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UniProtKB/Swiss-Prot entry Q16555


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DPYL2_HUMAN
Primary accession number Q16555
Secondary accession number O00424
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 90)
Name and origin of the protein
Protein name Dihydropyrimidinase-related protein 2
Synonyms DRP-2
Collapsin response mediator protein 2
CRMP-2
N2A3
Gene name
Name: DPYSL2
Synonyms: CRMP2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1038/376509a0; PubMed=7637782 [NCBI, ExPASy, EBI, Israel, Japan]
Goshima Y., Nakamura F., Strittmatter P., Strittmatter S.M.;
"Collapsin-induced growth cone collapse mediated by an intracellular protein related to UNC-33.";
Nature 376:509-514(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
DOI=10.1016/S0378-1119(96)00445-3; PubMed=8973361 [NCBI, ExPASy, EBI, Israel, Japan]
Hamajima N., Matsuda K., Sakata S., Tamaki N., Sasaki M., Nonaka M.;
"A novel gene family defined by human dihydropyrimidinase and three related proteins with differential tissue distribution.";
Gene 180:157-163(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fetal liver;
Zhou J., Chen Y., Gu J.R.;
"A cDNA clone highly expressed in human brain and deleted in liver cancer.";
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1093/dnares/6.5.291; PubMed=10574455 [NCBI, ExPASy, EBI, Israel, Japan]
Kitamura K., Takayama M., Hamajima N., Nakanishi M., Sasaki M., Endo Y., Takemoto T., Kimura H., Iwaki M., Nonaka M.;
"Characterization of the human dihydropyrimidinase-related protein 2 (DRP-2) gene.";
DNA Res. 6:291-297(1999).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye, and Testis;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 44-56; 64-75; 147-157; 174-211; 239-254; 375-390; 401-418; 424-467; 497-511 AND 533-552, AND MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[7]
PHOSPHORYLATION AT SER-518; SER-522 AND THR-509, AND MUTAGENESIS OF SER-507; THR-509; THR-512; THR-514; SER-517; SER-518; THR-521 AND SER-522.
DOI=10.1021/bi992323h; PubMed=10757975 [NCBI, ExPASy, EBI, Israel, Japan]
Gu Y., Hamajima N., Ihara Y.;
"Neurofibrillary tangle-associated collapsin response mediator protein-2 (CRMP-2) is highly phosphorylated on Thr-509, Ser-518, and Ser-522.";
Biochemistry 39:4267-4275(2000).
[8]
FUNCTION.
DOI=10.1038/90476; PubMed=11477421 [NCBI, ExPASy, EBI, Israel, Japan]
Inagaki N., Chihara K., Arimura N., Menager C., Kawano Y., Matsuo N., Nishimura T., Amano M., Kaibuchi K.;
"CRMP-2 induces axons in cultured hippocampal neurons.";
Nat. Neurosci. 4:781-782(2001).
[9]
INTERACTION WITH CYFIP1, AND MUTAGENESIS OF ASP-71.
DOI=10.1128/MCB.25.22.9920-9935.2005; PubMed=16260607 [NCBI, ExPASy, EBI, Israel, Japan]
Kawano Y., Yoshimura T., Tsuboi D., Kawabata S., Kaneko-Kawano T., Shirataki H., Takenawa T., Kaibuchi K.;
"CRMP-2 is involved in kinesin-1-dependent transport of the Sra-1/WAVE1 complex and axon formation.";
Mol. Cell. Biol. 25:9920-9935(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[11]
INTERACTION WITH PLEXNA1, AND SUBUNIT.
DOI=10.1038/sj.emboj.7600021; PubMed=14685275 [NCBI, ExPASy, EBI, Israel, Japan]
Deo R.C., Schmidt E.F., Elhabazi A., Togashi H., Burley S.K., Strittmatter S.M.;
"Structural bases for CRMP function in plexin-dependent semaphorin3A signaling.";
EMBO J. 23:9-22(2004).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[14]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 12-490, AND SUBUNIT.
DOI=10.1111/j.1471-4159.2006.04401.x; PubMed=17250651 [NCBI, ExPASy, EBI, Israel, Japan]
Stenmark P., Ogg D., Flodin S., Flores A., Kotenyova T., Nyman T., Nordlund P., Kursula P.;
"The structure of human collapsin response mediator protein 2, a regulator of axonal growth.";
J. Neurochem. 101:906-917(2007).
[15]
VARIANT [LARGE SCALE ANALYSIS] CYS-481.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U17279; AAA93202.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D78013; BAA11191.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U97105; AAC05793.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB020777; BAA86991.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC056408; AAH56408.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC067109; AAH67109.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00257508; -.
PIR JC5317; JC5317.
RefSeq NP_001377.1; -.
UniGene Hs.173381
3D structure databases
PDB
2GSE; X-ray; 2.40 A; A/B/C/D=13-490.[ExPASy / RCSB / EBI]
2VM8; X-ray; 1.90 A; A/B/C/D=13-490.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2GSE; -.
2VM8; -.
ModBase Q16555.
Protein-protein interaction databases
IntAct Q16555; 1.
Protein family/group databases
MEROPS M38.975; -.
PTM databases
PhosphoSite Q16555; -.
