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E3 ubiquitin-protein ligase MYLIP (EC 2.3.2.27) (Inducible degrader of the LDL-receptor) (Idol) (Myosin regulatory light chain interacting protein) (MIR) (RING-type E3 ubiquitin transferase MYLIP)

 MYLIP_HUMAN             Reviewed;         445 AA.
Q8WY64; Q5TIA4; Q9BU73; Q9NRL9; Q9UHE7;
09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
20-DEC-2005, sequence version 2.
13-FEB-2019, entry version 161.
RecName: Full=E3 ubiquitin-protein ligase MYLIP;
EC=2.3.2.27;
AltName: Full=Inducible degrader of the LDL-receptor;
Short=Idol;
AltName: Full=Myosin regulatory light chain interacting protein;
Short=MIR;
AltName: Full=RING-type E3 ubiquitin transferase MYLIP {ECO:0000305};
Name=MYLIP; Synonyms=BZF1, IDOL; ORFNames=BM-023, PP5242;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, FUNCTION, INTERACTION WITH MYOSIN REGULATORY
LIGHT CHAIN (MRLC), AND VARIANT SER-342.
TISSUE=Brain;
PubMed=10593918; DOI=10.1074/jbc.274.51.36288;
Olsson P.-A., Korhonen L., Mercer E.A., Lindholm D.;
"MIR is a novel ERM-like protein that interacts with myosin regulatory
light chain and inhibits neurite outgrowth.";
J. Biol. Chem. 274:36288-36292(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-342.
Shi W., Mullersman J.E.;
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
SER-342.
TISSUE=Bone marrow;
PubMed=11042152; DOI=10.1101/gr.140200;
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.;
"Cloning and functional analysis of cDNAs with open reading frames for
300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
SER-342.
PubMed=15498874; DOI=10.1073/pnas.0404089101;
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.;
"Large-scale cDNA transfection screening for genes related to cancer
development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
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.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
MUTAGENESIS OF CYS-387, FUNCTION, SUBCELLULAR LOCATION, AND
AUTOUBIQUITINATION.
PubMed=14550572; DOI=10.1016/S0014-5793(03)01010-X;
Bornhauser B.C., Johansson C., Lindholm D.;
"Functional activities and cellular localization of the ezrin,
radixin, moesin (ERM) and RING zinc finger domains in MIR.";
FEBS Lett. 553:195-199(2003).
[10]
FUNCTION, AND INTERACTION WITH TMEM4.
PubMed=12826659; DOI=10.1074/jbc.M306271200;
Bornhauser B.C., Olsson P.-A., Lindholm D.;
"MSAP is a novel MIR-interacting protein that enhances neurite
outgrowth and increases myosin regulatory light chain.";
J. Biol. Chem. 278:35412-35420(2003).
[11]
FUNCTION, INDUCTION, AND MUTAGENESIS OF CYS-387.
PubMed=19520913; DOI=10.1126/science.1168974;
Zelcer N., Hong C., Boyadjian R., Tontonoz P.;
"LXR regulates cholesterol uptake through Idol-dependent
ubiquitination of the LDL receptor.";
Science 325:100-104(2009).
[12]
FUNCTION.
PubMed=20427281; DOI=10.1074/jbc.M110.123729;
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.;
"The E3 ubiquitin ligase IDOL induces the degradation of the low
density lipoprotein receptor family members VLDLR and ApoER2.";
J. Biol. Chem. 285:19720-19726(2010).
[13]
FUNCTION, AUTOUBIQUITINATION, AND MUTAGENESIS OF TYR-265 AND THR-269.
PubMed=22109552; DOI=10.1073/pnas.1111589108;
Calkin A.C., Goult B.T., Zhang L., Fairall L., Hong C., Schwabe J.W.,
Tontonoz P.;
"FERM-dependent E3 ligase recognition is a conserved mechanism for
targeted degradation of lipoprotein receptors.";
Proc. Natl. Acad. Sci. U.S.A. 108:20107-20112(2011).
[14]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 369-445 IN COMPLEX WITH
UBE2D1, SUBUNIT, ACTIVITY REGULATION, IRON-BINDING SITES, AND
MUTAGENESIS OF CYS-387; VAL-389 AND LEU-415.
