Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q16555

- DPYL2_HUMAN

UniProt

Q16555 - DPYL2_HUMAN

Protein

Dihydropyrimidinase-related protein 2

Gene

DPYSL2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Plays a role in neuronal development and polarity, as well as in axon growth and guidance, neuronal growth cone collapse and cell migration. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. May play a role in endocytosis.3 Publications

    GO - Molecular functioni

    1. dihydropyrimidinase activity Source: ProtInc
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. cytoskeleton organization Source: UniProtKB
    3. endocytosis Source: UniProtKB
    4. nervous system development Source: ProtInc
    5. nucleobase-containing compound metabolic process Source: ProtInc
    6. olfactory bulb development Source: Ensembl
    7. positive regulation of glutamate secretion Source: Ensembl
    8. pyrimidine nucleobase catabolic process Source: InterPro
    9. regulation of neuron differentiation Source: Ensembl
    10. response to amphetamine Source: Ensembl
    11. response to cocaine Source: Ensembl
    12. response to drug Source: Ensembl
    13. signal transduction Source: ProtInc
    14. spinal cord development Source: Ensembl
    15. synaptic vesicle transport Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Differentiation, Neurogenesis

    Enzyme and pathway databases

    ReactomeiREACT_19199. CRMPs in Sema3A signaling.
    REACT_22365. Recycling pathway of L1.

    Protein family/group databases

    MEROPSiM38.975.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydropyrimidinase-related protein 2
    Short name:
    DRP-2
    Alternative name(s):
    Collapsin response mediator protein 2
    Short name:
    CRMP-2
    N2A3
    Unc-33-like phosphoprotein 2
    Short name:
    ULIP-2
    Gene namesi
    Name:DPYSL2
    Synonyms:CRMP2, ULIP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:3014. DPYSL2.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication. Cytoplasmcytoskeleton 1 Publication. Membrane 1 Publication
    Note: Tightly but non-covalently associated with membranes.

    GO - Cellular componenti

    1. axon Source: Ensembl
    2. cytoskeleton Source: UniProtKB-SubCell
    3. cytosol Source: UniProtKB
    4. dendrite Source: Ensembl
    5. extracellular vesicular exosome Source: UniProt
    6. growth cone Source: Ensembl
    7. membrane Source: UniProtKB-SubCell
    8. mitochondrion Source: Ensembl
    9. neuronal cell body Source: Ensembl
    10. protein complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi71 – 711D → N: Inhibits axon outgrowth formation in hippocampal neurons and decreases binding to CYFIP1. 1 Publication
    Mutagenesisi507 – 5071S → A: No effect. 1 Publication
    Mutagenesisi509 – 5091T → A: Greatly diminishes binding to 3F4 antibody. 1 Publication
    Mutagenesisi512 – 5121T → A: No effect. 1 Publication
    Mutagenesisi514 – 5141T → A: No effect. 1 Publication
    Mutagenesisi517 – 5171S → A: No effect. 1 Publication
    Mutagenesisi518 – 5181S → A: Greatly diminishes binding to 3F4 antibody. 1 Publication
    Mutagenesisi521 – 5211T → A: No effect. 1 Publication
    Mutagenesisi522 – 5221S → A: Greatly diminishes binding to 3F4 antibody. 1 Publication

    Organism-specific databases

    PharmGKBiPA27472.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 572572Dihydropyrimidinase-related protein 2PRO_0000165913Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei32 – 321Phosphotyrosine; by FYN1 Publication
    Modified residuei258 – 2581N6-succinyllysineBy similarity
    Modified residuei431 – 4311PhosphotyrosineBy similarity
    Modified residuei465 – 4651PhosphoserineBy similarity
    Modified residuei499 – 4991PhosphotyrosineBy similarity
    Modified residuei504 – 5041S-nitrosocysteineBy similarity
    Modified residuei509 – 5091Phosphothreonine4 Publications
    Modified residuei514 – 5141Phosphothreonine; by GSK3-beta1 Publication
    Modified residuei517 – 5171Phosphoserine1 Publication
    Modified residuei518 – 5181Phosphoserine2 Publications
    Modified residuei522 – 5221Phosphoserine; by DYRK24 Publications
    Modified residuei555 – 5551Phosphothreonine; by ROCK2By similarity

    Post-translational modificationi

    3F4, a monoclonal antibody which strongly stains neurofibrillary tangles in Alzheimer disease brains, specifically labels DPYSL2 when phosphorylated on Ser-518, Ser-522 and Thr-509.5 Publications
    Phosphorylation at Thr-514 by GSK3B abolishes tubulin-binding leading to destabilization of microtubule assembly in axons and neurodegeneration By similarity. Phosphorylation by DYRK2 at Ser-522 is required for subsequent phosphorylation by GSK3B.By similarity4 Publications

    Keywords - PTMi

    Phosphoprotein, S-nitrosylation

    Proteomic databases

    MaxQBiQ16555.
    PaxDbiQ16555.
    PeptideAtlasiQ16555.
    PRIDEiQ16555.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00257508.
    Q16555.
    UCD-2DPAGEQ16555.

