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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

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
ProteomesiUP000005640 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi59 – 613LAD → AAA: No effect on tubulin binding. 1 Publication
Mutagenesisi192 – 1921R → S: Abolishes tubulin binding; when associated with S-194; A-547; T-626; S-627; A-646 and A-786. 1 Publication
Mutagenesisi194 – 1941R → S: Abolishes tubulin binding; when associated with S-192; A-547; T-626; S-627; A-646 and A-786. 1 Publication
Mutagenesisi547 – 5471W → A: Abolishes tubulin binding; when associated with S-192; S-194; T-626; S-627; A-646 and A-786. 1 Publication
Mutagenesisi626 – 6261N → T: Abolishes tubulin binding; when associated with S-192; S-194; A-547; S-627; A-646 and A-786. 1 Publication
Mutagenesisi627 – 6271E → S: Abolishes tubulin binding; when associated with S-192; S-194; A-547; T-626; A-646 and A-786. 1 Publication
Mutagenesisi646 – 6461H → A: Abolishes tubulin binding; when associated with S-192; S-194; A-547; T-626; S-627 and A-786. 1 Publication
Mutagenesisi786 – 7861H → A: Abolishes tubulin binding; when associated with S-192; S-194; A-547; T-626; S-627 and A-646. 1 Publication

Keywords - Diseasei

Disease mutation, Epilepsy, Mental retardation

Organism-specific databases

PharmGKBiPA27767.

Polymorphism and mutation databases

BioMutaiEML1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 815815Echinoderm microtubule-associated protein-like 1PRO_0000050961Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei113 – 1131Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO00423.
PaxDbiO00423.
PRIDEiO00423.

PTM databases

PhosphoSiteiO00423.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiO00423.
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

Protein-protein interaction databases

BioGridi108324. 6 interactions.
IntActiO00423. 2 interactions.
MINTiMINT-1457362.
STRINGi9606.ENSP00000334314.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi179 – 1813Combined sources
Turni182 – 1854Combined sources
Beta strandi186 – 19914Combined sources
Helixi202 – 2054Combined sources
Beta strandi220 – 2278Combined sources
Beta strandi238 – 2403Combined sources
Beta strandi246 – 2505Combined sources
Beta strandi253 – 2586Combined sources
Turni259 – 2624Combined sources
Beta strandi263 – 2675Combined sources
Beta strandi274 – 2796Combined sources
Beta strandi283 – 2919Combined sources
Beta strandi305 – 3095Combined sources
Turni310 – 3123Combined sources
Beta strandi315 – 3195Combined sources
Turni321 – 3233Combined sources
Beta strandi326 – 3338Combined sources
Beta strandi335 – 3395Combined sources
Beta strandi342 – 3465Combined sources
Beta strandi348 – 3503Combined sources
Beta strandi352 – 3576Combined sources
Helixi358 – 3603Combined sources
Beta strandi362 – 3687Combined sources
Beta strandi374 – 3796Combined sources
Beta strandi386 – 3927Combined sources
Beta strandi394 – 4018Combined sources
Beta strandi404 – 4096Combined sources
Beta strandi419 – 4268Combined sources
Beta strandi432 – 4365Combined sources
Beta strandi441 – 4444Combined sources
Beta strandi449 – 4557Combined sources
Beta strandi458 – 4614Combined sources
Beta strandi463 – 4686Combined sources
Beta strandi474 – 4785Combined sources
Turni479 – 4813Combined sources
Beta strandi483 – 4875Combined sources
Beta strandi493 – 4986Combined sources
Turni501 – 5033Combined sources
Beta strandi505 – 5117Combined sources
Beta strandi517 – 5215Combined sources
Beta strandi526 – 5294Combined sources
Beta strandi536 – 5394Combined sources
Beta strandi546 – 5516Combined sources
Beta strandi553 – 56210Combined sources
Beta strandi565 – 5717Combined sources
Turni572 – 5754Combined sources
Beta strandi576 – 5827Combined sources
Beta strandi587 – 5926Combined sources
Beta strandi596 – 61217Combined sources
Turni613 – 6153Combined sources
Beta strandi618 – 6236Combined sources
Beta strandi625 – 6273Combined sources
Beta strandi629 – 6346Combined sources
Beta strandi638 – 6458Combined sources
Beta strandi650 – 6567Combined sources
Turni657 – 6604Combined sources
Beta strandi661 – 6688Combined sources
Beta strandi675 – 6817Combined sources
Beta strandi687 – 6915Combined sources
Beta strandi697 – 7004Combined sources
Helixi701 – 7033Combined sources
Helixi710 – 7134Combined sources
Beta strandi724 – 7263Combined sources
Turni727 – 7315Combined sources
Beta strandi741 – 7477Combined sources
Beta strandi749 – 75810Combined sources
Beta strandi763 – 7686Combined sources
Beta strandi772 – 7743Combined sources
Beta strandi778 – 7803Combined sources
Beta strandi789 – 7924Combined sources
Beta strandi796 – 8027Combined sources
Beta strandi809 – 8157Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CI8X-ray2.60A/B167-815[»]
ProteinModelPortaliO00423.
SMRiO00423. Positions 32-72, 176-815.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati269 – 31850WD 1Add
BLAST
Repeati323 – 36644WD 2Add
BLAST
Repeati369 – 40840WD 3Add
BLAST
Repeati416 – 45439WD 4Add
BLAST
Repeati458 – 49740WD 5Add
BLAST
Repeati541 – 58040WD 6Add
BLAST
Repeati582 – 62140WD 7Add
BLAST
Repeati624 – 66340WD 8Add
BLAST
Repeati670 – 70940WD 9Add
BLAST
Repeati737 – 77640WD 10Add
BLAST
Repeati782 – 81534WD 11Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni176 – 815640Tandem atypical propeller in EMLsAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi160 – 1667Poly-Ser

