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Q8WY64

- MYLIP_HUMAN

UniProt

Q8WY64 - MYLIP_HUMAN

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Protein
E3 ubiquitin-protein ligase MYLIP
Gene
MYLIP, BZF1, IDOL, BM-023, PP5242
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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-type
Add
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
Complete GO annotation...

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 Inferred. Cell membrane; 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
Complete GO annotation...

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 MYLIP
PRO_0000055972Add
BLAST

Post-translational modificationi

Autoubiquitinated.

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.2 Publications

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

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 279279FERM
Add
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.

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

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.
VSP_011828Add
BLAST
Alternative sequencei316 – 445130Missing in isoform 2.
VSP_011829Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti199 – 1991K → R in AAF18974. 1 Publication
Sequence conflicti262 – 2632SG → TR in AAF87323. 1 Publication
Sequence conflicti309 – 3102KK → PRN in AAF87323. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 115 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

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