O00423 · EMAL1_HUMAN
- ProteinEchinoderm microtubule-associated protein-like 1
- GeneEML1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids815 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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 | cytosol | |
Cellular Component | microtubule | |
Cellular Component | microtubule associated complex | |
Cellular Component | mitotic spindle midzone | |
Cellular Component | mitotic spindle pole | |
Cellular Component | perinuclear region of cytoplasm | |
Molecular Function | calcium ion binding | |
Molecular Function | microtubule binding | |
Molecular Function | tubulin binding | |
Biological Process | brain development | |
Biological Process | hematopoietic progenitor cell differentiation | |
Biological Process | microtubule cytoskeleton organization | |
Biological Process | mitotic spindle organization | |
Biological Process | neuroblast proliferation |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEchinoderm microtubule-associated protein-like 1
- Short namesEMAP-1; HuEMAP-1
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO00423
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Enriched in perinuclear regions during interphase and in the region of spindle microtubules during metaphase. Enriched at the midzone during telophase and cytokinesis. Detected at growth cones in neurons (By similarity).
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Band heterotopia (BH)
- Note
- DescriptionA brain malformation of the lissencephaly spectrum, resulting from disordered neuronal migration and characterized by bands of gray matter interposed in the central white matter. Disease features include severe developmental delay with intellectual disability, enlarged head circumference, periventricular and ribbon-like subcortical heterotopia, polymicrogyria and agenesis of the corpus callosum.
- See alsoMIM:600348
Natural variants in BH
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_071075 | 225 | W>R | in BH; dbSNP:rs886037937 | |
VAR_071076 | 243 | T>A | in BH; decreased microtubule-binding; dbSNP:rs886037936 | |
VAR_081119 | 523-815 | missing | in BH |
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 59-61 | No effect on tubulin binding. Does not disrupt self-association. Decreased association with microtubules. | ||||
Sequence: LAD → AAA | ||||||
Mutagenesis | 192 | Abolishes tubulin binding; when associated with S-194; A-547; T-626; S-627; A-646 and A-786. | ||||
Sequence: R → S | ||||||
Mutagenesis | 194 | Abolishes tubulin binding; when associated with S-192; A-547; T-626; S-627; A-646 and A-786. | ||||
Sequence: R → S | ||||||
Natural variant | VAR_071075 | 225 | in BH; dbSNP:rs886037937 | |||
Sequence: W → R | ||||||
Natural variant | VAR_071076 | 243 | in BH; decreased microtubule-binding; dbSNP:rs886037936 | |||
Sequence: T → A | ||||||
Natural variant | VAR_031720 | 377 | in dbSNP:rs34198557 | |||
Sequence: A → V | ||||||
Natural variant | VAR_081119 | 523-815 | in BH | |||
Sequence: Missing | ||||||
Mutagenesis | 547 | Abolishes tubulin binding; when associated with S-192; S-194; T-626; S-627; A-646 and A-786. | ||||
Sequence: W → A | ||||||
