Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q16555 (DPYL2_HUMAN)

Last modified November 3, 2009. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Dihydropyrimidinase-related protein 2
      Short name=DRP-2
Alternative name(s):
    Collapsin response mediator protein 2
      Short name=CRMP-2
    N2A3
Gene names
Name: DPYSL2
Synonyms: CRMP2
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length572 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, neuronal growth cone collapse and cell migration By similarity.

Subunit structure

Homotetramer, and heterotetramer with CRMP1, DPYSL3, DPYSL4 or DPYSL5 By similarity. Interacts through its C-terminus with the C-terminus of CYFIP1/SRA1. Interacts with HTR4 By similarity.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Ubiquitous.

Post-translational modification

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. Ref.7 Ref.10 Ref.12

Sequence similarities

Belongs to the DHOase family. Hydantoinase/dihydropyrimidinase subfamily.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 572572Dihydropyrimidinase-related protein 2
PRO_0000165913

Amino acid modifications

Modified residue321Phosphotyrosine By similarity
Modified residue4311Phosphotyrosine By similarity
Modified residue4621Phosphothreonine By similarity
Modified residue4651Phosphoserine By similarity
Modified residue4991Phosphotyrosine By similarity
Modified residue5091Phosphothreonine Ref.7 Ref.10 Ref.12
Modified residue5141Phosphothreonine; in vitro
Modified residue5171Phosphoserine By similarity
Modified residue5181Phosphoserine Ref.7
Modified residue5221Phosphoserine Ref.7
Modified residue5421Phosphoserine By similarity

Natural variations

Natural variant1181A → T: dbSNP rs2289593.
VAR_022016
Natural variant4811R → C in a colorectal cancer sample; somatic mutation. Ref.15
VAR_036316

Experimental info

Mutagenesis711D → N: Inhibits axon outgrowth formation in hippocampal neurons and decreases binding to CYFIP1. Ref.9
Mutagenesis5071S → A: No effect. Ref.7
Mutagenesis5091T → A: Greatly diminishes binding to 3F4 antibody. Ref.7
Mutagenesis5121T → A: No effect. Ref.7
Mutagenesis5141T → A: No effect. Ref.7
Mutagenesis5171S → A: No effect. Ref.7
Mutagenesis5181S → A: Greatly diminishes binding to 3F4 antibody. Ref.7
Mutagenesis5211T → A: No effect. Ref.7
Mutagenesis5221S → A: Greatly diminishes binding to 3F4 antibody. Ref.7

Secondary structure

................................................................................ 572
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q16555-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 5CDB6CF7F5C308AD

FASTA57262,294
        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 

« Hide

References

« Hide 'large scale' references
[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: 7637782] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 8973361] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
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].
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: 10574455] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye and Testis.
[6]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, MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[7]"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: 10757975] [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.
[8]"CRMP-2 induces axons in cultured hippocampal neurons."
Inagaki N., Chihara K., Arimura N., Menager C., Kawano Y., Matsuo N., Nishimura T., Amano M., Kaibuchi K.
Nat. Neurosci. 4:781-782(2001) [PubMed: 11477421] [Abstract]
Cited for: FUNCTION.
[9]"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: 16260607] [Abstract]
Cited for: INTERACTION WITH CYFIP1, MUTAGENESIS OF ASP-71.
[10]"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: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509, MASS SPECTROMETRY.
Tissue: Epithelium.
[11]"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: 14685275] [Abstract]
Cited for: INTERACTION WITH PLEXNA1, SUBUNIT.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509, MASS SPECTROMETRY.
[13]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[14]"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: 17250651] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 12-490, SUBUNIT.
[15]"The consensus coding sequences of human breast and colorectal cancers."
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. expand/collapse author list , 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.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-481.
+Additional computationally mapped references.

Cross-references

Sequence databases

U17279 mRNA. Translation: AAA93202.1.
D78013 mRNA. Translation: BAA11191.1.
U97105 mRNA. Translation: AAC05793.1.
AB020777 Genomic DNA. Translation: BAA86991.1.
BC056408 mRNA. Translation: AAH56408.1.
BC067109 mRNA. Translation: AAH67109.1.
IPIIPI00257508.
PIRJC5317.
RefSeqNP_001377.1.
UniGeneHs.173381

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2GSEX-ray2.40A/B/C/D13-490[»]
2VM8X-ray1.90A/B/C/D13-490[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ16555. 1 interaction.
STRINGQ16555.

Protein family/group databases

MEROPSM38.975.

PTM databases

PhosphoSiteQ16555.

2-D gel databases

REPRODUCTION-2DPAGEIPI00257508.
Q16555.

Proteomic databases

PeptideAtlasQ16555.
PRIDEQ16555.

Genome annotation databases

EnsemblENST00000311151; ENSP00000309539; ENSG00000092964; Homo sapiens. [Genome view]
ENST00000436721; ENSP00000413876; ENSG00000092964; Homo sapiens. [Genome view]
GeneID1808.
KEGGhsa:1808.
NMPDRfig|9606.3.peg.30095.
UCSCuc003xfb.1. human.

Organism-specific databases

CTD1808.
GeneCardsGC08P026491.
H-InvDBHIX0007403.
HGNCHGNC:3014. DPYSL2.
HPACAB018719.
HPA002381.
MIM602463. gene.
PharmGKBPA27472.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ16555.
OMAAQARKKX.

Enzyme and pathway databases

ReactomeREACT_18266. Axon guidance.

Gene expression databases

ArrayExpressQ16555.
BgeeQ16555.
CleanExHS_DPYSL2.
GenevestigatorQ16555.
GermOnlineENSG00000092964. Homo sapiens.

Family and domain databases

InterProIPR006680. Amidohydro_1.
IPR011778. D-hydantoinase.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
ProDomPD000518. DHOase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR02033. D-hydantoinase. 1 hit.
ProtoNetSearch...

Other Resources

NextBio7369.
SOURCESearch...

Entry information

Entry nameDPYL2_HUMAN
AccessionPrimary (citable) accession number: Q16555
Secondary accession number(s): O00424
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: November 3, 2009
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents