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Database: UniProt
Entry: Q16555
LinkDB: Q16555
Original site: Q16555 
ID   DPYL2_HUMAN             Reviewed;         572 AA.
AC   Q16555; A8K5H2; B4DR31; D3DSS7; O00424;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   11-DEC-2019, entry version 201.
DE   RecName: Full=Dihydropyrimidinase-related protein 2;
DE            Short=DRP-2;
DE   AltName: Full=Collapsin response mediator protein 2;
DE            Short=CRMP-2;
DE   AltName: Full=N2A3;
DE   AltName: Full=Unc-33-like phosphoprotein 2;
DE            Short=ULIP-2;
GN   Name=DPYSL2; Synonyms=CRMP2, ULIP2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=7637782; DOI=10.1038/376509a0;
RA   Goshima Y., Nakamura F., Strittmatter P., Strittmatter S.M.;
RT   "Collapsin-induced growth cone collapse mediated by an intracellular
RT   protein related to UNC-33.";
RL   Nature 376:509-514(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=8973361; DOI=10.1016/s0378-1119(96)00445-3;
RA   Hamajima N., Matsuda K., Sakata S., Tamaki N., Sasaki M., Nonaka M.;
RT   "A novel gene family defined by human dihydropyrimidinase and three related
RT   proteins with differential tissue distribution.";
RL   Gene 180:157-163(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Fetal liver;
RA   Zhou J., Chen Y., Gu J.R.;
RT   "A cDNA clone highly expressed in human brain and deleted in liver
RT   cancer.";
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10574455; DOI=10.1093/dnares/6.5.291;
RA   Kitamura K., Takayama M., Hamajima N., Nakanishi M., Sasaki M., Endo Y.,
RA   Takemoto T., Kimura H., Iwaki M., Nonaka M.;
RT   "Characterization of the human dihydropyrimidinase-related protein 2 (DRP-
RT   2) gene.";
RL   DNA Res. 6:291-297(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA   Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA   O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Eye, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   PROTEIN SEQUENCE OF 44-56; 64-75; 147-157; 174-211; 239-254; 375-390;
RP   401-418; 424-467; 497-511 AND 533-552, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA   Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [10]
RP   PHOSPHORYLATION AT SER-518; SER-522 AND THR-509, AND MUTAGENESIS OF
RP   SER-507; THR-509; THR-512; THR-514; SER-517; SER-518; THR-521 AND SER-522.
RX   PubMed=10757975; DOI=10.1021/bi992323h;
RA   Gu Y., Hamajima N., Ihara Y.;
RT   "Neurofibrillary tangle-associated collapsin response mediator protein-2
RT   (CRMP-2) is highly phosphorylated on Thr-509, Ser-518, and Ser-522.";
RL   Biochemistry 39:4267-4275(2000).
RN   [11]
RP   FUNCTION.
RX   PubMed=11477421; DOI=10.1038/90476;
RA   Inagaki N., Chihara K., Arimura N., Menager C., Kawano Y., Matsuo N.,
RA   Nishimura T., Amano M., Kaibuchi K.;
RT   "CRMP-2 induces axons in cultured hippocampal neurons.";
RL   Nat. Neurosci. 4:781-782(2001).
RN   [12]
RP   FUNCTION, AND PHOSPHORYLATION AT SER-522.
RX   PubMed=15466863; DOI=10.1074/jbc.c400412200;
RA   Cole A.R., Knebel A., Morrice N.A., Robertson L.A., Irving A.J.,
RA   Connolly C.N., Sutherland C.;
RT   "GSK-3 phosphorylation of the Alzheimer epitope within collapsin response
RT   mediator proteins regulates axon elongation in primary neurons.";
RL   J. Biol. Chem. 279:50176-50180(2004).
RN   [13]
RP   INTERACTION WITH CYFIP1, AND MUTAGENESIS OF ASP-71.