PubMed=21685362; DOI=10.1101/gad.2056211;
Zhang L., Fairall L., Goult B.T., Calkin A.C., Hong C., Millard C.J.,
Tontonoz P., Schwabe J.W.;
"The IDOL-UBE2D complex mediates sterol-dependent degradation of the
LDL receptor.";
Genes Dev. 25:1262-1274(2011).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:10593918, ECO:0000269|PubMed:12826659,
ECO:0000269|PubMed:14550572, ECO:0000269|PubMed:19520913,
ECO:0000269|PubMed:20427281, ECO:0000269|PubMed:22109552}.
-!- CATALYTIC ACTIVITY:
Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-
cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.; EC=2.3.2.27;
-!- ACTIVITY REGULATION: Can bind 1 iron ion per dimer. Iron binding
seems to decrease LDLR degradation activity.
{ECO:0000269|PubMed:21685362}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Homodimer. Interacts with the E2 ubiquitin-conjugating
enzyme, UBE2D1 (via RING-type zinc finger). Interacts with myosin
regulatory light chain (MRLC) and TMEM4.
{ECO:0000269|PubMed:10593918, ECO:0000269|PubMed:12826659,
ECO:0000269|PubMed:21685362}.
-!- INTERACTION:
Q9Y2B0:CNPY2; NbExp=3; IntAct=EBI-6952711, EBI-1054195;
Q96D03:DDIT4L; NbExp=4; IntAct=EBI-6952711, EBI-742054;
Q8TD10:MIPOL1; NbExp=3; IntAct=EBI-6952711, EBI-2548751;
P55771:PAX9; NbExp=4; IntAct=EBI-6952711, EBI-12111000;
Q8WWW0:RASSF5; NbExp=3; IntAct=EBI-6952711, EBI-367390;
Q9Y3Q8:TSC22D4; NbExp=3; IntAct=EBI-6952711, EBI-739485;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:14550572}.
Cell membrane {ECO:0000269|PubMed:14550572}; Peripheral membrane
protein {ECO:0000269|PubMed:14550572}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8WY64-1; Sequence=Displayed;
Name=2;
IsoId=Q8WY64-2; Sequence=VSP_011828, VSP_011829;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:10593918}.
-!- DEVELOPMENTAL STAGE: Expressed in fetal tissues and higher levels
were detected in placenta and fetal lung.
{ECO:0000269|PubMed:10593918}.
-!- INDUCTION: 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.
{ECO:0000269|PubMed:19520913}.
-!- DOMAIN: The RING domain mediates ubiquitination and the neurite
outgrowth inhibitory activity.
-!- DOMAIN: The FERM domain binds phospholipids and mediates
lipoprotein receptors recognition at the plasma membrane through
their cytoplasmic tails.
-!- DOMAIN: The RING-type zinc finger mediates the interaction with
UBE2D E2 enzymes.
-!- PTM: Autoubiquitinated. {ECO:0000269|PubMed:14550572,
ECO:0000269|PubMed:22109552}.
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EMBL; AF187016; AAF18974.1; -; mRNA.
EMBL; AF006003; AAQ13408.1; -; mRNA.
EMBL; AF006004; AAQ13409.1; -; Genomic_DNA.
EMBL; AF212221; AAF87323.1; -; mRNA.
EMBL; AF258586; AAG23789.1; -; mRNA.
EMBL; BT007055; AAP35704.1; -; mRNA.
EMBL; AL021407; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471087; EAW55366.1; -; Genomic_DNA.
EMBL; BC002860; AAH02860.1; -; mRNA.
CCDS; CCDS4536.1; -. [Q8WY64-1]
RefSeq; NP_037394.2; NM_013262.3. [Q8WY64-1]
UniGene; Hs.484738; -.
PDB; 2YHN; X-ray; 3.00 A; A/B=369-445.
PDB; 2YHO; X-ray; 2.10 A; A/C/E/G=369-445.
PDBsum; 2YHN; -.
PDBsum; 2YHO; -.
ProteinModelPortal; Q8WY64; -.
SMR; Q8WY64; -.
BioGrid; 118882; 27.
IntAct; Q8WY64; 31.
MINT; Q8WY64; -.
STRING; 9606.ENSP00000349298; -.
iPTMnet; Q8WY64; -.
PhosphoSitePlus; Q8WY64; -.
BioMuta; MYLIP; -.
DMDM; 84028296; -.
jPOST; Q8WY64; -.
PaxDb; Q8WY64; -.
PeptideAtlas; Q8WY64; -.
PRIDE; Q8WY64; -.