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

eggNOGiCOG2319.
GeneTreeiENSGT00550000074369.
HOGENOMiHOG000294061.
HOVERGENiHBG051470.
InParanoidiO00423.
KOiK18595.
OMAiRKYTRVG.
PhylomeDBiO00423.
TreeFamiTF317832.

Family and domain databases

Gene3Di2.130.10.10. 3 hits.
InterProiIPR005108. HELP.
IPR011047. Quinonprotein_ADH-like_supfam.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF03451. HELP. 1 hit.
PF00400. WD40. 5 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 AAB57824.1 differs from that shown. Reason: Frameshift at positions 168, 392, 405, 414 and 420. Curated
The sequence CAD62313.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti93 – 953LRT → FRS in AAB57824 (PubMed:9226380).Curated
Sequence conflicti106 – 1061K → I in AAB57824 (PubMed:9226380).Curated
Sequence conflicti117 – 1171V → F in AAB57824 (PubMed:9226380).Curated
Sequence conflicti120 – 1201E → D in AAB57824 (PubMed:9226380).Curated
Sequence conflicti189 – 1891M → L in AAB57824 (PubMed:9226380).Curated
Sequence conflicti464 – 4652FA → SP in AAB57824 (PubMed:9226380).Curated
Sequence conflicti464 – 4652FA → SP in CAD12600 (Ref. 2) Curated
Sequence conflicti499 – 5002IP → VS in CAD62313 (Ref. 4) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti225 – 2251W → R Probable disease-associated mutation found in a patient with atypical heterotopia and mental retardation. 1 Publication
VAR_071075
Natural varianti243 – 2431T → 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 Publication
VAR_071076
Natural varianti377 – 3771A → V.
Corresponds to variant rs34198557 [ dbSNP | Ensembl ].
VAR_031720
Natural varianti552 – 5521H → N.1 Publication
Corresponds to variant rs17853154 [ dbSNP | Ensembl ].
VAR_031721
Natural varianti556 – 5561S → P.3 Publications
Corresponds to variant rs2250718 [ dbSNP | Ensembl ].
VAR_031722

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei127 – 1271K → KRLNRSVSLLNACKLNRSTP in isoform 3. 1 PublicationVSP_024476

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.
ENST00000334192; ENSP00000334314; ENSG00000066629. [O00423-3]
GeneIDi2009.
KEGGihsa:2009.
UCSCiuc001ygq.3. human. [O00423-3]
uc001ygs.3. 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
EntryMethodResolution (Å)ChainPositionsPDBsum
4CI8X-ray2.60A/B167-815[»]
ProteinModelPortaliO00423.
SMRiO00423. Positions 32-72, 176-815.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108324. 6 interactions.
IntActiO00423. 2 interactions.
MINTiMINT-1457362.
STRINGi9606.ENSP00000334314.