RX   PubMed=16260607; DOI=10.1128/mcb.25.22.9920-9935.2005;
RA   Kawano Y., Yoshimura T., Tsuboi D., Kawabata S., Kaneko-Kawano T.,
RA   Shirataki H., Takenawa T., Kaibuchi K.;
RT   "CRMP-2 is involved in kinesin-1-dependent transport of the Sra-1/WAVE1
RT   complex and axon formation.";
RL   Mol. Cell. Biol. 25:9920-9935(2005).
RN   [14]
RP   INTERACTION WITH PLEXNA1, AND SUBUNIT.
RX   PubMed=14685275; DOI=10.1038/sj.emboj.7600021;
RA   Deo R.C., Schmidt E.F., Elhabazi A., Togashi H., Burley S.K.,
RA   Strittmatter S.M.;
RT   "Structural bases for CRMP function in plexin-dependent semaphorin3A
RT   signaling.";
RL   EMBO J. 23:9-22(2004).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509 AND SER-522, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [17]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [18]
RP   PHOSPHORYLATION AT TYR-32 BY FYN.
RX   PubMed=19652227; DOI=10.1074/jbc.m109.000240;
RA   Uchida Y., Ohshima T., Yamashita N., Ogawara M., Sasaki Y., Nakamura F.,
RA   Goshima Y.;
RT   "Semaphorin3A signaling mediated by Fyn-dependent tyrosine phosphorylation
RT   of collapsin response mediator protein 2 at tyrosine 32.";
RL   J. Biol. Chem. 284:27393-27401(2009).
RN   [19]
RP   INTERACTION WITH CLN6.
RX   PubMed=19235893; DOI=10.1002/jnr.22032;
RA   Benedict J.W., Getty A.L., Wishart T.M., Gillingwater T.H., Pearce D.A.;
RT   "Protein product of CLN6 gene responsible for variant late-onset infantile
RT   neuronal ceroid lipofuscinosis interacts with CRMP-2.";
RL   J. Neurosci. Res. 87:2157-2166(2009).
RN   [20]
RP   FUNCTION IN ENDOCYTOSIS, INTERACTION WITH MICALL1, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=20801876; DOI=10.1074/jbc.c110.166066;
RA   Rahajeng J., Giridharan S.S., Naslavsky N., Caplan S.;
RT   "Collapsin response mediator protein-2 (Crmp2) regulates trafficking by
RT   linking endocytic regulatory proteins to dynein motors.";
RL   J. Biol. Chem. 285:31918-31922(2010).
RN   [21]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [22]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [23]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509; THR-514; SER-517;
RP   SER-518 AND SER-522, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [24]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22905912; DOI=10.1021/pr300539b;
RA   Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P.,
RA   Mariman E.C., Renes J.;
RT   "Resveratrol-induced changes of the human adipocyte secretion profile.";
RL   J. Proteome Res. 11:4733-4743(2012).
RN   [25]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [26]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [27]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [28]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 12-490, AND SUBUNIT.
RX   PubMed=17250651; DOI=10.1111/j.1471-4159.2006.04401.x;
RA   Stenmark P., Ogg D., Flodin S., Flores A., Kotenyova T., Nyman T.,
RA   Nordlund P., Kursula P.;
RT   "The structure of human collapsin response mediator protein 2, a regulator
RT   of axonal growth.";
RL   J. Neurochem. 101:906-917(2007).
RN   [29]
RP   VARIANT [LARGE SCALE ANALYSIS] CYS-481.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Plays a role in neuronal development and polarity, as well as
CC       in axon growth and guidance, neuronal growth cone collapse and cell
CC       migration. Necessary for signaling by class 3 semaphorins and
CC       subsequent remodeling of the cytoskeleton. May play a role in
CC       endocytosis. {ECO:0000269|PubMed:11477421, ECO:0000269|PubMed:15466863,
CC       ECO:0000269|PubMed:20801876}.
