Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lambda-crystallin homolog

Gene

CRYL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-gulonate + NAD+ = 3-dehydro-L-gulonate + NADH.

Enzyme regulationi

Inhibited by malonate.1 Publication

Kineticsi

  1. KM=0.01 mM for NAD1 Publication
  2. KM=0.0008 mM for NADH1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei36 – 361NAD1 Publication
    Binding sitei97 – 971NAD1 Publication
    Binding sitei102 – 1021NAD1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi16 – 172NAD1 Publication

    GO - Molecular functioni

    • 3-hydroxyacyl-CoA dehydrogenase activity Source: InterPro
    • L-gulonate 3-dehydrogenase activity Source: UniProtKB
    • NAD+ binding Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    ReactomeiR-HSA-5661270. Catabolism of glucuronate to xylulose-5-phosphate.
    SABIO-RKQ9Y2S2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lambda-crystallin homolog (EC:1.1.1.45)
    Alternative name(s):
    L-gulonate 3-dehydrogenase
    Short name:
    Gul3DH
    Gene namesi
    Name:CRYL1
    Synonyms:CRY
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:18246. CRYL1.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26923.

    Polymorphism and mutation databases

    BioMutaiCRYL1.
    DMDMi93141249.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemovedBy similarity
    Chaini2 – 319318Lambda-crystallin homologPRO_0000109320Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3 – 31PhosphoserineBy similarity
    Modified residuei111 – 1111PhosphoserineCombined sources

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9Y2S2.
    PeptideAtlasiQ9Y2S2.
    PRIDEiQ9Y2S2.

    2D gel databases

    OGPiQ9Y2S2.
    REPRODUCTION-2DPAGEIPI00645031.

    PTM databases

    iPTMnetiQ9Y2S2.
    PhosphoSiteiQ9Y2S2.

    Expressioni

    Tissue specificityi

    Widely expressed, with highest levels in liver and kidney.1 Publication

    Gene expression databases

    BgeeiQ9Y2S2.
    CleanExiHS_CRYL1.
    ExpressionAtlasiQ9Y2S2. baseline and differential.
    GenevisibleiQ9Y2S2. HS.

    Organism-specific databases

    HPAiHPA040403.
    HPA058848.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    GO - Molecular functioni

    • protein homodimerization activity Source: UniProtKB

    Protein-protein interaction databases

    BioGridi119274. 36 interactions.
    IntActiQ9Y2S2. 1 interaction.
    MINTiMINT-5005752.
    STRINGi9606.ENSP00000298248.

    Structurei

    Secondary structure

    1
    319
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 135Combined sources
    Helixi16 – 2712Combined sources
    Beta strandi32 – 354Combined sources
    Helixi39 – 5820Combined sources
    Beta strandi64 – 663Combined sources
    Helixi68 – 736Combined sources
    Beta strandi75 – 773Combined sources
    Helixi81 – 855Combined sources
    Beta strandi89 – 935Combined sources
    Helixi99 – 11012Combined sources
    Beta strandi118 – 1214Combined sources
    Helixi128 – 1314Combined sources
    Turni132 – 1343Combined sources
    Helixi138 – 1403Combined sources
    Beta strandi141 – 1466Combined sources
    Turni150 – 1523Combined sources
    Beta strandi155 – 1606Combined sources
    Helixi166 – 17813Combined sources
    Beta strandi182 – 1854Combined sources
    Turni191 – 1944Combined sources
    Helixi195 – 21117Combined sources
    Helixi217 – 2259Combined sources
    Helixi228 – 2325Combined sources
    Helixi237 – 2448Combined sources
    Helixi248 – 26316Combined sources
    Helixi274 – 28714Combined sources
    Helixi292 – 31524Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3F3SX-ray2.00A/B6-316[»]
    ProteinModelPortaliQ9Y2S2.
    SMRiQ9Y2S2. Positions 6-316.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y2S2.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG2305. Eukaryota.
    COG1250. LUCA.
    GeneTreeiENSGT00390000007182.
    HOGENOMiHOG000141499.
    HOVERGENiHBG051126.
    InParanoidiQ9Y2S2.
    KOiK13247.
    OMAiSWAMVFA.
    OrthoDBiEOG7XPZ65.
    PhylomeDBiQ9Y2S2.
    TreeFamiTF313501.

