SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q14194

- DPYL1_HUMAN

UniProt

Q14194 - DPYL1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Dihydropyrimidinase-related protein 1
Gene
CRMP1, DPYSL1, ULIP3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. May participate in cytokinesis.2 Publications

GO - Molecular functioni

  1. hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides Source: InterPro
  2. protein binding Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. axon guidance Source: Reactome
  2. nervous system development Source: ProtInc
  3. nucleobase-containing compound metabolic process Source: ProtInc
  4. pyrimidine nucleobase catabolic process Source: InterPro
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_19199. CRMPs in Sema3A signaling.

Protein family/group databases

MEROPSiM38.974.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydropyrimidinase-related protein 1
Short name:
DRP-1
Alternative name(s):
Collapsin response mediator protein 1
Short name:
CRMP-1
Unc-33-like phosphoprotein 3
Short name:
ULIP-3
Gene namesi
Name:CRMP1
Synonyms:DPYSL1, ULIP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:2365. CRMP1.

Subcellular locationi

Cytoplasm. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle
Note: Associated with centrosomes and the mitotic spindle during metaphase.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. dendrite Source: Ensembl
  4. microtubule organizing center Source: UniProtKB-SubCell
  5. neuronal cell body Source: Ensembl
  6. spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi101 – 1022TT → AA: 2.5-fold increase in cells with a defect of cytokinesis. 1 Publication

Organism-specific databases

PharmGKBiPA26885.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 572572Dihydropyrimidinase-related protein 1
PRO_0000165909Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei101 – 1011Phosphothreonine; by AURKA1 Publication
Modified residuei102 – 1021Phosphothreonine; by AURKA1 Publication
Modified residuei316 – 3161Nitrated tyrosine By similarity
Modified residuei504 – 5041Phosphotyrosine By similarity
Modified residuei509 – 5091Phosphothreonine By similarity

Keywords - PTMi

Nitration, Phosphoprotein

Proteomic databases

MaxQBiQ14194.
PaxDbiQ14194.
PRIDEiQ14194.

PTM databases

PhosphoSiteiQ14194.

Expressioni

Tissue specificityi

Brain.

Gene expression databases

ArrayExpressiQ14194.
BgeeiQ14194.
CleanExiHS_CRMP1.
GenevestigatoriQ14194.

Organism-specific databases

HPAiHPA035640.

Interactioni

Subunit structurei

Homotetramer, and heterotetramer with DPYSL2, DPYSL3, DPYSL4 or DPYSL5. Interacts with PLXNA1 By similarity.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
AXIN1O151692EBI-473101,EBI-710484
HTTP428582EBI-473101,EBI-466029
VIMP086703EBI-473101,EBI-353844

Protein-protein interaction databases

BioGridi107790. 83 interactions.
IntActiQ14194. 71 interactions.
MINTiMINT-1423114.
STRINGi9606.ENSP00000321606.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 2510
Beta strandi30 – 389
Beta strandi41 – 488
Beta strandi53 – 597
Beta strandi64 – 674
Beta strandi69 – 746
Helixi89 – 9911
Beta strandi101 – 1088
Helixi116 – 13015
Beta strandi132 – 1409
Helixi148 – 15710
Beta strandi163 – 1708
Turni171 – 1744
Helixi178 – 19013
Beta strandi194 – 1985
Helixi202 – 21312
Turni214 – 2163
Helixi221 – 2255
Helixi229 – 24618
Beta strandi250 – 2556
Helixi258 – 27013
Beta strandi274 – 2796
Helixi280 – 2845
Helixi288 – 2914
Helixi295 – 3006
Helixi313 – 32210
Helixi338 – 3414
Helixi342 – 3443
Helixi348 – 3503
Turni358 – 3603
Helixi361 – 3699
Turni370 – 3734
Helixi377 – 3848
Helixi386 – 3916
Turni395 – 3973
Beta strandi409 – 41911
Beta strandi426 – 4305
Turni433 – 4364
Beta strandi438 – 44811
Beta strandi451 – 4555
Helixi476 – 48914

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B3ZX-ray3.05A/B/C/D1-572[»]
ProteinModelPortaliQ14194.
SMRiQ14194. Positions 15-490.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0044.
HOGENOMiHOG000219145.
HOVERGENiHBG000806.
OMAiEDIHTGT.
OrthoDBiEOG7SJD48.
PhylomeDBiQ14194.
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: Q14194-1) [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

