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Protein enabled homolog (NPC-derived proline-rich protein 1) (NDPP-1)

 ENAH_MOUSE              Reviewed;         802 AA.
Q03173; P70430; P70431; P70432; P70433; Q5D053;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-APR-2003, sequence version 2.
20-DEC-2017, entry version 162.
RecName: Full=Protein enabled homolog;
AltName: Full=NPC-derived proline-rich protein 1;
Short=NDPP-1;
Name=Enah; Synonyms=Mena, Ndpp1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=1420303; DOI=10.1016/0167-4781(92)90156-T;
Sazuka T., Tomooka Y., Kathju S., Ikawa Y., Noda M., Kumar S.;
"Identification of a developmentally regulated gene in the mouse
central nervous system which encodes a novel proline rich protein.";
Biochim. Biophys. Acta 1132:240-248(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), FUNCTION, TISSUE
SPECIFICITY, SUBCELLULAR LOCATION, ROLE IN L.MONOCYTOGENES MOBILITY,
MISCELLANEOUS, AND INTERACTION WITH PFN1.
TISSUE=Brain;
PubMed=8861907; DOI=10.1016/S0092-8674(00)81341-0;
Gertler F.B., Niebuhr K., Reinhard M., Wehland J., Soriano P.;
"Mena, a relative of VASP and Drosophila Enabled, is implicated in the
control of microfilament dynamics.";
Cell 87:227-239(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Brain;
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).
[4]
INTERACTION WITH APBB1; NEDD4 AND YAP1.
PubMed=9407065; DOI=10.1074/jbc.272.52.32869;
Ermekova K.S., Zambrano N., Linn H., Minopoli G., Gertler F.,
Russo T., Sudol M.;
"The WW domain of neural protein FE65 interacts with proline-rich
motifs in Mena, the mammalian homolog of Drosophila enabled.";
J. Biol. Chem. 272:32869-32877(1997).
[5]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL
STAGE, AND DISRUPTION PHENOTYPE.
PubMed=10069337; DOI=10.1016/S0896-6273(00)81092-2;
Lanier L.M., Gates M.A., Witke W., Menzies A.S., Wehman A.M.,
Macklis J.D., Kwiatkowski D., Soriano P., Gertler F.B.;
"Mena is required for neurulation and commissure formation.";
Neuron 22:313-325(1999).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-255 AND
SER-637.
PubMed=12134088; DOI=10.1091/mbc.E01-10-0102;
Loureiro J.J., Rubinson D.A., Bear J.E., Baltus G.A.,
Kwiatkowski A.V., Gertler F.B.;
"Critical roles of phosphorylation and actin binding motifs, but not
the central proline-rich region, for Ena/vasodilator-stimulated
phosphoprotein (VASP) function during cell migration.";
Mol. Biol. Cell 13:2533-2546(2002).
[7]
INTERACTION WITH ROBO4.
STRAIN=FVB/N;
PubMed=12941633; DOI=10.1016/S0012-1606(03)00258-6;
Park K.W., Morrison C.M., Sorensen L.K., Jones C.A., Rao Y.,
Chien C.-B., Wu J.Y., Urness L.D., Li D.Y.;
"Robo4 is a vascular-specific receptor that inhibits endothelial
migration.";
Dev. Biol. 261:251-267(2003).
[8]
ALTERNATIVE SPLICING (ISOFORM 6), PHOSPHORYLATION AT TYR-557, AND
INTERACTION WITH ABI1.
PubMed=12672821; DOI=10.1074/jbc.M301447200;
Tani K., Sato S., Sukezane T., Kojima H., Hirose H., Hanafusa H.,
Shishido T.;
"Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian
enabled (Mena) by c-Abl kinase.";
J. Biol. Chem. 278:21685-21692(2003).
[9]
INTERACTION WITH DNMBP.
PubMed=14506234; DOI=10.1074/jbc.M308104200;
Salazar M.A., Kwiatkowski A.V., Pellegrini L., Cestra G., Butler M.H.,
Rossman K.L., Serna D.M., Sondek J., Gertler F.B., De Camilli P.;
"Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology
domains, links dynamin to regulation of the actin cytoskeleton.";
J. Biol. Chem. 278:49031-49043(2003).
[10]
INTERACTION WITH FAT1.