    Family and domain databases

    Gene3Di1.10.1040.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR022694. 3-OHacyl-CoA_DH.
    IPR006180. 3-OHacyl-CoA_DH_CS.
    IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
    IPR006108. 3HC_DH_C.
    IPR008927. 6-PGluconate_DH_C-like.
    IPR013328. 6PGD_dom_2.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00725. 3HCDH. 1 hit.
    PF02737. 3HCDH_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000105. HCDH. 1 hit.
    SUPFAMiSSF48179. SSF48179. 1 hit.
    SSF51735. SSF51735. 1 hit.
    PROSITEiPS00067. 3HCDH. 1 hit.
    [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 splicing. AlignAdd to basket

    Isoform 1 (identifier: Q9Y2S2-1) [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
    MASSAAGCVV IVGSGVIGRS WAMLFASGGF QVKLYDIEQQ QIRNALENIR
    60 70 80 90 100
    KEMKLLEQAG SLKGSLSVEE QLSLISGCPN IQEAVEGAMH IQECVPEDLE
    110 120 130 140 150
    LKKKIFAQLD SIIDDRVILS SSTSCLMPSK LFAGLVHVKQ CIVAHPVNPP
    160 170 180 190 200
    YYIPLVELVP HPETAPTTVD RTHALMKKIG QCPMRVQKEV AGFVLNRLQY
    210 220 230 240 250
    AIISEAWRLV EEGIVSPSDL DLVMSEGLGM RYAFIGPLET MHLNAEGMLS
    260 270 280 290 300
    YCDRYSEGIK HVLQTFGPIP EFSRATAEKV NQDMCMKVPD DPEHLAARRQ
    310
    WRDECLMRLA KLKSQVQPQ
    Length:319
    Mass (Da):35,419
    Last modified:January 23, 2007 - v3
    Checksum:iC8DCF74DDE2FDE21
    GO
    Isoform 2 (identifier: Q9Y2S2-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-22: Missing.

    Show »
    Length:297
    Mass (Da):33,359
    Checksum:i3D6F3C29E14292F4
    GO

    Sequence cautioni

    The sequence AAD27782.1 differs from that shown.Unknown reasons.Curated
    The sequence AAD27782.1 differs from that shown. Reason: Frameshift at several positions. Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2222Missing in isoform 2. 2 PublicationsVSP_034641Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF077049 mRNA. Translation: AAD27782.1. Sequence problems.
    AF087898 mRNA. Translation: AAP97197.1.
    AF160216 mRNA. Translation: AAF67017.1.
    AK024041 mRNA. Translation: BAG51254.1.
    AL161715, AL590096 Genomic DNA. Translation: CAH71074.1.
    AL590096, AL161715 Genomic DNA. Translation: CAI14389.1.
    AL161715, AL590096 Genomic DNA. Translation: CAH71073.1.
    AL590096, AL161715 Genomic DNA. Translation: CAI14388.1.
    CH471075 Genomic DNA. Translation: EAX08259.1.
    CH471075 Genomic DNA. Translation: EAX08260.1.
    BC008562 mRNA. Translation: AAH08562.2.
    BC071810 mRNA. Translation: AAH71810.1.
    BC119660 mRNA. Translation: AAI19661.2.
    BC119661 mRNA. Translation: AAI19662.2.
    CCDSiCCDS41871.1. [Q9Y2S2-1]
    RefSeqiNP_057058.2. NM_015974.2. [Q9Y2S2-1]
    UniGeneiHs.370703.

    Genome annotation databases

    EnsembliENST00000298248; ENSP00000298248; ENSG00000165475. [Q9Y2S2-1]
    ENST00000382812; ENSP00000372262; ENSG00000165475. [Q9Y2S2-2]
    GeneIDi51084.
    KEGGihsa:51084.
    UCSCiuc001ung.4. human. [Q9Y2S2-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF077049 mRNA. Translation: AAD27782.1. Sequence problems.
    AF087898 mRNA. Translation: AAP97197.1.
    AF160216 mRNA. Translation: AAF67017.1.
    AK024041 mRNA. Translation: BAG51254.1.
    AL161715, AL590096 Genomic DNA. Translation: CAH71074.1.
    AL590096, AL161715 Genomic DNA. Translation: CAI14389.1.
    AL161715, AL590096 Genomic DNA. Translation: CAH71073.1.
    AL590096, AL161715 Genomic DNA. Translation: CAI14388.1.
    CH471075 Genomic DNA. Translation: EAX08259.1.
    CH471075 Genomic DNA. Translation: EAX08260.1.
    BC008562 mRNA. Translation: AAH08562.2.
    BC071810 mRNA. Translation: AAH71810.1.
    BC119660 mRNA. Translation: AAI19661.2.
    BC119661 mRNA. Translation: AAI19662.2.
    CCDSiCCDS41871.1. [Q9Y2S2-1]
    RefSeqiNP_057058.2. NM_015974.2. [Q9Y2S2-1]
    UniGeneiHs.370703.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3F3SX-ray2.00A/B6-316[»]
    ProteinModelPortaliQ9Y2S2.
    SMRiQ9Y2S2. Positions 6-316.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi119274. 36 interactions.
    IntActiQ9Y2S2. 1 interaction.
    MINTiMINT-5005752.
    STRINGi9606.ENSP00000298248.