2D gel databases
REPRODUCTION-2DPAGE IPI00257508; -.
Q16555; -.
Organism-specific databases
GeneCards GC08P026491; -.
H-InvDB HIX0007403; -.
HGNC HGNC:3014; DPYSL2.
GenAtlas DPYSL2.
HPA HPA002381; -.
MIM 602463; gene. [NCBI / EBI]
PharmGKB PA27472; -.
Gene expression databases
ArrayExpress Q16555; -.
Bgee Q16555; -.
CleanEx HS_DPYSL2; -.
GermOnline ENSG00000092964; Homo sapiens.
Ontologies
GO
GO:0005856; Cellular component: cytoskeleton (inferred from direct assay from HPA).
GO:0004157; Molecular function: dihydropyrimidinase activity (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0030154; Biological process: cell differentiation (inferred from electronic annotation from UniProtKB-KW).
GO:0007399; Biological process: nervous system development (traceable author statement from ProtInc).
GO:0006139; Biological process: nucleobase, nucleoside, nucleotide and nucleic acid metabolic process (traceable author statement from ProtInc).
GO:0007165; Biological process: signal transduction (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR006680; Amidohydro_1.
IPR011778; D-hydantoinase.
Graphical view of domain structure.
Pfam PF01979; Amidohydro_1; 1.
Pfam graphical view of domain structure.
ProDom PD000518; DHOase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR02033; D-hydantoinase; 1.
Proteomic databases
PeptideAtlas Q16555; -.
PRIDE Q16555; -.
Genome annotation databases
Ensembl ENSG00000092964; Homo sapiens. [Contig view]
GeneID 1808; -.
KEGG hsa:1808; -.
NMPDR fig|9606.3.peg.30095; -.
Phylogenomic databases
HOVERGEN Q16555; -.
OMA Q16555; AQARKKX.
Other
NextBio 7369; -.
SOURCE DPYSL2; Homo sapiens.
ProtoNet Q16555.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Developmental protein; Differentiation; Direct protein sequencing; Neurogenesis; Phosphoprotein; Polymorphism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   572  572     Dihydropyrimidinase-related protein 2. PRO_0000165913
MOD_RES   32    32        Phosphotyrosine (By similarity). 
MOD_RES   431   431        Phosphotyrosine (By similarity). 
MOD_RES   462   462        Phosphothreonine (By similarity). 
MOD_RES   465   465        Phosphoserine (By similarity). 
MOD_RES   499   499        Phosphotyrosine (By similarity). 
MOD_RES   509   509        Phosphothreonine. 
MOD_RES   514   514        Phosphothreonine; in vitro. 
MOD_RES   517   517        Phosphoserine (By similarity). 
MOD_RES   518   518        Phosphoserine. 
MOD_RES   522   522        Phosphoserine. 
VARIANT   118   118  1     A -> T (in dbSNP:rs2289593 [NCBI]). VAR_022016 [3D]
VARIANT   481   481  1     R -> C (in a colorectal cancer sample; somatic mutation). VAR_036316 [3D]
MUTAGEN   71    71        D->N: Inhibits axon outgrowth formation in hippocampal neurons and decreases binding to CYFIP1. 
MUTAGEN   507   507        S->A: No effect. 
MUTAGEN   509   509        T->A: Greatly diminishes binding to 3F4 antibody. 
MUTAGEN   512   512        T->A: No effect. 
MUTAGEN   514   514        T->A: No effect. 
MUTAGEN   517   517        S->A: No effect. 
MUTAGEN   518   518        S->A: Greatly diminishes binding to 3F4 antibody. 
MUTAGEN   521   521        T->A: No effect. 
MUTAGEN   522   522        S->A: Greatly diminishes binding to 3F4 antibody. 
STRAND   17    25  9      
STRAND   30    38  9      
STRAND   41    48  8      
STRAND   56    59  4      
STRAND   64    67  4      
STRAND   69    74  6      
HELIX   89    98  10      
STRAND   101   108  8      
HELIX   116   130  15      
STRAND   132   142  11      
HELIX   148   158  11      
STRAND   163   168  6      
TURN   171   174  4      
HELIX   178   191  14      
STRAND   194   198  5      
HELIX   202   213  12      
TURN   214   216  3      
HELIX   221   226  6      
HELIX   229   246  18      
STRAND   250   255  6      
HELIX   258   268  11      
TURN   269   271  3      
STRAND   274   279  6      
HELIX   280   284  5      
HELIX   287   291  5      
HELIX   295   300  6      
HELIX   313   322  10      
HELIX   338   341  4      
HELIX   342   344  3      
HELIX   348   350  3      
TURN   358   360  3      
HELIX   361   369  9      
TURN   370   373  4      
HELIX   377   384  8      
HELIX   386   391  6      
TURN   395   397  3      
STRAND   409   419  11      
TURN   422   424  3      
STRAND   425   428  4      
TURN   433   436  4      
STRAND   438   448  11      
STRAND   451   455  5      
HELIX   476   486  11      
Sequence information
Length: 572 AA [This is the length of the unprocessed precursor] Molecular weight: 62294 Da [This is the MW of the unprocessed precursor] CRC64: 5CDB6CF7F5C308AD [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSYQGKKNIP RITSDRLLIK GGKIVNDDQS FYADIYMEDG LIKQIGENLI VPGGVKTIEA 

