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O08553

- DPYL2_MOUSE

UniProt

O08553 - DPYL2_MOUSE

Protein

Dihydropyrimidinase-related protein 2

Gene

Dpysl2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (02 May 2006)
      Previous versions | rss
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    Functioni

    Plays a role in neuronal development and polarity, as well as in axon growth and guidance, neuronal growth cone collapse and cell migration. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. May play a role in endocytosis.1 Publication

    GO - Molecular functioni

    1. hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides Source: InterPro
    2. protein kinase binding Source: UniProtKB

    GO - Biological processi

    1. cytoskeleton organization Source: UniProtKB
    2. endocytosis Source: UniProtKB
    3. olfactory bulb development Source: Ensembl
    4. positive regulation of glutamate secretion Source: Ensembl
    5. pyrimidine nucleobase catabolic process Source: InterPro
    6. regulation of neuron differentiation Source: Ensembl
    7. response to amphetamine Source: Ensembl
    8. response to cocaine Source: Ensembl
    9. response to drug Source: Ensembl
    10. spinal cord development Source: Ensembl
    11. synaptic vesicle transport Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Differentiation, Neurogenesis

    Protein family/group databases

    MEROPSiM38.975.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydropyrimidinase-related protein 2
    Short name:
    DRP-2
    Alternative name(s):
    Unc-33-like phosphoprotein 2
    Short name:
    ULIP-2
    Gene namesi
    Name:Dpysl2
    Synonyms:Crmp2, Ulip2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:1349763. Dpysl2.

    Subcellular locationi

    Cytoplasmcytosol By similarity. Cytoplasmcytoskeleton By similarity. Membrane By similarity
    Note: Tightly but non-covalently associated with membranes.By similarity

    GO - Cellular componenti

    1. axon Source: MGI
    2. cytosol Source: UniProtKB
    3. dendrite Source: MGI
    4. growth cone Source: Ensembl
    5. membrane Source: UniProtKB-SubCell
    6. microtubule Source: Ensembl
    7. mitochondrion Source: MGI
    8. neuronal cell body Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi514 – 5141T → A: Delayed neurite degeneration. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 572572Dihydropyrimidinase-related protein 2PRO_0000165914Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei32 – 321Phosphotyrosine; by FYNBy similarity
    Modified residuei258 – 2581N6-succinyllysine1 Publication
    Modified residuei431 – 4311Phosphotyrosine1 Publication
    Modified residuei465 – 4651Phosphoserine1 Publication
    Modified residuei499 – 4991Phosphotyrosine1 Publication
    Modified residuei504 – 5041S-nitrosocysteineBy similarity
    Modified residuei509 – 5091Phosphothreonine1 Publication
    Modified residuei514 – 5141Phosphothreonine; by GSK3-beta2 Publications
    Modified residuei517 – 5171Phosphoserine1 Publication
    Modified residuei518 – 5181Phosphoserine1 Publication
    Modified residuei522 – 5221Phosphoserine; alternate1 Publication
    Modified residuei522 – 5221Phosphoserine; by DYRK2; alternateBy similarity
    Modified residuei555 – 5551Phosphothreonine; by ROCK2By similarity

    Post-translational modificationi

    Phosphorylation by DYRK2 at Ser-522 is required for subsequent phosphorylation by GSK3B By similarity. Phosphorylation at Thr-514 by GSK3B abolishes tubulin-binding leading to destabilization of microtubule assembly in axons and neurodegeneration.By similarity4 Publications

    Keywords - PTMi

    Phosphoprotein, S-nitrosylation

    Proteomic databases

    MaxQBiO08553.
    PaxDbiO08553.
    PRIDEiO08553.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00114375.
    O08553.
    UCD-2DPAGEO08553.

    PTM databases

    PhosphoSiteiO08553.

    Expressioni

    Gene expression databases

    BgeeiO08553.
    CleanExiMM_DPYSL2.
    GenevestigatoriO08553.

