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Receptor-like protein kinase 5 (EC 2.7.10.1) (EC 2.7.11.1) (Protein HAESA)

 RLK5_ARATH              Reviewed;         999 AA.
P47735; C0LGR4;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
07-JUN-2017, entry version 159.
RecName: Full=Receptor-like protein kinase 5;
EC=2.7.10.1;
EC=2.7.11.1;
AltName: Full=Protein HAESA;
Flags: Precursor;
Name=RLK5; Synonyms=HAE; OrderedLocusNames=At4g28490;
ORFNames=F21O9.180;
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].
STRAIN=cv. Columbia;
PubMed=8220453; DOI=10.1111/j.1365-313X.1993.tb00164.x;
Walker J.C.;
"Receptor-like protein kinase genes of Arabidopsis thaliana.";
Plant J. 3:451-456(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
PubMed=20064227; DOI=10.1186/1471-2164-11-19;
Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
"Genome-wide cloning and sequence analysis of leucine-rich repeat
receptor-like protein kinase genes in Arabidopsis thaliana.";
BMC Genomics 11:19-19(2010).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
CHARACTERIZATION, AND MUTAGENESIS OF LYS-711.
PubMed=8086440; DOI=10.1016/0167-4838(94)90160-0;
Horn M.A., Walker J.C.;
"Biochemical properties of the autophosphorylation of RLK5, a
receptor-like protein kinase from Arabidopsis thaliana.";
Biochim. Biophys. Acta 1208:65-74(1994).
[6]
FUNCTION, AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=10640280;
Jinn T.-L., Stone J.M., Walker J.C.;
"HAESA, an Arabidopsis leucine-rich repeat receptor kinase, controls
floral organ abscission.";
Genes Dev. 14:108-117(2000).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18660431; DOI=10.1105/tpc.108.059139;
Stenvik G.-E., Tandstad N.M., Guo Y., Shi C.-L., Kristiansen W.,
Holmgren A., Clark S.E., Aalen R.B., Butenko M.A.;
"The EPIP peptide of INFLORESCENCE DEFICIENT IN ABSCISSION is
sufficient to induce abscission in arabidopsis through the receptor-
like kinases HAESA and HAESA-LIKE2.";
Plant Cell 20:1805-1817(2008).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18809915; DOI=10.1073/pnas.0805539105;
Cho S.K., Larue C.T., Chevalier D., Wang H., Jinn T.-L., Zhang S.,
Walker J.C.;
"Regulation of floral organ abscission in Arabidopsis thaliana.";
Proc. Natl. Acad. Sci. U.S.A. 105:15629-15634(2008).
[9]
AUTOPHOSPHORYLATION.
PubMed=19124768; DOI=10.1073/pnas.0810249106;
Oh M.-H., Wang X., Kota U., Goshe M.B., Clouse S.D., Huber S.C.;
"Tyrosine phosphorylation of the BRI1 receptor kinase emerges as a
component of brassinosteroid signaling in Arabidopsis.";
Proc. Natl. Acad. Sci. U.S.A. 106:658-663(2009).
[10]
INTERACTION WITH CST.
PubMed=21628627; DOI=10.1104/pp.111.175224;
Burr C.A., Leslie M.E., Orlowski S.K., Chen I., Wright C.E.,
Daniels M.J., Liljegren S.J.;
"CAST AWAY, a membrane-associated receptor-like kinase, inhibits organ
abscission in Arabidopsis.";
Plant Physiol. 156:1837-1850(2011).
[11]
X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 20-620, AND GLYCOSYLATION AT
ASN-98; ASN-102; ASN-150; ASN-185; ASN-269; ASN-282 AND ASN-576.
PubMed=27058169; DOI=10.7554/eLife.15075;
Santiago J., Brandt B., Wildhagen M., Hohmann U., Hothorn L.A.,
Butenko M.A., Hothorn M.;
"Mechanistic insight into a peptide hormone signaling complex
mediating floral organ abscission.";
Elife 5:0-0(2016).
-!- FUNCTION: Receptor with a dual specificity kinase activity acting
on both serine/threonine- and tyrosine-containing substrates that
controls floral organ abscission. May interact with the
'INFLORESCENCE DEFICIENT IN ABSCISSION' (IDA) ligands family.
{ECO:0000269|PubMed:10640280, ECO:0000269|PubMed:18660431,
ECO:0000269|PubMed:18809915}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10027}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Note=Have significantly greater activity in the presence of Mn(2+)
than Mg(2+).;
-!- SUBUNIT: Interacts with CST. {ECO:0000269|PubMed:21628627}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10640280};
Single-pass type I membrane protein {ECO:0000269|PubMed:10640280}.
-!- TISSUE SPECIFICITY: Expressed in roots and rosettes. Expressed at
the base of petioles and pedicels, and in the abscission zones of
the floral organs. {ECO:0000269|PubMed:10640280}.
-!- PTM: Autophosphorylated on Ser, Thr and Tyr residues.
-!- DISRUPTION PHENOTYPE: No visible phenotype; due to the redundancy
with HSL2. Hae and hsl2 double mutants have a strong abscission
defect. {ECO:0000269|PubMed:18660431,
ECO:0000269|PubMed:18809915}.
-!- MISCELLANEOUS: The name HAESA derives from a Latin word meaning
'to adhere to'.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- WEB RESOURCE: Name=PlantP kinase Classification PPC;
URL="http://plantsp.genomics.purdue.edu/family/class.html";
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EMBL; M84660; AAA32859.1; -; mRNA.
EMBL; FJ708755; ACN59349.1; -; mRNA.
EMBL; AL021749; CAA16889.1; -; Genomic_DNA.
EMBL; AL161572; CAB79651.1; -; Genomic_DNA.
EMBL; CP002687; AEE85494.1; -; Genomic_DNA.
PIR; S27756; S27756.
RefSeq; NP_194578.1; NM_118991.3.
UniGene; At.19985; -.
PDB; 5IXO; X-ray; 1.74 A; A=20-620.
PDB; 5IXQ; X-ray; 1.86 A; A=20-620.
PDB; 5IXT; X-ray; 1.94 A; A=20-620.
PDB; 5IYV; X-ray; 2.56 A; A=20-620.
PDB; 5IYX; X-ray; 2.43 A; A=20-620.
PDBsum; 5IXO; -.
PDBsum; 5IXQ; -.
PDBsum; 5IXT; -.
PDBsum; 5IYV; -.
PDBsum; 5IYX; -.
ProteinModelPortal; P47735; -.
SMR; P47735; -.
BioGrid; 14254; 8.
IntAct; P47735; 1.
STRING; 3702.AT4G28490.1; -.
PaxDb; P47735; -.
PRIDE; P47735; -.
EnsemblPlants; AT4G28490.1; AT4G28490.1; AT4G28490.
GeneID; 828967; -.
Gramene; AT4G28490.1; AT4G28490.1; AT4G28490.
KEGG; ath:AT4G28490; -.
Araport; AT4G28490; -.
TAIR; locus:2005540; AT4G28490.
eggNOG; ENOG410JTIH; Eukaryota.
eggNOG; COG4886; LUCA.
HOGENOM; HOG000116551; -.
InParanoid; P47735; -.
KO; K08286; -.
OMA; RGWKNLN; -.
OrthoDB; EOG09360168; -.
PhylomeDB; P47735; -.
BRENDA; 2.7.10.2; 399.
PRO; PR:P47735; -.
Proteomes; UP000006548; Chromosome 4.
Genevisible; P47735; AT.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
GO; GO:0010227; P:floral organ abscission; IMP:TAIR.
GO; GO:0010102; P:lateral root morphogenesis; IMP:TAIR.
GO; GO:0045490; P:pectin catabolic process; IMP:TAIR.
GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
GO; GO:0010468; P:regulation of gene expression; IMP:TAIR.
Gene3D; 3.80.10.10; -; 5.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR032675; L_dom-like.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR013210; LRR_N_plant-typ.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF13855; LRR_8; 2.
Pfam; PF08263; LRRNT_2; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00369; LRR_TYP; 8.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF52058; SSF52058; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51450; LRR; 16.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell membrane; Complete proteome;
Glycoprotein; Kinase; Leucine-rich repeat; Membrane;
Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
Transmembrane helix.
SIGNAL 1 14 {ECO:0000255}.
CHAIN 15 999 Receptor-like protein kinase 5.
/FTId=PRO_0000024381.
TOPO_DOM 15 621 Extracellular. {ECO:0000255}.
TRANSMEM 622 641 Helical. {ECO:0000255}.
TOPO_DOM 642 999 Cytoplasmic. {ECO:0000255}.
REPEAT 90 112 LRR 1.