Natural variant | VAR_031721 | 552 | in dbSNP:rs17853154 | |||
Sequence: H → N | ||||||
Natural variant | VAR_031722 | 556 | in dbSNP:rs2250718 | |||
Sequence: S → P | ||||||
Mutagenesis | 626 | Abolishes tubulin binding; when associated with S-192; S-194; A-547; S-627; A-646 and A-786. | ||||
Sequence: N → T | ||||||
Mutagenesis | 627 | Abolishes tubulin binding; when associated with S-192; S-194; A-547; T-626; A-646 and A-786. | ||||
Sequence: E → S | ||||||
Mutagenesis | 646 | Abolishes tubulin binding; when associated with S-192; S-194; A-547; T-626; S-627 and A-786. | ||||
Sequence: H → A | ||||||
Mutagenesis | 786 | Abolishes tubulin binding; when associated with S-192; S-194; A-547; T-626; S-627 and A-646. | ||||
Sequence: H → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 883 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000050961 | 1-815 | UniProt | Echinoderm microtubule-associated protein-like 1 | |||
Sequence: MEDGFSSYSSLYDTSSLLQFCNDDSASAASSMEVTDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRKGPTKARPLMQTLPLRTTVNNGTVLPKKPTGSLPSPSGVRKETAVPATKSNIKRTSSSERVSPGGRRESNGDSRGNRNRTGSTSSSSSGKKNSESKPKEPVFSAEEGYVKMFLRGRPVTMYMPKDQVDSYSLEAKVELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNVEEQLQRHYAGHNDDVKCLAVHPDRITIATGQVAGTSKDGKQLPPHVRIWDSVTLNTLHVIGIGFFDRAVTCIAFSKSNGGTNLCAVDDSNDHVLSVWDWQKEEKLADVKCSNEAVFAADFHPTDTNIIVTCGKSHLYFWTLEGSSLNKKQGLFEKQEKPKFVLCVTFSENGDTITGDSSGNILVWGKGTNRISYAVQGAHEGGIFALCMLRDGTLVSGGGKDRKLISWSGNYQKLRKTEIPEQFGPIRTVAEGKGDVILIGTTRNFVLQGTLSGDFTPITQGHTDELWGLAIHASKSQFLTCGHDKHATLWDAVGHRPVWDKIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVSDNGRKYTRVGKCSGHSSFITHLDWSVNSQFLVSNSGDYEILYWVPSACKQVVSVETTRDIEWATYTCTLGFHVFGVWPEGSDGTDINAVCRAHEKKLLSTGDDFGKVHLFSYPCSQFRAPSHIYGGHSSHVTNVDFLCEDSHLISTGGKDTSIMQWRVI | |||||||
Modified residue | 113 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 113 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 115 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 133 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 135 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 140 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 160 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Does not interact with EML3 (PubMed:25740311).
Binds repolymerizing microtubules (PubMed:24859200).
Binds unpolymerized tubulins via its WD repeat region (PubMed:24706829).
Interacts with TASOR (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O00423 | CASP6 P55212 | 3 | EBI-751327, EBI-718729 | |
BINARY | O00423 | FXR1 P51114 | 2 | EBI-751327, EBI-713291 | |
BINARY | O00423 | ISG20L2 Q9H9L3 | 3 | EBI-751327, EBI-751335 | |
BINARY | O00423 | LAMP2 P13473-2 | 3 | EBI-751327, EBI-21591415 | |
BINARY | O00423 | NUDC Q9Y266 | 2 | EBI-751327, EBI-357298 | |
BINARY | O00423 | STIP1 P31948 | 3 | EBI-751327, EBI-1054052 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for coiled coil, region, compositional bias, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 31-72 | |||||
Sequence: SMEVTDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQ | ||||||
Region | 77-179 | Disordered | ||||
Sequence: NRKGPTKARPLMQTLPLRTTVNNGTVLPKKPTGSLPSPSGVRKETAVPATKSNIKRTSSSERVSPGGRRESNGDSRGNRNRTGSTSSSSSGKKNSESKPKEPV | ||||||
