. lens development in camera-type eye Source: Ensembl
  2. visual perception Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Eye lens protein

Names & Taxonomyi

Protein namesi
Gene namesi
Name:CRYBA1
Synonyms:CRYB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:2394. CRYBA1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Cataract 10, multiple types (CTRCT10) [MIM:600881]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. CTRCT10 includes congenital zonular with sutural opacities, among others. This is a form of zonular cataract with an erect Y-shaped anterior and an inverted Y-shaped posterior sutural opacities. Zonular or lamellar cataracts are opacities, broad or narrow, usually consisting of powdery white dots affecting only certain layers or zones between the cortex and nucleus of an otherwise clear lens. The opacity may be so dense as to render the entire central region of the lens completely opaque, or so translucent that vision is hardly if at all impeded. Zonular cataracts generally do not involve the embryonic nucleus, though sometimes they involve the fetal nucleus. Usually sharply separated from a clear cortex outside them, they may have projections from their outer edges known as riders or spokes.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Cataract

Organism-specific databases

MIMi600881. phenotype.
Orphaneti98985. Cataract with Y-shaped suture opacities.
98995. Zonular cataract.
PharmGKBiPA26908.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 215215Beta-crystallin A3PRO_0000006331Add
BLAST
Chaini23 – 215193Beta-crystallin A3, isoform A1, Delta4 formPRO_0000226692Add
BLAST
Chaini26 – 215190Beta-crystallin A3, isoform A1, Delta7 formPRO_0000226693Add
BLAST
Chaini27 – 215189Beta-crystallin A3, isoform A1, Delta8 formPRO_0000226694Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei82 – 821S-glutathionyl cysteine; alternate1 Publication
Modified residuei82 – 821S-methylcysteine; alternate1 Publication
Modified residuei117 – 1171S-glutathionyl cysteine; alternate1 Publication
Modified residuei117 – 1171S-methylcysteine; alternate1 Publication
Modified residuei185 – 1851S-methylcysteine1 Publication

Post-translational modificationi

Specific cleavages in the N-terminal arm occur during lens maturation and give rise to several truncated forms. Cleavages do not seem to have adverse effects on solubility.1 Publication
S-methylation and glutathionylation occur in normal young lenses and do not seem to be detrimental.1 Publication
Isoform A1 initiator methionine is removed. The new N-terminal amino acid is then N-acetylated.2 Publications

Keywords - PTMi

Acetylation, Glutathionylation, Methylation, Oxidation

Proteomic databases

PaxDbiP05813.
PRIDEiP05813.

PTM databases

PhosphoSiteiP05813.

Expressioni

Gene expression databases

BgeeiP05813.
CleanExiHS_CRYBA1.
GenevestigatoriP05813.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
CRYABP025112EBI-7043337,EBI-739060

Protein-protein interaction databases

BioGridi107801. 3 interactions.
IntActiP05813. 4 interactions.
MINTiMINT-3388142.
STRINGi9606.ENSP00000225387.

Structurei

3D structure databases

ProteinModelPortaliP05813.
SMRiP05813. Positions 27-215.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 7040Beta/gamma crystallin 'Greek key' 1PROSITE-ProRule annotationAdd
BLAST
Domaini71 – 11747Beta/gamma crystallin 'Greek key' 2PROSITE-ProRule annotationAdd
BLAST
Domaini124 – 16542Beta/gamma crystallin 'Greek key' 3PROSITE-ProRule annotationAdd
BLAST
Domaini166 – 21449Beta/gamma crystallin 'Greek key' 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 3030N-terminal armAdd
BLAST
Regioni118 – 1236Connecting peptide

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

eggNOGiNOG47808.
GeneTreeiENSGT00760000118812.
HOGENOMiHOG000234388.
HOVERGENiHBG003364.
InParanoidiP05813.
OrthoDBiEOG7K9K40.
PhylomeDBiP05813.
TreeFamiTF331401.