PTM databases

PhosphoSiteiO00423.

Polymorphism and mutation databases

BioMutaiEML1.

Proteomic databases

MaxQBiO00423.
PaxDbiO00423.
PRIDEiO00423.

Protocols and materials databases

DNASUi2009.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262233; ENSP00000262233; ENSG00000066629.
ENST00000334192; ENSP00000334314; ENSG00000066629. [O00423-3]
GeneIDi2009.
KEGGihsa:2009.
UCSCiuc001ygq.3. human. [O00423-3]
uc001ygs.3. human. [O00423-1]

Organism-specific databases

CTDi2009.
GeneCardsiGC14P100259.
H-InvDBHIX0011963.
HGNCiHGNC:3330. EML1.
HPAiCAB033137.
HPA049105.
MIMi602033. gene.
neXtProtiNX_O00423.
PharmGKBiPA27767.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00550000074369.
HOGENOMiHOG000294061.
HOVERGENiHBG051470.
InParanoidiO00423.
KOiK18595.
OMAiRKYTRVG.
PhylomeDBiO00423.
TreeFamiTF317832.

Enzyme and pathway databases

SignaLinkiO00423.

Miscellaneous databases

ChiTaRSiEML1. human.
GeneWikiiEML1.
GenomeRNAii2009.
NextBioi8131.
PROiO00423.
SOURCEiSearch...

Gene expression databases

BgeeiO00423.
CleanExiHS_EML1.
ExpressionAtlasiO00423. baseline and differential.
GenevisibleiO00423. HS.

Family and domain databases

Gene3Di2.130.10.10. 3 hits.
InterProiIPR005108. HELP.
IPR011047. Quinonprotein_ADH-like_supfam.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF03451. HELP. 1 hit.
PF00400. WD40. 5 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...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of a novel human homologue of the gene coding for echinoderm microtubule-associated protein (EMAP) from the Usher syndrome type 1a locus at 14q32."
    Eudy J.D., Ma-Edmonds M., Yao S.F., Talmadge C.B., Kelley P.M., Weston M.D., Kimberling W.J., Sumegi J.
    Genomics 43:104-106(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PRO-556.
  2. "Complete exon-intron structure of human homologue of the gene coding the echinoderm microtubule-associated protein (EMAP)."
    Gerber S., Sumegi J., Rozet J.-M., Perrault I., Ducroq D., Munnich A., Kaplan J.
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PRO-556.
  3. "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), VARIANTS ASN-552 AND PRO-556.
    Tissue: Brain and Uterus.
  4. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-500 (ISOFORM 3).
    Tissue: Fetal brain.
  5. "Sequence and expression patterns of a human EMAP-related protein-2 (HuEMAP-2)."
    Lepley D.M., Palange J.M., Suprenant K.A.
    Gene 237:343-349(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. Cited for: ROLE IN DISEASE, VARIANTS ARG-225 AND ALA-243.
  8. "Crystal structure of EML1 reveals the basis for Hsp90 dependence of oncogenic EML4-ALK by disruption of an atypical ?-propeller domain."
    Richards M.W., Law E.W., Rennalls L.P., Busacca S., O'Regan L., Fry A.M., Fennell D.A., Bayliss R.
    Proc. Natl. Acad. Sci. U.S.A. 111:5195-5200(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 167-815, DOMAIN, INTERACTION WITH TUBULIN, MUTAGENESIS OF 59-LEU--ASP-61; ARG-192; ARG-194; TRP-547; ASN-626; GLU-627; HIS-646 AND HIS-786.

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: July 22, 2015
This is version 139 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

External Data

Dasty 3

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 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.