ProteomicsDB; 75131; -.
ProteomicsDB; 75132; -. [Q8WY64-2]
DNASU; 29116; -.
Ensembl; ENST00000356840; ENSP00000349298; ENSG00000007944. [Q8WY64-1]
GeneID; 29116; -.
KEGG; hsa:29116; -.
UCSC; uc003nbq.4; human. [Q8WY64-1]
CTD; 29116; -.
DisGeNET; 29116; -.
EuPathDB; HostDB:ENSG00000007944.14; -.
GeneCards; MYLIP; -.
HGNC; HGNC:21155; MYLIP.
MIM; 610082; gene.
neXtProt; NX_Q8WY64; -.
OpenTargets; ENSG00000007944; -.
Orphanet; 426; NON RARE IN EUROPE: Familial hypobetalipoproteinemia.
PharmGKB; PA134942677; -.
eggNOG; ENOG410IG7I; Eukaryota.
eggNOG; ENOG410XRZN; LUCA.
GeneTree; ENSGT00940000156206; -.
HOGENOM; HOG000007353; -.
HOVERGEN; HBG052549; -.
InParanoid; Q8WY64; -.
KO; K10637; -.
OMA; LNIICEM; -.
OrthoDB; 1340284at2759; -.
PhylomeDB; Q8WY64; -.
TreeFam; TF351936; -.
Reactome; R-HSA-8866427; VLDLR internalisation and degradation.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
ChiTaRS; MYLIP; human.
GeneWiki; MYLIP; -.
GenomeRNAi; 29116; -.
PRO; PR:Q8WY64; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000007944; Expressed in 229 organ(s), highest expression level in oocyte.
ExpressionAtlas; Q8WY64; baseline and differential.
Genevisible; Q8WY64; HS.
GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005622; C:intracellular; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0008092; F:cytoskeletal protein binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
GO; GO:0032802; P:low-density lipoprotein particle receptor catabolic process; TAS:Reactome.
GO; GO:0010989; P:negative regulation of low-density lipoprotein particle clearance; IEA:Ensembl.
GO; GO:0010977; P:negative regulation of neuron projection development; IMP:UniProtKB.
GO; GO:0007399; P:nervous system development; IMP:UniProtKB.
GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0032803; P:regulation of low-density lipoprotein particle receptor catabolic process; IEA:Ensembl.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
CDD; cd14473; FERM_B-lobe; 1.
Gene3D; 1.20.80.10; -; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR019749; Band_41_domain.
InterPro; IPR000798; Ez/rad/moesin-like.
InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
InterPro; IPR035963; FERM_2.
InterPro; IPR019748; FERM_central.
InterPro; IPR000299; FERM_domain.
InterPro; IPR018979; FERM_N.
InterPro; IPR018980; FERM_PH-like_C.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR029071; Ubiquitin-like_domsf.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF09380; FERM_C; 1.
Pfam; PF00373; FERM_M; 1.
Pfam; PF09379; FERM_N; 1.
PRINTS; PR00935; BAND41.
PRINTS; PR00661; ERMFAMILY.
SMART; SM00295; B41; 1.
SMART; SM01196; FERM_C; 1.
SUPFAM; SSF47031; SSF47031; 1.
SUPFAM; SSF54236; SSF54236; 1.
PROSITE; PS50057; FERM_3; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Cytoplasm; Iron; Membrane; Metal-binding; Polymorphism;
Reference proteome; Transferase; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 445 E3 ubiquitin-protein ligase MYLIP.
/FTId=PRO_0000055972.
DOMAIN 1 279 FERM. {ECO:0000255|PROSITE-
ProRule:PRU00084}.
ZN_FING 387 422 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
REGION 431 433 Critical for homodimerization.
METAL 360 360 Iron.
METAL 363 363 Iron.
METAL 368 368 Iron.
VAR_SEQ 1 181 Missing (in isoform 2).
{ECO:0000303|PubMed:11042152}.
/FTId=VSP_011828.
VAR_SEQ 316 445 Missing (in isoform 2).
{ECO:0000303|PubMed:11042152}.
/FTId=VSP_011829.
VARIANT 342 342 N -> S (in dbSNP:rs9370867).
{ECO:0000269|PubMed:10593918,
ECO:0000269|PubMed:11042152,
ECO:0000269|PubMed:15498874,
ECO:0000269|Ref.2}.