PubMed=15148305; DOI=10.1083/jcb.200403006;
Tanoue T., Takeichi M.;
"Mammalian Fat1 cadherin regulates actin dynamics and cell-cell
contact.";
J. Cell Biol. 165:517-528(2004).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[12]
FUNCTION, AND PHOSPHORYLATION AT SER-255.
PubMed=15066263; DOI=10.1016/S0896-6273(04)00108-4;
Lebrand C., Dent E.W., Strasser G.A., Lanier L.M., Krause M.,
Svitkina T.M., Borisy G.G., Gertler F.B.;
"Critical role of Ena/VASP proteins for filopodia formation in neurons
and in function downstream of netrin-1.";
Neuron 42:37-49(2004).
[13]
INTERACTION WITH APBB1IP.
PubMed=15642358; DOI=10.1016/j.febslet.2004.10.110;
Jenzora A., Behrendt B., Small J.V., Wehland J., Stradal T.E.;
"PREL1 provides a link from Ras signalling to the actin cytoskeleton
via Ena/VASP proteins.";
FEBS Lett. 579:455-463(2005).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 AND SER-383, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Kidney, Lung, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[15]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-112 IN COMPLEX WITH
PRO-RICH PEPTIDE OF L.MONOCYTOGENES ACTA.
PubMed=10338211; DOI=10.1016/S0092-8674(00)80757-6;
Prehoda K.E., Lee D.J., Lim W.A.;
"Structure of the enabled/VASP homology 1 domain-peptide complex: a
key component in the spatial control of actin assembly.";
Cell 97:471-480(1999).
-!- FUNCTION: Ena/VASP proteins are actin-associated proteins involved
in a range of processes dependent on cytoskeleton remodeling and
cell polarity such as axon guidance and lamellipodial and
filopodial dynamics in migrating cells. ENAH induces the formation
of F-actin rich outgrowths in fibroblasts. Acts synergistically
with BAIAP2-alpha and downstream of NTN1 to promote filipodia
formation. {ECO:0000269|PubMed:10069337,
ECO:0000269|PubMed:12134088, ECO:0000269|PubMed:15066263,
ECO:0000269|PubMed:8861907}.
-!- SUBUNIT: Homotetramer (By similarity). Interacts with APBB1IP,
APBB1, PFN1 and ROBO4. Isoforms, containing the polyproline-rich
regions with PPLP motifs, bind the WW domain of APBB1IP. Isoforms,
containing the PPSY motif, bind, in vitro, to the WW2 and WW3
domains of NEDD4 and to the WW1 domain of YAP1. Binds the SH3
domain of BAIAP2-alpha but only after the autoinhibitory region of
BAIAP2-alpha has been blocked by interaction with CDC42.
Interacts, via the EVH1/WH1 domain, with the Pro-rich domains from
VCL, ZYX and Listeria monocytogenes actA and with TES (via LIM
domain). The TES LIM domain and the Pro-rich domains from VCL or
ZYX compete for the same binding site. Interaction with ZYX is
important for targeting ENAH to focal adhesions and enhances
production of actin-rich structures at the apical surface of
cells. Interacts, through the Pro-rich region, with the C-terminal
SH3 domain of DNMPB. Binds GPHN. Heterotrimer with TES and ACTL7A
(By similarity). Interacts with FAT1 (via EVH1 domains).
{ECO:0000250, ECO:0000269|PubMed:10338211,
ECO:0000269|PubMed:12672821, ECO:0000269|PubMed:12941633,
ECO:0000269|PubMed:14506234, ECO:0000269|PubMed:15148305,
ECO:0000269|PubMed:15642358, ECO:0000269|PubMed:8861907,
ECO:0000269|PubMed:9407065}.
-!- INTERACTION:
Q9UQB8:BAIAP2 (xeno); NbExp=3; IntAct=EBI-6083294, EBI-525456;
Q6XZF7-1:DNMBP (xeno); NbExp=2; IntAct=EBI-16085647, EBI-16085546;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10069337,
ECO:0000269|PubMed:12134088, ECO:0000269|PubMed:8861907}.
Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection,
lamellipodium {ECO:0000250}. Cell projection, filopodium
{ECO:0000250}. Cell junction, synapse {ECO:0000250}. Cell
junction, focal adhesion {ECO:0000250}. Note=Targeted to the
leading edge of lamellipodia and filopodia by MRL family members.