    PTM databases

    PhosphoSiteiQ16555.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ16555.
    BgeeiQ16555.
    CleanExiHS_DPYSL2.
    GenevestigatoriQ16555.

    Organism-specific databases

    HPAiCAB018719.
    HPA002381.

    Interactioni

    Subunit structurei

    Homotetramer, and heterotetramer with CRMP1, DPYSL3, DPYSL4 or DPYSL5. Interacts through its C-terminus with the C-terminus of CYFIP1/SRA1. Interacts with HTR4. Interacts with CLN6. Interacts with MICALL1.5 Publications

    Protein-protein interaction databases

    BioGridi108142. 25 interactions.
    IntActiQ16555. 14 interactions.
    MINTiMINT-3032752.
    STRINGi9606.ENSP00000309539.

    Structurei

    Secondary structure

    1
    572
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi17 – 259
    Beta strandi30 – 389
    Beta strandi41 – 488
    Beta strandi53 – 553
    Beta strandi57 – 593
    Beta strandi64 – 674
    Beta strandi69 – 746
    Helixi89 – 9810
    Beta strandi101 – 1088
    Helixi116 – 13015
    Beta strandi132 – 1409
    Helixi146 – 15813
    Beta strandi163 – 1708
    Turni171 – 1733
    Helixi178 – 19114
    Beta strandi194 – 1985
    Helixi202 – 21312
    Turni214 – 2163
    Helixi221 – 2266
    Helixi229 – 24618
    Beta strandi250 – 2556
    Helixi258 – 26912
    Beta strandi274 – 2796
    Helixi280 – 2845
    Helixi287 – 2915
    Helixi295 – 3006
    Helixi313 – 32210
    Helixi338 – 3414
    Helixi342 – 3443
    Helixi348 – 3503
    Turni358 – 3603
    Helixi361 – 3699
    Turni370 – 3734
    Helixi377 – 3848
    Helixi386 – 3927
    Turni395 – 3973
    Beta strandi409 – 41911
    Turni422 – 4243
    Beta strandi425 – 4284
    Turni433 – 4364
    Beta strandi438 – 44811
    Beta strandi451 – 4555
    Helixi476 – 48712

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GSEX-ray2.40A/B/C/D13-490[»]
    2VM8X-ray1.90A/B/C/D13-490[»]
    ProteinModelPortaliQ16555.
    SMRiQ16555. Positions 14-490.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16555.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0044.
    HOVERGENiHBG000806.
    InParanoidiQ16555.
    KOiK07528.
    OMAiEVPAFFK.
    OrthoDBiEOG7SJD48.
    PhylomeDBiQ16555.
    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.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q16555-1) [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

    MSYQGKKNIP RITSDRLLIK GGKIVNDDQS FYADIYMEDG LIKQIGENLI    50
    VPGGVKTIEA HSRMVIPGGI DVHTRFQMPD QGMTSADDFF QGTKAALAGG 100
    TTMIIDHVVP EPGTSLLAAF DQWREWADSK SCCDYSLHVD ISEWHKGIQE 150
    EMEALVKDHG VNSFLVYMAF KDRFQLTDCQ IYEVLSVIRD IGAIAQVHAE 200
    NGDIIAEEQQ RILDLGITGP EGHVLSRPEE VEAEAVNRAI TIANQTNCPL 250
    YITKVMSKSS AEVIAQARKK GTVVYGEPIT ASLGTDGSHY WSKNWAKAAA 300
    FVTSPPLSPD PTTPDFLNSL LSCGDLQVTG SAHCTFNTAQ KAVGKDNFTL 350
    IPEGTNGTEE RMSVIWDKAV VTGKMDENQF VAVTSTNAAK VFNLYPRKGR 400
    IAVGSDADLV IWDPDSVKTI SAKTHNSSLE YNIFEGMECR GSPLVVISQG 450
    KIVLEDGTLH VTEGSGRYIP RKPFPDFVYK RIKARSRLAE LRGVPRGLYD 500
    GPVCEVSVTP KTVTPASSAK TSPAKQQAPP VRNLHQSGFS LSGAQIDDNI 550
    PRRTTQRIVA PPGGRANITS LG 572
    Length:572
    Mass (Da):62,294
    Last modified:November 1, 1996 - v1
    Checksum:i5CDB6CF7F5C308AD
    GO
    Isoform 2 (identifier: Q16555-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-36: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:536
    Mass (Da):58,163
    Checksum:i31806BFCB5FAE16D
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti118 – 1181A → T.
    Corresponds to variant rs2289593 [ dbSNP | Ensembl ].
    VAR_022016
    Natural varianti481 – 4811R → C in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036316

