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Protein

E3 ubiquitin-protein ligase MYLIP

Gene

MYLIP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. cholesterol homeostasis Source: Ensembl
  2. movement of cell or subcellular component Source: UniProtKB
  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 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:21155. MYLIP.

Subcellular locationi

  1. Cytoplasm 1 Publication
  2. 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
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.

Polymorphism and mutation databases

BioMutaiMYLIP.
DMDMi84028296.

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

MaxQBiQ8WY64.
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

BgeeiQ8WY64.
CleanExiHS_MYLIP.
ExpressionAtlasiQ8WY64. baseline and differential.
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

Binary interactionsi

WithEntry#Exp.IntActNotes
MIPOL1Q8TD103EBI-6952711,EBI-2548751
RASSF5Q8WWW03EBI-6952711,EBI-367390
TSC22D4Q9Y3Q83EBI-6952711,EBI-739485

Protein-protein interaction databases

BioGridi118882. 16 interactions.
IntActiQ8WY64. 5 interactions.
MINTiMINT-268789.
STRINGi9606.ENSP00000349298.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000119078.
HOGENOMiHOG000007353.
HOVERGENiHBG052549.
InParanoidiQ8WY64.
KOiK10637.
OMAiLLCMLCC.
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.
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. AlignAdd to basket

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

        10         20         30         40         50
MLCYVTRPDA VLMEVEVEAK ANGEDCLNQV CRRLGIIEVD YFGLQFTGSK
60 70 80 90 100
GESLWLNLRN RISQQMDGLA PYRLKLRVKF FVEPHLILQE QTRHIFFLHI
110 120 130 140 150
KEALLAGHLL CSPEQAVELS ALLAQTKFGD YNQNTAKYNY EELCAKELSS
160 170 180 190 200
ATLNSIVAKH KELEGTSQAS AEYQVLQIVS AMENYGIEWH SVRDSEGQKL
210 220 230 240 250
LIGVGPEGIS ICKDDFSPIN RIAYPVVQMA TQSGKNVYLT VTKESGNSIV
260 270 280 290 300
LLFKMISTRA ASGLYRAITE THAFYRCDTV TSAVMMQYSR DLKGHLASLF
310 320 330 340 350
LNENINLGKK YVFDIKRTSK EVYDHARRAL YNAGVVDLVS RNNQSPSHSP
360 370 380 390 400
LKSSESSMNC SSCEGLSCQQ TRVLQEKLRK LKEAMLCMVC CEEEINSTFC
410 420 430 440
PCGHTVCCES CAAQLQSCPV CRSRVEHVQH VYLPTHTSLL NLTVI
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:
EMBLi
GenBanki
DDBJi
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 and mutation databases

BioMutaiMYLIP.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi118882. 16 interactions.
IntActiQ8WY64. 5 interactions.
MINTiMINT-268789.
STRINGi9606.ENSP00000349298.

Polymorphism and mutation databases

BioMutaiMYLIP.
DMDMi84028296.

Proteomic databases

MaxQBiQ8WY64.
PaxDbiQ8WY64.
PRIDEiQ8WY64.

Protocols and materials databases

DNASUi29116.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi29116.
GeneCardsiGC06P016129.
HGNCiHGNC:21155. MYLIP.
MIMi610082. gene.
neXtProtiNX_Q8WY64.
PharmGKBiPA134942677.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG149394.
GeneTreeiENSGT00760000119078.
HOGENOMiHOG000007353.
HOVERGENiHBG052549.
InParanoidiQ8WY64.
KOiK10637.
OMAiLLCMLCC.
OrthoDBiEOG7060QK.
PhylomeDBiQ8WY64.
TreeFamiTF351936.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiMYLIP. human.
GeneWikiiMYLIP.
GenomeRNAii29116.
NextBioi52199.
PROiQ8WY64.
SOURCEiSearch...

Gene expression databases

BgeeiQ8WY64.
CleanExiHS_MYLIP.
ExpressionAtlasiQ8WY64. baseline and differential.
GenevestigatoriQ8WY64.

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.
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]
ProtoNetiSearch...

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: April 29, 2015
This is version 122 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

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.