Colocalizes at filopodial tips with a number of other proteins
including vinculin and zyxlin. Colocalizes with N-WASP at the
leading edge. Colocalizes with GPHN and PFN at synapses (By
similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=5; Synonyms=Neural variant Mena+++, 140 kDa isoform;
IsoId=Q03173-1; Sequence=Displayed;
Name=1;
IsoId=Q03173-2; Sequence=VSP_007255;
Note=No experimental confirmation available. Ref.1 (BAA01570)
sequence differs from that shown due to several frameshifts.
{ECO:0000305};
Name=2; Synonyms=Mena, 80 kDa isoform;
IsoId=Q03173-3; Sequence=VSP_007259, VSP_007260;
Name=3; Synonyms=Neural variant Mena+;
IsoId=Q03173-4; Sequence=VSP_007259;
Note=Phosphorylated during neural development.;
Name=4; Synonyms=Neural variant Mena++;
IsoId=Q03173-5; Sequence=VSP_007257, VSP_007258;
Name=6; Synonyms=Mena(S);
IsoId=Q03173-6; Sequence=VSP_007259, VSP_007260, VSP_010565;
-!- TISSUE SPECIFICITY: Expressed in heart and testis, lower levels in
lung, skeletal muscle, kidney, pancreas and brain. Isoform 5 is
expressed exclusively in the brain. Isoform 2 is expressed
predominantly in brain, testis, ovary and fat. In the brain,
isoforms 2 and 5 are expressed at highest levels in the
hippocampus, cortex and midbrain, and at lowest levels in the
striatum and cerebellum. Isoform 6 is expressed in brain and
spleen. {ECO:0000269|PubMed:10069337, ECO:0000269|PubMed:1420303,
ECO:0000269|PubMed:8861907}.
-!- DEVELOPMENTAL STAGE: At 8.5 dpc, particularly enriched in the
neuroepithelium, the forebrain and the somites. Highly expressed
in the edges of the neural folds. By 10.5 dpc, detected in the
brain, dorsal root ganglia (DRG), somites and limb buds. Highly
expressed in the branchial and pharyngeal arches, neural crest-
derived structures that give rise to portions of the face and
neck. At 11 dpc, isoform 2, isoform 3 and isoform 5 are expressed
in embryonic brain (at protein level). Expression of isoform 3
decreases steadily and becomes almost undetectable by 16 dpc,
while expression of isoform 5 begins to increase from 13 dpc and
peaks between 16 and 18 dpc (at protein level).
{ECO:0000269|PubMed:10069337}.
-!- DOMAIN: The EVH2 domain is comprised of 3 regions. Block A is a
thymosin-like domain required for G-actin binding. The KLKR motif
within this block is essential for the G-actin binding and for
actin polymerization. Block B is required for F-actin binding and
subcellular location, and Block C for tetramerization.
-!- PTM: NTN1-induced PKA phosphorylation on Ser-255 directly
parallels the formation of filopodial protrusions.
{ECO:0000269|PubMed:12672821, ECO:0000269|PubMed:15066263}.
-!- DISRUPTION PHENOTYPE: Mutant animals are viable and recovered in
the appropriate Mendelian ratios. they are smaller than their
littermates until adulthood and exhibit abnormal cage behavior,
including reduced activity. {ECO:0000269|PubMed:10069337}.
-!- MISCELLANEOUS: Required to transform actin polymerization into
active movement for the propulsive force of Listeria
monocytogenes.
-!- SIMILARITY: Belongs to the Ena/VASP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA01570.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
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EMBL; D10727; BAA01570.1; ALT_FRAME; mRNA.
EMBL; U72520; AAC52863.1; -; mRNA.
EMBL; U72521; AAC52864.1; -; mRNA.
EMBL; U72522; AAC52865.1; -; mRNA.
EMBL; U72523; AAC52866.1; -; mRNA.
EMBL; BC062927; AAH62927.1; -; mRNA.
CCDS; CCDS78764.1; -. [Q03173-3]
PIR; S27200; S27200.
RefSeq; NP_001076590.1; NM_001083121.2. [Q03173-3]
UniGene; Mm.389224; -.
UniGene; Mm.87759; -.
PDB; 1EVH; X-ray; 1.80 A; A=1-112.
PDB; 4CC3; X-ray; 1.97 A; B/D/F/H=547-558.
PDBsum; 1EVH; -.
PDBsum; 4CC3; -.
ProteinModelPortal; Q03173; -.
SMR; Q03173; -.
BioGrid; 199446; 14.
DIP; DIP-29359N; -.
