Q14194 · DPYL1_HUMAN
- ProteinDihydropyrimidinase-related protein 1
- GeneCRMP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids572 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton (PubMed:25358863).
Plays a role in axon guidance (PubMed:25358863).
During the axon guidance process, acts downstream of SEMA3A to promote FLNA dissociation from F-actin which results in the rearrangement of the actin cytoskeleton and the collapse of the growth cone (PubMed:25358863).
Involved in invasive growth and cell migration (PubMed:11562390).
May participate in cytokinesis (PubMed:19799413).
Plays a role in axon guidance (PubMed:25358863).
During the axon guidance process, acts downstream of SEMA3A to promote FLNA dissociation from F-actin which results in the rearrangement of the actin cytoskeleton and the collapse of the growth cone (PubMed:25358863).
Involved in invasive growth and cell migration (PubMed:11562390).
May participate in cytokinesis (PubMed:19799413).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | centrosome | |
Cellular Component | cytosol | |
Cellular Component | growth cone | |
Cellular Component | midbody | |
Cellular Component | perikaryon | |
Cellular Component | spindle | |
Molecular Function | filamin binding | |
Molecular Function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides | |
Molecular Function | identical protein binding | |
Biological Process | negative regulation of neuron projection development | |
Biological Process | nervous system development | |
Biological Process | nucleobase-containing compound metabolic process |
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameDihydropyrimidinase-related protein 1
- Short namesDRP-1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ14194
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Associated with centrosomes and the mitotic spindle during metaphase (PubMed:11562390).
Colocalizes with FLNA and tubulin in the central region of DRG neuron growth cone (By similarity).
Following SEMA3A stimulation of DRG neurons, colocalizes with F-actin (By similarity).
Colocalizes with FLNA and tubulin in the central region of DRG neuron growth cone (By similarity).
Following SEMA3A stimulation of DRG neurons, colocalizes with F-actin (By similarity).
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 101-102 | 2.5-fold increase in cells with a defect of cytokinesis. | ||||
Sequence: TT → AA | ||||||
Natural variant | VAR_037745 | 461 | in dbSNP:rs34611001 | |||
Sequence: V → I |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 719 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000165909 | 1-572 | UniProt | Dihydropyrimidinase-related protein 1 | |||
Sequence: MSYQGKKSIPHITSDRLLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPSQGMTAADDFFQGTRAALVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSWYDGVREELEVLVQDKGVNSFQVYMAYKDVYQMSDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRINCPVYITKVMSKSAADIIALARKKGPLVFGEPIAASLGTDGTHYWSKNWAKAAAFVTSPPLSPDPTTPDYLTSLLACGDLQVTGSGHCPYSTAQKAVGKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNINVNKGMGRFIPRKAFPEHLYQRVKIRNKVFGLQGVSRGMYDGPVYEVPATPKYATPAPSAKSSPSKHQPPPIRNLHQSNFSLSGAQIDDNNPRRTGHRIVAPPGGRSNITSLG | |||||||
Modified residue (large scale data) | 2 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 8 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 8 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 14 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 101 | UniProt | Phosphothreonine; by AURKA | ||||
Sequence: T | |||||||
Modified residue | 102 | UniProt | Phosphothreonine; by AURKA | ||||
Sequence: T | |||||||
Modified residue | 316 | UniProt | 3'-nitrotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 504 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 504 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 509 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 509 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 514 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 518 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 521 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 521 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 522 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 522 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 524 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 537 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 540 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 540 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 542 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 542 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylation at Ser-522 enhances CRMP1-mediated alteration of FLNA ternary structure and FLNA dissociation from F-actin.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Homotetramer, and heterotetramer with DPYSL2, DPYSL3, DPYSL4 or DPYSL5 (By similarity).
Interacts with PLXNA1 (By similarity).
Interacts with FLNA (via calponin-homology (CH) domain 1 and filamin repeat 24); the interaction alters FLNA ternary structure and thus promotes FLNA dissociation from F-actin (PubMed:25358863).
Interacts with PLXNA1 (By similarity).