CC   -!- SUBUNIT: Homotetramer, and heterotetramer with CRMP1, DPYSL3, DPYSL4 or
CC       DPYSL5. Interacts through its C-terminus with the C-terminus of
CC       CYFIP1/SRA1. Interacts with HTR4. Interacts with CLN6. Interacts with
CC       MICALL1. {ECO:0000269|PubMed:14685275, ECO:0000269|PubMed:16260607,
CC       ECO:0000269|PubMed:17250651, ECO:0000269|PubMed:19235893,
CC       ECO:0000269|PubMed:20801876}.
CC   -!- INTERACTION:
CC       Self; NbExp=4; IntAct=EBI-1104711, EBI-1104711;
CC       Q14194:CRMP1; NbExp=4; IntAct=EBI-1104711, EBI-473101;
CC       Q14195-2:DPYSL3; NbExp=7; IntAct=EBI-1104711, EBI-10232496;
CC       Q8IXW6:DPYSL3; NbExp=3; IntAct=EBI-1104711, EBI-10262612;
CC       Q9BPU6:DPYSL5; NbExp=10; IntAct=EBI-1104711, EBI-724653;
CC       Q9H8Y8:GORASP2; NbExp=7; IntAct=EBI-1104711, EBI-739467;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20801876}.
CC       Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20801876}. Membrane
CC       {ECO:0000269|PubMed:20801876}. Note=Tightly but non-covalently
CC       associated with membranes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q16555-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q16555-2; Sequence=VSP_044941;
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- PTM: 3F4, a monoclonal antibody which strongly stains neurofibrillary
CC       tangles in Alzheimer disease brains, specifically labels DPYSL2 when
CC       phosphorylated on Ser-518, Ser-522 and Thr-509.
CC       {ECO:0000269|PubMed:10757975, ECO:0000269|PubMed:15466863}.
CC   -!- PTM: Phosphorylation at Thr-514 by GSK3B abolishes tubulin-binding
CC       leading to destabilization of microtubule assembly in axons and
CC       neurodegeneration (By similarity). Phosphorylation by DYRK2 at Ser-522
CC       is required for subsequent phosphorylation by GSK3B. {ECO:0000250,
CC       ECO:0000269|PubMed:10757975, ECO:0000269|PubMed:15466863}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Hydantoinase/dihydropyrimidinase family. {ECO:0000305}.
CC   -!- CAUTION: Lacks most of the conserved residues that are essential for
CC       binding the metal cofactor and hence for dihydropyrimidinase activity.
CC       Its enzyme activity is therefore unsure. {ECO:0000305}.
DR   EMBL; U17279; AAA93202.1; -; mRNA.
DR   EMBL; D78013; BAA11191.1; -; mRNA.
DR   EMBL; U97105; AAC05793.1; -; mRNA.
DR   EMBL; AB020777; BAA86991.1; -; Genomic_DNA.
DR   EMBL; AK291287; BAF83976.1; -; mRNA.
DR   EMBL; AK299077; BAG61143.1; -; mRNA.
DR   EMBL; AC015564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC015743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471080; EAW63573.1; -; Genomic_DNA.
DR   EMBL; CH471080; EAW63574.1; -; Genomic_DNA.
DR   EMBL; BC056408; AAH56408.1; -; mRNA.
DR   EMBL; BC067109; AAH67109.1; -; mRNA.
DR   CCDS; CCDS59096.1; -. [Q16555-2]
DR   CCDS; CCDS6051.1; -. [Q16555-1]
DR   PIR; JC5317; JC5317.
DR   RefSeq; NP_001184222.1; NM_001197293.2.
DR   RefSeq; NP_001231533.1; NM_001244604.1. [Q16555-2]
DR   RefSeq; NP_001377.1; NM_001386.5. [Q16555-1]
DR   PDB; 2GSE; X-ray; 2.40 A; A/B/C/D=13-490.
DR   PDB; 2VM8; X-ray; 1.90 A; A/B/C/D=13-490.
DR   PDB; 5LXX; X-ray; 1.25 A; A/B=13-490.
