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Protein

Dihydropyrimidinase-related protein 5

Gene

DPYSL5

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

Functioni

May have a function in neuronal differentiation and/or axon growth.

GO - Molecular functioni

GO - Biological processi

  • axon guidance Source: ProtInc
  • nervous system development Source: ProtInc
  • signal transduction Source: ProtInc
Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:ENSG00000157851-MONOMER.
ReactomeiR-HSA-399956. CRMPs in Sema3A signaling.

Protein family/group databases

MEROPSiM38.978.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydropyrimidinase-related protein 5
Short name:
DRP-5
Alternative name(s):
CRMP3-associated molecule
Short name:
CRAM
Collapsin response mediator protein 5
Short name:
CRMP-5
UNC33-like phosphoprotein 6
Short name:
ULIP-6
Gene namesi
Name:DPYSL5
Synonyms:CRMP5, ULIP6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:20637. DPYSL5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi56896.
OpenTargetsiENSG00000157851.
PharmGKBiPA134927413.

Polymorphism and mutation databases

BioMutaiDPYSL5.
DMDMi20137929.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001659241 – 564Dihydropyrimidinase-related protein 5Add BLAST564

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei509PhosphothreonineBy similarity1
Modified residuei514PhosphothreonineBy similarity1
Modified residuei532PhosphoserineBy similarity1
Modified residuei538PhosphoserineBy similarity1
Modified residuei559Omega-N-methylarginineBy similarity1

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

EPDiQ9BPU6.
MaxQBiQ9BPU6.
PaxDbiQ9BPU6.
PeptideAtlasiQ9BPU6.
PRIDEiQ9BPU6.

2D gel databases

UCD-2DPAGEQ9BPU6.

PTM databases

iPTMnetiQ9BPU6.
PhosphoSitePlusiQ9BPU6.

Expressioni

Gene expression databases

BgeeiENSG00000157851.
CleanExiHS_DPYSL5.
ExpressionAtlasiQ9BPU6. baseline and differential.
GenevisibleiQ9BPU6. HS.

Organism-specific databases

HPAiHPA034544.

Interactioni

Subunit structurei

Homotetramer, and heterotetramer with other DPYS-like proteins. Interacts with DPYSL2, DPYSL3 and DPYSL4 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
DPYSL2Q165557EBI-724653,EBI-1104711

Protein-protein interaction databases

BioGridi121226. 22 interactors.
IntActiQ9BPU6. 5 interactors.
MINTiMINT-1401135.
STRINGi9606.ENSP00000288699.

Structurei

Secondary structure

1564
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 14Combined sources6
Beta strandi16 – 18Combined sources3
Beta strandi23 – 25Combined sources3
Beta strandi27 – 31Combined sources5
Beta strandi34 – 41Combined sources8
Beta strandi49 – 52Combined sources4
Beta strandi57 – 60Combined sources4
Beta strandi62 – 67Combined sources6
Helixi82 – 91Combined sources10
Beta strandi94 – 101Combined sources8
Helixi109 – 120Combined sources12
Turni121 – 123Combined sources3
Beta strandi125 – 133Combined sources9
Helixi139 – 151Combined sources13
Beta strandi156 – 161Combined sources6
Turni164 – 166Combined sources3
Helixi171 – 183Combined sources13
Beta strandi187 – 191Combined sources5
Helixi195 – 207Combined sources13
Helixi215 – 218Combined sources4
Helixi223 – 239Combined sources17
Beta strandi243 – 245Combined sources3
Helixi251 – 262Combined sources12
Beta strandi267 – 272Combined sources6
Helixi273 – 277Combined sources5
Helixi280 – 284Combined sources5
Helixi288 – 292Combined sources5
Helixi306 – 315Combined sources10
Beta strandi321 – 323Combined sources3
Helixi331 – 334Combined sources4
Helixi335 – 337Combined sources3
Helixi341 – 343Combined sources3
Turni351 – 353Combined sources3
Helixi354 – 362Combined sources9
Turni363 – 366Combined sources4
Helixi370 – 377Combined sources8
Helixi379 – 384Combined sources6
Turni388 – 390Combined sources3
Beta strandi402 – 406Combined sources5
Helixi415 – 417Combined sources3
Beta strandi420 – 423Combined sources4
Turni426 – 429Combined sources4
Beta strandi435 – 441Combined sources7
Beta strandi444 – 448Combined sources5
Helixi469 – 478Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4B90X-ray2.20A/B1-564[»]
4B91X-ray1.70A/B1-483[»]
4B92X-ray2.90A/B1-483[»]
ProteinModelPortaliQ9BPU6.
SMRiQ9BPU6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2584. Eukaryota.
COG0044. LUCA.
GeneTreeiENSGT00760000119241.
HOGENOMiHOG000219145.
HOVERGENiHBG000806.
InParanoidiQ9BPU6.
KOiK07529.
OMAiCRGLADP.
OrthoDBiEOG091G05F3.
PhylomeDBiQ9BPU6.
TreeFamiTF314706.

