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Protein

Dihydropyrimidinase-related protein 2

Gene

Dpysl2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Enzyme and pathway databases

ReactomeiREACT_314392. CRMPs in Sema3A signaling.
REACT_353475. Recycling pathway of L1.

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 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1349763. Dpysl2.

Subcellular locationi

GO - Cellular componenti

  • axon Source: MGI
  • cytosol Source: UniProtKB
  • dendrite Source: MGI
  • extracellular exosome Source: MGI
  • growth cone Source: Ensembl
  • membrane Source: UniProtKB-SubCell
  • microtubule Source: Ensembl
  • mitochondrion Source: MGI
  • myelin sheath Source: UniProtKB
  • neuronal cell body Source: MGI
  • terminal bouton Source: Ensembl
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 2PRO_0000165914Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321Phosphotyrosine; by FYNBy similarity
Modified residuei101 – 1011PhosphothreonineBy similarity
Modified residuei102 – 1021PhosphothreonineBy similarity
Modified residuei258 – 2581N6-succinyllysine1 Publication
Modified residuei259 – 2591PhosphoserineBy similarity
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 similarity1 Publication

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.
GenevisibleiO08553. MM.

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. 10 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.
GeneTreeiENSGT00760000119241.
HOGENOMiHOG000219145.
HOVERGENiHBG000806.
InParanoidiO08553.
KOiK07528.
OMAiMFCPVEG.
OrthoDBiEOG7SJD48.
PhylomeDBiO08553.
TreeFamiTF314706.

Family and domain databases

Gene3Di2.30.40.10. 2 hits.
InterProiIPR006680. Amidohydro_1.
IPR030615. DRP2.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
PANTHERiPTHR11647:SF56. PTHR11647:SF56. 1 hit.
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

        10         20         30         40         50
MSYQGKKNIP RITSDRLLIK GGKIVNDDQS FYADIYMEDG LIKQIGENLI
60 70 80 90 100
VPGGVKTIEA HSRMVIPGGI DVHTRFQMPD QGMTSADDFF QGTKAALAGG
110 120 130 140 150
TTMIIDHVVP EPGTSLLAAF DQWREWADSK SCCDYSLHVD ITEWHKGIQE
160 170 180 190 200
EMEALVKDHG VNSFLVYMAF KDRFQLTDSQ IYEVLSVIRD IGAIAQVHAE
210 220 230 240 250
NGDIIAEEQQ RILDLGITGP EGHVLSRPEE VEAEAVNRSI TIANQTNCPL
260 270 280 290 300
YVTKVMSKSA AEVIAQARKK GTVVYGEPIT ASLGTDGSHY WSKNWAKAAA
310 320 330 340 350
FVTSPPLSPD PTTPDFLNSL LSCGDLQVTG SAHCTFNTAQ KAVGKDNFTL
360 370 380 390 400
IPEGTNGTEE RMSVIWDKAV VTGKMDENQF VAVTSTNAAK VFNLYPRKGR
410 420 430 440 450
ISVGSDADLV IWDPDSVKTI SAKTHNSALE YNIFEGMECR GSPLVVISQG
460 470 480 490 500
KIVLEDGTLH VTEGSGRYIP RKPFPDFVYK RIKARSRLAE LRGVPRGLYD
510 520 530 540 550
GPVCEVSVTP KTVTPASSAK TSPAKQQAPP VRNLHQSGFS LSGAQIDDNI
560 570
PRRTTQRIVA PPGGRANITS LG
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
Y10339 mRNA. Translation: CAA71370.1.
BC062955 mRNA. Translation: AAH62955.1.
CCDSiCCDS27224.1.
RefSeqiNP_034085.2. NM_009955.3.
UniGeneiMm.352648.
Mm.475100.

3D structure databases

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

Protein-protein interaction databases

BioGridi198891. 10 interactions.
IntActiO08553. 9 interactions.
MINTiMINT-4093534.
STRINGi10090.ENSMUSP00000022629.

Chemistry

ChEMBLiCHEMBL1075160.

Protein family/group databases

MEROPSiM38.975.

PTM databases

PhosphoSiteiO08553.

2D gel databases

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

Proteomic databases

MaxQBiO08553.
PaxDbiO08553.
PRIDEiO08553.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1808.
MGIiMGI:1349763. Dpysl2.

Phylogenomic databases

eggNOGiCOG0044.
GeneTreeiENSGT00760000119241.
HOGENOMiHOG000219145.
HOVERGENiHBG000806.
InParanoidiO08553.
KOiK07528.
OMAiMFCPVEG.
OrthoDBiEOG7SJD48.
PhylomeDBiO08553.
TreeFamiTF314706.

Enzyme and pathway databases

ReactomeiREACT_314392. CRMPs in Sema3A signaling.
REACT_353475. Recycling pathway of L1.

Miscellaneous databases

ChiTaRSiDpysl2. mouse.
NextBioi282608.
PROiO08553.
SOURCEiSearch...

Gene expression databases

BgeeiO08553.
CleanExiMM_DPYSL2.
GenevisibleiO08553. MM.

Family and domain databases

Gene3Di2.30.40.10. 2 hits.
InterProiIPR006680. Amidohydro_1.
IPR030615. DRP2.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
PANTHERiPTHR11647:SF56. PTHR11647:SF56. 1 hit.
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
TIGRFAMsiTIGR02033. D-hydantoinase. 1 hit.
ProtoNetiSearch...

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 22, 2015
This is version 137 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

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 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.