DR   PDB; 5MKV; X-ray; 1.80 A; A/B/C/D=13-516.
DR   PDB; 5MLE; X-ray; 2.48 A; A/C=13-516.
DR   PDB; 5X1A; X-ray; 1.82 A; A=1-525.
DR   PDB; 5X1C; X-ray; 2.10 A; A/B=13-490.
DR   PDB; 5X1D; X-ray; 2.20 A; A=1-525.
DR   PDB; 5YZ5; X-ray; 1.80 A; A=1-525.
DR   PDB; 5YZA; X-ray; 2.30 A; A=1-525.
DR   PDB; 5YZB; X-ray; 2.80 A; A=1-525.
DR   PDBsum; 2GSE; -.
DR   PDBsum; 2VM8; -.
DR   PDBsum; 5LXX; -.
DR   PDBsum; 5MKV; -.
DR   PDBsum; 5MLE; -.
DR   PDBsum; 5X1A; -.
DR   PDBsum; 5X1C; -.
DR   PDBsum; 5X1D; -.
DR   PDBsum; 5YZ5; -.
DR   PDBsum; 5YZA; -.
DR   PDBsum; 5YZB; -.
DR   SMR; Q16555; -.
DR   BioGrid; 108142; 69.
DR   IntAct; Q16555; 35.
DR   MINT; Q16555; -.
DR   STRING; 9606.ENSP00000309539; -.
DR   DrugBank; DB11638; Artenimol.
DR   DrugCentral; Q16555; -.
DR   MEROPS; M38.975; -.
DR   iPTMnet; Q16555; -.
DR   PhosphoSitePlus; Q16555; -.
DR   SwissPalm; Q16555; -.
DR   BioMuta; DPYSL2; -.
DR   DMDM; 3122051; -.
DR   REPRODUCTION-2DPAGE; IPI00257508; -.
DR   REPRODUCTION-2DPAGE; Q16555; -.
DR   UCD-2DPAGE; Q16555; -.
DR   CPTAC; CPTAC-60; -.
DR   CPTAC; CPTAC-61; -.
DR   EPD; Q16555; -.
DR   jPOST; Q16555; -.
DR   MassIVE; Q16555; -.
DR   MaxQB; Q16555; -.
DR   PaxDb; Q16555; -.
DR   PeptideAtlas; Q16555; -.
DR   PRIDE; Q16555; -.
DR   ProteomicsDB; 4921; -.
DR   ProteomicsDB; 60912; -. [Q16555-1]
DR   TopDownProteomics; Q16555-1; -. [Q16555-1]
DR   ABCD; Q16555; -.
DR   Ensembl; ENST00000311151; ENSP00000309539; ENSG00000092964. [Q16555-1]
DR   Ensembl; ENST00000523027; ENSP00000431117; ENSG00000092964. [Q16555-2]
DR   GeneID; 1808; -.
DR   KEGG; hsa:1808; -.
DR   UCSC; uc003xfb.3; human. [Q16555-1]
DR   CTD; 1808; -.
DR   DisGeNET; 1808; -.
DR   EuPathDB; HostDB:ENSG00000092964.16; -.
DR   GeneCards; DPYSL2; -.
DR   HGNC; HGNC:3014; DPYSL2.
DR   HPA; CAB018719; -.
DR   HPA; HPA002381; -.
DR   MIM; 602463; gene.
DR   neXtProt; NX_Q16555; -.
DR   OpenTargets; ENSG00000092964; -.
DR   PharmGKB; PA27472; -.
DR   eggNOG; KOG2584; Eukaryota.
DR   eggNOG; COG0044; LUCA.
DR   GeneTree; ENSGT00950000182699; -.
DR   HOGENOM; HOG000219145; -.
DR   InParanoid; Q16555; -.
DR   KO; K07528; -.
DR   OrthoDB; 719800at2759; -.
DR   PhylomeDB; Q16555; -.
DR   TreeFam; TF314706; -.