MSYQGKKSIP HITSDRLLIK GGRIINDDQS LYADVYLEDG LIKQIGENLI    50
VPGGVKTIEA NGRMVIPGGI DVNTYLQKPS QGMTAADDFF QGTRAALVGG 100
TTMIIDHVVP EPGSSLLTSF EKWHEAADTK SCCDYSLHVD ITSWYDGVRE 150
ELEVLVQDKG VNSFQVYMAY KDVYQMSDSQ LYEAFTFLKG LGAVILVHAE 200
NGDLIAQEQK RILEMGITGP EGHALSRPEE LEAEAVFRAI TIAGRINCPV 250
YITKVMSKSA ADIIALARKK GPLVFGEPIA ASLGTDGTHY WSKNWAKAAA 300
FVTSPPLSPD PTTPDYLTSL LACGDLQVTG SGHCPYSTAQ KAVGKDNFTL 350
IPEGVNGIEE RMTVVWDKAV ATGKMDENQF VAVTSTNAAK IFNLYPRKGR 400
IAVGSDADVV IWDPDKLKTI TAKSHKSAVE YNIFEGMECH GSPLVVISQG 450
KIVFEDGNIN VNKGMGRFIP RKAFPEHLYQ RVKIRNKVFG LQGVSRGMYD 500
GPVYEVPATP KYATPAPSAK SSPSKHQPPP IRNLHQSNFS LSGAQIDDNN 550
PRRTGHRIVA PPGGRSNITS LG 572
Length:572
Mass (Da):62,184
Last modified:November 1, 1996 - v1
Checksum:iA5385FCC79328A30
GO
Isoform LCRMP-1 (identifier: Q14194-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: MSYQGKKSIPHIT → MADRRRAWNT...DLPLGRDNGQ

Show »
Length:686
Mass (Da):74,262
Checksum:i2C897F656E5F34FA
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti461 – 4611V → I.
Corresponds to variant rs34611001 [ dbSNP | Ensembl ].
VAR_037745

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1313MSYQG…IPHIT → MADRRRAWNTEDDLPVYLAR PGSAAQTPRQKYGGMFAAVE GAYENKTIDFDAYSVGRRGS ARTPRSAGRPDAVGLPGPGG SEDTASDVSEPSGSAVSSPG ERDERPPTLRIRRPAPRDLP LGRDNGQ in isoform LCRMP-1.
VSP_042545Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti351 – 37020Missing in AAK55500. 1 Publication
Add
BLAST
Sequence conflicti504 – 5041Y → H in AAA93201. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D78012 mRNA. Translation: BAA11190.1.
DQ206871 mRNA. Translation: ABB22046.1.
BT006806 mRNA. Translation: AAP35452.1.
AC105915 Genomic DNA. Translation: AAY40959.1.
CH471131 Genomic DNA. Translation: EAW82405.1.
CH471131 Genomic DNA. Translation: EAW82407.1.
BC000252 mRNA. Translation: AAH00252.1.
BC007613 mRNA. Translation: AAH07613.1.
AH010780 Genomic DNA. Translation: AAK55500.1.
U17278 mRNA. Translation: AAA93201.1.
CCDSiCCDS33950.1. [Q14194-2]
CCDS43207.1. [Q14194-1]
PIRiJC5316.
RefSeqiNP_001014809.1. NM_001014809.2. [Q14194-2]
NP_001275590.1. NM_001288661.1.
NP_001275591.1. NM_001288662.1.
NP_001304.1. NM_001313.4. [Q14194-1]
UniGeneiHs.135270.

Genome annotation databases

EnsembliENST00000324989; ENSP00000321606; ENSG00000072832. [Q14194-2]
ENST00000397890; ENSP00000380987; ENSG00000072832. [Q14194-1]
GeneIDi1400.
KEGGihsa:1400.
UCSCiuc003giq.3. human. [Q14194-1]
uc003gis.3. human. [Q14194-2]

Polymorphism databases

DMDMi3122031.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D78012 mRNA. Translation: BAA11190.1 .
DQ206871 mRNA. Translation: ABB22046.1 .
BT006806 mRNA. Translation: AAP35452.1 .
AC105915 Genomic DNA. Translation: AAY40959.1 .
CH471131 Genomic DNA. Translation: EAW82405.1 .
CH471131 Genomic DNA. Translation: EAW82407.1 .
BC000252 mRNA. Translation: AAH00252.1 .
BC007613 mRNA. Translation: AAH07613.1 .
AH010780 Genomic DNA. Translation: AAK55500.1 .
U17278 mRNA. Translation: AAA93201.1 .
CCDSi CCDS33950.1. [Q14194-2 ]
CCDS43207.1. [Q14194-1 ]
PIRi JC5316.
RefSeqi NP_001014809.1. NM_001014809.2. [Q14194-2 ]
NP_001275590.1. NM_001288661.1.
NP_001275591.1. NM_001288662.1.
NP_001304.1. NM_001313.4. [Q14194-1 ]
UniGenei Hs.135270.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4B3Z X-ray 3.05 A/B/C/D 1-572 [» ]
ProteinModelPortali Q14194.
SMRi Q14194. Positions 15-490.
ModBasei Search...