Interacts with FLNA (via calponin-homology (CH) domain 1 and filamin repeat 24); the interaction alters FLNA ternary structure and thus promotes FLNA dissociation from F-actin (PubMed:25358863).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q14194 | AP3M1 Q9Y2T2 | 6 | EBI-473101, EBI-2371151 | |
BINARY | Q14194 | AXIN1 O15169 | 2 | EBI-473101, EBI-710484 | |
BINARY | Q14194 | BDNF P23560-2 | 3 | EBI-473101, EBI-12275524 | |
BINARY | Q14194 | CRMP1 Q14194 | 3 | EBI-473101, EBI-473101 | |
BINARY | Q14194 | CRYAB P02511 | 3 | EBI-473101, EBI-739060 | |
BINARY | Q14194 | DPYSL2 Q16555 | 5 | EBI-473101, EBI-1104711 | |
BINARY | Q14194 | DPYSL3 Q14195-2 | 6 | EBI-473101, EBI-10232496 | |
BINARY | Q14194 | GAPDH P04406 | 3 | EBI-473101, EBI-354056 | |
BINARY | Q14194 | HSP90AA1 P07900 | 3 | EBI-473101, EBI-296047 | |
BINARY | Q14194 | HTT P42858 | 14 | EBI-473101, EBI-466029 | |
BINARY | Q14194 | RACK1 P63244 | 3 | EBI-473101, EBI-296739 | |
BINARY | Q14194 | VIM P08670 | 3 | EBI-473101, EBI-353844 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for motif, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 246-247 | Required for interaction with FLNA | ||||
Sequence: IN | ||||||
Region | 513-572 | Disordered | ||||
Sequence: ATPAPSAKSSPSKHQPPPIRNLHQSNFSLSGAQIDDNNPRRTGHRIVAPPGGRSNITSLG | ||||||
Compositional bias | 515-549 | Polar residues | ||||
Sequence: PAPSAKSSPSKHQPPPIRNLHQSNFSLSGAQIDDN |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q14194-1
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.
- Name1
- Length572
- Mass (Da)62,184
- Last updated1996-11-01 v1
- ChecksumA5385FCC79328A30
Q14194-2
- NameLCRMP-1
- Differences from canonical
- 1-13: MSYQGKKSIPHIT → MADRRRAWNTEDDLPVYLARPGSAAQTPRQKYGGMFAAVEGAYENKTIDFDAYSVGRRGSARTPRSAGRPDAVGLPGPGGSEDTASDVSEPSGSAVSSPGERDERPPTLRIRRPAPRDLPLGRDNGQ
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E9PD68 | E9PD68_HUMAN | CRMP1 | 570 |
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_042545 | 1-13 | in isoform LCRMP-1 | |||
Sequence: MSYQGKKSIPHIT → MADRRRAWNTEDDLPVYLARPGSAAQTPRQKYGGMFAAVEGAYENKTIDFDAYSVGRRGSARTPRSAGRPDAVGLPGPGGSEDTASDVSEPSGSAVSSPGERDERPPTLRIRRPAPRDLPLGRDNGQ | ||||||
Sequence conflict | 351-370 | in Ref. 7; AAK55500 | ||||
Sequence: Missing | ||||||
Sequence conflict | 504 | in Ref. 8; AAA93201 | ||||
Sequence: Y → H | ||||||
Compositional bias | 515-549 | Polar residues | ||||
Sequence: PAPSAKSSPSKHQPPPIRNLHQSNFSLSGAQIDDN |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D78012 EMBL· GenBank· DDBJ | BAA11190.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ206871 EMBL· GenBank· DDBJ | ABB22046.1 EMBL· GenBank· DDBJ | mRNA | ||
BT006806 EMBL· GenBank· DDBJ | AAP35452.1 EMBL· GenBank· DDBJ | mRNA | ||
AC105915 EMBL· GenBank· DDBJ | AAY40959.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471131 EMBL· GenBank· DDBJ | EAW82405.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471131 EMBL· GenBank· DDBJ | EAW82407.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC000252 EMBL· GenBank· DDBJ | AAH00252.1 EMBL· GenBank· DDBJ | mRNA | ||
BC007613 EMBL· GenBank· DDBJ | AAH07613.1 EMBL· GenBank· DDBJ | mRNA | ||
AH010780 EMBL· GenBank· DDBJ | AAK55500.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U17278 EMBL· GenBank· DDBJ | AAA93201.1 EMBL· GenBank· DDBJ | mRNA |