    Interactioni

    Subunit structurei

    Homotetramer, and heterotetramer with CRMP1, DPYSL3, DPYSL4 or DPYSL5. Interacts through its C-terminus with the C-terminus of CYFIP1/SRA1. Interacts with HTR4. Interacts with CLN6. Interacts with MICALL1.3 Publications

    Protein-protein interaction databases

    BioGridi198891. 8 interactions.
    IntActiO08553. 9 interactions.
    MINTiMINT-4093534.
    STRINGi10090.ENSMUSP00000022629.

    Structurei

    3D structure databases

    ProteinModelPortaliO08553.
    SMRiO08553. Positions 14-490.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0044.
    GeneTreeiENSGT00740000115123.
    HOGENOMiHOG000219145.
    HOVERGENiHBG000806.
    InParanoidiO08553.
    KOiK07528.
    OMAiEVPAFFK.
    OrthoDBiEOG7SJD48.
    PhylomeDBiO08553.
    TreeFamiTF314706.

    Family and domain databases

    Gene3Di2.30.40.10. 2 hits.
    InterProiIPR006680. Amidohydro_1.
    IPR011778. Hydantoinase/dihydroPyrase.
    IPR011059. Metal-dep_hydrolase_composite.
    [Graphical view]
    PfamiPF01979. Amidohydro_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF51338. SSF51338. 2 hits.
    TIGRFAMsiTIGR02033. D-hydantoinase. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O08553-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSYQGKKNIP RITSDRLLIK GGKIVNDDQS FYADIYMEDG LIKQIGENLI    50
    VPGGVKTIEA HSRMVIPGGI DVHTRFQMPD QGMTSADDFF QGTKAALAGG 100
    TTMIIDHVVP EPGTSLLAAF DQWREWADSK SCCDYSLHVD ITEWHKGIQE 150
    EMEALVKDHG VNSFLVYMAF KDRFQLTDSQ IYEVLSVIRD IGAIAQVHAE 200
    NGDIIAEEQQ RILDLGITGP EGHVLSRPEE VEAEAVNRSI TIANQTNCPL 250
    YVTKVMSKSA AEVIAQARKK GTVVYGEPIT ASLGTDGSHY WSKNWAKAAA 300
    FVTSPPLSPD PTTPDFLNSL LSCGDLQVTG SAHCTFNTAQ KAVGKDNFTL 350
    IPEGTNGTEE RMSVIWDKAV VTGKMDENQF VAVTSTNAAK VFNLYPRKGR 400
    ISVGSDADLV IWDPDSVKTI SAKTHNSALE YNIFEGMECR GSPLVVISQG 450
    KIVLEDGTLH VTEGSGRYIP RKPFPDFVYK RIKARSRLAE LRGVPRGLYD 500
    GPVCEVSVTP KTVTPASSAK TSPAKQQAPP VRNLHQSGFS LSGAQIDDNI 550
    PRRTTQRIVA PPGGRANITS LG 572
    Length:572
    Mass (Da):62,278
    Last modified:May 2, 2006 - v2
    Checksum:iC031F3BC038AA737
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 111R → P in CAA71370. (PubMed:9652388)Curated
    Sequence conflicti208 – 2081E → A in CAA71370. (PubMed:9652388)Curated
    Sequence conflicti257 – 2571S → P in CAA71370. (PubMed:9652388)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y10339 mRNA. Translation: CAA71370.1.
    BC062955 mRNA. Translation: AAH62955.1.
    CCDSiCCDS27224.1.
    RefSeqiNP_034085.2. NM_009955.3.
    UniGeneiMm.352648.
    Mm.475100.

    Genome annotation databases

    EnsembliENSMUST00000022629; ENSMUSP00000022629; ENSMUSG00000022048.
    GeneIDi12934.
    KEGGimmu:12934.
    UCSCiuc007uko.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y10339 mRNA. Translation: CAA71370.1 .
    BC062955 mRNA. Translation: AAH62955.1 .
    CCDSi CCDS27224.1.
    RefSeqi NP_034085.2. NM_009955.3.
    UniGenei Mm.352648.
    Mm.475100.

    3D structure databases

    ProteinModelPortali O08553.
    SMRi O08553. Positions 14-490.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198891. 8 interactions.
    IntActi O08553. 9 interactions.
    MINTi MINT-4093534.
    STRINGi 10090.ENSMUSP00000022629.

