Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Perilipin-3 (47 kDa mannose 6-phosphate receptor-binding protein) (47 kDa MPR-binding protein) (Cargo selection protein TIP47) (Mannose-6-phosphate receptor-binding protein 1) (Placental protein 17) (PP17)

 PLIN3_HUMAN             Reviewed;         434 AA.
O60664; A8K4Y9; K7EQF4; Q53G77; Q9BS03; Q9UBD7; Q9UP92;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 3.
25-OCT-2017, entry version 166.
RecName: Full=Perilipin-3;
AltName: Full=47 kDa mannose 6-phosphate receptor-binding protein;
Short=47 kDa MPR-binding protein;
AltName: Full=Cargo selection protein TIP47;
AltName: Full=Mannose-6-phosphate receptor-binding protein 1;
AltName: Full=Placental protein 17;
Short=PP17;
Name=PLIN3; Synonyms=M6PRBP1, TIP47;
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), VARIANTS VAL-56 AND ALA-275,
FUNCTION, INTERACTION WITH M6PR AND IGF2R, HOMOOLIGOMERIZATION, AND
SUBCELLULAR LOCATION.
PubMed=9590177; DOI=10.1016/S0092-8674(00)81171-X;
Diaz E., Pfeffer S.R.;
"TIP47: a cargo selection device for mannose 6-phosphate receptor
trafficking.";
Cell 93:433-443(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS VAL-56 AND
ALA-275.
TISSUE=Placenta;
PubMed=9874244; DOI=10.1046/j.1432-1327.1998.2580752.x;
Than N.G., Sumegi B., Than G.N., Kispal G., Bohn H.;
"Cloning and sequence analysis of cDNAs encoding human placental
tissue protein 17 (PP17) variants.";
Eur. J. Biochem. 258:752-757(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS VAL-56 AND
ALA-275.
TISSUE=Placenta;
PubMed=10393528; DOI=10.1159/000030062;
Than N.G., Sumegi B., Than G.N., Kispal G., Bohn H.;
"Cloning and sequencing of human oncodevelopmental soluble placental
tissue protein 17 (PP17): homology with adipophilin and the mouse
adipose differentiation-related protein.";
Tumor Biol. 20:184-192(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ALA-275.
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ALA-275.
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
ALA-275.
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
VAL-56 AND ALA-275.
TISSUE=Colon, and Muscle;
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]
CHARACTERIZATION.
TISSUE=Placenta;
PubMed=6856484;
Bohn H., Kraus W., Winckler W.;
"Purification and characterization of two new soluble placental tissue
proteins (PP13 and PP17).";
Oncodev. Biol. Med. 4:343-350(1983).
[10]
SUBCELLULAR LOCATION.
PubMed=15545278; DOI=10.1074/jbc.M407194200;
Robenek H., Lorkowski S., Schnoor M., Troyer D.;
"Spatial integration of TIP47 and adipophilin in macrophage lipid
bodies.";
J. Biol. Chem. 280:5789-5794(2005).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130; THR-170; SER-175
AND SER-179, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-65, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-91; SER-130;
SER-148; THR-216; SER-217 AND SER-241, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[20]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-122, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[21]
SUBCELLULAR LOCATION.
PubMed=26357594; DOI=10.7717/peerj.1213;
Chughtai A.A., Kassak F., Kostrouchova M., Novotny J.P., Krause M.W.,
Saudek V., Kostrouch Z., Kostrouchova M.;
"Perilipin-related protein regulates lipid metabolism in C. elegans.";
PeerJ 3:E1213-E1213(2015).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Required for the transport of mannose 6-phosphate
receptors (MPR) from endosomes to the trans-Golgi network.
{ECO:0000269|PubMed:9590177}.
-!- SUBUNIT: Homooligomer. Interacts with M6PR (via the cytoplasmic
domain). Interacts with IGF2R (via the cytoplasmic domain).
Isoform 2 may exist as a homodimer (known as PP17C).
{ECO:0000269|PubMed:9590177}.
-!- INTERACTION:
Q9WMX2:- (xeno); NbExp=5; IntAct=EBI-725795, EBI-6863748;
Q96DZ9:CMTM5; NbExp=3; IntAct=EBI-725795, EBI-2548702;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15545278,
ECO:0000269|PubMed:26357594, ECO:0000269|PubMed:9590177}. Endosome
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. Lipid droplet {ECO:0000305}.
