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Q16555

- DPYL2_HUMAN

UniProt

Q16555 - DPYL2_HUMAN

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Protein

Dihydropyrimidinase-related protein 2

Gene

DPYSL2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Molecular functioni

  1. dihydropyrimidinase activity Source: ProtInc

GO - Biological processi

  1. axon guidance Source: Reactome
  2. cytoskeleton organization Source: UniProtKB
  3. endocytosis Source: UniProtKB
  4. nervous system development Source: ProtInc
  5. nucleobase-containing compound metabolic process Source: ProtInc
  6. olfactory bulb development Source: Ensembl
  7. positive regulation of glutamate secretion Source: Ensembl
  8. pyrimidine nucleobase catabolic process Source: InterPro
  9. regulation of neuron differentiation Source: Ensembl
  10. response to amphetamine Source: Ensembl
  11. response to cocaine Source: Ensembl
  12. response to drug Source: Ensembl
  13. signal transduction Source: ProtInc
  14. spinal cord development Source: Ensembl
  15. synaptic vesicle transport Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Enzyme and pathway databases

ReactomeiREACT_19199. CRMPs in Sema3A signaling.
REACT_22365. Recycling pathway of L1.

Protein family/group databases

MEROPSiM38.975.

Names & Taxonomyi

Protein namesi
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 namesi
Name:DPYSL2
Synonyms:CRMP2, ULIP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:3014. DPYSL2.

Subcellular locationi

Cytoplasmcytosol 1 Publication. Cytoplasmcytoskeleton 1 Publication. Membrane 1 Publication
Note: Tightly but non-covalently associated with membranes.

GO - Cellular componenti

  1. axon Source: Ensembl
  2. cytoskeleton Source: UniProtKB-KW
  3. cytosol Source: UniProtKB
  4. dendrite Source: Ensembl
  5. extracellular vesicular exosome Source: UniProt
  6. growth cone Source: Ensembl
  7. membrane Source: UniProtKB-KW
  8. mitochondrion Source: Ensembl
  9. neuronal cell body Source: Ensembl
  10. protein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi71 – 711D → N: Inhibits axon outgrowth formation in hippocampal neurons and decreases binding to CYFIP1. 1 Publication
Mutagenesisi507 – 5071S → A: No effect. 1 Publication
Mutagenesisi509 – 5091T → A: Greatly diminishes binding to 3F4 antibody. 1 Publication
Mutagenesisi512 – 5121T → A: No effect. 1 Publication
Mutagenesisi514 – 5141T → A: No effect. 1 Publication
Mutagenesisi517 – 5171S → A: No effect. 1 Publication
Mutagenesisi518 – 5181S → A: Greatly diminishes binding to 3F4 antibody. 1 Publication
Mutagenesisi521 – 5211T → A: No effect. 1 Publication
Mutagenesisi522 – 5221S → A: Greatly diminishes binding to 3F4 antibody. 1 Publication

Organism-specific databases

PharmGKBiPA27472.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 572572Dihydropyrimidinase-related protein 2PRO_0000165913Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321Phosphotyrosine; by FYN1 Publication
Modified residuei258 – 2581N6-succinyllysineBy similarity
Modified residuei431 – 4311PhosphotyrosineBy similarity
Modified residuei465 – 4651PhosphoserineBy similarity
Modified residuei499 – 4991PhosphotyrosineBy similarity
Modified residuei504 – 5041S-nitrosocysteineBy similarity
Modified residuei509 – 5091Phosphothreonine4 Publications
Modified residuei514 – 5141Phosphothreonine; by GSK3-beta1 Publication
Modified residuei517 – 5171Phosphoserine1 Publication
Modified residuei518 – 5181Phosphoserine2 Publications
Modified residuei522 – 5221Phosphoserine; by DYRK24 Publications
Modified residuei555 – 5551Phosphothreonine; by ROCK2By similarity

Post-translational modificationi

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-509.5 Publications
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.By similarity4 Publications

Keywords - PTMi

Phosphoprotein, S-nitrosylation

Proteomic databases

MaxQBiQ16555.
PaxDbiQ16555.
PeptideAtlasiQ16555.
PRIDEiQ16555.

2D gel databases

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

PTM databases

PhosphoSiteiQ16555.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ16555.
CleanExiHS_DPYSL2.
ExpressionAtlasiQ16555. baseline and differential.
GenevestigatoriQ16555.

Organism-specific databases

HPAiCAB018719.
HPA002381.