Family and domain databases

CDDicd01314. D-HYD. 1 hit.
Gene3Di2.30.40.10. 2 hits.
InterProiIPR006680. Amidohydro-rel.
IPR030626. DRP5.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
[Graphical view]
PANTHERiPTHR11647:SF58. PTHR11647:SF58. 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.

Q9BPU6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLANSASVRI LIKGGKVVND DCTHEADVYI ENGIIQQVGR ELMIPGGAKV
60 70 80 90 100
IDATGKLVIP GGIDTSTHFH QTFMNATCVD DFYHGTKAAL VGGTTMIIGH
110 120 130 140 150
VLPDKETSLV DAYEKCRGLA DPKVCCDYAL HVGITWWAPK VKAEMETLVR
160 170 180 190 200
EKGVNSFQMF MTYKDLYMLR DSELYQVLHA CKDIGAIARV HAENGELVAE
210 220 230 240 250
GAKEALDLGI TGPEGIEISR PEELEAEATH RVITIANRTH CPIYLVNVSS
260 270 280 290 300
ISAGDVIAAA KMQGKVVLAE TTTAHATLTG LHYYHQDWSH AAAYVTVPPL
310 320 330 340 350
RLDTNTSTYL MSLLANDTLN IVASDHRPFT TKQKAMGKED FTKIPHGVSG
360 370 380 390 400
VQDRMSVIWE RGVVGGKMDE NRFVAVTSSN AAKLLNLYPR KGRIIPGADA
410 420 430 440 450
DVVVWDPEAT KTISASTQVQ GGDFNLYENM RCHGVPLVTI SRGRVVYENG
460 470 480 490 500
VFMCAEGTGK FCPLRSFPDT VYKKLVQREK TLKVRGVDRT PYLGDVAVVV
510 520 530 540 550
HPGKKEMGTP LADTPTRPVT RHGGMRDLHE SSFSLSGSQI DDHVPKRASA
560
RILAPPGGRS SGIW
Length:564
Mass (Da):61,421
Last modified:June 1, 2001 - v1
Checksum:iFF9DD1D44C599928
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti380N → S in CAB95124 (PubMed:11034345).Curated1
Sequence conflicti382A → S in AAF80348 (PubMed:11220734).Curated1
Sequence conflicti399D → H in AAF80348 (PubMed:11220734).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF264015 mRNA. Translation: AAK16830.1.
AJ251275 mRNA. Translation: CAB95124.1.
AF157634 mRNA. Translation: AAF80348.1.
BT006871 mRNA. Translation: AAP35517.1.
BC002874 mRNA. Translation: AAH02874.1.
AL713706 mRNA. Translation: CAD28503.1.
CCDSiCCDS1730.1.
RefSeqiNP_001240652.1. NM_001253723.1.
NP_001240653.1. NM_001253724.1.
NP_064519.2. NM_020134.3.
UniGeneiHs.299315.