Family and domain databases

InterProiIPR001064. Beta/gamma_crystallin.
IPR011024. G_crystallin-rel.
[Graphical view]
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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative initiation. Align

Isoform A3 (identifier: P05813-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
METQAEQQEL ETLPTTKMAQ TNPTPGSLGP WKITIYDQEN FQGKRMEFTS
60 70 80 90 100
SCPNVSERSF DNVRSLKVES GAWIGYEHTS FCGQQFILER GEYPRWDAWS
110 120 130 140 150
GSNAYHIERL MSFRPICSAN HKESKMTIFE KENFIGRQWE ISDDYPSLQA
160 170 180 190 200
MGWFNNEVGS MKIQSGAWVC YQYPGYRGYQ YILECDHHGG DYKHWREWGS
210
HAQTSQIQSI RRIQQ
Length:215
Mass (Da):25,150
Last modified:November 1, 1997 - v4
Checksum:iC544564835688A19
GO
Isoform A1 (identifier: P05813-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: Missing.

Note: Initiator Met-1 is removed. Contains a N-acetylalanine at position 2.

Show »
Length:198
Mass (Da):23,191
Checksum:i95954586F78B1B4C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti107 – 1071I → M in AAA52107. (PubMed:3745196)Curated
Sequence conflicti116 – 1161I → F in AAA52107. (PubMed:3745196)Curated
Sequence conflicti172 – 1743QYP → HYL in AAA52107. (PubMed:3745196)Curated
Sequence conflicti184 – 1841E → K in AAA52107. (PubMed:3745196)Curated
Sequence conflicti189 – 1891G → E in AAA52107. (PubMed:3745196)Curated

Mass spectrometryi

Molecular mass is 25192±3 Da from positions 1 - 215. Determined by ESI. 1 Publication
Molecular mass is 25192 Da from positions 1 - 215. Determined by ESI. 1 Publication
Molecular mass is 23101±3 Da from positions 19 - 215. Determined by ESI. 1 Publication
Molecular mass is 23102 Da from positions 19 - 215. Determined by ESI. 1 Publication
Molecular mass is 22646 Da from positions 23 - 215. Determined by ESI. 1 Publication
Molecular mass is 22351 Da from positions 26 - 215. Determined by ESI. 1 Publication
Molecular mass is 22294 Da from positions 27 - 215. Determined by ESI. 1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1717Missing in isoform A1. CuratedVSP_018710Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14306
, M14301, M14302, M14303, M14304, M14305 Genomic DNA. Translation: AAA52107.1.
BC069537 mRNA. Translation: AAH69537.1.
BC113693 mRNA. Translation: AAI13694.1.
U59058 mRNA. Translation: AAC50971.1.
CCDSiCCDS11249.1. [P05813-1]
PIRiA25202. CYHUB3.
RefSeqiNP_005199.2. NM_005208.4. [P05813-1]
UniGeneiHs.46275.

Genome annotation databases

EnsembliENST00000225387; ENSP00000225387; ENSG00000108255. [P05813-1]
GeneIDi1411.
KEGGihsa:1411.
UCSCiuc002hdw.3. human. [P05813-1]

Polymorphism databases

DMDMi2506317.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Web resourcesi

Eye disease Crystallin, beta-A1 (CRYBA1)

Leiden Open Variation Database (LOVD)

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14306
, M14301 , M14302 , M14303 , M14304 , M14305 Genomic DNA. Translation: AAA52107.1 .
BC069537 mRNA. Translation: AAH69537.1 .
BC113693 mRNA. Translation: AAI13694.1 .
U59058 mRNA. Translation: AAC50971.1 .
CCDSi CCDS11249.1. [P05813-1 ]
PIRi A25202. CYHUB3.
RefSeqi NP_005199.2. NM_005208.4. [P05813-1 ]
UniGenei Hs.46275.

3D structure databases

ProteinModelPortali P05813.
SMRi P05813. Positions 27-215.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107801. 3 interactions.
IntActi P05813. 4 interactions.
MINTi MINT-3388142.
STRINGi 9606.ENSP00000225387.

PTM databases

PhosphoSitei P05813.

Polymorphism databases

DMDMi 2506317.

Proteomic databases

PaxDbi P05813.
PRIDEi P05813.