Compositional bias | 89-108 | Polar residues | ||||
Sequence: QTLPLRTTVNNGTVLPKKPT | ||||||
Compositional bias | 126-142 | Polar residues | ||||
Sequence: TKSNIKRTSSSERVSPG | ||||||
Compositional bias | 153-169 | Polar residues | ||||
Sequence: GNRNRTGSTSSSSSGKK | ||||||
Region | 176-815 | Tandem atypical propeller in EMLs | ||||
Sequence: KEPVFSAEEGYVKMFLRGRPVTMYMPKDQVDSYSLEAKVELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNVEEQLQRHYAGHNDDVKCLAVHPDRITIATGQVAGTSKDGKQLPPHVRIWDSVTLNTLHVIGIGFFDRAVTCIAFSKSNGGTNLCAVDDSNDHVLSVWDWQKEEKLADVKCSNEAVFAADFHPTDTNIIVTCGKSHLYFWTLEGSSLNKKQGLFEKQEKPKFVLCVTFSENGDTITGDSSGNILVWGKGTNRISYAVQGAHEGGIFALCMLRDGTLVSGGGKDRKLISWSGNYQKLRKTEIPEQFGPIRTVAEGKGDVILIGTTRNFVLQGTLSGDFTPITQGHTDELWGLAIHASKSQFLTCGHDKHATLWDAVGHRPVWDKIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVSDNGRKYTRVGKCSGHSSFITHLDWSVNSQFLVSNSGDYEILYWVPSACKQVVSVETTRDIEWATYTCTLGFHVFGVWPEGSDGTDINAVCRAHEKKLLSTGDDFGKVHLFSYPCSQFRAPSHIYGGHSSHVTNVDFLCEDSHLISTGGKDTSIMQWRVI | ||||||
Repeat | 261-310 | WD 1 | ||||
Sequence: EQLQRHYAGHNDDVKCLAVHPDRITIATGQVAGTSKDGKQLPPHVRIWDS | ||||||
Repeat | 315-358 | WD 2 | ||||
Sequence: TLHVIGIGFFDRAVTCIAFSKSNGGTNLCAVDDSNDHVLSVWDW | ||||||
Repeat | 363-400 | WD 3 | ||||
Sequence: KLADVKCSNEAVFAADFHPTDTNIIVTCGKSHLYFWTL | ||||||
Repeat | 409-446 | WD 4 | ||||
Sequence: QGLFEKQEKPKFVLCVTFSENGDTITGDSSGNILVWGK | ||||||
Repeat | 450-489 | WD 5 | ||||
Sequence: RISYAVQGAHEGGIFALCMLRDGTLVSGGGKDRKLISWSG | ||||||
Repeat | 493-530 | WD 6 | ||||
Sequence: KLRKTEIPEQFGPIRTVAEGKGDVILIGTTRNFVLQGT | ||||||
Repeat | 535-572 | WD 7 | ||||
Sequence: FTPITQGHTDELWGLAIHASKSQFLTCGHDKHATLWDA | ||||||
Repeat | 578-613 | WD 8 | ||||
Sequence: VWDKIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDT | ||||||
Repeat | 617-655 | WD 9 | ||||
Sequence: DLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGV | ||||||
Repeat | 664-701 | WD 10 | ||||
Sequence: RVGKCSGHSSFITHLDWSVNSQFLVSNSGDYEILYWVP | ||||||
Repeat | 709-768 | WD 11 | ||||
Sequence: SVETTRDIEWATYTCTLGFHVFGVWPEGSDGTDINAVCRAHEKKLLSTGDDFGKVHLFSY | ||||||
Repeat | 775-814 | WD 12 | ||||
Sequence: APSHIYGGHSSHVTNVDFLCEDSHLISTGGKDTSIMQWRV |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
O00423-1
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
- Length815
- Mass (Da)89,861
- Last updated2009-07-28 v3
- ChecksumA1476F75F3537205
O00423-3
- Name3
- Differences from canonical
- 127-127: K → KRLNRSVSLLNACKLNRSTP
Computationally mapped potential isoform sequences
There are 15 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H0YJS9 | H0YJS9_HUMAN | EML1 | 66 | ||
H0YJK4 | H0YJK4_HUMAN | EML1 | 121 | ||
H0YJD8 | H0YJD8_HUMAN | EML1 | 76 | ||
H0YJY3 | H0YJY3_HUMAN | EML1 | 182 | ||
F8W717 | F8W717_HUMAN | EML1 | 803 | ||
G3V538 | G3V538_HUMAN | EML1 | 156 | ||
G3V4U5 | G3V4U5_HUMAN | EML1 | 85 | ||
G3V5C8 | G3V5C8_HUMAN | EML1 | 92 | ||
G3V497 | G3V497_HUMAN | EML1 | 107 | ||
G3V4H6 | G3V4H6_HUMAN | EML1 | 128 | ||
G3V500 | G3V500_HUMAN | EML1 | 285 | ||
G3V3J1 | G3V3J1_HUMAN | EML1 | 85 | ||
G3V3N9 | G3V3N9_HUMAN | EML1 | 379 | ||
A0A8V8TKR4 | A0A8V8TKR4_HUMAN | EML1 | 72 | ||
A0A3B3IU69 | A0A3B3IU69_HUMAN | EML1 | 840 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 89-108 | Polar residues | ||||