Note=Membrane associated on endosomes. Detected in the envelope
and the core of lipid bodies and in lipid sails. {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=O60664-1; Sequence=Displayed;
Note=PP17b.;
Name=2;
IsoId=O60664-2; Sequence=VSP_004664;
Note=PP17a.;
Name=3;
IsoId=O60664-3; Sequence=VSP_040325;
Name=4;
IsoId=O60664-4; Sequence=VSP_047038;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the perilipin family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF057140; AAC39751.1; -; mRNA.
EMBL; AF055574; AAD11622.1; -; mRNA.
EMBL; AF051314; AAD11619.1; -; mRNA.
EMBL; AF051315; AAD11620.1; -; mRNA.
EMBL; BT007235; AAP35899.1; -; mRNA.
EMBL; AK291104; BAF83793.1; -; mRNA.
EMBL; AK223054; BAD96774.1; -; mRNA.
EMBL; AK225045; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC027319; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001590; AAH01590.1; -; mRNA.
EMBL; BC005818; AAH05818.1; -; mRNA.
EMBL; BC007566; AAH07566.1; -; mRNA.
EMBL; BC019278; AAH19278.1; -; mRNA.
CCDS; CCDS12137.1; -. [O60664-1]
CCDS; CCDS59337.1; -. [O60664-4]
CCDS; CCDS59338.1; -. [O60664-3]
RefSeq; NP_001157661.1; NM_001164189.1. [O60664-3]
RefSeq; NP_001157666.1; NM_001164194.1. [O60664-4]
RefSeq; NP_005808.3; NM_005817.4. [O60664-1]
UniGene; Hs.140452; -.
ProteinModelPortal; O60664; -.
SMR; O60664; -.
BioGrid; 115520; 72.
CORUM; O60664; -.
IntAct; O60664; 31.
MINT; MINT-5000803; -.
STRING; 9606.ENSP00000221957; -.
DrugBank; DB01279; Galsulfase.
DrugBank; DB01271; Idursulfase.
iPTMnet; O60664; -.
PhosphoSitePlus; O60664; -.
SwissPalm; O60664; -.
BioMuta; PLIN3; -.
REPRODUCTION-2DPAGE; IPI00303882; -.
EPD; O60664; -.
MaxQB; O60664; -.
PaxDb; O60664; -.
PeptideAtlas; O60664; -.
PRIDE; O60664; -.
TopDownProteomics; O60664-1; -. [O60664-1]
TopDownProteomics; O60664-2; -. [O60664-2]
TopDownProteomics; O60664-3; -. [O60664-3]
DNASU; 10226; -.
Ensembl; ENST00000221957; ENSP00000221957; ENSG00000105355. [O60664-1]
Ensembl; ENST00000585479; ENSP00000465596; ENSG00000105355. [O60664-3]
Ensembl; ENST00000592528; ENSP00000467803; ENSG00000105355. [O60664-4]
GeneID; 10226; -.
KEGG; hsa:10226; -.
UCSC; uc002mbj.3; human. [O60664-1]
CTD; 10226; -.
DisGeNET; 10226; -.
EuPathDB; HostDB:ENSG00000105355.8; -.
GeneCards; PLIN3; -.
H-InvDB; HIX0014673; -.
HGNC; HGNC:16893; PLIN3.
HPA; HPA006427; -.
HPA; HPA066538; -.
MIM; 602702; gene.
neXtProt; NX_O60664; -.
OpenTargets; ENSG00000105355; -.
PharmGKB; PA165394001; -.
eggNOG; ENOG410IJG1; Eukaryota.
eggNOG; ENOG410XTQ5; LUCA.
GeneTree; ENSGT00500000044795; -.
HOGENOM; HOG000033816; -.
HOVERGEN; HBG002935; -.
InParanoid; O60664; -.
KO; K20287; -.
OMA; LGKSEEW; -.
OrthoDB; EOG091G0D6Q; -.
PhylomeDB; O60664; -.
TreeFam; TF328397; -.
Reactome; R-HSA-163560; Triglyceride catabolism.
Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
SIGNOR; O60664; -.
ChiTaRS; PLIN3; human.
GeneWiki; M6PRBP1; -.
GenomeRNAi; 10226; -.
PMAP-CutDB; O60664; -.
PRO; PR:O60664; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105355; -.
CleanEx; HS_M6PRBP1; -.
ExpressionAtlas; O60664; baseline and differential.
