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Protein

Echinoderm microtubule-associated protein-like 1

Gene

EML1

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

Functioni

Modulates the assembly and organization of the microtubule cytoskeleton, and probably plays a role in regulating the orientation of the mitotic spindle and the orientation of the plane of cell division. Required for normal proliferation of neuronal progenitor cells in the developing brain and for normal brain development. Does not affect neuron migration per se (By similarity).By similarity

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • tubulin binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:ENSG00000066629-MONOMER.
SignaLinkiO00423.

Names & Taxonomyi

Protein namesi
Recommended name:
Echinoderm microtubule-associated protein-like 1
Short name:
EMAP-1
Short name:
HuEMAP-1
Gene namesi
Name:EML1
Synonyms:EMAP1, EMAPL, EMAPL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:3330. EML1.

Subcellular locationi

  • Cytoplasm By similarity
  • Cytoplasmperinuclear region By similarity
  • Cytoplasmcytoskeleton By similarity

  • Note: Detected in cytoplasmic punctae. Co-localizes with microtubules. 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).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Involvement in diseasei

Mutations in this gene are associated with atypical heterotopia, epilepsy and mental retardation. Patients present giant bilateral periventricular and ribbon-like subcortical heterotopia with polymicrogyria and agenesis of the corpus callosum.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi59 – 61LAD → AAA: No effect on tubulin binding. 1 Publication3
Mutagenesisi192R → S: Abolishes tubulin binding; when associated with S-194; A-547; T-626; S-627; A-646 and A-786. 1 Publication1
Mutagenesisi194R → S: Abolishes tubulin binding; when associated with S-192; A-547; T-626; S-627; A-646 and A-786. 1 Publication1
Mutagenesisi547W → A: Abolishes tubulin binding; when associated with S-192; S-194; T-626; S-627; A-646 and A-786. 1 Publication1
Mutagenesisi626N → T: Abolishes tubulin binding; when associated with S-192; S-194; A-547; S-627; A-646 and A-786. 1 Publication1
Mutagenesisi627E → S: Abolishes tubulin binding; when associated with S-192; S-194; A-547; T-626; A-646 and A-786. 1 Publication1
Mutagenesisi646H → A: Abolishes tubulin binding; when associated with S-192; S-194; A-547; T-626; S-627 and A-786. 1 Publication1
Mutagenesisi786H → A: Abolishes tubulin binding; when associated with S-192; S-194; A-547; T-626; S-627 and A-646. 1 Publication1

Keywords - Diseasei

Disease mutation, Epilepsy, Mental retardation

Organism-specific databases

DisGeNETi2009.
OpenTargetsiENSG00000066629.
PharmGKBiPA27767.

Polymorphism and mutation databases

BioMutaiEML1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000509611 – 815Echinoderm microtubule-associated protein-like 1Add BLAST815

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei113PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO00423.
PaxDbiO00423.
PeptideAtlasiO00423.
PRIDEiO00423.

PTM databases

iPTMnetiO00423.
PhosphoSitePlusiO00423.

Expressioni

Tissue specificityi

Ubiquitous; expressed in most tissues with the exception of thymus and peripheral blood lymphocytes.1 Publication

Gene expression databases

BgeeiENSG00000066629.
CleanExiHS_EML1.
ExpressionAtlasiO00423. baseline and differential.
GenevisibleiO00423. HS.

Organism-specific databases

HPAiCAB033137.
HPA049105.

Interactioni

Subunit structurei

Binds repolymerizing microtubules (By similarity). Binds unpolymerized tubulins via its WD repeat region.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ISG20L2Q9H9L33EBI-751327,EBI-751335

GO - Molecular functioni

  • microtubule binding Source: UniProtKB
  • tubulin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108324. 13 interactors.
IntActiO00423. 3 interactors.
MINTiMINT-1457362.
STRINGi9606.ENSP00000334314.