Sequence: QTLPLRTTVNNGTVLPKKPT | ||||||
Sequence conflict | 93-95 | in Ref. 1; AAB57824 | ||||
Sequence: LRT → FRS | ||||||
Sequence conflict | 106 | in Ref. 1; AAB57824 | ||||
Sequence: K → I | ||||||
Sequence conflict | 117 | in Ref. 1; AAB57824 | ||||
Sequence: V → F | ||||||
Sequence conflict | 120 | in Ref. 1; AAB57824 | ||||
Sequence: E → D | ||||||
Compositional bias | 126-142 | Polar residues | ||||
Sequence: TKSNIKRTSSSERVSPG | ||||||
Alternative sequence | VSP_024476 | 127 | in isoform 3 | |||
Sequence: K → KRLNRSVSLLNACKLNRSTP | ||||||
Compositional bias | 153-169 | Polar residues | ||||
Sequence: GNRNRTGSTSSSSSGKK | ||||||
Sequence conflict | 189 | in Ref. 1; AAB57824 | ||||
Sequence: M → L | ||||||
Sequence conflict | 464-465 | in Ref. 1; AAB57824 and 2; CAD12600 | ||||
Sequence: FA → SP | ||||||
Sequence conflict | 499-500 | in Ref. 4; CAD62313 | ||||
Sequence: IP → VS |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U97018 EMBL· GenBank· DDBJ | AAB57824.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AJ420603 EMBL· GenBank· DDBJ | CAD12600.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ428183 EMBL· GenBank· DDBJ | CAD12600.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ428184 EMBL· GenBank· DDBJ | CAD12600.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ428185 EMBL· GenBank· DDBJ | CAD12600.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ428189 EMBL· GenBank· DDBJ | CAD12600.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ428191 EMBL· GenBank· DDBJ | CAD12600.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ428193 EMBL· GenBank· DDBJ | CAD12600.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ428195 EMBL· GenBank· DDBJ | CAD12600.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ428197 EMBL· GenBank· DDBJ | CAD12600.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ496645 EMBL· GenBank· DDBJ | CAD12600.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ496644 EMBL· GenBank· DDBJ | CAD12600.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ428200 EMBL· GenBank· DDBJ | CAD12600.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ428199 EMBL· GenBank· DDBJ | CAD12600.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ428198 EMBL· GenBank· DDBJ | CAD12600.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ428196 EMBL· GenBank· DDBJ | CAD12600.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ428194 EMBL· GenBank· DDBJ | CAD12600.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ428192 EMBL· GenBank· DDBJ | CAD12600.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ428190 EMBL· GenBank· DDBJ | CAD12600.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ428188 EMBL· GenBank· DDBJ | CAD12600.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ428187 EMBL· GenBank· DDBJ | CAD12600.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ428186 EMBL· GenBank· DDBJ | CAD12600.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC032541 EMBL· GenBank· DDBJ | AAH32541.1 EMBL· GenBank· DDBJ | mRNA | ||
BC033043 EMBL· GenBank· DDBJ | AAH33043.1 EMBL· GenBank· DDBJ | mRNA | ||
BX247979 EMBL· GenBank· DDBJ | CAD62313.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |