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O08553

- DPYL2_MOUSE

UniProt

O08553 - DPYL2_MOUSE

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Protein
Dihydropyrimidinase-related protein 2
Gene
Dpysl2, Crmp2, Ulip2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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 2
PRO_0000165914Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321Phosphotyrosine; by FYN By similarity
Modified residuei258 – 2581N6-succinyllysine1 Publication
Modified residuei431 – 4311Phosphotyrosine1 Publication
Modified residuei465 – 4651Phosphoserine1 Publication
Modified residuei499 – 4991Phosphotyrosine1 Publication
Modified residuei504 – 5041S-nitrosocysteine By 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; alternate By similarity
Modified residuei555 – 5551Phosphothreonine; by ROCK2 By 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.

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.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111R → P in CAA71370. 1 Publication
Sequence conflicti208 – 2081E → A in CAA71370. 1 Publication
Sequence conflicti257 – 2571S → P in CAA71370. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 126 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.

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

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