Protein-protein interaction databases

BioGridi 107790. 83 interactions.
IntActi Q14194. 71 interactions.
MINTi MINT-1423114.
STRINGi 9606.ENSP00000321606.

Protein family/group databases

MEROPSi M38.974.

PTM databases

PhosphoSitei Q14194.

Polymorphism databases

DMDMi 3122031.

Proteomic databases

MaxQBi Q14194.
PaxDbi Q14194.
PRIDEi Q14194.

Protocols and materials databases

DNASUi 1400.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000324989 ; ENSP00000321606 ; ENSG00000072832 . [Q14194-2 ]
ENST00000397890 ; ENSP00000380987 ; ENSG00000072832 . [Q14194-1 ]
GeneIDi 1400.
KEGGi hsa:1400.
UCSCi uc003giq.3. human. [Q14194-1 ]
uc003gis.3. human. [Q14194-2 ]

Organism-specific databases

CTDi 1400.
GeneCardsi GC04M005815.
HGNCi HGNC:2365. CRMP1.
HPAi HPA035640.
MIMi 602462. gene.
neXtProti NX_Q14194.
PharmGKBi PA26885.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0044.
HOGENOMi HOG000219145.
HOVERGENi HBG000806.
OMAi EDIHTGT.
OrthoDBi EOG7SJD48.
PhylomeDBi Q14194.
TreeFami TF314706.

Enzyme and pathway databases

Reactomei REACT_19199. CRMPs in Sema3A signaling.

Miscellaneous databases

ChiTaRSi CRMP1. human.
GeneWikii CRMP1.
GenomeRNAii 1400.
NextBioi 5731.
PROi Q14194.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q14194.
Bgeei Q14194.
CleanExi HS_CRMP1.
Genevestigatori Q14194.

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. "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.
  2. "Long form collapsin response mediator protein-1 (LCRMP-1) expression is associated with clinical outcome and lymph node metastasis in non-small cell lung cancer patients."
    Pan S.-H., Chao Y.-C., Chen H.Y., Hung P.F., Lin P.Y., Lin C.W., Chang Y.L., Wu C.T., Lee Y.C., Yang S.-C., Hong T.-M., Yang P.-C.
    Lung Cancer 67:93-100(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LCRMP-1), ALTERNATIVE SPLICING.
    Tissue: Lung adenocarcinoma.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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.
  7. "Genomic organization and localization of the human CRMP-1 gene."
    Torres R., Polymeropoulos M.H.
    DNA Res. 5:393-395(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-572 (ISOFORM 1).
  8. "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] OF 64-572 (ISOFORM 1).
    Tissue: Brain.
  9. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 44-56; 190-210; 246-254; 259-268; 346-361; 391-397; 452-463; 472-481; 488-511 AND 533-552, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  10. "Brain CRMP forms heterotetramers similar to liver dihydropyrimidinase."
    Wang L.H., Strittmatter S.M.
    J. Neurochem. 69:2261-2269(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH DPYSL2 AND DPYSL4.
  11. "Collapsin response mediator protein-1 and the invasion and metastasis of cancer cells."
    Shih J.-Y., Yang S.-C., Hong T.-M., Yuan A., Chen J.J.W., Yu C.-J., Chang Y.-L., Lee Y.-C., Peck K., Wu C.-W., Yang P.-C.
    J. Natl. Cancer Inst. 93:1392-1400(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  12. "From midbody protein-protein interaction network construction to novel regulators in cytokinesis."
    Chen T.C., Lee S.A., Hong T.M., Shih J.Y., Lai J.M., Chiou H.Y., Yang S.C., Chan C.H., Kao C.Y., Yang P.C., Huang C.Y.
    J. Proteome Res. 8:4943-4953(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT THR-101 AND THR-102, MUTAGENESIS OF 101-THR-THR-102.

Entry informationi

Entry nameiDPYL1_HUMAN
AccessioniPrimary (citable) accession number: Q14194
Secondary accession number(s): A0EJG6
, Q13024, Q4W5F1, Q96TC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: September 3, 2014
This is version 144 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

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.

Keywords - Technical termi

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

Documents

  1. Human chromosome 4
    Human chromosome 4: 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

Similar proteinsi