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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

ReactomeiR-MMU-399956. CRMPs in Sema3A signaling.
R-MMU-437239. 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
Proteomesi
  • UP000000589 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
  • protein complex Source: Ensembl
  • terminal bouton Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi514T → A: Delayed neurite degeneration. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL1075160.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001659141 – 572Dihydropyrimidinase-related protein 2Add BLAST572

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei32Phosphotyrosine; by FYNBy similarity1
Modified residuei101PhosphothreonineBy similarity1
Modified residuei102PhosphothreonineBy similarity1
Modified residuei258N6-succinyllysineCombined sources1
Modified residuei259PhosphoserineBy similarity1
Modified residuei402PhosphoserineCombined sources1
Modified residuei431PhosphotyrosineCombined sources1
Modified residuei465PhosphoserineCombined sources1
Modified residuei499PhosphotyrosineCombined sources1
Modified residuei504S-nitrosocysteineBy similarity1
Modified residuei507PhosphoserineCombined sources1
Modified residuei509PhosphothreonineCombined sources1
Modified residuei512PhosphothreonineCombined sources1
Modified residuei514Phosphothreonine; by GSK3-betaCombined sources1 Publication1
Modified residuei517PhosphoserineCombined sources1
Modified residuei518PhosphoserineCombined sources1
Modified residuei521PhosphothreonineCombined sources1
Modified residuei522PhosphoserineCombined sources1
Modified residuei537PhosphoserineCombined sources1
Modified residuei540PhosphoserineCombined sources1
Modified residuei542PhosphoserineCombined sources1
Modified residuei555Phosphothreonine; by ROCK2By similarity1
Modified residuei565Asymmetric dimethylarginineCombined sources1

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

Methylation, Phosphoprotein, S-nitrosylation

Proteomic databases

EPDiO08553.
MaxQBiO08553.
PaxDbiO08553.
PeptideAtlasiO08553.
PRIDEiO08553.

2D gel databases

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

PTM databases

iPTMnetiO08553.
PhosphoSitePlusiO08553.
SwissPalmiO08553.

Expressioni

Gene expression databases

BgeeiENSMUSG00000022048.
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

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi198891. 12 interactors.
IntActiO08553. 12 interactors.
MINTiMINT-4093534.
STRINGi10090.ENSMUSP00000022629.

Structurei

3D structure databases

ProteinModelPortaliO08553.
SMRiO08553.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2584. Eukaryota.
COG0044. LUCA.
GeneTreeiENSGT00760000119241.
HOGENOMiHOG000219145.
HOVERGENiHBG000806.
InParanoidiO08553.
KOiK07528.
OMAiQQRDVAH.
OrthoDBiEOG091G05F3.
PhylomeDBiO08553.
TreeFamiTF314706.

Family and domain databases

CDDicd01314. D-HYD. 1 hit.
Gene3Di2.30.40.10. 2 hits.
InterProiIPR006680. Amidohydro-rel.
IPR030615. DRP2.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
[Graphical view]
PANTHERiPTHR11647:SF56. PTHR11647:SF56. 1 hit.
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti11R → P in CAA71370 (PubMed:9652388).Curated1
Sequence conflicti208E → A in CAA71370 (PubMed:9652388).Curated1
Sequence conflicti257S → P in CAA71370 (PubMed:9652388).Curated1

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198891. 12 interactors.
IntActiO08553. 12 interactors.
MINTiMINT-4093534.
STRINGi10090.ENSMUSP00000022629.

Chemistry databases

ChEMBLiCHEMBL1075160.

Protein family/group databases

MEROPSiM38.975.

PTM databases

iPTMnetiO08553.
PhosphoSitePlusiO08553.
SwissPalmiO08553.

2D gel databases

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

Proteomic databases

EPDiO08553.
MaxQBiO08553.
PaxDbiO08553.
PeptideAtlasiO08553.
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

eggNOGiKOG2584. Eukaryota.
COG0044. LUCA.
GeneTreeiENSGT00760000119241.
HOGENOMiHOG000219145.
HOVERGENiHBG000806.
InParanoidiO08553.
KOiK07528.
OMAiQQRDVAH.
OrthoDBiEOG091G05F3.
PhylomeDBiO08553.
TreeFamiTF314706.

Enzyme and pathway databases

ReactomeiR-MMU-399956. CRMPs in Sema3A signaling.
R-MMU-437239. Recycling pathway of L1.

Miscellaneous databases

ChiTaRSiDpysl2. mouse.
PROiO08553.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000022048.
CleanExiMM_DPYSL2.
GenevisibleiO08553. MM.

Family and domain databases

CDDicd01314. D-HYD. 1 hit.
Gene3Di2.30.40.10. 2 hits.
InterProiIPR006680. Amidohydro-rel.
IPR030615. DRP2.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
[Graphical view]
PANTHERiPTHR11647:SF56. PTHR11647:SF56. 1 hit.
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR02033. D-hydantoinase. 1 hit.
ProtoNetiSearch...

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: November 2, 2016
This is version 150 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

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 one 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.