Interactioni

Subunit structurei

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 MICALL1.5 Publications

Protein-protein interaction databases

BioGridi108142. 34 interactions.
IntActiQ16555. 14 interactions.
MINTiMINT-3032752.
STRINGi9606.ENSP00000309539.

Structurei

Secondary structure

1
572
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 259Combined sources
Beta strandi30 – 389Combined sources
Beta strandi41 – 488Combined sources
Beta strandi53 – 553Combined sources
Beta strandi57 – 593Combined sources
Beta strandi64 – 674Combined sources
Beta strandi69 – 746Combined sources
Helixi89 – 9810Combined sources
Beta strandi101 – 1088Combined sources
Helixi116 – 13015Combined sources
Beta strandi132 – 1409Combined sources
Helixi146 – 15813Combined sources
Beta strandi163 – 1708Combined sources
Turni171 – 1733Combined sources
Helixi178 – 19114Combined sources
Beta strandi194 – 1985Combined sources
Helixi202 – 21312Combined sources
Turni214 – 2163Combined sources
Helixi221 – 2266Combined sources
Helixi229 – 24618Combined sources
Beta strandi250 – 2556Combined sources
Helixi258 – 26912Combined sources
Beta strandi274 – 2796Combined sources
Helixi280 – 2845Combined sources
Helixi287 – 2915Combined sources
Helixi295 – 3006Combined sources
Helixi313 – 32210Combined sources
Helixi338 – 3414Combined sources
Helixi342 – 3443Combined sources
Helixi348 – 3503Combined sources
Turni358 – 3603Combined sources
Helixi361 – 3699Combined sources
Turni370 – 3734Combined sources
Helixi377 – 3848Combined sources
Helixi386 – 3927Combined sources
Turni395 – 3973Combined sources
Beta strandi409 – 41911Combined sources
Turni422 – 4243Combined sources
Beta strandi425 – 4284Combined sources
Turni433 – 4364Combined sources
Beta strandi438 – 44811Combined sources
Beta strandi451 – 4555Combined sources
Helixi476 – 48712Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GSEX-ray2.40A/B/C/D13-490[»]
2VM8X-ray1.90A/B/C/D13-490[»]
ProteinModelPortaliQ16555.
SMRiQ16555. Positions 14-490.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16555.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0044.
GeneTreeiENSGT00760000119241.
HOVERGENiHBG000806.
InParanoidiQ16555.
KOiK07528.
OMAiEVPAFFK.
OrthoDBiEOG7SJD48.
PhylomeDBiQ16555.
TreeFamiTF314706.

Family and domain databases

Gene3Di2.30.40.10. 2 hits.
InterProiIPR006680. Amidohydro_1.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
TIGRFAMsiTIGR02033. D-hydantoinase. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q16555-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSYQGKKNIP RITSDRLLIK GGKIVNDDQS FYADIYMEDG LIKQIGENLI
60 70 80 90 100
VPGGVKTIEA HSRMVIPGGI DVHTRFQMPD QGMTSADDFF QGTKAALAGG
110 120 130 140 150
TTMIIDHVVP EPGTSLLAAF DQWREWADSK SCCDYSLHVD ISEWHKGIQE
160 170 180 190 200
EMEALVKDHG VNSFLVYMAF KDRFQLTDCQ IYEVLSVIRD IGAIAQVHAE
210 220 230 240 250
NGDIIAEEQQ RILDLGITGP EGHVLSRPEE VEAEAVNRAI TIANQTNCPL
260 270 280 290 300
YITKVMSKSS AEVIAQARKK GTVVYGEPIT ASLGTDGSHY WSKNWAKAAA
310 320 330 340 350
FVTSPPLSPD PTTPDFLNSL LSCGDLQVTG SAHCTFNTAQ KAVGKDNFTL
360 370 380 390 400
IPEGTNGTEE RMSVIWDKAV VTGKMDENQF VAVTSTNAAK VFNLYPRKGR
410 420 430 440 450
IAVGSDADLV IWDPDSVKTI SAKTHNSSLE YNIFEGMECR GSPLVVISQG
460 470 480 490 500
KIVLEDGTLH VTEGSGRYIP RKPFPDFVYK RIKARSRLAE LRGVPRGLYD
510 520 530 540 550
GPVCEVSVTP KTVTPASSAK TSPAKQQAPP VRNLHQSGFS LSGAQIDDNI
560 570
PRRTTQRIVA PPGGRANITS LG
Length:572
Mass (Da):62,294
Last modified:November 1, 1996 - v1
Checksum:i5CDB6CF7F5C308AD
GO
Isoform 2 (identifier: Q16555-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:536
Mass (Da):58,163
Checksum:i31806BFCB5FAE16D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti118 – 1181A → T.
Corresponds to variant rs2289593 [ dbSNP | Ensembl ].
VAR_022016
Natural varianti481 – 4811R → C in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036316