Protocols and materials databases

DNASUi 1411.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000225387 ; ENSP00000225387 ; ENSG00000108255 . [P05813-1 ]
GeneIDi 1411.
KEGGi hsa:1411.
UCSCi uc002hdw.3. human. [P05813-1 ]

Organism-specific databases

CTDi 1411.
GeneCardsi GC17P027573.
HGNCi HGNC:2394. CRYBA1.
MIMi 123610. gene.
600881. phenotype.
neXtProti NX_P05813.
Orphaneti 98985. Cataract with Y-shaped suture opacities.
98995. Zonular cataract.
PharmGKBi PA26908.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG47808.
GeneTreei ENSGT00760000118812.
HOGENOMi HOG000234388.
HOVERGENi HBG003364.
InParanoidi P05813.
OrthoDBi EOG7K9K40.
PhylomeDBi P05813.
TreeFami TF331401.

Miscellaneous databases

ChiTaRSi CRYBA1. human.
GeneWikii Crystallin,_beta_A1.
GenomeRNAii 1411.
NextBioi 5769.
PROi P05813.
SOURCEi Search...

Gene expression databases

Bgeei P05813.
CleanExi HS_CRYBA1.
Genevestigatori P05813.

Family and domain databases

InterProi IPR001064. Beta/gamma_crystallin.
IPR011024. G_crystallin-rel.
[Graphical view ]
Pfami PF00030. Crystall. 2 hits.
[Graphical view ]
PRINTSi PR01367. BGCRYSTALLIN.
SMARTi SM00247. XTALbg. 2 hits.
[Graphical view ]
SUPFAMi SSF49695. SSF49695. 1 hit.
PROSITEi PS50915. CRYSTALLIN_BETA_GAMMA. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the human beta-crystallin gene Hu beta A3/A1 reveals ancestral relationships among the beta gamma-crystallin superfamily."
    Hogg D., Tsui L.-C., Gorin M., Breitman M.L.
    J. Biol. Chem. 261:12420-12427(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "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].
  3. "Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the identification of the major proteins in young human lens."
    Lampi K.J., Ma Z., Shih M., Shearer T.R., Smith J.B., Smith D.L., David L.L.
    J. Biol. Chem. 272:2268-2275(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 44-215, PROTEIN SEQUENCE OF 23-30 AND 197-211, ACETYLATION AT MET-1, CLEAVAGE OF INITIATOR METHIONINE (ISOFORM A1), ACETYLATION AT ALA-2 (ISOFORM A1), MASS SPECTROMETRY.
  4. "Autosomal dominant zonular cataract with sutural opacities is associated with a splice mutation in the betaA3/A1-crystallin gene."
    Kannabiran C., Rogan P.K., Olmos L., Basti S., Rao G.N., Kaiser-Kupfer M., Hejtmancik J.F.
    Mol. Vis. 4:21-21(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CTRCT10.
  5. "Characterization of the G91del CRYBA1/3-crystallin protein: a cause of human inherited cataract."
    Reddy M.A., Bateman O.A., Chakarova C., Ferris J., Berry V., Lomas E., Sarra R., Smith M.A., Moore A.T., Bhattacharya S.S., Slingsby C.
    Hum. Mol. Genet. 13:945-953(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CTRCT10.
  6. "Modifications of human betaA1/betaA3-crystallins include S-methylation, glutathiolation, and truncation."
    Lapko V.N., Cerny R.L., Smith D.L., Smith J.B.
    Protein Sci. 14:45-54(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF N-TERMINUS, ACETYLATION AT MET-1, CLEAVAGE OF INITIATOR METHIONINE (ISOFORM A1), ACETYLATION AT ALA-2 (ISOFORM A1), METHYLATION AT CYS-82; CYS-117 AND CYS-185, GLUTATHIONYLATION AT CYS-82 AND CYS-117, MASS SPECTROMETRY.

Entry informationi

Entry nameiCRBA1_HUMAN
AccessioniPrimary (citable) accession number: P05813
Secondary accession number(s): Q13633, Q14CM9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1997
Last modified: November 26, 2014
This is version 150 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3