Structurei

Secondary structure

1815
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi179 – 181Combined sources3
Turni182 – 185Combined sources4
Beta strandi186 – 199Combined sources14
Helixi202 – 205Combined sources4
Beta strandi220 – 227Combined sources8
Beta strandi238 – 240Combined sources3
Beta strandi246 – 250Combined sources5
Beta strandi253 – 258Combined sources6
Turni259 – 262Combined sources4
Beta strandi263 – 267Combined sources5
Beta strandi274 – 279Combined sources6
Beta strandi283 – 291Combined sources9
Beta strandi305 – 309Combined sources5
Turni310 – 312Combined sources3
Beta strandi315 – 319Combined sources5
Turni321 – 323Combined sources3
Beta strandi326 – 333Combined sources8
Beta strandi335 – 339Combined sources5
Beta strandi342 – 346Combined sources5
Beta strandi348 – 350Combined sources3
Beta strandi352 – 357Combined sources6
Helixi358 – 360Combined sources3
Beta strandi362 – 368Combined sources7
Beta strandi374 – 379Combined sources6
Beta strandi386 – 392Combined sources7
Beta strandi394 – 401Combined sources8
Beta strandi404 – 409Combined sources6
Beta strandi419 – 426Combined sources8
Beta strandi432 – 436Combined sources5
Beta strandi441 – 444Combined sources4
Beta strandi449 – 455Combined sources7
Beta strandi458 – 461Combined sources4
Beta strandi463 – 468Combined sources6
Beta strandi474 – 478Combined sources5
Turni479 – 481Combined sources3
Beta strandi483 – 487Combined sources5
Beta strandi493 – 498Combined sources6
Turni501 – 503Combined sources3
Beta strandi505 – 511Combined sources7
Beta strandi517 – 521Combined sources5
Beta strandi526 – 529Combined sources4
Beta strandi536 – 539Combined sources4
Beta strandi546 – 551Combined sources6
Beta strandi553 – 562Combined sources10
Beta strandi565 – 571Combined sources7
Turni572 – 575Combined sources4
Beta strandi576 – 582Combined sources7
Beta strandi587 – 592Combined sources6
Beta strandi596 – 612Combined sources17
Turni613 – 615Combined sources3
Beta strandi618 – 623Combined sources6
Beta strandi625 – 627Combined sources3
Beta strandi629 – 634Combined sources6
Beta strandi638 – 645Combined sources8
Beta strandi650 – 656Combined sources7
Turni657 – 660Combined sources4
Beta strandi661 – 668Combined sources8
Beta strandi675 – 681Combined sources7
Beta strandi687 – 691Combined sources5
Beta strandi697 – 700Combined sources4
Helixi701 – 703Combined sources3
Helixi710 – 713Combined sources4
Beta strandi724 – 726Combined sources3
Turni727 – 731Combined sources5
Beta strandi741 – 747Combined sources7
Beta strandi749 – 758Combined sources10
Beta strandi763 – 768Combined sources6
Beta strandi772 – 774Combined sources3
Beta strandi778 – 780Combined sources3
Beta strandi789 – 792Combined sources4
Beta strandi796 – 802Combined sources7
Beta strandi809 – 815Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4CI8X-ray2.60A/B167-815[»]
ProteinModelPortaliO00423.
SMRiO00423.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati269 – 318WD 1Add BLAST50
Repeati323 – 366WD 2Add BLAST44
Repeati369 – 408WD 3Add BLAST40
Repeati416 – 454WD 4Add BLAST39
Repeati458 – 497WD 5Add BLAST40
Repeati541 – 580WD 6Add BLAST40
Repeati582 – 621WD 7Add BLAST40
Repeati624 – 663WD 8Add BLAST40
Repeati670 – 709WD 9Add BLAST40
Repeati737 – 776WD 10Add BLAST40
Repeati782 – 815WD 11Add BLAST34

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni176 – 815Tandem atypical propeller in EMLsAdd BLAST640

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi160 – 166Poly-Ser7

Domaini

Contains a tandem atypical propeller in EMLs (TAPE) domain. The N-terminal beta-propeller is formed by canonical WD repeats; in contrast, the second beta-propeller contains one blade that is formed by discontinuous parts of the polypeptide chain.1 Publication

Sequence similaritiesi

Belongs to the WD repeat EMAP family.Curated
Contains 11 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG2106. Eukaryota.
ENOG410XNTQ. LUCA.
GeneTreeiENSGT00550000074369.
HOGENOMiHOG000294061.
HOVERGENiHBG051470.
InParanoidiO00423.
KOiK18595.
OMAiRKYTRVG.
OrthoDBiEOG091G04Z4.
PhylomeDBiO00423.
TreeFamiTF317832.

