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Q16555 (DPYL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
Unc-33-like phosphoprotein 2
Short name=ULIP-2
Gene names
Name:DPYSL2
Synonyms:CRMP2, ULIP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length572 AA.
Sequence statusComplete.
Protein existenceEvidence 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. May play a role in endocytosis. Ref.11 Ref.12 Ref.20

Subunit structure

Homotetramer, and heterotetramer with CRMP1, DPYSL3, DPYSL4 or DPYSL5. Interacts through its C-terminus with the C-terminus of CYFIP1/SRA1. Interacts with HTR4. Interacts with CLN6. Interacts with MICALL1. Ref.13 Ref.14 Ref.19 Ref.20 Ref.24

Subcellular location

Cytoplasmcytosol. Cytoplasmcytoskeleton. Membrane. Note: Tightly but non-covalently associated with membranes. Ref.20

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.18

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 processDifferentiation
Neurogenesis
   Cellular componentCytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionDevelopmental protein
   PTMPhosphoprotein
S-nitrosylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Traceable author statement. Source: Reactome

cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

endocytosis

Inferred from mutant phenotype Ref.20. Source: UniProtKB

nucleobase-containing compound metabolic process

Traceable author statement Ref.2. Source: ProtInc

olfactory bulb development

Inferred from electronic annotation. Source: Ensembl

positive regulation of glutamate secretion

Inferred from electronic annotation. Source: Ensembl

pyrimidine nucleobase catabolic process

Inferred from electronic annotation. Source: InterPro

regulation of neuron differentiation

Inferred from electronic annotation. Source: Ensembl

response to amphetamine

Inferred from electronic annotation. Source: Ensembl

response to cocaine

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement Ref.2. Source: ProtInc

spinal cord development

Inferred from electronic annotation. Source: Ensembl

synaptic vesicle transport

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentaxon

Inferred from electronic annotation. Source: Ensembl

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from direct assay Ref.20. Source: UniProtKB

dendrite

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

growth cone

Inferred from electronic annotation. Source: Ensembl

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functiondihydropyrimidinase 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 572572Dihydropyrimidinase-related protein 2
PRO_0000165913

Amino acid modifications

Modified residue321Phosphotyrosine; by FYN Ref.18
Modified residue2581N6-succinyllysine By similarity
Modified residue4311Phosphotyrosine By similarity
Modified residue4651Phosphoserine By similarity
Modified residue4991Phosphotyrosine By similarity
Modified residue5041S-nitrosocysteine By similarity
Modified residue5091Phosphothreonine Ref.10 Ref.15 Ref.16 Ref.23
Modified residue5141Phosphothreonine; by GSK3-beta Ref.23
Modified residue5171Phosphoserine Ref.23
Modified residue5181Phosphoserine Ref.10 Ref.23
Modified residue5221Phosphoserine; by DYRK2 Ref.10 Ref.12 Ref.15 Ref.23
Modified residue5551Phosphothreonine; by ROCK2 By similarity

Natural variations

Alternative sequence1 – 3636Missing in isoform 2.
VSP_044941
Natural variant1181A → T.
Corresponds to variant rs2289593 [ dbSNP | Ensembl ].
VAR_022016
Natural variant4811R → C in a colorectal cancer sample; somatic mutation. Ref.25
VAR_036316

Experimental info

Mutagenesis711D → N: Inhibits axon outgrowth formation in hippocampal neurons and decreases binding to CYFIP1. Ref.13
Mutagenesis5071S → A: No effect. Ref.10
Mutagenesis5091T → A: Greatly diminishes binding to 3F4 antibody. Ref.10
Mutagenesis5121T → A: No effect. Ref.10
Mutagenesis5141T → A: No effect. Ref.10
Mutagenesis5171S → A: No effect. Ref.10
Mutagenesis5181S → A: Greatly diminishes binding to 3F4 antibody. Ref.10
Mutagenesis5211T → A: No effect. Ref.10
Mutagenesis5221S → A: Greatly diminishes binding to 3F4 antibody. Ref.10

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 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

Isoform 2 [UniParc].

Checksum: 31806BFCB5FAE16D
Show »

FASTA53658,163

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] [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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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.
[19]"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.
[20]"Collapsin response mediator protein-2 (Crmp2) regulates trafficking by linking endocytic regulatory proteins to dynein motors."
Rahajeng J., Giridharan S.S., Naslavsky N., Caplan S.
J. Biol. Chem. 285:31918-31922(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ENDOCYTOSIS, INTERACTION WITH MICALL1, SUBCELLULAR LOCATION.
[21]"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.
[22]"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].
[23]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"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.
[25]"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] [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.
PIRJC5317.
RefSeqNP_001184222.1. NM_001197293.2.
NP_001231533.1. NM_001244604.1.
NP_001377.1. NM_001386.5.
UniGeneHs.593187.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GSEX-ray2.40A/B/C/D13-490[»]
2VM8X-ray1.90A/B/C/D13-490[»]
ProteinModelPortalQ16555.
SMRQ16555. Positions 14-490.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108142. 25 interactions.
IntActQ16555. 13 interactions.
MINTMINT-3032752.
STRING9606.ENSP00000309539.

Protein family/group databases

MEROPSM38.975.

PTM databases

PhosphoSiteQ16555.

Polymorphism databases

DMDM3122051.

2D gel databases

REPRODUCTION-2DPAGEIPI00257508.
Q16555.
UCD-2DPAGEQ16555.

Proteomic databases

PaxDbQ16555.
PeptideAtlasQ16555.
PRIDEQ16555.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000311151; ENSP00000309539; ENSG00000092964. [Q16555-1]
ENST00000521913; ENSP00000427985; ENSG00000092964. [Q16555-2]
ENST00000523027; ENSP00000431117; ENSG00000092964. [Q16555-2]
GeneID1808.
KEGGhsa:1808.
UCSCuc003xfb.2. human. [Q16555-1]

Organism-specific databases

CTD1808.
GeneCardsGC08P026371.
HGNCHGNC:3014. DPYSL2.
HPACAB018719.
HPA002381.
MIM602463. gene.
neXtProtNX_Q16555.
PharmGKBPA27472.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0044.
HOVERGENHBG000806.
InParanoidQ16555.
KOK07528.
OMAEVPAFFK.
OrthoDBEOG7SJD48.
PhylomeDBQ16555.
TreeFamTF314706.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.

Gene expression databases

ArrayExpressQ16555.
BgeeQ16555.
CleanExHS_DPYSL2.
GenevestigatorQ16555.

Family and domain databases

InterProIPR006680. Amidohydro_1.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMSSF51338. SSF51338. 2 hits.
TIGRFAMsTIGR02033. D-hydantoinase. 1 hit.
ProtoNetSearch...

Other

ChiTaRSDPYSL2. human.
EvolutionaryTraceQ16555.
GeneWikiDPYSL2.
GenomeRNAi1808.
NextBio7369.
PROQ16555.
SOURCESearch...

Entry information

Entry nameDPYL2_HUMAN
AccessionPrimary (citable) accession number: Q16555
Secondary accession number(s): A8K5H2 expand/collapse secondary AC list , B4DR31, D3DSS7, O00424
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: March 19, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

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