Genome annotation databases

EnsembliENST00000288699; ENSP00000288699; ENSG00000157851.
ENST00000401478; ENSP00000385549; ENSG00000157851.
ENST00000614712; ENSP00000481305; ENSG00000157851.
GeneIDi56896.
KEGGihsa:56896.
UCSCiuc002rhu.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF264015 mRNA. Translation: AAK16830.1.
AJ251275 mRNA. Translation: CAB95124.1.
AF157634 mRNA. Translation: AAF80348.1.
BT006871 mRNA. Translation: AAP35517.1.
BC002874 mRNA. Translation: AAH02874.1.
AL713706 mRNA. Translation: CAD28503.1.
CCDSiCCDS1730.1.
RefSeqiNP_001240652.1. NM_001253723.1.
NP_001240653.1. NM_001253724.1.
NP_064519.2. NM_020134.3.
UniGeneiHs.299315.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4B90X-ray2.20A/B1-564[»]
4B91X-ray1.70A/B1-483[»]
4B92X-ray2.90A/B1-483[»]
ProteinModelPortaliQ9BPU6.
SMRiQ9BPU6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121226. 22 interactors.
IntActiQ9BPU6. 5 interactors.
MINTiMINT-1401135.
STRINGi9606.ENSP00000288699.

Protein family/group databases

MEROPSiM38.978.

PTM databases

iPTMnetiQ9BPU6.
PhosphoSitePlusiQ9BPU6.

Polymorphism and mutation databases

BioMutaiDPYSL5.
DMDMi20137929.

2D gel databases

UCD-2DPAGEQ9BPU6.

Proteomic databases

EPDiQ9BPU6.
MaxQBiQ9BPU6.
PaxDbiQ9BPU6.
PeptideAtlasiQ9BPU6.
PRIDEiQ9BPU6.

Protocols and materials databases

DNASUi56896.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000288699; ENSP00000288699; ENSG00000157851.
ENST00000401478; ENSP00000385549; ENSG00000157851.
ENST00000614712; ENSP00000481305; ENSG00000157851.
GeneIDi56896.
KEGGihsa:56896.
UCSCiuc002rhu.4. human.

Organism-specific databases

CTDi56896.
DisGeNETi56896.
GeneCardsiDPYSL5.
HGNCiHGNC:20637. DPYSL5.
HPAiHPA034544.
MIMi608383. gene.
neXtProtiNX_Q9BPU6.
OpenTargetsiENSG00000157851.
PharmGKBiPA134927413.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2584. Eukaryota.
COG0044. LUCA.
GeneTreeiENSGT00760000119241.
HOGENOMiHOG000219145.
HOVERGENiHBG000806.
InParanoidiQ9BPU6.
KOiK07529.
OMAiCRGLADP.
OrthoDBiEOG091G05F3.
PhylomeDBiQ9BPU6.
TreeFamiTF314706.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000157851-MONOMER.
ReactomeiR-HSA-399956. CRMPs in Sema3A signaling.

Miscellaneous databases

ChiTaRSiDPYSL5. human.
GeneWikiiDPYSL5.
GenomeRNAii56896.
PROiQ9BPU6.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000157851.
CleanExiHS_DPYSL5.
ExpressionAtlasiQ9BPU6. baseline and differential.
GenevisibleiQ9BPU6. HS.

Family and domain databases

CDDicd01314. D-HYD. 1 hit.
Gene3Di2.30.40.10. 2 hits.
InterProiIPR006680. Amidohydro-rel.
IPR030626. DRP5.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
[Graphical view]
PANTHERiPTHR11647:SF58. PTHR11647:SF58. 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 nameiDPYL5_HUMAN
AccessioniPrimary (citable) accession number: Q9BPU6
Secondary accession number(s): Q8TCL6, Q9NQC4, Q9NRY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: June 1, 2001
Last modified: November 30, 2016
This is version 144 of the entry and version 1 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

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

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.