ELM; Q03173; -.
IntAct; Q03173; 8.
MINT; MINT-1215621; -.
STRING; 10090.ENSMUSP00000077781; -.
iPTMnet; Q03173; -.
PhosphoSitePlus; Q03173; -.
MaxQB; Q03173; -.
PaxDb; Q03173; -.
PeptideAtlas; Q03173; -.
PRIDE; Q03173; -.
Ensembl; ENSMUST00000111025; ENSMUSP00000106654; ENSMUSG00000022995. [Q03173-6]
Ensembl; ENSMUST00000193703; ENSMUSP00000141462; ENSMUSG00000022995. [Q03173-3]
GeneID; 13800; -.
KEGG; mmu:13800; -.
UCSC; uc007dxs.2; mouse. [Q03173-3]
CTD; 55740; -.
MGI; MGI:108360; Enah.
eggNOG; KOG4590; Eukaryota.
eggNOG; ENOG41101TS; LUCA.
GeneTree; ENSGT00730000110272; -.
HOGENOM; HOG000013015; -.
HOVERGEN; HBG006655; -.
InParanoid; Q03173; -.
KO; K05746; -.
PhylomeDB; Q03173; -.
Reactome; R-MMU-376176; Signaling by ROBO receptors.
ChiTaRS; Enah; mouse.
EvolutionaryTrace; Q03173; -.
PRO; PR:Q03173; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000022995; -.
CleanEx; MM_ENAH; -.
ExpressionAtlas; Q03173; baseline and differential.
Genevisible; Q03173; MM.
GO; GO:0015629; C:actin cytoskeleton; TAS:MGI.
GO; GO:0030054; C:cell junction; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0030175; C:filopodium; IDA:MGI.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; IDA:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0001725; C:stress fiber; IDA:MGI.
GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0005522; F:profilin binding; IDA:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; IDA:MGI.
GO; GO:0050699; F:WW domain binding; ISO:MGI.
GO; GO:0030036; P:actin cytoskeleton organization; IGI:MGI.
GO; GO:0007015; P:actin filament organization; IDA:UniProtKB.
GO; GO:0008154; P:actin polymerization or depolymerization; IDA:MGI.
GO; GO:0007411; P:axon guidance; IMP:MGI.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
GO; GO:0006928; P:movement of cell or subcellular component; IDA:UniProtKB.
GO; GO:0001843; P:neural tube closure; IGI:MGI.
Gene3D; 2.130.10.10; -; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR014885; VASP_tetra.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR000697; WH1/EVH1_dom.
Pfam; PF08776; VASP_tetra; 1.
Pfam; PF00568; WH1; 1.
SMART; SM00461; WH1; 1.
SUPFAM; SSF50729; SSF50729; 1.
PROSITE; PS50229; WH1; 1.
1: Evidence at protein level;
3D-structure; Actin-binding; Alternative splicing; Cell junction;
Cell projection; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Developmental protein; Differentiation; Neurogenesis;
Phosphoprotein; Reference proteome; Repeat; SH3-binding; Synapse.
CHAIN 1 802 Protein enabled homolog.
/FTId=PRO_0000086972.
DOMAIN 1 111 WH1. {ECO:0000255|PROSITE-
ProRule:PRU00410}.
REPEAT 175 179 1.
REPEAT 180 184 2.
REPEAT 185 189 3.
REPEAT 190 194 4.
REPEAT 195 199 5.
REPEAT 200 204 6.
REPEAT 205 209 7.
REGION 175 209 7 X 5 AA tandem repeats of [LM]-E-[QR]-
[EQ]-[QR].
REGION 623 799 EVH2.
REGION 623 643 EVH2 block A.
REGION 674 691 EVH2 block B.
REGION 765 799 EVH2 block C.
COILED 154 258 {ECO:0000255}.
COILED 767 797 {ECO:0000255}.
MOTIF 632 635 KLKR.
COMPBIAS 269 605 Pro-rich.
MOD_RES 144 144 Phosphoserine.
{ECO:0000244|PubMed:15345747}.
MOD_RES 255 255 Phosphoserine; by PKA.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:15066263}.
MOD_RES 383 383 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 557 557 Phosphotyrosine.
{ECO:0000269|PubMed:12672821}.
MOD_RES 738 738 Phosphoserine.
{ECO:0000250|UniProtKB:Q8N8S7}.
MOD_RES 740 740 Phosphoserine.