DR   Reactome; R-HSA-399956; CRMPs in Sema3A signaling.
DR   Reactome; R-HSA-437239; Recycling pathway of L1.
DR   SIGNOR; Q16555; -.
DR   ChiTaRS; DPYSL2; human.
DR   EvolutionaryTrace; Q16555; -.
DR   GeneWiki; DPYSL2; -.
DR   GenomeRNAi; 1808; -.
DR   Pharos; Q16555; Tbio.
DR   PRO; PR:Q16555; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q16555; protein.
DR   Bgee; ENSG00000092964; Expressed in 251 organ(s), highest expression level in brain.
DR   ExpressionAtlas; Q16555; baseline and differential.
DR   Genevisible; Q16555; HS.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0004157; F:dihydropyrimidinase activity; TAS:ProtInc.
DR   GO; GO:0016812; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0007411; P:axon guidance; IEA:InterPro.
DR   GO; GO:0007420; P:brain development; IEA:InterPro.
DR   GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0006897; P:endocytosis; IMP:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
DR   GO; GO:0030516; P:regulation of axon extension; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   CDD; cd01314; D-HYD; 1.
DR   Gene3D; 2.30.40.10; -; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR030615; DRP2.
DR   InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR11647:SF56; PTHR11647:SF56; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; SSF51338; 2.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR02033; D-hydantoinase; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Cytoskeleton;
KW   Developmental protein; Differentiation; Direct protein sequencing;
KW   Membrane; Methylation; Neurogenesis; Phosphoprotein; Polymorphism;
KW   Reference proteome; S-nitrosylation.
FT   CHAIN           1..572
FT                   /note="Dihydropyrimidinase-related protein 2"
FT                   /id="PRO_0000165913"
FT   MOD_RES         32
FT                   /note="Phosphotyrosine; by FYN"
FT                   /evidence="ECO:0000269|PubMed:19652227"
FT   MOD_RES         258
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O08553"
FT   MOD_RES         259
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47942"
FT   MOD_RES         431
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O08553"
FT   MOD_RES         465
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O08553"
FT   MOD_RES         499
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O08553"
FT   MOD_RES         504
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P47942"
FT   MOD_RES         507
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O08553"
FT   MOD_RES         509
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:16964243,
FT                   ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:21406692,
FT                   ECO:0000244|PubMed:23186163, ECO:0000269|PubMed:10757975"
FT   MOD_RES         512
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O08553"
FT   MOD_RES         514
FT                   /note="Phosphothreonine; by GSK3-beta"
FT                   /evidence="ECO:0000244|PubMed:21406692"
FT   MOD_RES         517
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21406692"
FT   MOD_RES         518
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21406692,
FT                   ECO:0000269|PubMed:10757975"
FT   MOD_RES         521
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O08553"
FT   MOD_RES         522
FT                   /note="Phosphoserine; by DYRK2"
FT                   /evidence="ECO:0000244|PubMed:16964243,
FT                   ECO:0000244|PubMed:21406692, ECO:0000269|PubMed:10757975,
FT                   ECO:0000269|PubMed:15466863"
FT   MOD_RES         537
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O08553"
FT   MOD_RES         540
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O08553"
FT   MOD_RES         542
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O08553"
FT   MOD_RES         555
FT                   /note="Phosphothreonine; by ROCK2"
FT                   /evidence="ECO:0000250|UniProtKB:O02675"
FT   MOD_RES         565
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:O08553"
FT   VAR_SEQ         1..36
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_044941"
FT   VARIANT         118
FT                   /note="A -> T (in dbSNP:rs2228979)"
FT                   /id="VAR_022016"
FT   VARIANT         481
FT                   /note="R -> C (in a colorectal cancer sample; somatic
FT                   mutation; dbSNP:rs1337153084)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036316"
FT   MUTAGEN         71
FT                   /note="D->N: Inhibits axon outgrowth formation in
FT                   hippocampal neurons and decreases binding to CYFIP1."