/FTId=VAR_019805.
MUTAGEN 265 265 Y->A: Unable to clear LDLR from the
plasma membrane.
{ECO:0000269|PubMed:22109552}.
MUTAGEN 269 269 T->R: Unable to clear LDLR from the
plasma membrane.
{ECO:0000269|PubMed:22109552}.
MUTAGEN 387 387 C->A: Abolishes autoubiquitination.
{ECO:0000269|PubMed:14550572,
ECO:0000269|PubMed:19520913,
ECO:0000269|PubMed:21685362}.
MUTAGEN 387 387 C->A: Abolishes ubiquitin ligase
activity. {ECO:0000269|PubMed:14550572,
ECO:0000269|PubMed:19520913,
ECO:0000269|PubMed:21685362}.
MUTAGEN 389 389 V->R: Inhibits LDLR degradation.
{ECO:0000269|PubMed:21685362}.
MUTAGEN 415 415 L->E: Inhibits LDLR degradation.
{ECO:0000269|PubMed:21685362}.
CONFLICT 199 199 K -> R (in Ref. 1; AAF18974).
{ECO:0000305}.
CONFLICT 262 263 SG -> TR (in Ref. 3; AAF87323).
{ECO:0000305}.
CONFLICT 309 310 KK -> PRN (in Ref. 3; AAF87323).
{ECO:0000305}.
HELIX 374 384 {ECO:0000244|PDB:2YHO}.
TURN 388 390 {ECO:0000244|PDB:2YHO}.
STRAND 391 394 {ECO:0000244|PDB:2YHO}.
STRAND 397 400 {ECO:0000244|PDB:2YHO}.
HELIX 409 412 {ECO:0000244|PDB:2YHO}.
TURN 419 421 {ECO:0000244|PDB:2YHO}.
STRAND 427 430 {ECO:0000244|PDB:2YHO}.
SEQUENCE 445 AA; 49910 MW; 342E643B0532B45C CRC64;
MLCYVTRPDA VLMEVEVEAK ANGEDCLNQV CRRLGIIEVD YFGLQFTGSK GESLWLNLRN
RISQQMDGLA PYRLKLRVKF FVEPHLILQE QTRHIFFLHI KEALLAGHLL CSPEQAVELS
ALLAQTKFGD YNQNTAKYNY EELCAKELSS ATLNSIVAKH KELEGTSQAS AEYQVLQIVS
AMENYGIEWH SVRDSEGQKL LIGVGPEGIS ICKDDFSPIN RIAYPVVQMA TQSGKNVYLT
VTKESGNSIV LLFKMISTRA ASGLYRAITE THAFYRCDTV TSAVMMQYSR DLKGHLASLF
LNENINLGKK YVFDIKRTSK EVYDHARRAL YNAGVVDLVS RNNQSPSHSP LKSSESSMNC
SSCEGLSCQQ TRVLQEKLRK LKEAMLCMVC CEEEINSTFC PCGHTVCCES CAAQLQSCPV
CRSRVEHVQH VYLPTHTSLL NLTVI


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Catalog number Product name Quantity
EIAAB26019 BM-023,BZF1,E3 ubiquitin-protein ligase MYLIP,Homo sapiens,Human,Idol,IDOL,Inducible degrader of the LDL-receptor,MIR,MYLIP,Myosin regulatory light chain interacting protein,PP5242
EIAAB26020 E3 ubiquitin-protein ligase MYLIP,Idol,Inducible degrader of the LDL-receptor,MIR,Mylip,Myosin regulatory light chain interacting protein,Rat,Rattus norvegicus
EIAAB26021 E3 ubiquitin-protein ligase MYLIP,Idol,Inducible degrader of the LDL-receptor,MIR,Mouse,Mus musculus,Mylip,Myosin regulatory light chain-interacting protein
CSB-EL015319RA Rat myosin regulatory light chain interacting protein (MYLIP) ELISA kit, Species Rat, Sample Type serum, plasma 96T
201-20-3589 MYLIP{myosin regulatory light chain interacting protein}rabbit.pAb 0.2ml
MYLK2 MYLIP Gene myosin regulatory light chain interacting protein
CSB-EL015319MO Mouse E3 ubiquitin-protein ligase MYLIP(MYLIP) ELISA kit SpeciesMouse 96T
CSB-EL015319HU Human E3 ubiquitin-protein ligase MYLIP(MYLIP) ELISA kit SpeciesHuman 96T
CSB-EL015319RA Rat E3 ubiquitin-protein ligase MYLIP(MYLIP) ELISA kit SpeciesRat 96T
CSB-EL015319HU Human E3 ubiquitin-protein ligase MYLIP(MYLIP) ELISA kit 96T
CSB-EL015319MO Mouse E3 ubiquitin-protein ligase MYLIP(MYLIP) ELISA kit 96T
MYLIP_MOUSE ELISA Kit FOR E3 ubiquitin-protein ligase MYLIP; organism: Mouse; gene name: Mylip 96T
CSB-EL015319RA Rat E3 ubiquitin-protein ligase MYLIP(MYLIP) ELISA kit 96T
