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Q9BPU6

- DPYL5_HUMAN

UniProt

Q9BPU6 - DPYL5_HUMAN

Protein

Dihydropyrimidinase-related protein 5

Gene

DPYSL5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    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

    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

    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

    ArrayExpressiQ9BPU6.
    BgeeiQ9BPU6.
    CleanExiHS_DPYSL5.
    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. 5 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 – 146
    Beta strandi16 – 183
    Beta strandi23 – 253
    Beta strandi27 – 315
    Beta strandi34 – 418
    Beta strandi49 – 524
    Beta strandi57 – 604
    Beta strandi62 – 676
    Helixi82 – 9110
    Beta strandi94 – 1018
    Helixi109 – 12012
    Turni121 – 1233
    Beta strandi125 – 1339
    Helixi139 – 15113
    Beta strandi156 – 1616
    Turni164 – 1663
    Helixi171 – 18313
    Beta strandi187 – 1915
    Helixi195 – 20713
    Helixi215 – 2184
    Helixi223 – 23917
    Beta strandi243 – 2453
    Helixi251 – 26212
    Beta strandi267 – 2726
    Helixi273 – 2775
    Helixi280 – 2845
    Helixi288 – 2925
    Helixi306 – 31510
    Beta strandi321 – 3233
    Helixi331 – 3344
    Helixi335 – 3373
    Helixi341 – 3433
    Turni351 – 3533
    Helixi354 – 3629
    Turni363 – 3664
    Helixi370 – 3778
    Helixi379 – 3846
    Turni388 – 3903
    Beta strandi402 – 4065
    Helixi415 – 4173
    Beta strandi420 – 4234
    Turni426 – 4294
    Beta strandi435 – 4417
    Beta strandi444 – 4485
    Helixi469 – 47810

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000219145.
    HOVERGENiHBG000806.
    InParanoidiQ9BPU6.
    KOiK07529.
    OMAiCRGLADP.
    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

    MLANSASVRI LIKGGKVVND DCTHEADVYI ENGIIQQVGR ELMIPGGAKV    50
    IDATGKLVIP GGIDTSTHFH QTFMNATCVD DFYHGTKAAL VGGTTMIIGH 100
    VLPDKETSLV DAYEKCRGLA DPKVCCDYAL HVGITWWAPK VKAEMETLVR 150
    EKGVNSFQMF MTYKDLYMLR DSELYQVLHA CKDIGAIARV HAENGELVAE 200
    GAKEALDLGI TGPEGIEISR PEELEAEATH RVITIANRTH CPIYLVNVSS 250
    ISAGDVIAAA KMQGKVVLAE TTTAHATLTG LHYYHQDWSH AAAYVTVPPL 300
    RLDTNTSTYL MSLLANDTLN IVASDHRPFT TKQKAMGKED FTKIPHGVSG 350
    VQDRMSVIWE RGVVGGKMDE NRFVAVTSSN AAKLLNLYPR KGRIIPGADA 400
    DVVVWDPEAT KTISASTQVQ GGDFNLYENM RCHGVPLVTI SRGRVVYENG 450
    VFMCAEGTGK FCPLRSFPDT VYKKLVQREK TLKVRGVDRT PYLGDVAVVV 500
    HPGKKEMGTP LADTPTRPVT RHGGMRDLHE SSFSLSGSQI DDHVPKRASA 550
    RILAPPGGRS SGIW 564
    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:
    EMBL
    GenBank
    DDBJ
    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.
    GeneIDi56896.
    KEGGihsa:56896.
    UCSCiuc002rhu.4. human.

    Polymorphism databases

    DMDMi20137929.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS1730.1.
    RefSeqi NP_001240652.1. NM_001253723.1.
    NP_001240653.1. NM_001253724.1.
    NP_064519.2. NM_020134.3.
    UniGenei Hs.299315.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4B90 X-ray 2.20 A/B 1-564 [» ]
    4B91 X-ray 1.70 A/B 1-483 [» ]
    4B92 X-ray 2.90 A/B 1-483 [» ]
    ProteinModelPortali Q9BPU6.
    SMRi Q9BPU6. Positions 8-492.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121226. 5 interactions.
    IntActi Q9BPU6. 3 interactions.
    MINTi MINT-1401135.
    STRINGi 9606.ENSP00000288699.

    Protein family/group databases

    MEROPSi M38.978.

    PTM databases

    PhosphoSitei Q9BPU6.

    Polymorphism databases

    DMDMi 20137929.

    2D gel databases

    UCD-2DPAGE Q9BPU6.

    Proteomic databases

    MaxQBi Q9BPU6.
    PaxDbi Q9BPU6.
    PRIDEi Q9BPU6.

    Protocols and materials databases

    DNASUi 56896.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000288699 ; ENSP00000288699 ; ENSG00000157851 .
    ENST00000401478 ; ENSP00000385549 ; ENSG00000157851 .
    GeneIDi 56896.
    KEGGi hsa:56896.
    UCSCi uc002rhu.4. human.

    Organism-specific databases

    CTDi 56896.
    GeneCardsi GC02P027070.
    HGNCi HGNC:20637. DPYSL5.
    HPAi HPA034544.
    MIMi 608383. gene.
    neXtProti NX_Q9BPU6.
    PharmGKBi PA134927413.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0044.
    HOGENOMi HOG000219145.
    HOVERGENi HBG000806.
    InParanoidi Q9BPU6.
    KOi K07529.
    OMAi CRGLADP.
    OrthoDBi EOG7SJD48.
    PhylomeDBi Q9BPU6.
    TreeFami TF314706.

    Enzyme and pathway databases

    Reactomei REACT_19199. CRMPs in Sema3A signaling.

    Miscellaneous databases

    ChiTaRSi DPYSL5. human.
    GeneWikii DPYSL5.
    GenomeRNAii 56896.
    NextBioi 62329.
    PROi Q9BPU6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BPU6.
    Bgeei Q9BPU6.
    CleanExi HS_DPYSL5.
    Genevestigatori Q9BPU6.

    Family and domain databases

    Gene3Di 2.30.40.10. 2 hits.
    InterProi IPR006680. Amidohydro_1.
    IPR011778. Hydantoinase/dihydroPyrase.
    IPR011059. Metal-dep_hydrolase_composite.
    [Graphical view ]
    Pfami PF01979. Amidohydro_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51338. SSF51338. 2 hits.
    TIGRFAMsi TIGR02033. D-hydantoinase. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 124 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