FT                   /evidence="ECO:0000269|PubMed:16260607"
FT   MUTAGEN         507
FT                   /note="S->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:10757975"
FT   MUTAGEN         509
FT                   /note="T->A: Greatly diminishes binding to 3F4 antibody."
FT                   /evidence="ECO:0000269|PubMed:10757975"
FT   MUTAGEN         512
FT                   /note="T->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:10757975"
FT   MUTAGEN         514
FT                   /note="T->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:10757975"
FT   MUTAGEN         517
FT                   /note="S->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:10757975"
FT   MUTAGEN         518
FT                   /note="S->A: Greatly diminishes binding to 3F4 antibody."
FT                   /evidence="ECO:0000269|PubMed:10757975"
FT   MUTAGEN         521
FT                   /note="T->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:10757975"
FT   MUTAGEN         522
FT                   /note="S->A: Greatly diminishes binding to 3F4 antibody."
FT                   /evidence="ECO:0000269|PubMed:10757975"
FT   STRAND          17..21
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   STRAND          23..25
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   STRAND          30..32
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   STRAND          34..38
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   STRAND          41..48
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   STRAND          53..55
FT                   /evidence="ECO:0000244|PDB:2VM8"
FT   STRAND          56..59
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   STRAND          64..67
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   STRAND          69..72
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   HELIX           89..98
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   STRAND          101..108
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   HELIX           116..130
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   STRAND          132..140
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   HELIX           148..159
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   STRAND          163..168
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   TURN            171..173
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   HELIX           178..191
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   STRAND          194..198
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   HELIX           202..214
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   HELIX           220..226
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   HELIX           229..246
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   STRAND          250..255
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   HELIX           258..269
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   STRAND          274..279
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   HELIX           280..284
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   HELIX           287..291
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   HELIX           295..300
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   HELIX           313..322
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   HELIX           338..341
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   HELIX           342..344
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   HELIX           348..350
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   TURN            358..360
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   HELIX           361..369
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   TURN            370..373
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   HELIX           377..384
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   HELIX           386..391
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   TURN            395..397
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   STRAND          409..419
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   TURN            422..424
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   STRAND          425..428
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   TURN            433..436
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   STRAND          438..448
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   STRAND          451..455
FT                   /evidence="ECO:0000244|PDB:5LXX"
FT   HELIX           476..486
FT                   /evidence="ECO:0000244|PDB:5LXX"
SQ   SEQUENCE   572 AA;  62294 MW;  5CDB6CF7F5C308AD CRC64;
     MSYQGKKNIP RITSDRLLIK GGKIVNDDQS FYADIYMEDG LIKQIGENLI VPGGVKTIEA
     HSRMVIPGGI DVHTRFQMPD QGMTSADDFF QGTKAALAGG TTMIIDHVVP EPGTSLLAAF
     DQWREWADSK SCCDYSLHVD ISEWHKGIQE EMEALVKDHG VNSFLVYMAF KDRFQLTDCQ
     IYEVLSVIRD IGAIAQVHAE NGDIIAEEQQ RILDLGITGP EGHVLSRPEE VEAEAVNRAI
     TIANQTNCPL YITKVMSKSS AEVIAQARKK GTVVYGEPIT ASLGTDGSHY WSKNWAKAAA
     FVTSPPLSPD PTTPDFLNSL LSCGDLQVTG SAHCTFNTAQ KAVGKDNFTL IPEGTNGTEE
     RMSVIWDKAV VTGKMDENQF VAVTSTNAAK VFNLYPRKGR IAVGSDADLV IWDPDSVKTI
     SAKTHNSSLE YNIFEGMECR GSPLVVISQG KIVLEDGTLH VTEGSGRYIP RKPFPDFVYK
     RIKARSRLAE LRGVPRGLYD GPVCEVSVTP KTVTPASSAK TSPAKQQAPP VRNLHQSGFS
     LSGAQIDDNI PRRTTQRIVA PPGGRANITS LG
//
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