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Protein

Dihydropyrimidinase-related protein 3

Gene

DPYSL3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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

Enzyme and pathway databases

ReactomeiR-HSA-399956. CRMPs in Sema3A signaling.
SIGNORiQ14195.

Protein family/group databases

MEROPSiM38.976.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydropyrimidinase-related protein 3
Short name:
DRP-3
Alternative name(s):
Collapsin response mediator protein 4
Short name:
CRMP-4
Unc-33-like phosphoprotein 1
Short name:
ULIP-1
Gene namesi
Name:DPYSL3
Synonyms:CRMP4, DRP3, ULIP, ULIP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:3015. DPYSL3.

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cell projection, Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi1809.
OpenTargetsiENSG00000113657.
PharmGKBiPA27473.

Polymorphism and mutation databases

BioMutaiDPYSL3.
DMDMi3122050.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001659171 – 570Dihydropyrimidinase-related protein 3Add BLAST570

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei259PhosphoserineCombined sources1
Modified residuei431PhosphotyrosineBy similarity1
Modified residuei499PhosphotyrosineBy similarity1
Modified residuei509Phosphothreonine; by GSK3Combined sources1 Publication1
Modified residuei514Phosphothreonine; by GSK3Combined sources1 Publication1
Modified residuei518Phosphoserine; by GSK31 Publication1
Modified residuei522Phosphoserine; by DYRK2Combined sources1 Publication1
Modified residuei536PhosphoserineBy similarity1
Modified residuei539PhosphoserineBy similarity1
Modified residuei541PhosphoserineBy similarity1
Modified residuei543PhosphothreonineBy similarity1
Isoform LCRMP-4 (identifier: Q14195-2)
Modified residuei102PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylation on Ser-522 by DYRK2 promotes subsequent phosphorylation on Thr-509, Thr-514 and Ser-518 by GSK3.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ14195.
MaxQBiQ14195.
PaxDbiQ14195.
PeptideAtlasiQ14195.
PRIDEiQ14195.

2D gel databases

REPRODUCTION-2DPAGEiQ14195.
UCD-2DPAGEiQ14195.

PTM databases

iPTMnetiQ14195.
PhosphoSitePlusiQ14195.

Expressioni

Tissue specificityi

Mainly expressed in heart and skeletal muscle. Also strongly expressed in fetal brain and spinal cord.

Gene expression databases

BgeeiENSG00000113657.
CleanExiHS_DPYSL3.
ExpressionAtlasiQ14195. baseline and differential.
GenevisibleiQ14195. HS.

Organism-specific databases

HPAiHPA010948.

Interactioni

Subunit structurei

Homotetramer, and heterotetramer with CRMP1, DPYSL2, DPYSL4 or DPYSL5. Interacts with synaptic vesicle protein 2 and SH3A domain of intersectin.By similarity

Binary interactionsi

Show more details

GO - Molecular functioni

  • filamin binding Source: WormBase
  • SH3 domain binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108143. 39 interactors.
IntActiQ14195. 11 interactors.
STRINGi9606.ENSP00000343690.

Structurei

Secondary structure

1570
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 – 74Combined sources6
Helixi89 – 98Combined sources10
Beta strandi101 – 108Combined sources8
Helixi116 – 130Combined sources15
Beta strandi132 – 141Combined sources10
Helixi146 – 158Combined sources13
Beta strandi163 – 168Combined sources6
Turni171 – 174Combined sources4
Helixi178 – 191Combined sources14
Beta strandi194 – 198Combined sources5
Helixi202 – 214Combined sources13
Helixi221 – 225Combined sources5
Helixi229 – 245Combined sources17
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 – 487Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4BKNX-ray2.10A/B1-570[»]
4CNSX-ray2.40A/B/C/D13-490[»]
4CNTX-ray2.65A/B/C/D1-570[»]
4CNUX-ray2.80A/B1-570[»]
ProteinModelPortaliQ14195.
SMRiQ14195.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2584. Eukaryota.
COG0044. LUCA.
GeneTreeiENSGT00760000119241.
HOGENOMiHOG000219145.
HOVERGENiHBG000806.
InParanoidiQ14195.
OMAiYVCSPPP.
OrthoDBiEOG091G05F3.
PhylomeDBiQ14195.
TreeFamiTF314706.

