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O08553 (DPYL2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydropyrimidinase-related protein 2

Short name=DRP-2
Alternative name(s):
Unc-33-like phosphoprotein 2
Short name=ULIP-2
Gene names
Name:Dpysl2
Synonyms:Crmp2, Ulip2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length572 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11

Subunit structure

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. Ref.4 Ref.5 Ref.6

Subcellular location

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

Post-translational modification

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.

Sequence similarities

Belongs to the DHOase family. Hydantoinase/dihydropyrimidinase subfamily.

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.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
   Cellular componentCytoplasm
Cytoskeleton
Membrane
   Molecular functionDevelopmental protein
   PTMPhosphoprotein
S-nitrosylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcytoskeleton organization

Inferred from direct assay Ref.11. Source: UniProtKB

endocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

olfactory bulb development

Inferred from electronic annotation. Source: Ensembl

positive regulation of glutamate secretion

Inferred from electronic annotation. Source: Ensembl

pyrimidine nucleobase catabolic process

Inferred from electronic annotation. Source: InterPro

regulation of neuron differentiation

Inferred from electronic annotation. Source: Ensembl

response to amphetamine

Inferred from electronic annotation. Source: Ensembl

response to cocaine

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

spinal cord development

Inferred from electronic annotation. Source: Ensembl

synaptic vesicle transport

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentaxon

Inferred from direct assay PubMed 15834957. Source: MGI

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite

Inferred from direct assay PubMed 15834957. Source: MGI

growth cone

Inferred from electronic annotation. Source: Ensembl

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 14651853. Source: MGI

neuronal cell body

Inferred from direct assay PubMed 15834957. Source: MGI

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides

Inferred from electronic annotation. Source: InterPro

protein kinase binding

Inferred from physical interaction Ref.11. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 572572Dihydropyrimidinase-related protein 2
PRO_0000165914

Amino acid modifications

Modified residue321Phosphotyrosine; by FYN By similarity
Modified residue2581N6-succinyllysine Ref.12
Modified residue4311Phosphotyrosine Ref.9
Modified residue4651Phosphoserine Ref.8
Modified residue4991Phosphotyrosine Ref.9
Modified residue5041S-nitrosocysteine By similarity
Modified residue5091Phosphothreonine Ref.9
Modified residue5141Phosphothreonine; by GSK3-beta Ref.10 Ref.11
Modified residue5171Phosphoserine Ref.10
Modified residue5181Phosphoserine Ref.10
Modified residue5221Phosphoserine; alternate Ref.10
Modified residue5221Phosphoserine; by DYRK2; alternate By similarity
Modified residue5551Phosphothreonine; by ROCK2 By similarity

Experimental info

Mutagenesis5141T → A: Delayed neurite degeneration. Ref.11
Sequence conflict111R → P in CAA71370. Ref.1
Sequence conflict2081E → A in CAA71370. Ref.1
Sequence conflict2571S → P in CAA71370. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O08553 [UniParc].

Last modified May 2, 2006. Version 2.
Checksum: C031F3BC038AA737

FASTA57262,278
        10         20         30         40         50         60 
MSYQGKKNIP RITSDRLLIK GGKIVNDDQS FYADIYMEDG LIKQIGENLI VPGGVKTIEA 

        70         80         90        100        110        120 
HSRMVIPGGI DVHTRFQMPD QGMTSADDFF QGTKAALAGG TTMIIDHVVP EPGTSLLAAF 

       130        140        150        160        170        180 
DQWREWADSK SCCDYSLHVD ITEWHKGIQE EMEALVKDHG VNSFLVYMAF KDRFQLTDSQ 

       190        200        210        220        230        240 
IYEVLSVIRD IGAIAQVHAE NGDIIAEEQQ RILDLGITGP EGHVLSRPEE VEAEAVNRSI 

       250        260        270        280        290        300 
TIANQTNCPL YVTKVMSKSA AEVIAQARKK GTVVYGEPIT ASLGTDGSHY WSKNWAKAAA 

       310        320        330        340        350        360 
FVTSPPLSPD PTTPDFLNSL LSCGDLQVTG SAHCTFNTAQ KAVGKDNFTL IPEGTNGTEE 

       370        380        390        400        410        420 
RMSVIWDKAV VTGKMDENQF VAVTSTNAAK VFNLYPRKGR ISVGSDADLV IWDPDSVKTI 

       430        440        450        460        470        480 
SAKTHNSALE YNIFEGMECR GSPLVVISQG KIVLEDGTLH VTEGSGRYIP RKPFPDFVYK 

       490        500        510        520        530        540 
RIKARSRLAE LRGVPRGLYD GPVCEVSVTP KTVTPASSAK TSPAKQQAPP VRNLHQSGFS 

       550        560        570 
LSGAQIDDNI PRRTTQRIVA PPGGRANITS LG 

« Hide

References

« Hide 'large scale' references
[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]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y10339 mRNA. Translation: CAA71370.1.
BC062955 mRNA. Translation: AAH62955.1.
RefSeqNP_034085.2. NM_009955.3.
UniGeneMm.352648.
Mm.475100.

3D structure databases

ProteinModelPortalO08553.
SMRO08553. Positions 14-490.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198891. 8 interactions.
IntActO08553. 9 interactions.
MINTMINT-4093534.
STRING10090.ENSMUSP00000022629.

Chemistry

ChEMBLCHEMBL1075160.

Protein family/group databases

MEROPSM38.975.

PTM databases

PhosphoSiteO08553.

2D gel databases

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

Proteomic databases

PaxDbO08553.
PRIDEO08553.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022629; ENSMUSP00000022629; ENSMUSG00000022048.
GeneID12934.
KEGGmmu:12934.
UCSCuc007uko.1. mouse.

Organism-specific databases

CTD1808.
MGIMGI:1349763. Dpysl2.

Phylogenomic databases

eggNOGCOG0044.
GeneTreeENSGT00740000115123.
HOGENOMHOG000219145.
HOVERGENHBG000806.
InParanoidO08553.
KOK07528.
OMAEVPAFFK.
OrthoDBEOG7SJD48.
PhylomeDBO08553.
TreeFamTF314706.

Gene expression databases

BgeeO08553.
CleanExMM_DPYSL2.
GenevestigatorO08553.

Family and domain databases

Gene3D2.30.40.10. 2 hits.
InterProIPR006680. Amidohydro_1.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMSSF51338. SSF51338. 2 hits.
TIGRFAMsTIGR02033. D-hydantoinase. 1 hit.
ProtoNetSearch...

Other

ChiTaRSDPYSL2. mouse.
NextBio282608.
PROO08553.
SOURCESearch...

Entry information

Entry nameDPYL2_MOUSE
AccessionPrimary (citable) accession number: O08553
Secondary accession number(s): Q6P5D0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 2, 2006
Last modified: April 16, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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