CSB-EL015319MO Mouse myosin regulatory light chain interacting protein (MYLIP) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL015319HU Human myosin regulatory light chain interacting protein (MYLIP) ELISA kit, Species Human, Sample Type serum, plasma 96T
MYLIP MYL7 Gene myosin, light chain 7, regulatory
EIAAB33372 Kiaa0161,Mouse,Mus musculus,Probable E3 ubiquitin-protein ligase RNF144A,RING finger protein 144A,Rnf144,Rnf144a,Ubce7ip4,UbcM4-interacting protein 4,Ubiquitin-conjugating enzyme 7-interacting protein
EIAAB33371 Homo sapiens,Human,KIAA0161,Probable E3 ubiquitin-protein ligase RNF144A,RING finger protein 144A,RNF144,RNF144A,UBCE7IP4,UbcM4-interacting protein 4,Ubiquitin-conjugating enzyme 7-interacting protein
EIAAB35496 E3 ubiquitin-protein ligase RNF216,Homo sapiens,Human,RING finger protein 216,RNF216,Triad domain-containing protein 3,TRIAD3,UBCE7IP1,Ubiquitin-conjugating enzyme 7-interacting protein 1,ZIN,Zinc fin
EIAAB35497 E3 ubiquitin-protein ligase RNF216,Mouse,Mus musculus,RING finger protein 216,Rnf216,Triad domain-containing protein 3,Triad3,Ubce7ip1,UbcM4-interacting protein 83,Ubiquitin-conjugating enzyme 7-inter
EIAAB34857 BAP1,DING,E3 ubiquitin-protein ligase RING2,HIP2-interacting protein 3,HIPI3,Homo sapiens,Human,Huntingtin-interacting protein 2-interacting protein 3,Protein DinG,RING finger protein 1B,RING finger p
EIAAB45296 Ac2-121,E3 ubiquitin-protein ligase UHRF1,Liver regeneration-related protein LRRG126,Rat,Rattus norvegicus,Ubiquitin-like PHD and RING finger domain-containing protein 1,Ubiquitin-like-containing PHD
71208 MYLIP-IDOL Human Recombinant Protein 20
EIAAB47415 Androgen receptor N-terminal-interacting protein,ARNIP,CHIMP,CH-rich-interacting match with PLAG1,E3 ubiquitin-protein ligase Pirh2,Homo sapiens,hPirh2,Human,p53-induced RING-H2 protein,PIRH2,RCHY1,RI
18-003-42502 Ubiquitin ligase protein RING2 - EC 6.3.2.-; RING finger protein 2; RING finger protein 1B; RING1b; RING finger protein BAP-1; DinG protein; Huntingtin-interacting protein 2-interacting protein 3; HIP 0.1 mg Protein A

Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP2199: Seed Development
WP2292: Chemokine signaling pathway
WP211: BMP signaling pathway
WP2272: Pathogenic Escherichia coli infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1625: Base excision repair
WP1654: gamma-Hexachlorocyclohexane degradation
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1676: Non-homologous end-joining
WP1678: Nucleotide excision repair
WP1714: Tyrosine metabolism
WP1909: Signal regulatory protein (SIRP) family interactions
WP731: Sterol regulatory element binding protein related
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1614: 1- and 2-Methylnaphthalene degradation
WP1616: ABC transporters

Related Genes :
[RBX1 RNF75 ROC1] E3 ubiquitin-protein ligase RBX1 (EC 2.3.2.27) (EC 2.3.2.32) (E3 ubiquitin-protein transferase RBX1) (Protein ZYP) (RING finger protein 75) (RING-box protein 1) (Rbx1) (Regulator of cullins 1) (ROC1) [Cleaved into: E3 ubiquitin-protein ligase RBX1, N-terminally processed (E3 ubiquitin-protein transferase RBX1, N-terminally processed)]
