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O00423

- EMAL1_HUMAN

UniProt

O00423 - EMAL1_HUMAN

Protein

Echinoderm microtubule-associated protein-like 1

Gene

EML1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 3 (28 Jul 2009)
      Previous versions | rss
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    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

    1. calcium ion binding Source: UniProtKB
    2. microtubule binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. tubulin binding Source: UniProtKB

    GO - Biological processi

    1. brain development Source: UniProtKB
    2. microtubule cytoskeleton organization Source: UniProtKB
    3. mitotic spindle organization Source: UniProtKB
    4. neuroblast proliferation Source: UniProtKB

    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: 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

    1. cytosol Source: UniProtKB
    2. microtubule Source: UniProtKB-KW
    3. microtubule associated complex Source: ProtInc

    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.
    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.

    PTM / Processingi

    Molecule processing

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

    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

    ArrayExpressiO00423.
    BgeeiO00423.
    CleanExiHS_EML1.
    GenevestigatoriO00423.

    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. 2 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 – 1813
    Turni182 – 1854
    Beta strandi186 – 19914
    Helixi202 – 2054
    Beta strandi220 – 2278
    Beta strandi238 – 2403
    Beta strandi246 – 2505
    Beta strandi253 – 2586
    Turni259 – 2624
    Beta strandi263 – 2675
    Beta strandi274 – 2796
    Beta strandi283 – 2919
    Beta strandi305 – 3095
    Turni310 – 3123
    Beta strandi315 – 3195
    Turni321 – 3233
    Beta strandi326 – 3338
    Beta strandi335 – 3395
    Beta strandi342 – 3465
    Beta strandi348 – 3503
    Beta strandi352 – 3576
    Helixi358 – 3603
    Beta strandi362 – 3687
    Beta strandi374 – 3796
    Beta strandi386 – 3927
    Beta strandi394 – 4018
    Beta strandi404 – 4096
    Beta strandi419 – 4268
    Beta strandi432 – 4365
    Beta strandi441 – 4444
    Beta strandi449 – 4557
    Beta strandi458 – 4614
    Beta strandi463 – 4686
    Beta strandi474 – 4785
    Turni479 – 4813
    Beta strandi483 – 4875
    Beta strandi493 – 4986
    Turni501 – 5033
    Beta strandi505 – 5117
    Beta strandi517 – 5215
    Beta strandi526 – 5294
    Beta strandi536 – 5394
    Beta strandi546 – 5516
    Beta strandi553 – 56210
    Beta strandi565 – 5717
    Turni572 – 5754
    Beta strandi576 – 5827
    Beta strandi587 – 5926
    Beta strandi596 – 61217
    Turni613 – 6153
    Beta strandi618 – 6236
    Beta strandi625 – 6273
    Beta strandi629 – 6346
    Beta strandi638 – 6458
    Beta strandi650 – 6567
    Turni657 – 6604
    Beta strandi661 – 6688
    Beta strandi675 – 6817
    Beta strandi687 – 6915
    Beta strandi697 – 7004
    Helixi701 – 7033
    Helixi710 – 7134
    Beta strandi724 – 7263
    Turni727 – 7315
    Beta strandi741 – 7477
    Beta strandi749 – 75810
    Beta strandi763 – 7686
    Beta strandi772 – 7743
    Beta strandi778 – 7803
    Beta strandi789 – 7924
    Beta strandi796 – 8027
    Beta strandi809 – 8157

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4CI8X-ray2.60A/B167-815[»]
    ProteinModelPortaliO00423.
    SMRiO00423. Positions 210-792.
    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.
    HOGENOMiHOG000294061.
    HOVERGENiHBG051470.
    OMAiFRAPSHV.
    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. Align

