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Q8WY64

- MYLIP_HUMAN

UniProt

Q8WY64 - MYLIP_HUMAN

Protein

E3 ubiquitin-protein ligase MYLIP

Gene

MYLIP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (20 Dec 2005)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of myosin regulatory light chain (MRLC), LDLR, VLDLR and LRP8. Activity depends on E2 enzymes of the UBE2D family. Proteasomal degradation of MRLC leads to inhibit neurite outgrowth in presence of NGF by counteracting the stabilization of MRLC by saposin-like protein (CNPY2/MSAP) and reducing CNPY2-stimulated neurite outgrowth. Acts as a sterol-dependent inhibitor of cellular cholesterol uptake by mediating ubiquitination and subsequent degradation of LDLR.6 Publications

    Enzyme regulationi

    Can bind 1 iron ion per dimer. Iron binding seems to decrease LDLR degradation activity.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi360 – 3601Iron
    Metal bindingi363 – 3631Iron
    Metal bindingi368 – 3681Iron

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri387 – 42236RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. cytoskeletal protein binding Source: UniProtKB
    2. ligase activity Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. ubiquitin-protein transferase activity Source: UniProtKB
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cellular component movement Source: UniProtKB
    2. cholesterol homeostasis Source: Ensembl
    3. negative regulation of low-density lipoprotein particle clearance Source: Ensembl
    4. nervous system development Source: UniProtKB
    5. positive regulation of protein catabolic process Source: Ensembl
    6. protein destabilization Source: Ensembl
    7. protein ubiquitination Source: UniProtKB
    8. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: Ensembl
    9. regulation of low-density lipoprotein particle receptor catabolic process Source: Ensembl

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Iron, Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase MYLIP (EC:6.3.2.-)
    Alternative name(s):
    Inducible degrader of the LDL-receptor
    Short name:
    Idol
    Myosin regulatory light chain interacting protein
    Short name:
    MIR
    Gene namesi
    Name:MYLIP
    Synonyms:BZF1, IDOL
    ORF Names:BM-023, PP5242
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:21155. MYLIP.

    Subcellular locationi

    Cytoplasm 1 Publication. Cell membrane 1 Publication; Peripheral membrane protein 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. cytoskeleton Source: InterPro
    3. extrinsic component of membrane Source: InterPro
    4. intracellular Source: UniProtKB
    5. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi265 – 2651Y → A: Unable to clear LDLR from the plasma membrane. 1 Publication
    Mutagenesisi269 – 2691T → R: Unable to clear LDLR from the plasma membrane. 1 Publication
    Mutagenesisi387 – 3871C → A: Abolishes autoubiquitination. 3 Publications
    Mutagenesisi387 – 3871C → A: Abolishes ubiquitin ligase activity. 3 Publications
    Mutagenesisi389 – 3891V → R: Inhibits LDLR degradation. 1 Publication
    Mutagenesisi415 – 4151L → E: Inhibits LDLR degradation. 1 Publication

    Organism-specific databases

    PharmGKBiPA134942677.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 445445E3 ubiquitin-protein ligase MYLIPPRO_0000055972Add
    BLAST

    Post-translational modificationi

    Autoubiquitinated.2 Publications

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    PaxDbiQ8WY64.
    PRIDEiQ8WY64.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Developmental stagei

    Expressed in fetal tissues and higher levels were detected in placenta and fetal lung.1 Publication

    Inductioni

    Expression is directly activated by NR1H2 and NR1H3. Expression is not dependent of the sterol-response element-binding proteins (SREBPs). Expression is indirectly induced by LDL.1 Publication

    Gene expression databases

    ArrayExpressiQ8WY64.
    BgeeiQ8WY64.
    CleanExiHS_MYLIP.
    GenevestigatoriQ8WY64.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with the E2 ubiquitin-conjugating enzyme, UBE2D1 (via RING-type zinc finger). Interacts with myosin regulatory light chain (MRLC) and TMEM4.3 Publications

    Protein-protein interaction databases

    BioGridi118882. 13 interactions.
    IntActiQ8WY64. 2 interactions.
    MINTiMINT-268789.
    STRINGi9606.ENSP00000349298.