Family and domain databases

Gene3Di2.130.10.10. 3 hits.
InterProiIPR005108. HELP.
IPR011047. Quinoprotein_ADH-like_supfam.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF03451. HELP. 1 hit.
PF00400. WD40. 4 hits.
[Graphical view]
SMARTiSM00320. WD40. 10 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
SSF50998. SSF50998. 1 hit.
PROSITEiPS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O00423-1) [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
MEDGFSSYSS LYDTSSLLQF CNDDSASAAS SMEVTDRIAS LEQRVQMQED
60 70 80 90 100
DIQLLKSALA DVVRRLNITE EQQAVLNRKG PTKARPLMQT LPLRTTVNNG
110 120 130 140 150
TVLPKKPTGS LPSPSGVRKE TAVPATKSNI KRTSSSERVS PGGRRESNGD
160 170 180 190 200
SRGNRNRTGS TSSSSSGKKN SESKPKEPVF SAEEGYVKMF LRGRPVTMYM
210 220 230 240 250
PKDQVDSYSL EAKVELPTKR LKLEWVYGYR GRDCRNNLYL LPTGETVYFI
260 270 280 290 300
ASVVVLYNVE EQLQRHYAGH NDDVKCLAVH PDRITIATGQ VAGTSKDGKQ
310 320 330 340 350
LPPHVRIWDS VTLNTLHVIG IGFFDRAVTC IAFSKSNGGT NLCAVDDSND
360 370 380 390 400
HVLSVWDWQK EEKLADVKCS NEAVFAADFH PTDTNIIVTC GKSHLYFWTL
410 420 430 440 450
EGSSLNKKQG LFEKQEKPKF VLCVTFSENG DTITGDSSGN ILVWGKGTNR
460 470 480 490 500
ISYAVQGAHE GGIFALCMLR DGTLVSGGGK DRKLISWSGN YQKLRKTEIP
510 520 530 540 550
EQFGPIRTVA EGKGDVILIG TTRNFVLQGT LSGDFTPITQ GHTDELWGLA
560 570 580 590 600
IHASKSQFLT CGHDKHATLW DAVGHRPVWD KIIEDPAQSS GFHPSGSVVA
610 620 630 640 650
VGTLTGRWFV FDTETKDLVT VHTDGNEQLS VMRYSPDGNF LAIGSHDNCI
660 670 680 690 700
YIYGVSDNGR KYTRVGKCSG HSSFITHLDW SVNSQFLVSN SGDYEILYWV
710 720 730 740 750
PSACKQVVSV ETTRDIEWAT YTCTLGFHVF GVWPEGSDGT DINAVCRAHE
760 770 780 790 800
KKLLSTGDDF GKVHLFSYPC SQFRAPSHIY GGHSSHVTNV DFLCEDSHLI
810
STGGKDTSIM QWRVI
Length:815
Mass (Da):89,861
Last modified:July 28, 2009 - v3
Checksum:iA1476F75F3537205
GO
Isoform 3 (identifier: O00423-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     127-127: K → KRLNRSVSLLNACKLNRSTP

Note: No experimental confirmation available.
Show »
Length:834
Mass (Da):91,985
Checksum:i66B7AE5D761B3AA3
GO

Sequence cautioni

The sequence AAB57824 differs from that shown. Reason: Frameshift at positions 168, 392, 405, 414 and 420.Curated
The sequence CAD62313 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti93 – 95LRT → FRS in AAB57824 (PubMed:9226380).Curated3
Sequence conflicti106K → I in AAB57824 (PubMed:9226380).Curated1
Sequence conflicti117V → F in AAB57824 (PubMed:9226380).Curated1
Sequence conflicti120E → D in AAB57824 (PubMed:9226380).Curated1
Sequence conflicti189M → L in AAB57824 (PubMed:9226380).Curated1
Sequence conflicti464 – 465FA → SP in AAB57824 (PubMed:9226380).Curated2
Sequence conflicti464 – 465FA → SP in CAD12600 (Ref. 2) Curated2
Sequence conflicti499 – 500IP → VS in CAD62313 (Ref. 4) Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_071075225W → R Probable disease-associated mutation found in a patient with atypical heterotopia and mental retardation. 1 Publication1
Natural variantiVAR_071076243T → A Probable disease-associated mutation found in a patient with atypical heterotopia and mental retardation; the patient carries a truncating mutation in the other copy of this gene. 1 Publication1
Natural variantiVAR_031720377A → V.Corresponds to variant rs34198557dbSNPEnsembl.1
Natural variantiVAR_031721552H → N.1 PublicationCorresponds to variant rs17853154dbSNPEnsembl.1
Natural variantiVAR_031722556S → P.3 PublicationsCorresponds to variant rs2250718dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_024476127K → KRLNRSVSLLNACKLNRSTP in isoform 3. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U97018 mRNA. Translation: AAB57824.1. Frameshift.
AJ420603
, AJ428183, AJ428184, AJ428185, AJ428189, AJ428191, AJ428193, AJ428195, AJ428197, AJ496645, AJ496644, AJ428200, AJ428199, AJ428198, AJ428196, AJ428194, AJ428192, AJ428190, AJ428188, AJ428187, AJ428186 Genomic DNA. Translation: CAD12600.2.
BC032541 mRNA. Translation: AAH32541.1.
BC033043 mRNA. Translation: AAH33043.1.
BX247979 mRNA. Translation: CAD62313.1. Different initiation.
CCDSiCCDS32154.1. [O00423-3]
CCDS32155.1. [O00423-1]
RefSeqiNP_001008707.1. NM_001008707.1. [O00423-3]
NP_004425.2. NM_004434.2. [O00423-1]
UniGeneiHs.12451.