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3636Missing in isoform 2. 1 PublicationVSP_044941Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS59096.1. [Q16555-2]
CCDS6051.1. [Q16555-1]
PIRiJC5317.
RefSeqiNP_001184222.1. NM_001197293.2.
NP_001231533.1. NM_001244604.1. [Q16555-2]
NP_001377.1. NM_001386.5. [Q16555-1]
UniGeneiHs.593187.

Genome annotation databases

EnsembliENST00000311151; ENSP00000309539; ENSG00000092964. [Q16555-1]
ENST00000521913; ENSP00000427985; ENSG00000092964. [Q16555-2]
ENST00000523027; ENSP00000431117; ENSG00000092964. [Q16555-2]
GeneIDi1808.
KEGGihsa:1808.
UCSCiuc003xfb.2. human. [Q16555-1]

Polymorphism databases

DMDMi3122051.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS59096.1. [Q16555-2 ]
CCDS6051.1. [Q16555-1 ]
PIRi JC5317.
RefSeqi NP_001184222.1. NM_001197293.2.
NP_001231533.1. NM_001244604.1. [Q16555-2 ]
NP_001377.1. NM_001386.5. [Q16555-1 ]
UniGenei Hs.593187.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali Q16555.
SMRi Q16555. Positions 14-490.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108142. 34 interactions.
IntActi Q16555. 14 interactions.
MINTi MINT-3032752.
STRINGi 9606.ENSP00000309539.

Protein family/group databases

MEROPSi M38.975.

PTM databases

PhosphoSitei Q16555.

Polymorphism databases

DMDMi 3122051.

2D gel databases

REPRODUCTION-2DPAGE IPI00257508.
Q16555.
UCD-2DPAGE Q16555.

Proteomic databases

MaxQBi Q16555.
PaxDbi Q16555.
PeptideAtlasi Q16555.
PRIDEi Q16555.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000311151 ; ENSP00000309539 ; ENSG00000092964 . [Q16555-1 ]
ENST00000521913 ; ENSP00000427985 ; ENSG00000092964 . [Q16555-2 ]
ENST00000523027 ; ENSP00000431117 ; ENSG00000092964 . [Q16555-2 ]
GeneIDi 1808.
KEGGi hsa:1808.
UCSCi uc003xfb.2. human. [Q16555-1 ]

Organism-specific databases

CTDi 1808.
GeneCardsi GC08P026371.
HGNCi HGNC:3014. DPYSL2.
HPAi CAB018719.
HPA002381.
MIMi 602463. gene.
neXtProti NX_Q16555.
PharmGKBi PA27472.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0044.
GeneTreei ENSGT00760000119241.
HOVERGENi HBG000806.
InParanoidi Q16555.
KOi K07528.
OMAi EVPAFFK.
OrthoDBi EOG7SJD48.
PhylomeDBi Q16555.
TreeFami TF314706.

Enzyme and pathway databases

Reactomei REACT_19199. CRMPs in Sema3A signaling.
REACT_22365. Recycling pathway of L1.

Miscellaneous databases

ChiTaRSi DPYSL2. human.
EvolutionaryTracei Q16555.
GeneWikii DPYSL2.
GenomeRNAii 1808.
NextBioi 7369.
PROi Q16555.
SOURCEi Search...

Gene expression databases

Bgeei Q16555.
CleanExi HS_DPYSL2.
ExpressionAtlasi Q16555. baseline and differential.
Genevestigatori Q16555.

Family and domain databases

Gene3Di 2.30.40.10. 2 hits.
InterProi IPR006680. Amidohydro_1.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view ]
Pfami PF01979. Amidohydro_1. 1 hit.
[Graphical view ]
SUPFAMi SSF51338. SSF51338. 2 hits.
TIGRFAMsi TIGR02033. D-hydantoinase. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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, IDENTIFICATION BY 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. 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. 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. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-481.

Entry informationi

Entry nameiDPYL2_HUMAN
AccessioniPrimary (citable) accession number: Q16555
Secondary accession number(s): A8K5H2
, B4DR31, D3DSS7, O00424
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3