    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

    MEDGFSSYSS LYDTSSLLQF CNDDSASAAS SMEVTDRIAS LEQRVQMQED    50
    DIQLLKSALA DVVRRLNITE EQQAVLNRKG PTKARPLMQT LPLRTTVNNG 100
    TVLPKKPTGS LPSPSGVRKE TAVPATKSNI KRTSSSERVS PGGRRESNGD 150
    SRGNRNRTGS TSSSSSGKKN SESKPKEPVF SAEEGYVKMF LRGRPVTMYM 200
    PKDQVDSYSL EAKVELPTKR LKLEWVYGYR GRDCRNNLYL LPTGETVYFI 250
    ASVVVLYNVE EQLQRHYAGH NDDVKCLAVH PDRITIATGQ VAGTSKDGKQ 300
    LPPHVRIWDS VTLNTLHVIG IGFFDRAVTC IAFSKSNGGT NLCAVDDSND 350
    HVLSVWDWQK EEKLADVKCS NEAVFAADFH PTDTNIIVTC GKSHLYFWTL 400
    EGSSLNKKQG LFEKQEKPKF VLCVTFSENG DTITGDSSGN ILVWGKGTNR 450
    ISYAVQGAHE GGIFALCMLR DGTLVSGGGK DRKLISWSGN YQKLRKTEIP 500
    EQFGPIRTVA EGKGDVILIG TTRNFVLQGT LSGDFTPITQ GHTDELWGLA 550
    IHASKSQFLT CGHDKHATLW DAVGHRPVWD KIIEDPAQSS GFHPSGSVVA 600
    VGTLTGRWFV FDTETKDLVT VHTDGNEQLS VMRYSPDGNF LAIGSHDNCI 650
    YIYGVSDNGR KYTRVGKCSG HSSFITHLDW SVNSQFLVSN SGDYEILYWV 700
    PSACKQVVSV ETTRDIEWAT YTCTLGFHVF GVWPEGSDGT DINAVCRAHE 750
    KKLLSTGDDF GKVHLFSYPC SQFRAPSHIY GGHSSHVTNV DFLCEDSHLI 800
    STGGKDTSIM QWRVI 815
    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.
    The sequence CAD62313.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    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. 1 PublicationCurated
    Sequence conflicti499 – 5002IP → VS in CAD62313. 1 PublicationCurated

    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:
    EMBL
    GenBank
    DDBJ
    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.
    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:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS32154.1. [O00423-3 ]
    CCDS32155.1. [O00423-1 ]
    RefSeqi NP_001008707.1. NM_001008707.1. [O00423-3 ]
    NP_004425.2. NM_004434.2. [O00423-1 ]
    UniGenei Hs.12451.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4CI8 X-ray 2.60 A/B 167-815 [» ]
    ProteinModelPortali O00423.
    SMRi O00423. Positions 210-792.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108324. 2 interactions.
    IntActi O00423. 2 interactions.
    MINTi MINT-1457362.
    STRINGi 9606.ENSP00000334314.

    PTM databases

    PhosphoSitei O00423.

    Proteomic databases

    MaxQBi O00423.
    PaxDbi O00423.
    PRIDEi O00423.

    Protocols and materials databases

    DNASUi 2009.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262233 ; ENSP00000262233 ; ENSG00000066629 . [O00423-1 ]
    ENST00000334192 ; ENSP00000334314 ; ENSG00000066629 . [O00423-3 ]
    GeneIDi 2009.
    KEGGi hsa:2009.
    UCSCi uc001ygq.3. human. [O00423-3 ]
    uc001ygs.3. human. [O00423-1 ]

    Organism-specific databases

    CTDi 2009.
    GeneCardsi GC14P100259.
    H-InvDB HIX0011963.
    HGNCi HGNC:3330. EML1.
    HPAi CAB033137.
    HPA049105.
    MIMi 602033. gene.
    neXtProti NX_O00423.
    PharmGKBi PA27767.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2319.
    HOGENOMi HOG000294061.
    HOVERGENi HBG051470.
    OMAi FRAPSHV.
    PhylomeDBi O00423.
    TreeFami TF317832.

    Enzyme and pathway databases

    SignaLinki O00423.

    Miscellaneous databases

    ChiTaRSi EML1. human.
    GeneWikii EML1.
    GenomeRNAii 2009.
    NextBioi 8131.
    PROi O00423.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00423.
    Bgeei O00423.
    CleanExi HS_EML1.
    Genevestigatori O00423.

    Family and domain databases

    Gene3Di 2.130.10.10. 3 hits.
    InterProi IPR005108. HELP.
    IPR011047. Quinonprotein_ADH-like_supfam.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    Pfami PF03451. HELP. 1 hit.
    PF00400. WD40. 5 hits.
    [Graphical view ]
    SMARTi SM00320. WD40. 10 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 1 hit.
    SSF50998. SSF50998. 1 hit.
    PROSITEi PS50082. WD_REPEATS_2. 3 hits.
    PS50294. WD_REPEATS_REGION. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. Cited for: ROLE IN DISEASE, VARIANTS ARG-225 AND ALA-243.
    7. "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: October 1, 2014
    This is version 132 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