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Protein

Dihydropyrimidinase-related protein 2

Gene

Dpysl2

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

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDevelopmental protein
Biological processDifferentiation, 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1349763 Dpysl2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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-2DPAGEiIPI00114375
O08553
UCD-2DPAGEiO08553

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

  • identical protein binding Source: MGI
  • microtubule binding Source: InterPro
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi198891, 26 interactors
CORUMiO08553
IntActiO08553, 22 interactors
MINTiO08553
STRINGi10090.ENSMUSP00000022629

Structurei

Secondary structure

1572
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi17 – 25Combined sources9
Beta strandi30 – 38Combined sources9
Beta strandi41 – 48Combined sources8
Beta strandi56 – 59Combined sources4
Beta strandi64 – 67Combined sources4
Beta strandi69 – 72Combined sources4
Helixi89 – 98Combined sources10
Beta strandi101 – 108Combined sources8
Helixi116 – 130Combined sources15
Beta strandi132 – 140Combined sources9
Helixi148 – 158Combined sources11
Beta strandi163 – 170Combined sources8
Turni171 – 174Combined sources4
Helixi178 – 191Combined sources14
Beta strandi194 – 198Combined sources5
Helixi202 – 214Combined sources13
Helixi221 – 225Combined sources5
Helixi229 – 246Combined sources18
Beta strandi250 – 255Combined sources6
Helixi258 – 270Combined sources13
Beta strandi274 – 279Combined sources6
Helixi280 – 284Combined sources5
Helixi287 – 291Combined sources5
Helixi295 – 300Combined sources6
Helixi313 – 322Combined sources10
Helixi338 – 341Combined sources4
Helixi342 – 344Combined sources3
Helixi348 – 350Combined sources3
Turni358 – 360Combined sources3
Helixi361 – 369Combined sources9
Turni370 – 373Combined sources4
Helixi377 – 384Combined sources8
Helixi386 – 391Combined sources6
Turni395 – 397Combined sources3
Beta strandi409 – 419Combined sources11
Turni422 – 424Combined sources3
Beta strandi426 – 428Combined sources3
Turni433 – 436Combined sources4
Beta strandi438 – 448Combined sources11
Beta strandi451 – 455Combined sources5
Helixi476 – 488Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5UQCX-ray1.78A/B15-496[»]
ProteinModelPortaliO08553
SMRiO08553
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

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

Family and domain databases

CDDicd01314 D-HYD, 1 hit
Gene3Di2.30.40.10, 2 hits
InterProiView protein in InterPro
IPR006680 Amidohydro-rel
IPR030615 DRP2
IPR011778 Hydantoinase/dihydroPyrase
IPR011059 Metal-dep_hydrolase_composite
IPR032466 Metal_Hydrolase
PANTHERiPTHR11647:SF56 PTHR11647:SF56, 1 hit
PfamiView protein in Pfam
PF01979 Amidohydro_1, 1 hit
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

Similar proteinsi

Entry informationi

Entry nameiDPYL2_MOUSE
AccessioniPrimary (citable) accession number: O08553
Secondary accession number(s): Q6P5D0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 2, 2006
Last modified: April 25, 2018
This is version 165 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health