Genome annotation databases

EnsembliENST00000262233; ENSP00000262233; ENSG00000066629. [O00423-1]
ENST00000334192; ENSP00000334314; ENSG00000066629. [O00423-3]
GeneIDi2009.
KEGGihsa:2009.
UCSCiuc001ygr.4. human. [O00423-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U97018 mRNA. Translation: AAB57824.1. Frameshift.
AJ420603
, AJ428183, AJ428184, AJ428185, AJ428189, AJ428191, AJ428193, AJ428195, AJ428197, AJ496645, AJ496644, AJ428200, AJ428199, AJ428198, AJ428196, AJ428194, AJ428192, AJ428190, AJ428188, AJ428187, AJ428186 Genomic DNA. Translation: CAD12600.2.
BC032541 mRNA. Translation: AAH32541.1.
BC033043 mRNA. Translation: AAH33043.1.
BX247979 mRNA. Translation: CAD62313.1. Different initiation.
CCDSiCCDS32154.1. [O00423-3]
CCDS32155.1. [O00423-1]
RefSeqiNP_001008707.1. NM_001008707.1. [O00423-3]
NP_004425.2. NM_004434.2. [O00423-1]
UniGeneiHs.12451.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4CI8X-ray2.60A/B167-815[»]
ProteinModelPortaliO00423.
SMRiO00423.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108324. 13 interactors.
IntActiO00423. 3 interactors.
MINTiMINT-1457362.
STRINGi9606.ENSP00000334314.

PTM databases

iPTMnetiO00423.
PhosphoSitePlusiO00423.

Polymorphism and mutation databases

BioMutaiEML1.

Proteomic databases

MaxQBiO00423.
PaxDbiO00423.
PeptideAtlasiO00423.
PRIDEiO00423.

Protocols and materials databases

DNASUi2009.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262233; ENSP00000262233; ENSG00000066629. [O00423-1]
ENST00000334192; ENSP00000334314; ENSG00000066629. [O00423-3]
GeneIDi2009.
KEGGihsa:2009.
UCSCiuc001ygr.4. human. [O00423-1]

Organism-specific databases

CTDi2009.
DisGeNETi2009.
GeneCardsiEML1.
H-InvDBHIX0011963.
HGNCiHGNC:3330. EML1.
HPAiCAB033137.
HPA049105.
MIMi602033. gene.
neXtProtiNX_O00423.
OpenTargetsiENSG00000066629.
PharmGKBiPA27767.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2106. Eukaryota.
ENOG410XNTQ. LUCA.
GeneTreeiENSGT00550000074369.
HOGENOMiHOG000294061.
HOVERGENiHBG051470.
InParanoidiO00423.
KOiK18595.
OMAiRKYTRVG.
OrthoDBiEOG091G04Z4.
PhylomeDBiO00423.
TreeFamiTF317832.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000066629-MONOMER.
SignaLinkiO00423.

Miscellaneous databases

ChiTaRSiEML1. human.
GeneWikiiEML1.
GenomeRNAii2009.
PROiO00423.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000066629.
CleanExiHS_EML1.
ExpressionAtlasiO00423. baseline and differential.
GenevisibleiO00423. HS.

Family and domain databases

Gene3Di2.130.10.10. 3 hits.
InterProiIPR005108. HELP.
IPR011047. Quinoprotein_ADH-like_supfam.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF03451. HELP. 1 hit.
PF00400. WD40. 4 hits.
[Graphical view]
SMARTiSM00320. WD40. 10 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
SSF50998. SSF50998. 1 hit.
PROSITEiPS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEMAL1_HUMAN
AccessioniPrimary (citable) accession number: O00423
Secondary accession number(s): Q86U15
, Q8N536, Q8N5C4, Q8WWL6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: July 28, 2009
Last modified: November 2, 2016
This is version 151 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.