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3636Missing in isoform 2. 1 PublicationVSP_044941Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U17279 mRNA. Translation: AAA93202.1.
    D78013 mRNA. Translation: BAA11191.1.
    U97105 mRNA. Translation: AAC05793.1.
    AB020777 Genomic DNA. Translation: BAA86991.1.
    AK291287 mRNA. Translation: BAF83976.1.
    AK299077 mRNA. Translation: BAG61143.1.
    AC015564 Genomic DNA. No translation available.
    AC015743 Genomic DNA. No translation available.
    CH471080 Genomic DNA. Translation: EAW63573.1.
    CH471080 Genomic DNA. Translation: EAW63574.1.
    BC056408 mRNA. Translation: AAH56408.1.
    BC067109 mRNA. Translation: AAH67109.1.
    CCDSiCCDS59096.1. [Q16555-2]
    CCDS6051.1. [Q16555-1]
    PIRiJC5317.
    RefSeqiNP_001184222.1. NM_001197293.2.
    NP_001231533.1. NM_001244604.1. [Q16555-2]
    NP_001377.1. NM_001386.5. [Q16555-1]
    UniGeneiHs.593187.

    Genome annotation databases

    EnsembliENST00000311151; ENSP00000309539; ENSG00000092964. [Q16555-1]
    ENST00000521913; ENSP00000427985; ENSG00000092964. [Q16555-2]
    ENST00000523027; ENSP00000431117; ENSG00000092964. [Q16555-2]
    GeneIDi1808.
    KEGGihsa:1808.
    UCSCiuc003xfb.2. human. [Q16555-1]

    Polymorphism databases

    DMDMi3122051.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U17279 mRNA. Translation: AAA93202.1 .
    D78013 mRNA. Translation: BAA11191.1 .
    U97105 mRNA. Translation: AAC05793.1 .
    AB020777 Genomic DNA. Translation: BAA86991.1 .
    AK291287 mRNA. Translation: BAF83976.1 .
    AK299077 mRNA. Translation: BAG61143.1 .
    AC015564 Genomic DNA. No translation available.
    AC015743 Genomic DNA. No translation available.
    CH471080 Genomic DNA. Translation: EAW63573.1 .
    CH471080 Genomic DNA. Translation: EAW63574.1 .
    BC056408 mRNA. Translation: AAH56408.1 .
    BC067109 mRNA. Translation: AAH67109.1 .
    CCDSi CCDS59096.1. [Q16555-2 ]
    CCDS6051.1. [Q16555-1 ]
    PIRi JC5317.
    RefSeqi NP_001184222.1. NM_001197293.2.
    NP_001231533.1. NM_001244604.1. [Q16555-2 ]
    NP_001377.1. NM_001386.5. [Q16555-1 ]
    UniGenei Hs.593187.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2GSE X-ray 2.40 A/B/C/D 13-490 [» ]
    2VM8 X-ray 1.90 A/B/C/D 13-490 [» ]
    ProteinModelPortali Q16555.
    SMRi Q16555. Positions 14-490.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108142. 25 interactions.
    IntActi Q16555. 14 interactions.
    MINTi MINT-3032752.
    STRINGi 9606.ENSP00000309539.

    Protein family/group databases

    MEROPSi M38.975.

    PTM databases

    PhosphoSitei Q16555.

    Polymorphism databases

    DMDMi 3122051.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00257508.
    Q16555.
    UCD-2DPAGE Q16555.

    Proteomic databases

    MaxQBi Q16555.
    PaxDbi Q16555.
    PeptideAtlasi Q16555.
    PRIDEi Q16555.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000311151 ; ENSP00000309539 ; ENSG00000092964 . [Q16555-1 ]
    ENST00000521913 ; ENSP00000427985 ; ENSG00000092964 . [Q16555-2 ]
    ENST00000523027 ; ENSP00000431117 ; ENSG00000092964 . [Q16555-2 ]
    GeneIDi 1808.
    KEGGi hsa:1808.
    UCSCi uc003xfb.2. human. [Q16555-1 ]

    Organism-specific databases

    CTDi 1808.
    GeneCardsi GC08P026371.
    HGNCi HGNC:3014. DPYSL2.
    HPAi CAB018719.
    HPA002381.
    MIMi 602463. gene.
    neXtProti NX_Q16555.
    PharmGKBi PA27472.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0044.
    HOVERGENi HBG000806.
    InParanoidi Q16555.
    KOi K07528.
    OMAi EVPAFFK.
    OrthoDBi EOG7SJD48.
    PhylomeDBi Q16555.
    TreeFami TF314706.

    Enzyme and pathway databases

    Reactomei REACT_19199. CRMPs in Sema3A signaling.
    REACT_22365. Recycling pathway of L1.