Genevisible; O60664; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005768; C:endosome; TAS:ProtInc.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0030133; C:transport vesicle; TAS:Reactome.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0016192; P:vesicle-mediated transport; TAS:ProtInc.
InterPro; IPR004279; Perilipin.
Pfam; PF03036; Perilipin; 1.
PIRSF; PIRSF036881; PAT; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Coiled coil; Complete proteome;
Cytoplasm; Endosome; Isopeptide bond; Lipid droplet; Membrane;
Phosphoprotein; Polymorphism; Reference proteome; Transport;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
CHAIN 2 434 Perilipin-3.
/FTId=PRO_0000099890.
COILED 252 277 {ECO:0000255}.
COILED 353 377 {ECO:0000255}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 31 31 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 65 65 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 91 91 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 130 130 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 148 148 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 170 170 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 175 175 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 179 179 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 216 216 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 217 217 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 241 241 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 122 122 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
VAR_SEQ 1 183 Missing (in isoform 2).
{ECO:0000303|PubMed:10393528,
ECO:0000303|PubMed:9874244}.
/FTId=VSP_004664.
VAR_SEQ 116 127 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_047038.
VAR_SEQ 321 321 Missing (in isoform 3).
{ECO:0000303|Ref.6}.
/FTId=VSP_040325.
VARIANT 56 56 I -> V (in dbSNP:rs8289).
{ECO:0000269|PubMed:10393528,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9590177,
ECO:0000269|PubMed:9874244}.
/FTId=VAR_022780.
VARIANT 275 275 V -> A (in dbSNP:rs9973235).
{ECO:0000269|PubMed:10393528,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9590177,
ECO:0000269|PubMed:9874244,
ECO:0000269|Ref.4, ECO:0000269|Ref.6}.
/FTId=VAR_024559.
CONFLICT 77 77 G -> W (in Ref. 2; AAD11622).
{ECO:0000305}.
CONFLICT 109 111 ILQ -> MLR (in Ref. 2; AAD11622).
{ECO:0000305}.
SEQUENCE 434 AA; 47075 MW; 67B2B9CDBC523043 CRC64;
MSADGAEADG STQVTVEEPV QQPSVVDRVA SMPLISSTCD MVSAAYASTK ESYPHIKTVC
DAAEKGVRTL TAAAVSGAQP ILSKLEPQIA SASEYAHRGL DKLEENLPIL QQPTEKVLAD
TKELVSSKVS GAQEMVSSAK DTVATQLSEA VDATRGAVQS GVDKTKSVVT GGVQSVMGSR
LGQMVLSGVD TVLGKSEEWA DNHLPLTDAE LARIATSLDG FDVASVQQQR QEQSYFVRLG
SLSERLRQHA YEHSLGKLRA TKQRAQEALL QLSQVLSLME TVKQGVDQKL VEGQEKLHQM
WLSWNQKQLQ GPEKEPPKPE QVESRALTMF RDIAQQLQAT CTSLGSSIQG LPTNVKDQVQ
QARRQVEDLQ ATFSSIHSFQ DLSSSILAQS RERVASAREA LDHMVEYVAQ NTPVTWLVGP
FAPGITEKAP EEKK


Related products :

Catalog number Product name Quantity
15-288-22299F Mannose-6-phosphate receptor-binding protein 1 - Cargo selection protein TIP47; 47 kDa mannose 6-phosphate receptor-binding protein; 47 kDa MPR-binding protein; Placental protein 17; PP17 Polyclonal 0.1 mg
15-288-22299F Mannose-6-phosphate receptor-binding protein 1 - Cargo selection protein TIP47; 47 kDa mannose 6-phosphate receptor-binding protein; 47 kDa MPR-binding protein; Placental protein 17; PP17 Polyclonal 0.05 mg
10-288-22299F Mannose-6-phosphate receptor-binding protein 1 - Cargo selection protein TIP47; 47 kDa mannose 6-phosphate receptor-binding protein; 47 kDa MPR-binding protein; Placental protein 17; PP17 0.1 mg