        70         80         90        100        110        120 
HSRMVIPGGI DVHTRFQMPD QGMTSADDFF QGTKAALAGG TTMIIDHVVP EPGTSLLAAF 

       130        140        150        160        170        180 
DQWREWADSK SCCDYSLHVD ISEWHKGIQE EMEALVKDHG VNSFLVYMAF KDRFQLTDCQ 

       190        200        210        220        230        240 
IYEVLSVIRD IGAIAQVHAE NGDIIAEEQQ RILDLGITGP EGHVLSRPEE VEAEAVNRAI 

       250        260        270        280        290        300 
TIANQTNCPL YITKVMSKSS AEVIAQARKK GTVVYGEPIT ASLGTDGSHY WSKNWAKAAA 

       310        320        330        340        350        360 
FVTSPPLSPD PTTPDFLNSL LSCGDLQVTG SAHCTFNTAQ KAVGKDNFTL IPEGTNGTEE 

       370        380        390        400        410        420 
RMSVIWDKAV VTGKMDENQF VAVTSTNAAK VFNLYPRKGR IAVGSDADLV IWDPDSVKTI 

       430        440        450        460        470        480 
SAKTHNSSLE YNIFEGMECR GSPLVVISQG KIVLEDGTLH VTEGSGRYIP RKPFPDFVYK 

       490        500        510        520        530        540 
RIKARSRLAE LRGVPRGLYD GPVCEVSVTP KTVTPASSAK TSPAKQQAPP VRNLHQSGFS 

       550        560        570 
LSGAQIDDNI PRRTTQRIVA PPGGRANITS LG 

Q16555 in FASTA format

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