    Miscellaneous databases

    ChiTaRSi DPYSL2. human.
    EvolutionaryTracei Q16555.
    GeneWikii DPYSL2.
    GenomeRNAii 1808.
    NextBioi 7369.
    PROi Q16555.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16555.
    Bgeei Q16555.
    CleanExi HS_DPYSL2.
    Genevestigatori Q16555.

    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. "Collapsin-induced growth cone collapse mediated by an intracellular protein related to UNC-33."
      Goshima Y., Nakamura F., Strittmatter P., Strittmatter S.M.
      Nature 376:509-514(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "A novel gene family defined by human dihydropyrimidinase and three related proteins with differential tissue distribution."
      Hamajima N., Matsuda K., Sakata S., Tamaki N., Sasaki M., Nonaka M.
      Gene 180:157-163(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. "A cDNA clone highly expressed in human brain and deleted in liver cancer."
      Zhou J., Chen Y., Gu J.R.
      Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal liver.
    4. "Characterization of the human dihydropyrimidinase-related protein 2 (DRP-2) gene."
      Kitamura K., Takayama M., Hamajima N., Nakanishi M., Sasaki M., Endo Y., Takemoto T., Kimura H., Iwaki M., Nonaka M.
      DNA Res. 6:291-297(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    6. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORM 1).
      Tissue: Eye and Testis.
    9. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 44-56; 64-75; 147-157; 174-211; 239-254; 375-390; 401-418; 424-467; 497-511 AND 533-552, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    10. "Neurofibrillary tangle-associated collapsin response mediator protein-2 (CRMP-2) is highly phosphorylated on Thr-509, Ser-518, and Ser-522."
      Gu Y., Hamajima N., Ihara Y.
      Biochemistry 39:4267-4275(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-518; SER-522 AND THR-509, MUTAGENESIS OF SER-507; THR-509; THR-512; THR-514; SER-517; SER-518; THR-521 AND SER-522.
    11. Cited for: FUNCTION.
    12. "GSK-3 phosphorylation of the Alzheimer epitope within collapsin response mediator proteins regulates axon elongation in primary neurons."
      Cole A.R., Knebel A., Morrice N.A., Robertson L.A., Irving A.J., Connolly C.N., Sutherland C.
      J. Biol. Chem. 279:50176-50180(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-522.
    13. "CRMP-2 is involved in kinesin-1-dependent transport of the Sra-1/WAVE1 complex and axon formation."
      Kawano Y., Yoshimura T., Tsuboi D., Kawabata S., Kaneko-Kawano T., Shirataki H., Takenawa T., Kaibuchi K.
      Mol. Cell. Biol. 25:9920-9935(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CYFIP1, MUTAGENESIS OF ASP-71.
    14. "Structural bases for CRMP function in plexin-dependent semaphorin3A signaling."
      Deo R.C., Schmidt E.F., Elhabazi A., Togashi H., Burley S.K., Strittmatter S.M.
      EMBO J. 23:9-22(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PLEXNA1, SUBUNIT.
    15. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509 AND SER-522, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Semaphorin3A signaling mediated by Fyn-dependent tyrosine phosphorylation of collapsin response mediator protein 2 at tyrosine 32."
      Uchida Y., Ohshima T., Yamashita N., Ogawara M., Sasaki Y., Nakamura F., Goshima Y.
      J. Biol. Chem. 284:27393-27401(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-32 BY FYN.
    19. "Protein product of CLN6 gene responsible for variant late-onset infantile neuronal ceroid lipofuscinosis interacts with CRMP-2."
      Benedict J.W., Getty A.L., Wishart T.M., Gillingwater T.H., Pearce D.A.
      J. Neurosci. Res. 87:2157-2166(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CLN6.
    20. "Collapsin response mediator protein-2 (Crmp2) regulates trafficking by linking endocytic regulatory proteins to dynein motors."
      Rahajeng J., Giridharan S.S., Naslavsky N., Caplan S.
      J. Biol. Chem. 285:31918-31922(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ENDOCYTOSIS, INTERACTION WITH MICALL1, SUBCELLULAR LOCATION.
    21. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509; THR-514; SER-517; SER-518 AND SER-522, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "The structure of human collapsin response mediator protein 2, a regulator of axonal growth."
      Stenmark P., Ogg D., Flodin S., Flores A., Kotenyova T., Nyman T., Nordlund P., Kursula P.
      J. Neurochem. 101:906-917(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 12-490, SUBUNIT.
    25. Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-481.

    Entry informationi

    Entry nameiDPYL2_HUMAN
    AccessioniPrimary (citable) accession number: Q16555
    Secondary accession number(s): A8K5H2
    , B4DR31, D3DSS7, O00424
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 148 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

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 8
      Human chromosome 8: 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

    External Data

    Dasty 3