[K5] E3 ubiquitin-protein ligase MIR2 (EC 2.3.2.27) (IE1A protein) (Modulator of immune recognition 2) (ORF K5) (RING-type E3 ubiquitin transferase MIR2)
[Traf2] TNF receptor-associated factor 2 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF2) (RING-type E3 ubiquitin transferase TRAF2)
[K3] E3 ubiquitin-protein ligase MIR1 (EC 2.3.2.27) (IE1B protein) (Modulator of immune recognition 1) (ORF K3) (RING-type E3 ubiquitin transferase MIR1)
[TRAF2 TRAP3] TNF receptor-associated factor 2 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF2) (RING-type E3 ubiquitin transferase TRAF2) (Tumor necrosis factor type 2 receptor-associated protein 3)
[RCHY1 ARNIP CHIMP PIRH2 RNF199 ZNF363] RING finger and CHY zinc finger domain-containing protein 1 (EC 2.3.2.27) (Androgen receptor N-terminal-interacting protein) (CH-rich-interacting match with PLAG1) (E3 ubiquitin-protein ligase Pirh2) (RING finger protein 199) (RING-type E3 ubiquitin transferase RCHY1) (Zinc finger protein 363) (p53-induced RING-H2 protein) (hPirh2)
[Rbx1] E3 ubiquitin-protein ligase RBX1 (EC 2.3.2.27) (EC 2.3.2.32) (E3 ubiquitin-protein transferase RBX1) (RING finger protein 75) (RING-box protein 1) (Rbx1) [Cleaved into: E3 ubiquitin-protein ligase RBX1, N-terminally processed]
[TRAF6 RNF85] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (Interleukin-1 signal transducer) (RING finger protein 85) (RING-type E3 ubiquitin transferase TRAF6)
[RNF2 BAP1 DING HIPI3 RING1B] E3 ubiquitin-protein ligase RING2 (EC 2.3.2.27) (Huntingtin-interacting protein 2-interacting protein 3) (HIP2-interacting protein 3) (Protein DinG) (RING finger protein 1B) (RING1b) (RING finger protein 2) (RING finger protein BAP-1) (RING-type E3 ubiquitin transferase RING2)
[MDM2] E3 ubiquitin-protein ligase Mdm2 (EC 2.3.2.27) (Double minute 2 protein) (Hdm2) (Oncoprotein Mdm2) (RING-type E3 ubiquitin transferase Mdm2) (p53-binding protein Mdm2)
[TRIM28 KAP1 RNF96 TIF1B] Transcription intermediary factor 1-beta (TIF1-beta) (E3 SUMO-protein ligase TRIM28) (EC 2.3.2.27) (KRAB-associated protein 1) (KAP-1) (KRAB-interacting protein 1) (KRIP-1) (Nuclear corepressor KAP-1) (RING finger protein 96) (RING-type E3 ubiquitin transferase TIF1-beta) (Tripartite motif-containing protein 28)
[STUB1 CHIP PP1131] E3 ubiquitin-protein ligase CHIP (EC 2.3.2.27) (Antigen NY-CO-7) (CLL-associated antigen KW-8) (Carboxy terminus of Hsp70-interacting protein) (RING-type E3 ubiquitin transferase CHIP) (STIP1 homology and U box-containing protein 1)
[AMFR RNF45] E3 ubiquitin-protein ligase AMFR (EC 2.3.2.27) (Autocrine motility factor receptor) (AMF receptor) (RING finger protein 45) (RING-type E3 ubiquitin transferase AMFR) (gp78)
[Stub1 Chip] STIP1 homology and U box-containing protein 1 (EC 2.3.2.27) (Carboxy terminus of Hsp70-interacting protein) (E3 ubiquitin-protein ligase CHIP) (RING-type E3 ubiquitin transferase CHIP)
[Rnf2 DinG Ring1b] E3 ubiquitin-protein ligase RING2 (EC 2.3.2.27) (RING finger protein 1B) (RING1b) (RING finger protein 2) (RING-type E3 ubiquitin transferase RING2)
[Traf6] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (RING-type E3 ubiquitin transferase TRAF6)
