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Protein

Dihydropyrimidinase-related protein 4

Gene

DPYSL4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, neuronal growth cone collapse and cell migration (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • nervous system development Source: ProtInc
  • neuron death Source: InterPro
  • neuron projection guidance Source: InterPro
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-HSA-399956. CRMPs in Sema3A signaling.

Protein family/group databases

MEROPSiM38.977.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydropyrimidinase-related protein 4
Short name:
DRP-4
Alternative name(s):
Collapsin response mediator protein 3
Short name:
CRMP-3
UNC33-like phosphoprotein 4
Short name:
ULIP-4
Gene namesi
Name:DPYSL4
Synonyms:CRMP3, ULIP4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:3016. DPYSL4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27474.

Polymorphism and mutation databases

BioMutaiDPYSL4.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 572572Dihydropyrimidinase-related protein 4PRO_0000165921Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei537 – 5371PhosphoserineBy similarity
Modified residuei544 – 5441PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO14531.
MaxQBiO14531.
PaxDbiO14531.
PeptideAtlasiO14531.
PRIDEiO14531.
TopDownProteomicsiO14531.

PTM databases

iPTMnetiO14531.
PhosphoSiteiO14531.

Expressioni

Gene expression databases

BgeeiO14531.
CleanExiHS_DPYSL4.
ExpressionAtlasiO14531. baseline and differential.
GenevisibleiO14531. HS.

Organism-specific databases

HPAiHPA049066.

Interactioni

Subunit structurei

Homotetramer, and heterotetramer with CRMP1, DPYSL2, DPYSL3 or DPYSL5. Interacts with PLEXA1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
RBPMSQ930623EBI-719542,EBI-740322
TRIP13Q156453EBI-719542,EBI-358993

GO - Molecular functioni

  • filamin binding Source: WormBase

Protein-protein interaction databases

BioGridi115821. 26 interactions.
IntActiO14531. 7 interactions.
STRINGi9606.ENSP00000339850.

Structurei

3D structure databases

ProteinModelPortaliO14531.
SMRiO14531. Positions 14-490.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2584. Eukaryota.
COG0044. LUCA.
GeneTreeiENSGT00760000119241.
HOGENOMiHOG000219145.
HOVERGENiHBG000806.
InParanoidiO14531.
OMAiPRWHESI.
OrthoDBiEOG7SJD48.
PhylomeDBiO14531.
TreeFamiTF314706.

Family and domain databases

Gene3Di2.30.40.10. 2 hits.
InterProiIPR006680. Amidohydro-rel.
IPR030612. DRP4.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
[Graphical view]
PANTHERiPTHR11647:SF55. PTHR11647:SF55. 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.

O14531-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFQGKKSIP RITSDRLLIR GGRIVNDDQS FYADVHVEDG LIKQIGENLI
60 70 80 90 100
VPGGIKTIDA HGLMVLPGGV DVHTRLQMPV LGMTPADDFC QGTKAALAGG
110 120 130 140 150
TTMILDHVFP DTGVSLLAAY EQWRERADSA ACCDYSLHVD ITRWHESIKE
160 170 180 190 200
ELEALVKEKG VNSFLVFMAY KDRCQCSDSQ MYEIFSIIRD LGALAQVHAE
210 220 230 240 250
NGDIVEEEQK RLLELGITGP EGHVLSHPEE VEAEAVYRAV TIAKQANCPL
260 270 280 290 300
YVTKVMSKGA ADAIAQAKRR GVVVFGEPIT ASLGTDGSHY WSKNWAKAAA
310 320 330 340 350
FVTSPPVNPD PTTADHLTCL LSSGDLQVTG SAHCTFTTAQ KAVGKDNFAL
360 370 380 390 400
IPEGTNGIEE RMSMVWEKCV ASGKMDENEF VAVTSTNAAK IFNFYPRKGR
410 420 430 440 450
VAVGSDADLV IWNPKATKII SAKTHNLNVE YNIFEGVECR GAPAVVISQG
460 470 480 490 500
RVALEDGKMF VTPGAGRFVP RKTFPDFVYK RIKARNRLAE IHGVPRGLYD
510 520 530 540 550
GPVHEVMVPA KPGSGAPARA SCPGKISVPP VRNLHQSGFS LSGSQADDHI
560 570
ARRTAQKIMA PPGGRSNITS LS
Length:572
Mass (Da):61,878
Last modified:June 21, 2005 - v2
Checksum:iFCFF3212B4AEA5B4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti122 – 1221Q → R in BAA21886 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB006713 mRNA. Translation: BAA21886.1.
AL512622 Genomic DNA. Translation: CAI12185.1.
CH471066 Genomic DNA. Translation: EAW49132.1.
CH471066 Genomic DNA. Translation: EAW49134.1.
CH471066 Genomic DNA. Translation: EAW49135.1.
BC136329 mRNA. Translation: AAI36330.1.
BC136330 mRNA. Translation: AAI36331.1.
Y10976 mRNA. Translation: CAA71872.1.
CCDSiCCDS7665.1.
RefSeqiNP_006417.2. NM_006426.2.
UniGeneiHs.100058.

