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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.
31-JAN-2018, entry version 151.
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, ENZYME 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: 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.
-!- ENZYME 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;
Q8TD10:MIPOL1; NbExp=3; IntAct=EBI-6952711, EBI-2548751;
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; 26.
IntAct; Q8WY64; 25.
MINT; MINT-268789; -.
STRING; 9606.ENSP00000349298; -.
iPTMnet; Q8WY64; -.
PhosphoSitePlus; Q8WY64; -.
BioMuta; MYLIP; -.
DMDM; 84028296; -.
PaxDb; Q8WY64; -.
PRIDE; Q8WY64; -.
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; -.
PharmGKB; PA134942677; -.
eggNOG; ENOG410IG7I; Eukaryota.
eggNOG; ENOG410XRZN; LUCA.
GeneTree; ENSGT00890000139341; -.
HOGENOM; HOG000007353; -.
HOVERGEN; HBG052549; -.
InParanoid; Q8WY64; -.
KO; K10637; -.
OMA; NCRVKIT; -.
OrthoDB; EOG091G0A4V; -.
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; -.
CleanEx; HS_MYLIP; -.
ExpressionAtlas; Q8WY64; baseline and differential.
Genevisible; Q8WY64; HS.
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:0006928; P:movement of cell or subcellular component; IMP:UniProtKB.
GO; GO:0010989; P:negative regulation of low-density lipoprotein particle clearance; IEA:Ensembl.
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:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IBA:GO_Central.
GO; GO:0032803; P:regulation of low-density lipoprotein particle receptor catabolic process; IEA:Ensembl.
CDD; cd14473; FERM_B-lobe; 1.
Gene3D; 1.20.80.10; -; 1.
Gene3D; 2.30.29.30; -; 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.
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; SSF50729; SSF50729; 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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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


 

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