Dihydropyrimidinase-related protein 2

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O08553 (DPYL2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 115. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	572 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a role in neuronal development and polarity, as well as in neuron projection morphogenesis, axon growth and guidance, neuronal growth cone collapse and cell migration. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Ref.14
Subunit structure	Homotetramer, and heterotetramer with CRMP1, DPYSL3, DPYSL4 or DPYSL5. Interacts through its C-terminus with the C-terminus of CYFIP1/SRA1 By similarity. Interacts with HTR4. Interacts with CLN6 By similarity. Ref.4 Ref.5 Ref.6
Subcellular location	Cytoplasm 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 process	Differentiation Neurogenesis
Cellular component	Cytoplasm
Molecular function	Developmental protein
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cytoskeleton organization Inferred from direct assay Ref.14. Source: UniProtKB olfactory bulb development Inferred from electronic annotation. Source: Compara positive regulation of glutamate secretion Inferred from electronic annotation. Source: Compara pyrimidine nucleobase catabolic process Inferred from electronic annotation. Source: InterPro regulation of neuron differentiation Inferred from electronic annotation. Source: Compara response to amphetamine Inferred from electronic annotation. Source: Compara response to cocaine Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara spinal cord development Inferred from electronic annotation. Source: Compara synaptic vesicle transport Inferred from electronic annotation. Source: Compara
Cellular_component	axon Inferred from direct assay PubMed 15834957. Source: MGI cytosol Inferred from electronic annotation. Source: Compara dendrite Inferred from direct assay PubMed 15834957. Source: MGI growth cone Inferred from electronic annotation. Source: Compara 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: Compara
Molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 572

572

Dihydropyrimidinase-related protein 2

PRO_0000165914

Amino acid modifications

Modified residue

Phosphotyrosine; by FYN By similarity

Modified residue

431

Phosphotyrosine Ref.9

Modified residue

462

Phosphothreonine Ref.11

Modified residue

465

Phosphoserine Ref.7

Modified residue

499

Phosphotyrosine Ref.9

Modified residue

509

Phosphothreonine Ref.8 Ref.9 Ref.10

Modified residue

514

Phosphothreonine; by GSK3-beta Ref.8 Ref.13 Ref.14

Modified residue

517

Phosphoserine Ref.13

Modified residue

518

Phosphoserine Ref.13

Modified residue

522

Phosphoserine; alternate Ref.13

Modified residue

522

Phosphoserine; by DYRK2; alternate By similarity

Modified residue

542

Phosphoserine Ref.12

Modified residue

555

Phosphothreonine; by ROCK2 By similarity

Experimental info

Mutagenesis

514

T → A: Delayed neurite degeneration. Ref.14

Sequence conflict

R → P in CAA71370. Ref.1

Sequence conflict

208

E → A in CAA71370. Ref.1

Sequence conflict

257

S → P in CAA71370. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

O08553 [UniParc].

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

572

62,278

        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' referencesShow '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, 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]	"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, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[8]	"Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509 AND THR-514, MASS SPECTROMETRY. Tissue: Brain.
[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-32; TYR-431; TYR-499 AND THR-509, MASS SPECTROMETRY. Tissue: Brain.
[10]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509, MASS SPECTROMETRY. Tissue: Brain cortex.
[11]	Lubec G., Kang S. Submitted (APR-2007) to UniProtKB Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-462, MASS SPECTROMETRY. Tissue: Brain.
[12]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-542, MASS SPECTROMETRY. Tissue: Melanoma.
[13]	"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, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
[14]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y10339 mRNA. Translation: CAA71370.1. BC062955 mRNA. Translation: AAH62955.1.
IPI	IPI00114375.
RefSeq	NP_034085.2. NM_009955.3.
UniGene	Mm.352648. Mm.475100.
3D structure databases
ProteinModelPortal	O08553.
SMR	O08553. Positions 14-490.
ModBase	Search...
Protein-protein interaction databases
IntAct	O08553. 5 interactions.
STRING	10090.ENSMUSP00000022629.
Protein family/group databases
MEROPS	M38.975.
PTM databases
PhosphoSite	O08553.
2D gel databases
REPRODUCTION-2DPAGE	IPI00114375. O08553.
UCD-2DPAGE	O08553.
Proteomic databases
PaxDb	O08553.
PRIDE	O08553.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000022629; ENSMUSP00000022629; ENSMUSG00000022048.
GeneID	12934.
KEGG	mmu:12934.
UCSC	uc007uko.1. mouse.
Organism-specific databases
CTD	1808.
MGI	MGI:1349763. Dpysl2.
Phylogenomic databases
eggNOG	COG0044.
GeneTree	ENSGT00550000074371.
HOGENOM	HOG000219145.
HOVERGEN	HBG000806.
InParanoid	O08553.
KO	K07528.
OMA	TEWHKGV.
OrthoDB	EOG48PMJT.
Gene expression databases
Bgee	O08553.
CleanEx	MM_DPYSL2.
Genevestigator	O08553.
GermOnline	ENSMUSG00000022048. Mus musculus.
Family and domain databases
InterPro	IPR006680. Amidohydro_1. IPR011778. Hydantoinase/dihydroPyrase. IPR011059. Metal-dep_hydrolase_composite. [Graphical view]
Pfam	PF01979. Amidohydro_1. 1 hit. [Graphical view]
SUPFAM	SSF51338. Metalo_hydrolase. 2 hits.
TIGRFAMs	TIGR02033. D-hydantoinase. 1 hit.
ProtoNet	Search...
Other
ChEMBL	CHEMBL1075160.
ChiTaRS	DPYSL2. mouse.
NextBio	282608.
SOURCE	Search...

Entry information

Entry name

DPYL2_MOUSE

Accession

Primary (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 3, 2013
This is version 115 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents