DPYL2_HUMAN
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 03-AUG-2022, entry version 214.
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 Q16555; Q14194: CRMP1; NbExp=5; IntAct=EBI-1104711, EBI-473101;
CC Q16555; Q16555: DPYSL2; NbExp=7; IntAct=EBI-1104711, EBI-1104711;
CC Q16555; Q14195: DPYSL3; NbExp=4; IntAct=EBI-1104711, EBI-1104726;
CC Q16555; Q14195-2: DPYSL3; NbExp=10; IntAct=EBI-1104711, EBI-10232496;
CC Q16555; Q8IXW6: DPYSL3; NbExp=3; IntAct=EBI-1104711, EBI-10262612;
CC Q16555; Q9BPU6: DPYSL5; NbExp=14; IntAct=EBI-1104711, EBI-724653;
CC Q16555; Q9H8Y8: GORASP2; NbExp=15; IntAct=EBI-1104711, EBI-739467;
CC Q16555; P42858: HTT; NbExp=3; IntAct=EBI-1104711, EBI-466029;
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}.
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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 PDB; 6JV9; X-ray; 2.26 A; A/B/C/D=1-532.
DR PDB; 6JVB; X-ray; 2.00 A; A/B/C/D=1-532.
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 PDBsum; 6JV9; -.
DR PDBsum; 6JVB; -.
DR AlphaFoldDB; Q16555; -.
DR SMR; Q16555; -.
DR BioGRID; 108142; 104.
DR IntAct; Q16555; 41.
DR MINT; Q16555; -.
DR STRING; 9606.ENSP00000309539; -.
DR ChEMBL; CHEMBL4295834; -.
DR DrugBank; DB11638; Artenimol.
DR DrugCentral; Q16555; -.
DR MEROPS; M38.975; -.
DR GlyGen; Q16555; 6 sites, 1 O-linked glycan (6 sites).
DR iPTMnet; Q16555; -.
DR MetOSite; 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; 1 sequenced antibody.
DR Antibodypedia; 1039; 653 antibodies from 40 providers.
DR DNASU; 1808; -.
DR Ensembl; ENST00000311151.9; ENSP00000309539.5; ENSG00000092964.18. [Q16555-1]
DR Ensembl; ENST00000523027.1; ENSP00000431117.1; ENSG00000092964.18. [Q16555-2]
DR GeneID; 1808; -.
DR KEGG; hsa:1808; -.
DR UCSC; uc003xfb.3; human. [Q16555-1]
DR CTD; 1808; -.
DR DisGeNET; 1808; -.
DR GeneCards; DPYSL2; -.
DR HGNC; HGNC:3014; DPYSL2.
DR HPA; ENSG00000092964; Tissue enriched (brain).
DR MIM; 602463; gene.
DR neXtProt; NX_Q16555; -.
DR OpenTargets; ENSG00000092964; -.
DR PharmGKB; PA27472; -.
DR VEuPathDB; HostDB:ENSG00000092964; -.
DR eggNOG; KOG2584; Eukaryota.
DR GeneTree; ENSGT01030000234527; -.
DR HOGENOM; CLU_015572_2_2_1; -.
DR InParanoid; Q16555; -.
DR OrthoDB; 719800at2759; -.
DR PhylomeDB; Q16555; -.
DR TreeFam; TF314706; -.
DR PathwayCommons; Q16555; -.
DR Reactome; R-HSA-399956; CRMPs in Sema3A signaling.
DR Reactome; R-HSA-437239; Recycling pathway of L1.
DR SignaLink; Q16555; -.
DR SIGNOR; Q16555; -.
DR BioGRID-ORCS; 1808; 14 hits in 1073 CRISPR screens.
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 inferior vagus X ganglion and 205 other tissues.
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: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:0045664; P:regulation of neuron differentiation; 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; Reference proteome;
KW S-nitrosylation.
FT CHAIN 1..572
FT /note="Dihydropyrimidinase-related protein 2"
FT /id="PRO_0000165913"
FT REGION 512..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000269|PubMed:10757975,
FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
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:0007744|PubMed:21406692"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10757975,
FT ECO:0007744|PubMed:21406692"
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:0000269|PubMed:10757975,
FT ECO:0000269|PubMed:15466863, ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:21406692"
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:0007829|PDB:5LXX"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:5LXX"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:5LXX"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:5LXX"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:5LXX"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:2VM8"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:5LXX"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:5LXX"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:5LXX"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:5LXX"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:5LXX"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:5LXX"
FT STRAND 132..140
FT /evidence="ECO:0007829|PDB:5LXX"
FT HELIX 148..159
FT /evidence="ECO:0007829|PDB:5LXX"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:5LXX"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:5LXX"
FT HELIX 178..191
FT /evidence="ECO:0007829|PDB:5LXX"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:5LXX"
FT HELIX 202..214
FT /evidence="ECO:0007829|PDB:5LXX"
FT HELIX 220..226
FT /evidence="ECO:0007829|PDB:5LXX"
FT HELIX 229..246
FT /evidence="ECO:0007829|PDB:5LXX"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:5LXX"
FT HELIX 258..269
FT /evidence="ECO:0007829|PDB:5LXX"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:5LXX"
FT HELIX 280..284
FT /evidence="ECO:0007829|PDB:5LXX"
FT HELIX 287..291
FT /evidence="ECO:0007829|PDB:5LXX"
FT HELIX 295..300
FT /evidence="ECO:0007829|PDB:5LXX"
FT HELIX 313..322
FT /evidence="ECO:0007829|PDB:5LXX"
FT HELIX 338..341
FT /evidence="ECO:0007829|PDB:5LXX"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:5LXX"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:5LXX"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:5LXX"
FT HELIX 361..369
FT /evidence="ECO:0007829|PDB:5LXX"
FT TURN 370..373
FT /evidence="ECO:0007829|PDB:5LXX"
FT HELIX 377..384
FT /evidence="ECO:0007829|PDB:5LXX"
FT HELIX 386..391
FT /evidence="ECO:0007829|PDB:5LXX"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:5LXX"
FT STRAND 409..419
FT /evidence="ECO:0007829|PDB:5LXX"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:5LXX"
FT STRAND 425..428
FT /evidence="ECO:0007829|PDB:5LXX"
FT TURN 433..436
FT /evidence="ECO:0007829|PDB:5LXX"
FT STRAND 438..448
FT /evidence="ECO:0007829|PDB:5LXX"
FT STRAND 451..455
FT /evidence="ECO:0007829|PDB:5LXX"
FT HELIX 476..486
FT /evidence="ECO:0007829|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
