Q16555 (DPYL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	DPYSL2
Synonyms:	CRMP2, ULIP2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	572 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 By similarity. Plays a role in neuron projection morphogenesis. Ref.11 Ref.12
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. Interacts with CLN6. Ref.13 Ref.14 Ref.18 Ref.22
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.10 Ref.12 Ref.17 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.
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.

Ontologies

Keywords
Biological process	Differentiation Neurogenesis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Developmental protein
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	axon guidance Traceable author statement. Source: Reactome cytoskeleton organization Inferred from sequence or structural similarity. Source: UniProtKB nucleobase-containing compound metabolic process Traceable author statement Ref.2. Source: ProtInc olfactory bulb development Inferred from electronic annotation. Source: Compara positive regulation of glutamate secretion Inferred from electronic annotation. Source: Compara pyrimidine nucleobase catabolic process Inferred from electronic annotation. Source: InterPro regulation of neuron differentiation Inferred from electronic annotation. Source: Compara response to amphetamine Inferred from electronic annotation. Source: Compara response to cocaine Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara signal transduction Traceable author statement Ref.2. Source: ProtInc spinal cord development Inferred from electronic annotation. Source: Compara synaptic vesicle transport Inferred from electronic annotation. Source: Compara
Cellular_component	axon Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome dendrite Inferred from electronic annotation. Source: Compara growth cone Inferred from electronic annotation. Source: Compara mitochondrion Inferred from electronic annotation. Source: Compara neuronal cell body Inferred from electronic annotation. Source: Compara protein complex Inferred from electronic annotation. Source: Compara
Molecular_function	dihydropyrimidinase activity Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q16555-1)

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.

Isoform 2 (identifier: Q16555-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 572

572

Dihydropyrimidinase-related protein 2

PRO_0000165913

Amino acid modifications

Modified residue

32

1

Phosphotyrosine; by FYN Ref.17

Modified residue

431

1

Phosphotyrosine By similarity

Modified residue

462

1

Phosphothreonine By similarity

Modified residue

465

1

Phosphoserine By similarity

Modified residue

499

1

Phosphotyrosine By similarity

Modified residue

509

1

Phosphothreonine Ref.10 Ref.15 Ref.16 Ref.21

Modified residue

514

1

Phosphothreonine; by GSK3-beta Ref.21

Modified residue

517

1

Phosphoserine Ref.21

Modified residue

518

1

Phosphoserine Ref.10 Ref.21

Modified residue

522

1

Phosphoserine; by DYRK2 Ref.10 Ref.12 Ref.15 Ref.21

Modified residue

542

1

Phosphoserine By similarity

Modified residue

555

1

Phosphothreonine; by ROCK2 By similarity

Natural variations

Alternative sequence

1 – 36

36

Missing in isoform 2.

VSP_044941

Natural variant

118

1

A → T.
Corresponds to variant rs2289593 [ dbSNP | Ensembl ].

VAR_022016

Natural variant

481

1

R → C in a colorectal cancer sample; somatic mutation. Ref.23

VAR_036316

Experimental info

Mutagenesis

71

1

D → N: Inhibits axon outgrowth formation in hippocampal neurons and decreases binding to CYFIP1. Ref.13

Mutagenesis

507

1

S → A: No effect. Ref.10

Mutagenesis

509

1

T → A: Greatly diminishes binding to 3F4 antibody. Ref.10

Mutagenesis

512

1

T → A: No effect. Ref.10

Mutagenesis

514

1

T → A: No effect. Ref.10

Mutagenesis

517

1

S → A: No effect. Ref.10

Mutagenesis

518

1

S → A: Greatly diminishes binding to 3F4 antibody. Ref.10

Mutagenesis

521

1

T → A: No effect. Ref.10

Mutagenesis

522

1

S → A: Greatly diminishes binding to 3F4 antibody. Ref.10

Secondary structure

1

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572

Helix Strand Turn

Details...