{ECO:0000250|UniProtKB:Q8N8S7}.
VAR_SEQ 1 412 Missing (in isoform 1).
{ECO:0000303|PubMed:1420303}.
/FTId=VSP_007255.
VAR_SEQ 117 135 Missing (in isoform 2, isoform 3 and
isoform 6). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8861907}.
/FTId=VSP_007259.
VAR_SEQ 117 131 Missing (in isoform 4).
{ECO:0000303|PubMed:8861907}.
/FTId=VSP_007257.
VAR_SEQ 132 135 CIFC -> VFYL (in isoform 4).
{ECO:0000303|PubMed:8861907}.
/FTId=VSP_007258.
VAR_SEQ 259 500 Missing (in isoform 2 and isoform 6).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8861907}.
/FTId=VSP_007260.
VAR_SEQ 561 594 Missing (in isoform 6). {ECO:0000305}.
/FTId=VSP_010565.
MUTAGEN 255 255 S->A: No change in subcellular location
nor colocalization with vinculin at focal
adhesions nor with N-WASP at the leading
edge. Loss of cell mobility function;
when associated with A-637.
{ECO:0000269|PubMed:12134088}.
MUTAGEN 255 255 S->D: No change in subcellular location
nor colocalization with vinculin at focal
adhesions nor with N-WASP at the leading
edge. No loss of cell mobility function;
when associated with D-637.
{ECO:0000269|PubMed:12134088}.
MUTAGEN 637 637 S->A: No change in subcellular location
nor colocalization with vinculin at focal
adhesions nor with N-WASP at the leading
edge. No loss of cell mobility function.
when associated with A-255.
{ECO:0000269|PubMed:12134088}.
MUTAGEN 637 637 S->D: No change in subcellular location
nor colocalization with vinculin at focal
adhesions nor with N-WASP at the leading
edge. No loss of cell mobility function.
when associated with D-255.
{ECO:0000269|PubMed:12134088}.
CONFLICT 500 500 G -> A (in Ref. 1; BAA01570).
{ECO:0000305}.
STRAND 3 17 {ECO:0000244|PDB:1EVH}.
TURN 18 21 {ECO:0000244|PDB:1EVH}.
STRAND 22 25 {ECO:0000244|PDB:1EVH}.
HELIX 26 28 {ECO:0000244|PDB:1EVH}.
STRAND 33 40 {ECO:0000244|PDB:1EVH}.
TURN 41 44 {ECO:0000244|PDB:1EVH}.
STRAND 45 52 {ECO:0000244|PDB:1EVH}.
TURN 53 55 {ECO:0000244|PDB:1EVH}.
STRAND 58 64 {ECO:0000244|PDB:1EVH}.
STRAND 74 81 {ECO:0000244|PDB:1EVH}.
STRAND 86 93 {ECO:0000244|PDB:1EVH}.
HELIX 94 111 {ECO:0000244|PDB:1EVH}.
SEQUENCE 802 AA; 85844 MW; 592BB975EE20F77F CRC64;
MSEQSICQAR AAVMVYDDAN KKWVPAGGST GFSRVHIYHH TGNNTFRVVG RKIQDHQVVI
NCAIPKGLKY NQATQTFHQW RDARQVYGLN FGSKEDANVF ASAMMHALEV LNSQEAAQSK
VTATQDSTNL RCIFCGPTLP RQNSQLPAQV QNGPSQEELE IQRRQLQEQQ RQKELERERM
ERERLERERL ERERLERERL EQEQLERQRQ EREHVERLER ERLERLERER QERERERLEQ
LEREQVEWER ERRMSNAAPS SDSSLSSAPL PEYSSCQPPS APPPSYAKVI SAPVSDATPD
YAVVTALPPT STPPTPPLRH AATRFATSLG SAFHPVLPHY ATVPRPLNKN SRPSSPVNTP
SSQPPAAKSC AWPTSNFSPL PPSPPIMISS PPGKATGPRP VLPVCVSSPV PQMPPSPTAP
NGSLDSVTYP VSPPPTSGPA APPPPPPPPP PPPPPPLPPP PLPPLASLSH CGSQASPPPG
TPLASTPSSK PSVLPSPSAG APASAETPLN PELGDSSASE PGLQAASQPA ESPTPQGLVL
GPPAPPPPPP LPSGPAYASA LPPPPGPPPP PPLPSTGPPP PPPPPPPLPN QAPPPPPPPP
APPLPASGIF SGSTSEDNRP LTGLAAAIAG AKLRKVSRVE DGSFPGGGNT GSVSLASSKA
DAGRGNGPLP LGGSGLMEEM SALLARRRRI AEKGSTIETE QKEDRNEDAE PITAKAPSTS
TPEPTRKPWE RTNTMNGSKS PVISRPKSTP SSQPSANGVQ TEGLDYDRLK QDILDEMRKE