    PTM databases

    iPTMnetiQ9Y2S2.
    PhosphoSiteiQ9Y2S2.

    Polymorphism and mutation databases

    BioMutaiCRYL1.
    DMDMi93141249.

    2D gel databases

    OGPiQ9Y2S2.
    REPRODUCTION-2DPAGEIPI00645031.

    Proteomic databases

    PaxDbiQ9Y2S2.
    PeptideAtlasiQ9Y2S2.
    PRIDEiQ9Y2S2.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000298248; ENSP00000298248; ENSG00000165475. [Q9Y2S2-1]
    ENST00000382812; ENSP00000372262; ENSG00000165475. [Q9Y2S2-2]
    GeneIDi51084.
    KEGGihsa:51084.
    UCSCiuc001ung.4. human. [Q9Y2S2-1]

    Organism-specific databases

    CTDi51084.
    GeneCardsiCRYL1.
    HGNCiHGNC:18246. CRYL1.
    HPAiHPA040403.
    HPA058848.
    MIMi609877. gene.
    neXtProtiNX_Q9Y2S2.
    PharmGKBiPA26923.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG2305. Eukaryota.
    COG1250. LUCA.
    GeneTreeiENSGT00390000007182.
    HOGENOMiHOG000141499.
    HOVERGENiHBG051126.
    InParanoidiQ9Y2S2.
    KOiK13247.
    OMAiSWAMVFA.
    OrthoDBiEOG7XPZ65.
    PhylomeDBiQ9Y2S2.
    TreeFamiTF313501.

    Enzyme and pathway databases

    ReactomeiR-HSA-5661270. Catabolism of glucuronate to xylulose-5-phosphate.
    SABIO-RKQ9Y2S2.

    Miscellaneous databases

    ChiTaRSiCRYL1. human.
    EvolutionaryTraceiQ9Y2S2.
    GenomeRNAii51084.
    PROiQ9Y2S2.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9Y2S2.
    CleanExiHS_CRYL1.
    ExpressionAtlasiQ9Y2S2. baseline and differential.
    GenevisibleiQ9Y2S2. HS.

    Family and domain databases

    Gene3Di1.10.1040.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR022694. 3-OHacyl-CoA_DH.
    IPR006180. 3-OHacyl-CoA_DH_CS.
    IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
    IPR006108. 3HC_DH_C.
    IPR008927. 6-PGluconate_DH_C-like.
    IPR013328. 6PGD_dom_2.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00725. 3HCDH. 1 hit.
    PF02737. 3HCDH_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000105. HCDH. 1 hit.
    SUPFAMiSSF48179. SSF48179. 1 hit.
    SSF51735. SSF51735. 1 hit.
    PROSITEiPS00067. 3HCDH. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Human lambda-crystallin mRNA."
      Hu R., Song H., Peng Y., Fu G., Mao M., Zhang Q., Zhu H., Li G., Luo M., Hu R., Chen J.
      Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Pituitary.
    2. "Human CRYL1, a novel enzyme-crystallin overexpressed in liver and kidney and downregulated in 58% of liver cancer tissues from 60 Chinese patients, and four new homologs from other mammalians."
      Chen J., Yu L., Li D., Gao Q., Wang J., Huang X., Bi G., Wu H., Zhao S.
      Gene 302:103-113(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Liver.
    3. "A novel gene expressed in human hypothalamus."
      Li Y., Shi J., Huang C., Jiang C., Ren S., Zhou J., Yu Y., Xu S., Wang Y., Fu G., Chen Z., Han Z.
      Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Hypothalamus.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-319 (ISOFORM 1).
      Tissue: Brain.
    8. "Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase."
      Ishikura S., Usami N., Araki M., Hara A.
      J. Biochem. 137:303-314(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
      Tissue: Liver.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    11. "The crystal structure of human lambda-crystallin, CRYL1."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 6-316 IN COMPLEX WITH NAD.

    Entry informationi

    Entry nameiCRYL1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y2S2
    Secondary accession number(s): A0PJ43
    , B3KN92, Q0VDI1, Q7Z4Z9, Q9P0G7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 24, 2001
    Last sequence update: January 23, 2007
    Last modified: July 6, 2016
    This is version 130 of the entry and version 3 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 13
      Human chromosome 13: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. 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.