Beta strand

17 – 25

9

Beta strand

30 – 38

9

Beta strand

41 – 48

8

Beta strand

53 – 55

3

Beta strand

57 – 59

3

Beta strand

64 – 67

4

Beta strand

69 – 74

6

Helix

89 – 98

10

Beta strand

101 – 108

8

Helix

116 – 130

15

Beta strand

132 – 140

9

Helix

146 – 158

13

Beta strand

163 – 170

8

Turn

171 – 173

3

Helix

178 – 191

14

Beta strand

194 – 198

5

Helix

202 – 213

12

Turn

214 – 216

3

Helix

221 – 226

6

Helix

229 – 246

18

Beta strand

250 – 255

6

Helix

258 – 269

12

Beta 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 – 392

7

Turn

395 – 397

3

Beta strand

409 – 419

11

Turn

422 – 424

3

Beta strand

425 – 428

4

Turn

433 – 436

4

Beta strand

438 – 448

11

Beta strand

451 – 455

5

Helix

476 – 487

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 5CDB6CF7F5C308AD	FASTA	572	62,294
	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
	Isoform 2 [UniParc]. Checksum: 31806BFCB5FAE16D	FASTA	536	58,163
	10 20 30 40 50 60 MEDGLIKQIG ENLIVPGGVK TIEAHSRMVI PGGIDVHTRF QMPDQGMTSA DDFFQGTKAA 70 80 90 100 110 120 LAGGTTMIID HVVPEPGTSL LAAFDQWREW ADSKSCCDYS LHVDISEWHK GIQEEMEALV 130 140 150 160 170 180 KDHGVNSFLV YMAFKDRFQL TDCQIYEVLS VIRDIGAIAQ VHAENGDIIA EEQQRILDLG 190 200 210 220 230 240 ITGPEGHVLS RPEEVEAEAV NRAITIANQT NCPLYITKVM SKSSAEVIAQ ARKKGTVVYG 250 260 270 280 290 300 EPITASLGTD GSHYWSKNWA KAAAFVTSPP LSPDPTTPDF LNSLLSCGDL QVTGSAHCTF 310 320 330 340 350 360 NTAQKAVGKD NFTLIPEGTN GTEERMSVIW DKAVVTGKMD ENQFVAVTST NAAKVFNLYP 370 380 390 400 410 420 RKGRIAVGSD ADLVIWDPDS VKTISAKTHN SSLEYNIFEG MECRGSPLVV ISQGKIVLED 430 440 450 460 470 480 GTLHVTEGSG RYIPRKPFPD FVYKRIKARS RLAELRGVPR GLYDGPVCEV SVTPKTVTPA 490 500 510 520 530 SSAKTSPAKQ QAPPVRNLHQ SGFSLSGAQI DDNIPRRTTQ RIVAPPGGRA NITSLG

References

	« Hide 'large scale' referencesShow '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] [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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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, 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]	"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] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]	"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, MASS SPECTROMETRY.
[22]	"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.
[23]	"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. , 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] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-481.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00257508.
IPI00984387.

PIR

JC5317.

RefSeq

NP_001184222.1. NM_001197293.2.
NP_001231533.1. NM_001244604.1.
NP_001377.1. NM_001386.5.

UniGene

Hs.593187.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q16555.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q16555. 4 interactions.

MINT

MINT-3032752.

STRING

9606.ENSP00000309539.

Protein family/group databases

MEROPS

M38.975.

PTM databases

PhosphoSite

Q16555.

Polymorphism databases

DMDM

3122051.

2D gel databases

REPRODUCTION-2DPAGE

IPI00257508.
Q16555.

UCD-2DPAGE

Q16555.

Proteomic databases

PaxDb

Q16555.

PeptideAtlas

Q16555.

PRIDE

Q16555.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000311151; ENSP00000309539; ENSG00000092964.
ENST00000521913; ENSP00000427985; ENSG00000092964.
ENST00000522745; ENSP00000428909; ENSG00000092964.
ENST00000523027; ENSP00000431117; ENSG00000092964.

GeneID

1808.

KEGG

hsa:1808.

UCSC

uc003xfb.2. human.

Organism-specific databases

CTD

1808.

GeneCards

GC08P026371.

HGNC

HGNC:3014. DPYSL2.

HPA

CAB018719.
HPA002381.

MIM

602463. gene.

neXtProt

NX_Q16555.

PharmGKB

PA27472.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0044.

HOVERGEN

HBG000806.

InParanoid

Q16555.

KO

K07528.

OMA

TEWHKGV.

OrthoDB

EOG48PMJT.

PhylomeDB

Q16555.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.

Gene expression databases

ArrayExpress

Q16555.

Bgee

Q16555.

CleanEx

HS_DPYSL2.

Genevestigator

Q16555.

GermOnline

ENSG00000092964. Homo sapiens.

Family and domain databases

InterPro

IPR006680. Amidohydro_1.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]

Pfam

PF01979. Amidohydro_1. 1 hit.
[Graphical view]

SUPFAM

SSF51338. Metalo_hydrolase. 2 hits.

TIGRFAMs

TIGR02033. D-hydantoinase. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

DPYSL2. human.

EvolutionaryTrace

Q16555.

GenomeRNAi

1808.

NextBio

7369.

SOURCE

Search...

Entry information

Entry name

DPYL2_HUMAN

Accession

Primary (citable) accession number: Q16555
Secondary accession number(s): A8K5H2 , B4DR31, D3DSS7, O00424

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	May 29, 2013
This is version 135 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.