10-288-22299F Mannose-6-phosphate receptor-binding protein 1 - Cargo selection protein TIP47; 47 kDa mannose 6-phosphate receptor-binding protein; 47 kDa MPR-binding protein; Placental protein 17; PP17 0.05 mg
EIAAB31521 47 kDa mannose 6-phosphate receptor-binding protein,47 kDa MPR-binding protein,Cargo selection protein TIP47,Homo sapiens,Human,M6PRBP1,Mannose-6-phosphate receptor-binding protein 1,Perilipin-3,Place
EIAAB31522 Cargo selection protein TIP47,M6PRBP1,Mannose-6-phosphate receptor-binding protein 1,Perilipin-3,Pig,PLIN3,Sus scrofa,TIP47
EIAAB31520 Cargo selection protein TIP47,M6prbp1,Mannose-6-phosphate receptor-binding protein 1,Mouse,Mus musculus,Perilipin-3,Plin3,Tip47
201-20-3202 M6PRBP1{mannose-6-phosphate receptor binding protein 1}rabbit.pAb 0.2ml
E1480h ELISA COLEC1,Collectin-1,Homo sapiens,Human,Mannan-binding protein,Mannose-binding lectin,Mannose-binding protein C,MBL,MBL2,MBP1,MBP-C 96T
E1480h ELISA kit COLEC1,Collectin-1,Homo sapiens,Human,Mannan-binding protein,Mannose-binding lectin,Mannose-binding protein C,MBL,MBL2,MBP1,MBP-C 96T
U1480h CLIA COLEC1,Collectin-1,Homo sapiens,Human,Mannan-binding protein,Mannose-binding lectin,Mannose-binding protein C,MBL,MBL2,MBP1,MBP-C 96T
GS-1241a mannose-6-phosphate receptor binding protein 1 primary antibody, Host: Rabbit 200ul
E1480p ELISA kit 27 kDa mannan-binding protein monomeric subunit,Mannose-binding lectin,Mannose-binding protein C,MBL,MBL2,MBP-C,Pig,pMBP-27,Sus scrofa 96T
U1480p CLIA 27 kDa mannan-binding protein monomeric subunit,Mannose-binding lectin,Mannose-binding protein C,MBL,MBL2,MBP-C,Pig,pMBP-27,Sus scrofa 96T
E1480p ELISA 27 kDa mannan-binding protein monomeric subunit,Mannose-binding lectin,Mannose-binding protein C,MBL,MBL2,MBP-C,Pig,pMBP-27,Sus scrofa 96T
GWB-80657F Mannose-6-phosphate Receptor Binding Protein 1 (M6PRBP1) Rabbit anti-Human Polyclonal (N-Terminus) Antibody
CSB-EL013294HU Human mannose-6-phosphate receptor binding protein 1 (M6PRBP1) ELISA kit, Species Human, Sample Type serum, plasma 96T
U1629h CLIA 300 kDa mannose 6-phosphate receptor,Cation-independent mannose-6-phosphate receptor,CI Man-6-P receptor,CI-MPR,Homo sapiens,Human,IGF2R,IGF-II receptor,Insulin-like growth factor 2 receptor,Insu 96T
E1629h ELISA 300 kDa mannose 6-phosphate receptor,Cation-independent mannose-6-phosphate receptor,CI Man-6-P receptor,CI-MPR,Homo sapiens,Human,IGF2R,IGF-II receptor,Insulin-like growth factor 2 receptor,Ins 96T
E1629b ELISA 300 kDa mannose 6-phosphate receptor,Bos taurus,Bovine,Cation-independent mannose-6-phosphate receptor,CI Man-6-P receptor,CI-MPR,IGF2R,IGF-II receptor,Insulin-like growth factor 2 receptor,Insu 96T
U1629b CLIA 300 kDa mannose 6-phosphate receptor,Bos taurus,Bovine,Cation-independent mannose-6-phosphate receptor,CI Man-6-P receptor,CI-MPR,IGF2R,IGF-II receptor,Insulin-like growth factor 2 receptor,Insul 96T
E1629b ELISA kit 300 kDa mannose 6-phosphate receptor,Bos taurus,Bovine,Cation-independent mannose-6-phosphate receptor,CI Man-6-P receptor,CI-MPR,IGF2R,IGF-II receptor,Insulin-like growth factor 2 receptor 96T
CSB-PA013294GA01HU Rabbit anti-human mannose-6-phosphate receptor binding protein 1 polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
CSB-PA013294GA01HU Rabbit anti-human mannose-6-phosphate receptor binding protein 1 polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul
E1629h ELISA kit 300 kDa mannose 6-phosphate receptor,Cation-independent mannose-6-phosphate receptor,CI Man-6-P receptor,CI-MPR,Homo sapiens,Human,IGF2R,IGF-II receptor,Insulin-like growth factor 2 recepto 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur