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4-substituted benzoates-glutamate ligase GH3.12 (EC 6.3.2.-) (Auxin-responsive GH3-like protein 12) (AtGH3-12) (Protein GH3-LIKE DEFENSE GENE 1) (Protein GRETCHEN HAGEN 3.12) (Protein HOPW1-1-INTERACTING 3) (Protein avrPPHB SUSCEPTIBLE 3)

 GH312_ARATH             Reviewed;         575 AA.
Q9LYU4;
11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
22-NOV-2017, entry version 83.
RecName: Full=4-substituted benzoates-glutamate ligase GH3.12;
EC=6.3.2.-;
AltName: Full=Auxin-responsive GH3-like protein 12;
Short=AtGH3-12;
AltName: Full=Protein GH3-LIKE DEFENSE GENE 1;
AltName: Full=Protein GRETCHEN HAGEN 3.12;
AltName: Full=Protein HOPW1-1-INTERACTING 3;
AltName: Full=Protein avrPPHB SUSCEPTIBLE 3;
Name=GH3.12; Synonyms=GDG1, PBS3, WIN3; OrderedLocusNames=At5g13320;
ORFNames=T22N19.5, T31B5.140;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PSEUDOMONAS
SYRINGAE MACULICOLA HOPW1-1, AND INDUCTION BY PSEUDOMONAS SYRINGAE
MACULICOLA.
STRAIN=cv. Wassilewskija;
PubMed=18266921; DOI=10.1111/j.1365-313X.2008.03439.x;
Lee M.W., Jelenska J., Greenberg J.T.;
"Arabidopsis proteins important for modulating defense responses to
Pseudomonas syringae that secrete HopW1-1.";
Plant J. 54:452-465(2008).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=10224270;
Warren R.F., Merritt P.M., Holub E., Innes R.W.;
"Identification of three putative signal transduction genes involved
in R gene-specified disease resistance in Arabidopsis.";
Genetics 152:401-412(1999).
[5]
FUNCTION.
PubMed=11846877; DOI=10.1046/j.0960-7412.2001.01229.x;
van der Biezen E.A., Freddie C.T., Kahn K., Parker J.E., Jones J.D.;
"Arabidopsis RPP4 is a member of the RPP5 multigene family of TIR-NB-
LRR genes and confers downy mildew resistance through multiple
signalling components.";
Plant J. 29:439-451(2002).
[6]
FUNCTION.
PubMed=16353557; DOI=10.1094/MPMI-18-1226;
McDowell J.M., Williams S.G., Funderburg N.T., Eulgem T., Dangl J.L.;
"Genetic analysis of developmentally regulated resistance to downy
mildew (Hyaloperonospora parasitica) in Arabidopsis thaliana.";
Mol. Plant Microbe Interact. 18:1226-1234(2005).
[7]
FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY PSEUDOMONAS SYRINGAE
TOMATO, AND INDUCTION BY PAD4 AND SALICYLIC ACID.
PubMed=17918621; DOI=10.1094/MPMI-20-10-1192;
Lee M.W., Lu H., Jung H.W., Greenberg J.T.;
"A key role for the Arabidopsis WIN3 protein in disease resistance
triggered by Pseudomonas syringae that secrete AvrRpt2.";
Mol. Plant Microbe Interact. 20:1192-1200(2007).
[8]
FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY PSEUDOMONAS SYRINGAE
TOMATO, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=17521413; DOI=10.1111/j.1365-313X.2007.03130.x;
Jagadeeswaran G., Raina S., Acharya B.R., Maqbool S.B., Mosher S.L.,
Appel H.M., Schultz J.C., Klessig D.F., Raina R.;
"Arabidopsis GH3-LIKE DEFENSE GENE 1 is required for accumulation of
salicylic acid, activation of defense responses and resistance to
Pseudomonas syringae.";
Plant J. 51:234-246(2007).
[9]
FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLU-502 AND ILE-519,
AND INDUCTION BY PSEUDOMONAS SYRINGAE TOMATO.
STRAIN=cv. Columbia, and cv. No-0;
PubMed=17468220; DOI=10.1104/pp.107.097691;
Nobuta K., Okrent R.A., Stoutemyer M., Rodibaugh N., Kempema L.,
Wildermuth M.C., Innes R.W.;
"The GH3 acyl adenylase family member PBS3 regulates salicylic acid-
dependent defense responses in Arabidopsis.";
Plant Physiol. 144:1144-1156(2007).
[10]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND
MUTAGENESIS OF GLU-502 AND ILE-519.
STRAIN=cv. Columbia;
PubMed=19189963; DOI=10.1074/jbc.M806662200;
Okrent R.A., Brooks M.D., Wildermuth M.C.;
"Arabidopsis GH3.12 (PBS3) conjugates amino acids to 4-substituted
benzoates and is inhibited by salicylate.";
J. Biol. Chem. 284:9742-9754(2009).
[11]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH AMP AND
SALICYLIC ACID.
PubMed=22628555; DOI=10.1126/science.1221863;
Westfall C.S., Zubieta C., Herrmann J., Kapp U., Nanao M.H., Jez J.M.;
"Structural basis for prereceptor modulation of plant hormones by GH3
proteins.";
Science 336:1708-1711(2012).
-!- FUNCTION: Catalyzes the conjugation of specific amino acids (e.g.
Glu and possibly His, Lys, and Met) to their preferred acyl
substrates (e.g. 4-substituted benzoates), in a magnesium ion- and
ATP-dependent manner. Can use 4-substituted benzoates such as 4-
aminobenzoate (pABA), 4-fluorobenzoate and 4-hydroxybenzoate (4-
HBA), and, to a lesser extent, benzoate, vanillate and trans-
cinnamate, but not 2-substituted benzoates and salicylic acid
(SA), as conjugating acyl substrates. Involved in both basal and
induced resistance in a SA-dependent manner. Confers resistance to
virulent and avirulent pathogens (at least bacteria and
oomycetes), and promotes SA glucosides accumulation. Required for
the establishment of hyper-sensitive response (HR) upon
incompatible interaction and subsequent systemic acquired
resistance (SAR). {ECO:0000269|PubMed:10224270,
ECO:0000269|PubMed:11846877, ECO:0000269|PubMed:16353557,
ECO:0000269|PubMed:17468220, ECO:0000269|PubMed:17521413,
ECO:0000269|PubMed:17918621, ECO:0000269|PubMed:18266921,
ECO:0000269|PubMed:19189963}.
-!- ENZYME REGULATION: Specifically and reversibly inhibited by
salicylic acid (SA). {ECO:0000269|PubMed:19189963}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=153 uM for 4-aminobenzoate (at pH 8.5 and 30 degrees Celsius)
{ECO:0000269|PubMed:19189963};
KM=459 uM for 4-hydroxybenzoate (at pH 8.5 and 30 degrees
Celsius) {ECO:0000269|PubMed:19189963};
KM=867 uM for benzoate (at pH 8.5 and 30 degrees Celsius)
{ECO:0000269|PubMed:19189963};
KM=636 uM for ATP (with 4-aminobenzoate as cosubstrate at pH 8.5
and 30 degrees Celsius) {ECO:0000269|PubMed:19189963};
KM=791 uM for ATP (with 4-hydroxybenzoate as cosubstrate at pH
8.5 and 30 degrees Celsius) {ECO:0000269|PubMed:19189963};
pH dependence:
Optimum pH is 8-8.5. {ECO:0000269|PubMed:19189963};
-!- SUBUNIT: Interacts with the P.syringae pv. maculicola effector
HopW1-1 (via C-terminus). {ECO:0000269|PubMed:18266921}.
-!- TISSUE SPECIFICITY: Expressed in seedlings, mostly in cotyledons,
leaves, hypocotyls and sporadically in roots. Not detected in
unchallenged adult plants, except in flowers.
{ECO:0000269|PubMed:17521413}.
-!- DEVELOPMENTAL STAGE: Observed in young plants. In flowers, first
detected in flower buds at the beginning of the floral stage 13.
In petals, levels fade out during flower maturation do disappear
at floral opening. Present in sepals and to some extent in stamen
and carpel. {ECO:0000269|PubMed:17521413}.
-!- INDUCTION: By P.syringae pv. maculicola and pv. tomato. Induced by
PAD4 locally at the infection site and in a salicylic acid-
dependent manner systemically. {ECO:0000269|PubMed:17468220,
ECO:0000269|PubMed:17521413, ECO:0000269|PubMed:17918621,
ECO:0000269|PubMed:18266921}.
-!- DISRUPTION PHENOTYPE: Enhanced susceptibility to virulent and
avirulent bacterial pathogens P.syringae pv. tomato and pv.
maculicola ES4326 with or without DC3000(avrPphB, avrRpt2, avrB,
avrRpm1, or avrRps4) as well as to the oomycete pathogen
Hyaloperonospora parasitica (downy mildew) isolates Emoy2, Hind4,
Hiks1, Wela3, Cand5, and Wand1. Impaired hyper-sensitive response
(HR) and systemic acquired resistance (SAR). Compromised salicylic
acid glucosides (SAG) accumulation. Resistance is partially
rescued by SA treatment. {ECO:0000269|PubMed:10224270,
ECO:0000269|PubMed:17468220, ECO:0000269|PubMed:17521413,
ECO:0000269|PubMed:17918621}.
-!- SIMILARITY: Belongs to the IAA-amido conjugating enzyme family.
{ECO:0000305}.
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EMBL; EU214910; ABW84226.1; -; mRNA.
EMBL; AL163491; CAB86639.1; -; Genomic_DNA.
EMBL; CP002688; AED91880.1; -; Genomic_DNA.
EMBL; CP002688; ANM68312.1; -; Genomic_DNA.
PIR; T48579; T48579.
RefSeq; NP_001330076.1; NM_001343269.1.
RefSeq; NP_196836.1; NM_121335.4.
UniGene; At.32084; -.
PDB; 4EPM; X-ray; 2.10 A; A=1-575.
PDB; 4EQ4; X-ray; 2.07 A; A/B=1-575.
PDB; 4EQL; X-ray; 1.80 A; A/B=1-575.
PDB; 4EWV; X-ray; 2.90 A; A/B=1-575.
PDB; 4L39; X-ray; 2.81 A; A/B=1-575.
PDBsum; 4EPM; -.
PDBsum; 4EQ4; -.
PDBsum; 4EQL; -.
PDBsum; 4EWV; -.
PDBsum; 4L39; -.
ProteinModelPortal; Q9LYU4; -.
SMR; Q9LYU4; -.
STRING; 3702.AT5G13320.1; -.
PaxDb; Q9LYU4; -.
EnsemblPlants; AT5G13320.1; AT5G13320.1; AT5G13320.
EnsemblPlants; AT5G13320.2; AT5G13320.2; AT5G13320.
EnsemblPlants; AT5G13320.3; AT5G13320.3; AT5G13320.
GeneID; 831173; -.
Gramene; AT5G13320.1; AT5G13320.1; AT5G13320.
Gramene; AT5G13320.2; AT5G13320.2; AT5G13320.
Gramene; AT5G13320.3; AT5G13320.3; AT5G13320.
KEGG; ath:AT5G13320; -.
Araport; AT5G13320; -.
TAIR; locus:6530584248; AT5G13320.
eggNOG; ENOG410IHE6; Eukaryota.
eggNOG; ENOG410XQH0; LUCA.
HOGENOM; HOG000238302; -.
InParanoid; Q9LYU4; -.
KO; K14487; -.
OMA; KLISCWD; -.
OrthoDB; EOG093605J2; -.
PhylomeDB; Q9LYU4; -.
BioCyc; ARA:AT5G13320-MONOMER; -.
BioCyc; MetaCyc:AT5G13320-MONOMER; -.
Reactome; R-ATH-6798695; Neutrophil degranulation.
PRO; PR:Q9LYU4; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9LYU4; baseline and differential.
Genevisible; Q9LYU4; AT.
GO; GO:0052625; F:4-aminobenzoate amino acid synthetase activity; IDA:TAIR.
GO; GO:0052628; F:4-hydroxybenzoate amino acid synthetase activity; IDA:TAIR.
GO; GO:0052626; F:benzoate amino acid synthetase activity; IDA:TAIR.
GO; GO:0052627; F:vanillate amino acid synthetase activity; IDA:TAIR.
GO; GO:0018874; P:benzoate metabolic process; IDA:TAIR.
GO; GO:0071456; P:cellular response to hypoxia; IEP:TAIR.
GO; GO:0006952; P:defense response; IMP:TAIR.
GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
GO; GO:0009816; P:defense response to bacterium, incompatible interaction; IMP:TAIR.
GO; GO:0016046; P:detection of fungus; IMP:TAIR.
GO; GO:0044419; P:interspecies interaction between organisms; IPI:UniProtKB.
GO; GO:0009626; P:plant-type hypersensitive response; IEA:UniProtKB-KW.
GO; GO:0034052; P:positive regulation of plant-type hypersensitive response; IMP:UniProtKB.
GO; GO:0010112; P:regulation of systemic acquired resistance; IMP:UniProtKB.
GO; GO:0009863; P:salicylic acid mediated signaling pathway; IEP:TAIR.
InterPro; IPR004993; GH3.
PANTHER; PTHR31901; PTHR31901; 1.
Pfam; PF03321; GH3; 1.
1: Evidence at protein level;
3D-structure; Coiled coil; Complete proteome; Hypersensitive response;
Ligase; Plant defense; Reference proteome.
CHAIN 1 575 4-substituted benzoates-glutamate ligase
GH3.12.
/FTId=PRO_0000403642.
NP_BIND 95 96 AMP. {ECO:0000244|PDB:4EPM,
ECO:0000244|PDB:4EQ4,
ECO:0000244|PDB:4EQL,
ECO:0000269|PubMed:22628555}.
REGION 120 123 Salicylic acid binding.
{ECO:0000244|PDB:4EQ4,
ECO:0000244|PDB:4EQL,
ECO:0000269|PubMed:22628555}.
COILED 6 33 {ECO:0000255}.
BINDING 301 301 AMP. {ECO:0000244|PDB:4EPM,
ECO:0000244|PDB:4EQ4,
ECO:0000244|PDB:4EQL,
ECO:0000269|PubMed:22628555}.
BINDING 324 324 AMP; via carbonyl oxygen.
{ECO:0000244|PDB:4EPM,
ECO:0000244|PDB:4EQ4,
ECO:0000244|PDB:4EQL,
ECO:0000269|PubMed:22628555}.
BINDING 328 328 AMP. {ECO:0000244|PDB:4EPM,
ECO:0000244|PDB:4EQ4,
ECO:0000244|PDB:4EQL,
ECO:0000269|PubMed:22628555}.
BINDING 347 347 AMP. {ECO:0000244|PDB:4EPM,
ECO:0000244|PDB:4EQ4,
ECO:0000244|PDB:4EQL,
ECO:0000269|PubMed:22628555}.
BINDING 398 398 AMP. {ECO:0000244|PDB:4EPM,
ECO:0000244|PDB:4EQ4,
ECO:0000244|PDB:4EQL,
ECO:0000269|PubMed:22628555}.
BINDING 417 417 AMP. {ECO:0000244|PDB:4EQ4,
ECO:0000269|PubMed:22628555}.
MUTAGEN 502 502 E->K: In pbs3-1; loss of conjugating
activity, and impaired resistance to
virulent and avirulent pathogens; when
associated with T-519.
{ECO:0000269|PubMed:17468220,
ECO:0000269|PubMed:19189963}.
MUTAGEN 519 519 I->T: In pbs3-1; loss of conjugating
activity, and impaired resistance to
virulent and avirulent pathogens; when
associated with K-502.
{ECO:0000269|PubMed:17468220,
ECO:0000269|PubMed:19189963}.
HELIX 9 20 {ECO:0000244|PDB:4EQL}.
HELIX 22 37 {ECO:0000244|PDB:4EQL}.
HELIX 41 45 {ECO:0000244|PDB:4EQL}.
HELIX 53 59 {ECO:0000244|PDB:4EQL}.
HELIX 65 76 {ECO:0000244|PDB:4EQL}.
HELIX 81 83 {ECO:0000244|PDB:4EQL}.
STRAND 91 99 {ECO:0000244|PDB:4EQL}.
STRAND 102 108 {ECO:0000244|PDB:4EQL}.
HELIX 110 130 {ECO:0000244|PDB:4EQL}.
STRAND 137 141 {ECO:0000244|PDB:4EQL}.
STRAND 156 158 {ECO:0000244|PDB:4EQL}.
HELIX 160 165 {ECO:0000244|PDB:4EQL}.
HELIX 168 171 {ECO:0000244|PDB:4EQL}.
HELIX 177 179 {ECO:0000244|PDB:4EQL}.
STRAND 181 183 {ECO:0000244|PDB:4EQL}.
HELIX 185 189 {ECO:0000244|PDB:4EQL}.
HELIX 193 206 {ECO:0000244|PDB:4EQL}.
HELIX 208 210 {ECO:0000244|PDB:4EQL}.
STRAND 211 218 {ECO:0000244|PDB:4EQL}.
HELIX 219 242 {ECO:0000244|PDB:4EQL}.
HELIX 252 262 {ECO:0000244|PDB:4EQL}.
HELIX 267 277 {ECO:0000244|PDB:4EQL}.
HELIX 285 289 {ECO:0000244|PDB:4EQL}.
STRAND 295 299 {ECO:0000244|PDB:4EQL}.
HELIX 302 307 {ECO:0000244|PDB:4EQL}.
HELIX 308 315 {ECO:0000244|PDB:4EQL}.
STRAND 324 326 {ECO:0000244|PDB:4EQL}.
STRAND 331 334 {ECO:0000244|PDB:4EQL}.
HELIX 342 344 {ECO:0000244|PDB:4EQL}.
STRAND 347 349 {ECO:0000244|PDB:4EQL}.
STRAND 353 360 {ECO:0000244|PDB:4EQL}.
STRAND 368 371 {ECO:0000244|PDB:4EQ4}.
HELIX 372 374 {ECO:0000244|PDB:4EQL}.
STRAND 380 386 {ECO:0000244|PDB:4EQL}.
STRAND 388 390 {ECO:0000244|PDB:4EQL}.
STRAND 393 395 {ECO:0000244|PDB:4EQL}.
STRAND 398 406 {ECO:0000244|PDB:4EQL}.
STRAND 409 417 {ECO:0000244|PDB:4EQL}.
STRAND 420 422 {ECO:0000244|PDB:4EQL}.
STRAND 424 426 {ECO:0000244|PDB:4EQL}.
HELIX 431 440 {ECO:0000244|PDB:4EQL}.
HELIX 442 446 {ECO:0000244|PDB:4L39}.
TURN 447 449 {ECO:0000244|PDB:4EPM}.
STRAND 457 460 {ECO:0000244|PDB:4EQL}.
STRAND 462 471 {ECO:0000244|PDB:4EQL}.
HELIX 491 503 {ECO:0000244|PDB:4EQL}.
HELIX 507 514 {ECO:0000244|PDB:4EQL}.
STRAND 523 525 {ECO:0000244|PDB:4EQL}.
TURN 529 533 {ECO:0000244|PDB:4EQ4}.
TURN 536 540 {ECO:0000244|PDB:4EQ4}.
STRAND 546 548 {ECO:0000244|PDB:4EWV}.
HELIX 558 565 {ECO:0000244|PDB:4EQ4}.
STRAND 567 573 {ECO:0000244|PDB:4EQ4}.
SEQUENCE 575 AA; 65128 MW; 3762CE16A43A1E92 CRC64;
MKPIFDINET FEKQLKDLTS NVKSIQDNLL EEIITPNTKT EYLQRFLIDR FDKELFKKNV
PIVSYEDIKP YLDRVVNGES SDVISARTIT GFLLSSGTSG GAQKMMPWNN KYLDNLTFIY
DLRMQVITKH VKGVEEGKGM MFLFTKQESM TPSGLPARVA TSSYFKSDYF KNRPSNWYYS
YTSPDEVILC PNNTESLYCH LLCGLVQRDE VVRTGSIFAS VMVRAIEVLK NSWEELCSNI
RSGHLSNWVT DLGCQNSVSL VLGGPRPELA DTIEEICNQN SWKGIVKRLW PNTKYIETVV
TGSMGQYVPM LNYYCNDLPL VSTTYGSSET TFGINLDPLC KPEDVSYTFM PNMSYFEFIP
MDGGDKNDVV DLEDVKLGCT YEPVVTNFAG LYRMRVGDIV LVTGFYNNAP QFKFVRRENV
VLSIDSDKTN EEDLFKAVSQ AKLVLESSGL DLKDFTSYAD TSTFPGHYVV YLEVDTKEGE
EKETAQFELD EEALSTCCLV MEESLDNVYK RCRFKDGSIG PLEIRVVRQG TFDSLMDFFI
SQGASTGQYK TPRCIKSGKA LQVLETCVVA KFFSI


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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
18-003-43466 E3 SUMO-protein ligase PIAS2 - Protein inhibitor of activated STAT2; Protein inhibitor of activated STAT x; Msx-interacting zinc finger protein; DAB2-interacting protein; DIP; Androgen receptor-intera 0.05 mg Aff Pur
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
18-003-42501 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 0.05 mg Aff Pur
EIAAB28268 82 kDa FMRP-interacting protein,82-FIP,Cell proliferation-inducing gene 1 protein,FMRP-interacting protein 2,Homo sapiens,Human,KIAA1321,Nuclear fragile X mental retardation-interacting protein 2,NUFI
EIAAB44014 CEV14,Clonal evolution-related gene on chromosome 14 protein,GMAP-210,Golgi-associated microtubule-binding protein 210,Homo sapiens,Human,Thyroid receptor-interacting protein 11,TR-interacting protein
EIAAB31325 Casein kinase 2-interacting protein 1,C-Jun-binding protein,CK2-interacting protein 1,CKIP1,CKIP-1,Homo sapiens,HQ0024c,Human,JBP,OC120,Osteoclast maturation-associated gene 120 protein,PH domain-cont
EIAAB31218 Homo sapiens,hPIP1,Human,p21-activated protein kinase-interacting protein 1,PAK_PLC-interacting protein 1,PAK1-interacting protein 1,PAK1IP1,PIP1,WD repeat-containing protein 84,WDR84
EIAAB46349 Homo sapiens,Human,Protein PRPL-2,WAS_WASL-interacting protein family member 1,WASP-interacting protein,WASPIP,WIP,WIPF1,Wiskott-Aldrich syndrome protein-interacting protein
EIAAB39347 Mouse,Mus musculus,Spata24,Spermatogenesis-associated protein 24,TATA-binding protein-like factor-interacting protein,Testis protein T6441 homolog,Tipt,Tipt2,TLF-interacting protein,TRF2-interacting p
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
EIAAB07420 Cdc42-interacting protein 4,CIP4,Homo sapiens,hSTP,Human,Protein Felic,Salt tolerant protein,STOT,STP,Thyroid receptor-interacting protein 10,TR-interacting protein 10,TRIP10,TRIP-10
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
EIAAB39105 MAP-responsive gene protein,Methamphetamine-responsive transcript 1 protein,Mrt1,PDZ-protein Mrt1,Rat,Rattus norvegicus,Snx27,Sorting nexin-27
EIAAB42392 Homo sapiens,Human,RARRES3,RAR-responsive protein TIG3,Retinoic acid receptor responder protein 3,Retinoid-inducible gene 1 protein,RIG1,Tazarotene-induced gene 3 protein,TIG3
EIAAB27017 45 kDa NF-AT-interacting protein,45 kDa NFAT-interacting protein,Homo sapiens,Human,NFATC2-interacting protein,NFATC2IP,NIP45,Nuclear factor of activated T-cells, cytoplasmic 2-interacting protein
EIAAB27018 45 kDa NF-AT-interacting protein,45 kDa NFAT-interacting protein,Mouse,Mus musculus,NFATC2-interacting protein,Nfatc2ip,Nip45,Nuclear factor of activated T-cells, cytoplasmic 2-interacting protein
EIAAB44015 Homo sapiens,Human,KIAA0045,Probable E3 ubiquitin-protein ligase TRIP12,Thyroid receptor-interacting protein 12,TR-interacting protein 12,TRIP12,TRIP-12


 

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