Family and domain databases

CDDicd01314. D-HYD. 1 hit.
Gene3Di2.30.40.10. 1 hit.
InterProiView protein in InterPro
IPR006680. Amidohydro-rel.
IPR030628. DRP3.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
PANTHERiPTHR11647:SF86. PTHR11647:SF86. 1 hit.
PfamiView protein in Pfam
PF01979. Amidohydro_1. 1 hit.
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR02033. D-hydantoinase. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q14195-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSYQGKKNIP RITSDRLLIK GGRIVNDDQS FYADIYMEDG LIKQIGDNLI
60 70 80 90 100
VPGGVKTIEA NGKMVIPGGI DVHTHFQMPY KGMTTVDDFF QGTKAALAGG
110 120 130 140 150
TTMIIDHVVP EPESSLTEAY EKWREWADGK SCCDYALHVD ITHWNDSVKQ
160 170 180 190 200
EVQNLIKDKG VNSFMVYMAY KDLYQVSNTE LYEIFTCLGE LGAIAQVHAE
210 220 230 240 250
NGDIIAQEQT RMLEMGITGP EGHVLSRPEE LEAEAVFRAI TIASQTNCPL
260 270 280 290 300
YVTKVMSKSA ADLISQARKK GNVVFGEPIT ASLGIDGTHY WSKNWAKAAA
310 320 330 340 350
FVTSPPLSPD PTTPDYINSL LASGDLQLSG SAHCTFSTAQ KAIGKDNFTA
360 370 380 390 400
IPEGTNGVEE RMSVIWDKAV ATGKMDENQF VAVTSTNAAK IFNLYPRKGR
410 420 430 440 450
ISVGSDSDLV IWDPDAVKIV SAKNHQSAAE YNIFEGMELR GAPLVVICQG
460 470 480 490 500
KIMLEDGNLH VTQGAGRFIP CSPFSDYVYK RIKARRKMAD LHAVPRGMYD
510 520 530 540 550
GPVFDLTTTP KGGTPAGSAR GSPTRPNPPV RNLHQSGFSL SGTQVDEGVR
560 570
SASKRIVAPP GGRSNITSLS
Length:570
Mass (Da):61,963
Last modified:November 1, 1996 - v1
Checksum:i9D6AFE86CBB33AD5
GO
Isoform LCRMP-4 (identifier: Q14195-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: MSYQGKKNIPRIT → MASGRRGWDS...VLQNLGPKDK

Show »
Length:684
Mass (Da):73,911
Checksum:i1729A3ED4DA83D30
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti49L → V in CAA69153 (PubMed:9115293).Curated1
Sequence conflicti142T → A in CAA69153 (PubMed:9115293).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_020485442A → S. Corresponds to variant dbSNP:rs2304044Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0425461 – 13MSYQG…IPRIT → MASGRRGWDSSHEDDLPVYL ARPGTTDQVPRQKYGGMFCN VEGAFESKTLDFDALSVGQR GAKTPRSGQGSDRGSGSRPG IEGDTPRRGQGREESREPAP ASPAPAGVEIRSATGKEVLQ NLGPKDK in isoform LCRMP-4. 1 PublicationAdd BLAST13

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78014 mRNA. Translation: BAA11192.1.
Y07818 mRNA. Translation: CAA69153.1.
EU007906 mRNA. Translation: ABV80252.1.
AC011373 Genomic DNA. No translation available.
CCDSiCCDS43381.1. [Q14195-1]
CCDS56387.1. [Q14195-2]
PIRiJC5318.
RefSeqiNP_001184223.1. NM_001197294.1. [Q14195-2]
NP_001378.1. NM_001387.2. [Q14195-1]
UniGeneiHs.519659.

Genome annotation databases

EnsembliENST00000343218; ENSP00000343690; ENSG00000113657. [Q14195-2]
ENST00000398514; ENSP00000381526; ENSG00000113657. [Q14195-1]
GeneIDi1809.
KEGGihsa:1809.
UCSCiuc003lon.2. human. [Q14195-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiDPYL3_HUMAN
AccessioniPrimary (citable) accession number: Q14195
Secondary accession number(s): B3SXQ8, Q93012
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: August 30, 2017
This is version 167 of the entry and version 1 of the sequence. See 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families