    Chemistry

    ChEMBLi CHEMBL1075160.

    Protein family/group databases

    MEROPSi M38.975.

    PTM databases

    PhosphoSitei O08553.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00114375.
    O08553.
    UCD-2DPAGE O08553.

    Proteomic databases

    MaxQBi O08553.
    PaxDbi O08553.
    PRIDEi O08553.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000022629 ; ENSMUSP00000022629 ; ENSMUSG00000022048 .
    GeneIDi 12934.
    KEGGi mmu:12934.
    UCSCi uc007uko.1. mouse.

    Organism-specific databases

    CTDi 1808.
    MGIi MGI:1349763. Dpysl2.

    Phylogenomic databases

    eggNOGi COG0044.
    GeneTreei ENSGT00740000115123.
    HOGENOMi HOG000219145.
    HOVERGENi HBG000806.
    InParanoidi O08553.
    KOi K07528.
    OMAi EVPAFFK.
    OrthoDBi EOG7SJD48.
    PhylomeDBi O08553.
    TreeFami TF314706.

    Miscellaneous databases

    ChiTaRSi DPYSL2. mouse.
    NextBioi 282608.
    PROi O08553.
    SOURCEi Search...

    Gene expression databases

    Bgeei O08553.
    CleanExi MM_DPYSL2.
    Genevestigatori O08553.

    Family and domain databases

    Gene3Di 2.30.40.10. 2 hits.
    InterProi IPR006680. Amidohydro_1.
    IPR011778. Hydantoinase/dihydroPyrase.
    IPR011059. Metal-dep_hydrolase_composite.
    [Graphical view ]
    Pfami PF01979. Amidohydro_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51338. SSF51338. 2 hits.
    TIGRFAMsi TIGR02033. D-hydantoinase. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The Ulip family phosphoproteins -- common and specific properties."
      Byk T., Ozon S., Sobel A.
      Eur. J. Biochem. 254:14-24(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: ICR.
      Tissue: Brain.
    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].
      Strain: C57BL/6.
      Tissue: Brain.
    3. Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 44-56; 174-211; 239-254; 259-268; 391-397; 441-467 AND 533-552, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    4. "Brain CRMP forms heterotetramers similar to liver dihydropyrimidinase."
      Wang L.H., Strittmatter S.M.
      J. Neurochem. 69:2261-2269(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    5. "Molecular characterization of CRMP5, a novel member of the collapsin response mediator protein family."
      Fukada M., Watakabe I., Yuasa-Kawada J., Kawachi H., Kuroiwa A., Matsuda Y., Noda M.
      J. Biol. Chem. 275:37957-37965(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    6. "New sorting nexin (SNX27) and NHERF specifically interact with the 5-HT4a receptor splice variant: roles in receptor targeting."
      Joubert L., Hanson B., Barthet G., Sebben M., Claeysen S., Hong W., Marin P., Dumuis A., Bockaert J.
      J. Cell Sci. 117:5367-5379(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HTR4.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    8. "Quantitative analysis of both protein expression and serine / threonine post-translational modifications through stable isotope labeling with dithiothreitol."
      Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L., Hart G.W., Burlingame A.L.
      Proteomics 5:388-398(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-431; TYR-499 AND THR-509, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    10. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-514; SER-517; SER-518 AND SER-522, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    11. "ZNRF1 promotes Wallerian degeneration by degrading AKT to induce GSK3B-dependent CRMP2 phosphorylation."
      Wakatsuki S., Saitoh F., Araki T.
      Nat. Cell Biol. 13:1415-1423(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT THR-514, MUTAGENESIS OF THR-514.
    12. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-258, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiDPYL2_MOUSE
    AccessioniPrimary (citable) accession number: O08553
    Secondary accession number(s): Q6P5D0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: May 2, 2006
    Last modified: October 1, 2014
    This is version 127 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    Lacks most of the conserved residues that are essential for binding the metal cofactor and hence for dihydropyrimidinase activity. Its enzyme activity is therefore unsure.Curated

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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

    External Data

    Dasty 3