    Structurei

    Secondary structure

    1
    445
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi374 – 38411
    Turni388 – 3903
    Beta strandi391 – 3944
    Beta strandi397 – 4004
    Helixi409 – 4124
    Turni419 – 4213
    Beta strandi427 – 4304

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YHNX-ray3.00A/B369-445[»]
    2YHOX-ray2.10A/C/E/G369-445[»]
    ProteinModelPortaliQ8WY64.
    SMRiQ8WY64. Positions 3-276, 372-441.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 279279FERMPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni431 – 4333Critical for homodimerization

    Domaini

    The RING domain mediates ubiquitination and the neurite outgrowth inhibitory activity.
    The FERM domain binds phospholipids and mediates lipoprotein receptors recognition at the plasma membrane through their cytoplasmic tails.
    The RING-type zinc finger mediates the interaction with UBE2D E2 enzymes.

    Sequence similaritiesi

    Contains 1 FERM domain.PROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri387 – 42236RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG149394.
    HOGENOMiHOG000007353.
    HOVERGENiHBG052549.
    InParanoidiQ8WY64.
    KOiK10637.
    OMAiINSTFCP.
    OrthoDBiEOG7060QK.
    PhylomeDBiQ8WY64.
    TreeFamiTF351936.

    Family and domain databases

    Gene3Di1.20.80.10. 1 hit.
    2.30.29.30. 1 hit.
    3.30.40.10. 1 hit.
    InterProiIPR019749. Band_41_domain.
    IPR019750. Band_41_fam.
    IPR000798. Ez/rad/moesin_like.
    IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
    IPR019748. FERM_central.
    IPR000299. FERM_domain.
    IPR018979. FERM_N.
    IPR011993. PH_like_dom.
    IPR029071. Ubiquitin-rel_dom.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF00373. FERM_M. 1 hit.
    PF09379. FERM_N. 1 hit.
    [Graphical view]
    PRINTSiPR00935. BAND41.
    PR00661. ERMFAMILY.
    SMARTiSM00295. B41. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view]
    SUPFAMiSSF47031. SSF47031. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEiPS50057. FERM_3. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8WY64-1) [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

    MLCYVTRPDA VLMEVEVEAK ANGEDCLNQV CRRLGIIEVD YFGLQFTGSK    50
    GESLWLNLRN RISQQMDGLA PYRLKLRVKF FVEPHLILQE QTRHIFFLHI 100
    KEALLAGHLL CSPEQAVELS ALLAQTKFGD YNQNTAKYNY EELCAKELSS 150
    ATLNSIVAKH KELEGTSQAS AEYQVLQIVS AMENYGIEWH SVRDSEGQKL 200
    LIGVGPEGIS ICKDDFSPIN RIAYPVVQMA TQSGKNVYLT VTKESGNSIV 250
    LLFKMISTRA ASGLYRAITE THAFYRCDTV TSAVMMQYSR DLKGHLASLF 300
    LNENINLGKK YVFDIKRTSK EVYDHARRAL YNAGVVDLVS RNNQSPSHSP 350
    LKSSESSMNC SSCEGLSCQQ TRVLQEKLRK LKEAMLCMVC CEEEINSTFC 400
    PCGHTVCCES CAAQLQSCPV CRSRVEHVQH VYLPTHTSLL NLTVI 445
    Length:445
    Mass (Da):49,910
    Last modified:December 20, 2005 - v2
    Checksum:i342E643B0532B45C
    GO
    Isoform 2 (identifier: Q8WY64-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-181: Missing.
         316-445: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:134
    Mass (Da):14,989
    Checksum:i377CBE27A1FAEC6E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti199 – 1991K → R in AAF18974. (PubMed:10593918)Curated
    Sequence conflicti262 – 2632SG → TR in AAF87323. (PubMed:11042152)Curated
    Sequence conflicti309 – 3102KK → PRN in AAF87323. (PubMed:11042152)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti342 – 3421N → S.4 Publications
    Corresponds to variant rs9370867 [ dbSNP | Ensembl ].
    VAR_019805

