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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

  1. hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides Source: InterPro

GO - Biological processi

  1. axon guidance Source: Reactome
  2. nervous system development Source: ProtInc
  3. pyrimidine nucleobase catabolic process Source: InterPro
  4. signal transduction Source: ProtInc
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_19199. 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
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:20637. DPYSL5.

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. dendrite Source: Ensembl
  3. neuronal cell body Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134927413.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 564564Dihydropyrimidinase-related protein 5PRO_0000165924Add
BLAST

Proteomic databases

MaxQBiQ9BPU6.
PaxDbiQ9BPU6.
PRIDEiQ9BPU6.

2D gel databases

UCD-2DPAGEQ9BPU6.

PTM databases

PhosphoSiteiQ9BPU6.

Expressioni

Gene expression databases

BgeeiQ9BPU6.
CleanExiHS_DPYSL5.
ExpressionAtlasiQ9BPU6. baseline and differential.
GenevestigatoriQ9BPU6.

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

Protein-protein interaction databases

BioGridi121226. 13 interactions.
IntActiQ9BPU6. 3 interactions.
MINTiMINT-1401135.
STRINGi9606.ENSP00000288699.

Structurei

Secondary structure

1
564
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 146Combined sources
Beta strandi16 – 183Combined sources
Beta strandi23 – 253Combined sources
Beta strandi27 – 315Combined sources
Beta strandi34 – 418Combined sources
Beta strandi49 – 524Combined sources
Beta strandi57 – 604Combined sources
Beta strandi62 – 676Combined sources
Helixi82 – 9110Combined sources
Beta strandi94 – 1018Combined sources
Helixi109 – 12012Combined sources
Turni121 – 1233Combined sources
Beta strandi125 – 1339Combined sources
Helixi139 – 15113Combined sources
Beta strandi156 – 1616Combined sources
Turni164 – 1663Combined sources
Helixi171 – 18313Combined sources
Beta strandi187 – 1915Combined sources
Helixi195 – 20713Combined sources
Helixi215 – 2184Combined sources
Helixi223 – 23917Combined sources
Beta strandi243 – 2453Combined sources
Helixi251 – 26212Combined sources
Beta strandi267 – 2726Combined sources
Helixi273 – 2775Combined sources
Helixi280 – 2845Combined sources
Helixi288 – 2925Combined sources
Helixi306 – 31510Combined sources
Beta strandi321 – 3233Combined sources
Helixi331 – 3344Combined sources
Helixi335 – 3373Combined sources
Helixi341 – 3433Combined sources
Turni351 – 3533Combined sources
Helixi354 – 3629Combined sources
Turni363 – 3664Combined sources
Helixi370 – 3778Combined sources
Helixi379 – 3846Combined sources
Turni388 – 3903Combined sources
Beta strandi402 – 4065Combined sources
Helixi415 – 4173Combined sources
Beta strandi420 – 4234Combined sources
Turni426 – 4294Combined sources
Beta strandi435 – 4417Combined sources
Beta strandi444 – 4485Combined sources
Helixi469 – 47810Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B90X-ray2.20A/B1-564[»]
4B91X-ray1.70A/B1-483[»]
4B92X-ray2.90A/B1-483[»]
ProteinModelPortaliQ9BPU6.
SMRiQ9BPU6. Positions 8-492.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0044.
GeneTreeiENSGT00760000119241.
HOGENOMiHOG000219145.
HOVERGENiHBG000806.
InParanoidiQ9BPU6.
KOiK07529.
OMAiDHAPHHL.
OrthoDBiEOG7SJD48.
PhylomeDBiQ9BPU6.
TreeFamiTF314706.

Family and domain databases

Gene3Di2.30.40.10. 2 hits.
InterProiIPR006680. Amidohydro_1.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti380 – 3801N → S in CAB95124. (PubMed:11034345)Curated
Sequence conflicti382 – 3821A → S in AAF80348. (PubMed:11220734)Curated
Sequence conflicti399 – 3991D → H in AAF80348. (PubMed:11220734)Curated

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.

Polymorphism databases

DMDMi20137929.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
4B90X-ray2.20A/B1-564[»]
4B91X-ray1.70A/B1-483[»]
4B92X-ray2.90A/B1-483[»]
ProteinModelPortaliQ9BPU6.
SMRiQ9BPU6. Positions 8-492.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121226. 13 interactions.
IntActiQ9BPU6. 3 interactions.
MINTiMINT-1401135.
STRINGi9606.ENSP00000288699.

Protein family/group databases

MEROPSiM38.978.

PTM databases

PhosphoSiteiQ9BPU6.

Polymorphism databases

DMDMi20137929.

2D gel databases

UCD-2DPAGEQ9BPU6.

Proteomic databases

MaxQBiQ9BPU6.
PaxDbiQ9BPU6.
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.
GeneCardsiGC02P027070.
HGNCiHGNC:20637. DPYSL5.
HPAiHPA034544.
MIMi608383. gene.
neXtProtiNX_Q9BPU6.
PharmGKBiPA134927413.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0044.
GeneTreeiENSGT00760000119241.
HOGENOMiHOG000219145.
HOVERGENiHBG000806.
InParanoidiQ9BPU6.
KOiK07529.
OMAiDHAPHHL.
OrthoDBiEOG7SJD48.
PhylomeDBiQ9BPU6.
TreeFamiTF314706.

Enzyme and pathway databases

ReactomeiREACT_19199. CRMPs in Sema3A signaling.

Miscellaneous databases

ChiTaRSiDPYSL5. human.
GeneWikiiDPYSL5.
GenomeRNAii56896.
NextBioi62329.
PROiQ9BPU6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BPU6.
CleanExiHS_DPYSL5.
ExpressionAtlasiQ9BPU6. baseline and differential.
GenevestigatoriQ9BPU6.

Family and domain databases

Gene3Di2.30.40.10. 2 hits.
InterProiIPR006680. Amidohydro_1.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
TIGRFAMsiTIGR02033. D-hydantoinase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Ulip6, a new human Unc-33-like phosphoprotein."
    Aguera M., Antoine J.-C., Belin M.-F., Charrier E., Honnorat J., Rogemond V.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Spinal cord.
  2. "Ulip6, a novel unc-33 and dihydropyrimidinase related protein highly expressed in developing rat brain."
    Horiuchi M., El Far O., Betz H.
    FEBS Lett. 480:283-286(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Spinal cord.
  3. "CRMP-5 neuronal autoantibody: marker of lung cancer and thymoma-related autoimmunity."
    Yu Z., Kryzer T.J., Griesmann G.E., Kim K., Benarroch E.E., Lennon V.A.
    Ann. Neurol. 49:146-154(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "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: Lung.
  6. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 17-40; 204-231; 239-261; 373-383; 394-431; 490-504 AND 527-546, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-564.
    Tissue: Amygdala.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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: February 4, 2015
This is version 128 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

External Data

Dasty 3

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 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.