[TRIP12 KIAA0045 ULF] E3 ubiquitin-protein ligase TRIP12 (EC 2.3.2.26) (E3 ubiquitin-protein ligase for Arf) (ULF) (HECT-type E3 ubiquitin transferase TRIP12) (Thyroid receptor-interacting protein 12) (TR-interacting protein 12) (TRIP-12)
[RIN2 AMFR-1A At4g25230 F24A6.70] E3 ubiquitin protein ligase RIN2 (EC 2.3.2.27) (AMF receptor-like protein 1A) (RING-type E3 ubiquitin transferase RIN2) (RPM1-interacting protein 2)
[Ubr3 Kiaa2024 Zfp650 Znf650] E3 ubiquitin-protein ligase UBR3 (EC 2.3.2.27) (N-recognin-3) (RING-type E3 ubiquitin transferase UBR3) (Ubiquitin-protein ligase E3-alpha-3) (Ubiquitin-protein ligase E3-alpha-III) (Zinc finger protein 650)
[Rnf128 Grail Greul1 MNCb-3816] E3 ubiquitin-protein ligase RNF128 (EC 2.3.2.27) (Gene related to anergy in lymphocytes protein) (Goliath-related E3 ubiquitin-protein ligase 1) (RING finger protein 128) (RING-type E3 ubiquitin transferase RNF128)
[Mib1 Dip1 Kiaa1323 Mib] E3 ubiquitin-protein ligase MIB1 (EC 2.3.2.27) (DAPK-interacting protein 1) (DIP-1) (Mind bomb homolog 1) (RING-type E3 ubiquitin transferase MIB1)
[SIAH1 HUMSIAH] E3 ubiquitin-protein ligase SIAH1 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SIAH1) (Seven in absentia homolog 1) (Siah-1) (Siah-1a)
[Rnf31 Paul] E3 ubiquitin-protein ligase RNF31 (EC 2.3.2.31) (HOIL-1-interacting protein) (HOIP) (Putative Ariadne-like ubiquitin ligase) (PAUL) (RING finger protein 31) (RING-type E3 ubiquitin transferase RNF31)
[RNF4 SNURF RES4-26] E3 ubiquitin-protein ligase RNF4 (EC 2.3.2.27) (RING finger protein 4) (RING-type E3 ubiquitin transferase RNF4) (Small nuclear ring finger protein) (Protein SNURF)
[Amfr] E3 ubiquitin-protein ligase AMFR (EC 2.3.2.27) (Autocrine motility factor receptor) (AMF receptor) (RING-type E3 ubiquitin transferase AMFR)
[Pias2 Miz1 Piasx] E3 SUMO-protein ligase PIAS2 (EC 2.3.2.27) (Androgen receptor-interacting protein 3) (ARIP3) (DAB2-interacting protein) (DIP) (Msx-interacting zinc finger protein) (Protein inhibitor of activated STAT x) (Protein inhibitor of activated STAT2) (RING-type E3 ubiquitin transferase PIAS2)
[TRIM2 KIAA0517 RNF86] Tripartite motif-containing protein 2 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRIM2) (RING finger protein 86) (RING-type E3 ubiquitin transferase TRIM2)
[SH3RF2 POSH3 POSHER PPP1R39 RNF158] E3 ubiquitin-protein ligase SH3RF2 (EC 2.3.2.27) (Heart protein phosphatase 1-binding protein) (HEPP1) (POSH-eliminating RING protein) (Protein phosphatase 1 regulatory subunit 39) (RING finger protein 158) (RING-type E3 ubiquitin transferase SH3RF2) (SH3 domain-containing RING finger protein 2)
[XIAP API3 BIRC4 IAP3] E3 ubiquitin-protein ligase XIAP (EC 2.3.2.27) (Baculoviral IAP repeat-containing protein 4) (IAP-like protein) (ILP) (hILP) (Inhibitor of apoptosis protein 3) (IAP-3) (hIAP-3) (hIAP3) (RING-type E3 ubiquitin transferase XIAP) (X-linked inhibitor of apoptosis protein) (X-linked IAP)
[Uhrf1 Np95] E3 ubiquitin-protein ligase UHRF1 (EC 2.3.2.27) (Nuclear protein 95) (Nuclear zinc finger protein Np95) (RING-type E3 ubiquitin transferase UHRF1) (Ubiquitin-like PHD and RING finger domain-containing protein 1) (mUhrf1) (Ubiquitin-like-containing PHD and RING finger domains protein 1)

Bibliography :
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