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 181181Missing in isoform 2. 1 PublicationVSP_011828Add
    BLAST
    Alternative sequencei316 – 445130Missing in isoform 2. 1 PublicationVSP_011829Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF187016 mRNA. Translation: AAF18974.1.
    AF006003 mRNA. Translation: AAQ13408.1.
    AF006004 Genomic DNA. Translation: AAQ13409.1.
    AF212221 mRNA. Translation: AAF87323.1.
    AF258586 mRNA. Translation: AAG23789.1.
    BT007055 mRNA. Translation: AAP35704.1.
    AL021407 Genomic DNA. Translation: CAI19548.1.
    CH471087 Genomic DNA. Translation: EAW55366.1.
    BC002860 mRNA. Translation: AAH02860.1.
    CCDSiCCDS4536.1. [Q8WY64-1]
    RefSeqiNP_037394.2. NM_013262.3. [Q8WY64-1]
    UniGeneiHs.484738.

    Genome annotation databases

    EnsembliENST00000356840; ENSP00000349298; ENSG00000007944. [Q8WY64-1]
    GeneIDi29116.
    KEGGihsa:29116.
    UCSCiuc003nbq.3. human. [Q8WY64-1]

    Polymorphism databases

    DMDMi84028296.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF187016 mRNA. Translation: AAF18974.1 .
    AF006003 mRNA. Translation: AAQ13408.1 .
    AF006004 Genomic DNA. Translation: AAQ13409.1 .
    AF212221 mRNA. Translation: AAF87323.1 .
    AF258586 mRNA. Translation: AAG23789.1 .
    BT007055 mRNA. Translation: AAP35704.1 .
    AL021407 Genomic DNA. Translation: CAI19548.1 .
    CH471087 Genomic DNA. Translation: EAW55366.1 .
    BC002860 mRNA. Translation: AAH02860.1 .
    CCDSi CCDS4536.1. [Q8WY64-1 ]
    RefSeqi NP_037394.2. NM_013262.3. [Q8WY64-1 ]
    UniGenei Hs.484738.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2YHN X-ray 3.00 A/B 369-445 [» ]
    2YHO X-ray 2.10 A/C/E/G 369-445 [» ]
    ProteinModelPortali Q8WY64.
    SMRi Q8WY64. Positions 3-276, 372-441.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118882. 13 interactions.
    IntActi Q8WY64. 2 interactions.
    MINTi MINT-268789.
    STRINGi 9606.ENSP00000349298.

    Polymorphism databases

    DMDMi 84028296.

    Proteomic databases

    PaxDbi Q8WY64.
    PRIDEi Q8WY64.

    Protocols and materials databases

    DNASUi 29116.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356840 ; ENSP00000349298 ; ENSG00000007944 . [Q8WY64-1 ]
    GeneIDi 29116.
    KEGGi hsa:29116.
    UCSCi uc003nbq.3. human. [Q8WY64-1 ]

    Organism-specific databases

    CTDi 29116.
    GeneCardsi GC06P016129.
    HGNCi HGNC:21155. MYLIP.
    MIMi 610082. gene.
    neXtProti NX_Q8WY64.
    PharmGKBi PA134942677.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG149394.
    HOGENOMi HOG000007353.
    HOVERGENi HBG052549.
    InParanoidi Q8WY64.
    KOi K10637.
    OMAi INSTFCP.
    OrthoDBi EOG7060QK.
    PhylomeDBi Q8WY64.
    TreeFami TF351936.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    GeneWikii MYLIP.
    GenomeRNAii 29116.
    NextBioi 52199.
    PROi Q8WY64.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8WY64.
    Bgeei Q8WY64.
    CleanExi HS_MYLIP.
    Genevestigatori Q8WY64.