LAKLKEELID AIRQELSKSN TA


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EIAAB30895 Apoptosis-associated nuclear protein,Homo sapiens,Human,PHLDA1,PHRIP,Pleckstrin homology-like domain family A member 1,PQR protein,PQ-rich protein,Proline- and glutamine-rich protein,Proline- and hist
EIAAB38854 Homo sapiens,Human,PBI,PROL5,Proline-rich protein 5,Proline-rich protein PBI,SMR3A,Submaxillary gland androgen-regulated protein 3A
EIAAB31724 Homo sapiens,Human,PNRC1,PROL2,Proline-rich nuclear receptor coactivator 1,Proline-rich protein 2,Protein B4-2
EIAAB32454 Basic proline-rich lacrimal protein,BPLP,Homo sapiens,Human,PRL1,PROL1,Proline-rich protein 1
EIAAB38855 Homo sapiens,Human,PBII,PRL3,PROL3,Proline-rich peptide P-B,Proline-rich protein 3,SMR3B,Submaxillary gland androgen-regulated protein 3B
EIAAB32563 Homo sapiens,Human,Proline-rich protein 7,PRR7,Synaptic proline-rich membrane protein
EIAAB32565 Mouse,Mus musculus,Proline-rich protein 7,Prr7,Synaptic proline-rich membrane protein
EIAAB32564 Proline-rich protein 7,Prr7,Rat,Rattus norvegicus,Synaptic proline-rich membrane protein
EIAAB32357 Mouse,Mus musculus,Prh1,Proline-rich protein HaeIII subfamily 1,Proline-rich protein MP-2,Prp
EIAAB32274 BAT2,G2,HLA-B-associated transcript 2,Homo sapiens,Human,Large proline-rich protein BAT2,Proline-rich and coiled-coil-containing protein 2A,Protein G2,Protein PRRC2A,PRRC2A
EIAAB32488 Mouse,Mus musculus,Prh1,Proline-rich protein 2,Proline-rich protein MP-3,Prp,Prp2
E1626h ELISA kit Homo sapiens,Human,PRAP1,Proline-rich acidic protein 1,UNQ608_PRO1195,UPA,Uterine-specific proline-rich acidic protein 96T
U1626h CLIA Homo sapiens,Human,PRAP1,Proline-rich acidic protein 1,UNQ608_PRO1195,UPA,Uterine-specific proline-rich acidic protein 96T
E1626h ELISA Homo sapiens,Human,PRAP1,Proline-rich acidic protein 1,UNQ608_PRO1195,UPA,Uterine-specific proline-rich acidic protein 96T
EIAAB32270 Basic salivary proline-rich protein 3,Homo sapiens,Human,Parotid salivary glycoprotein G1,PRB3,Proline-rich protein G1
EIAAB32269 Basic salivary proline-rich protein 2,Con1 glycoprotein,Homo sapiens,Human,PRB2,Salivary proline-rich protein
EIAAB43047 Mouse,Mus musculus,N4wbp1,NEDD4 WW domain-binding protein 1,Proline-rich gamma-carboxyglutamic acid protein 2,Proline-rich Gla protein 2,Prrg2,Transmembrane gamma-carboxyglutamic acid protein 2
EIAAB32554 CAT56,Homo sapiens,Human,MHC class I region proline-rich protein CAT56,Proline-rich protein 3,PRR3
EIAAB31723 Pnrc1,Prol2,Proline-rich nuclear receptor coactivator 1,Proline-rich protein 2,Rat,Rattus norvegicus
EIAAB32512 Acidic proline-rich protein PRP18,Proline-rich proteoglycan 2,Prpg2,Rat,Rattus norvegicus
EIAAB32489 Acidic proline-rich protein PRP33,Proline-rich proteoglycan 1,Prpg1,Rat,Rattus norvegicus
EIAAB32555 Cat56,MHC class I region proline-rich protein CAT56,Proline-rich protein 3,Prr3,Rat,Rattus norvegicus


 

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