Genome annotation databases

EnsembliENST00000338492; ENSP00000339850; ENSG00000151640.
GeneIDi10570.
KEGGihsa:10570.
UCSCiuc009ybb.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB006713 mRNA. Translation: BAA21886.1.
AL512622 Genomic DNA. Translation: CAI12185.1.
CH471066 Genomic DNA. Translation: EAW49132.1.
CH471066 Genomic DNA. Translation: EAW49134.1.
CH471066 Genomic DNA. Translation: EAW49135.1.
BC136329 mRNA. Translation: AAI36330.1.
BC136330 mRNA. Translation: AAI36331.1.
Y10976 mRNA. Translation: CAA71872.1.
CCDSiCCDS7665.1.
RefSeqiNP_006417.2. NM_006426.2.
UniGeneiHs.100058.

3D structure databases

ProteinModelPortaliO14531.
SMRiO14531. Positions 14-490.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115821. 26 interactions.
IntActiO14531. 7 interactions.
STRINGi9606.ENSP00000339850.

Protein family/group databases

MEROPSiM38.977.

PTM databases

iPTMnetiO14531.
PhosphoSiteiO14531.

Polymorphism and mutation databases

BioMutaiDPYSL4.

Proteomic databases

EPDiO14531.
MaxQBiO14531.
PaxDbiO14531.
PeptideAtlasiO14531.
PRIDEiO14531.
TopDownProteomicsiO14531.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000338492; ENSP00000339850; ENSG00000151640.
GeneIDi10570.
KEGGihsa:10570.
UCSCiuc009ybb.4. human.

Organism-specific databases

CTDi10570.
GeneCardsiDPYSL4.
H-InvDBHIX0035298.
HGNCiHGNC:3016. DPYSL4.
HPAiHPA049066.
MIMi608407. gene.
neXtProtiNX_O14531.
PharmGKBiPA27474.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2584. Eukaryota.
COG0044. LUCA.
GeneTreeiENSGT00760000119241.
HOGENOMiHOG000219145.
HOVERGENiHBG000806.
InParanoidiO14531.
OMAiPRWHESI.
OrthoDBiEOG7SJD48.
PhylomeDBiO14531.
TreeFamiTF314706.

Enzyme and pathway databases

ReactomeiR-HSA-399956. CRMPs in Sema3A signaling.

Miscellaneous databases

GeneWikiiDPYSL4.
GenomeRNAii10570.
PROiO14531.
SOURCEiSearch...

Gene expression databases

BgeeiO14531.
CleanExiHS_DPYSL4.
ExpressionAtlasiO14531. baseline and differential.
GenevisibleiO14531. HS.

Family and domain databases

Gene3Di2.30.40.10. 2 hits.
InterProiIPR006680. Amidohydro-rel.
IPR030612. DRP4.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
[Graphical view]
PANTHERiPTHR11647:SF55. PTHR11647:SF55. 1 hit.
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR02033. D-hydantoinase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Novel members of dihydropyrimidinase related protein family."
    Hamajima N., Kato Y., Kouwaki M., Wada Y., Sasaski M., Nonaka M.
    Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Brain.
  5. "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] OF 1-553.
    Tissue: Retina.
  6. Lubec G., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 401-415, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain.

Entry informationi

Entry nameiDPYL4_HUMAN
AccessioniPrimary (citable) accession number: O14531
Secondary accession number(s): B2RMQ1
, D3DRG5, O00240, Q5T0Q7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: June 21, 2005
Last modified: July 6, 2016
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.