    Family and domain databases

    Gene3Di 1.20.80.10. 1 hit.
    2.30.29.30. 1 hit.
    3.30.40.10. 1 hit.
    InterProi IPR019749. Band_41_domain.
    IPR019750. Band_41_fam.
    IPR000798. Ez/rad/moesin_like.
    IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
    IPR019748. FERM_central.
    IPR000299. FERM_domain.
    IPR018979. FERM_N.
    IPR011993. PH_like_dom.
    IPR029071. Ubiquitin-rel_dom.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF00373. FERM_M. 1 hit.
    PF09379. FERM_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00935. BAND41.
    PR00661. ERMFAMILY.
    SMARTi SM00295. B41. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47031. SSF47031. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEi PS50057. FERM_3. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "MIR is a novel ERM-like protein that interacts with myosin regulatory light chain and inhibits neurite outgrowth."
      Olsson P.-A., Korhonen L., Mercer E.A., Lindholm D.
      J. Biol. Chem. 274:36288-36292(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, FUNCTION, INTERACTION WITH MYOSIN REGULATORY LIGHT CHAIN (MRLC), VARIANT SER-342.
      Tissue: Brain.
    2. Shi W., Mullersman J.E.
      Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-342.
    3. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT SER-342.
      Tissue: Bone marrow.
    4. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
      Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
      , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
      Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT SER-342.
    5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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).
      Tissue: Placenta.
    9. "Functional activities and cellular localization of the ezrin, radixin, moesin (ERM) and RING zinc finger domains in MIR."
      Bornhauser B.C., Johansson C., Lindholm D.
      FEBS Lett. 553:195-199(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-387, FUNCTION, SUBCELLULAR LOCATION, AUTOUBIQUITINATION.
    10. "MSAP is a novel MIR-interacting protein that enhances neurite outgrowth and increases myosin regulatory light chain."
      Bornhauser B.C., Olsson P.-A., Lindholm D.
      J. Biol. Chem. 278:35412-35420(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TMEM4.
    11. "LXR regulates cholesterol uptake through Idol-dependent ubiquitination of the LDL receptor."
      Zelcer N., Hong C., Boyadjian R., Tontonoz P.
      Science 325:100-104(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION, MUTAGENESIS OF CYS-387.
    12. "The E3 ubiquitin ligase IDOL induces the degradation of the low density lipoprotein receptor family members VLDLR and ApoER2."
      Hong C., Duit S., Jalonen P., Out R., Scheer L., Sorrentino V., Boyadjian R., Rodenburg K.W., Foley E., Korhonen L., Lindholm D., Nimpf J., van Berkel T.J., Tontonoz P., Zelcer N.
      J. Biol. Chem. 285:19720-19726(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "FERM-dependent E3 ligase recognition is a conserved mechanism for targeted degradation of lipoprotein receptors."
      Calkin A.C., Goult B.T., Zhang L., Fairall L., Hong C., Schwabe J.W., Tontonoz P.
      Proc. Natl. Acad. Sci. U.S.A. 108:20107-20112(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, AUTOUBIQUITINATION, MUTAGENESIS OF TYR-265 AND THR-269.
    14. "The IDOL-UBE2D complex mediates sterol-dependent degradation of the LDL receptor."
      Zhang L., Fairall L., Goult B.T., Calkin A.C., Hong C., Millard C.J., Tontonoz P., Schwabe J.W.
      Genes Dev. 25:1262-1274(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 369-445 IN COMPLEX WITH UBE2D1, SUBUNIT, ENZYME REGULATION, IRON-BINDING SITES, MUTAGENESIS OF CYS-387; VAL-389 AND LEU-415.

    Entry informationi

    Entry nameiMYLIP_HUMAN
    AccessioniPrimary (citable) accession number: Q8WY64
    Secondary accession number(s): Q5TIA4
    , Q9BU73, Q9NRL9, Q9UHE7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 9, 2004
    Last sequence update: December 20, 2005
    Last modified: October 1, 2014
    This is version 116 of the entry and version 2 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 6
      Human chromosome 6: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3