REPEAT 115 137 LRR 2.
REPEAT 140 161 LRR 3.
REPEAT 164 186 LRR 4.
REPEAT 188 208 LRR 5.
REPEAT 213 236 LRR 6.
REPEAT 237 259 LRR 7.
REPEAT 285 307 LRR 8.
REPEAT 308 330 LRR 9.
REPEAT 332 353 LRR 10.
REPEAT 356 378 LRR 11.
REPEAT 380 402 LRR 12.
REPEAT 404 427 LRR 13.
REPEAT 428 450 LRR 14.
REPEAT 452 474 LRR 15.
REPEAT 500 523 LRR 16.
REPEAT 524 546 LRR 17.
REPEAT 548 569 LRR 18.
REPEAT 571 593 LRR 19.
DOMAIN 683 968 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 689 697 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 819 819 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 711 711 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 766 766 Phosphotyrosine.
{ECO:0000250|UniProtKB:O22476}.
MOD_RES 806 806 Phosphotyrosine.
{ECO:0000250|UniProtKB:C0LGT6}.
MOD_RES 856 856 Phosphoserine.
{ECO:0000250|UniProtKB:Q9M0G7}.
MOD_RES 864 864 Phosphotyrosine.
{ECO:0000250|UniProtKB:C0LGT6}.
MOD_RES 871 871 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9M0G7}.
MOD_RES 872 872 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9M0G7}.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5IXO,
ECO:0000269|PubMed:27058169}.
CARBOHYD 102 102 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5IXO,
ECO:0000269|PubMed:27058169}.
CARBOHYD 150 150 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5IXO,
ECO:0000269|PubMed:27058169}.
CARBOHYD 185 185 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5IXO,
ECO:0000269|PubMed:27058169}.
CARBOHYD 210 210 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 269 269 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5IXO,
ECO:0000269|PubMed:27058169}.
CARBOHYD 282 282 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5IYX,
ECO:0000269|PubMed:27058169}.
CARBOHYD 452 452 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 576 576 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5IXO,
ECO:0000269|PubMed:27058169}.
MUTAGEN 711 711 K->E: Loss of catalytic activity.
{ECO:0000269|PubMed:8086440}.
HELIX 21 33 {ECO:0000244|PDB:5IXO}.
HELIX 43 46 {ECO:0000244|PDB:5IXO}.
HELIX 53 55 {ECO:0000244|PDB:5IXO}.
STRAND 59 61 {ECO:0000244|PDB:5IXO}.
STRAND 67 71 {ECO:0000244|PDB:5IXO}.
STRAND 78 80 {ECO:0000244|PDB:5IXO}.
HELIX 83 87 {ECO:0000244|PDB:5IXO}.
STRAND 93 95 {ECO:0000244|PDB:5IXO}.
STRAND 98 104 {ECO:0000244|PDB:5IXO}.
HELIX 108 110 {ECO:0000244|PDB:5IXO}.
STRAND 117 120 {ECO:0000244|PDB:5IXO}.
STRAND 123 129 {ECO:0000244|PDB:5IXO}.
HELIX 134 137 {ECO:0000244|PDB:5IXO}.
STRAND 142 145 {ECO:0000244|PDB:5IXO}.
STRAND 148 154 {ECO:0000244|PDB:5IXO}.
HELIX 157 161 {ECO:0000244|PDB:5IXO}.
STRAND 167 169 {ECO:0000244|PDB:5IXO}.
HELIX 181 185 {ECO:0000244|PDB:5IXO}.
STRAND 190 193 {ECO:0000244|PDB:5IXO}.
HELIX 206 210 {ECO:0000244|PDB:5IXO}.
STRAND 215 218 {ECO:0000244|PDB:5IXO}.
STRAND 224 226 {ECO:0000244|PDB:5IXO}.
HELIX 230 234 {ECO:0000244|PDB:5IXO}.
STRAND 239 242 {ECO:0000244|PDB:5IXO}.
STRAND 245 250 {ECO:0000244|PDB:5IXO}.
HELIX 254 258 {ECO:0000244|PDB:5IXO}.
STRAND 264 266 {ECO:0000244|PDB:5IXO}.
STRAND 269 272 {ECO:0000244|PDB:5IXO}.
HELIX 278 282 {ECO:0000244|PDB:5IXO}.
STRAND 288 290 {ECO:0000244|PDB:5IXO}.
STRAND 293 296 {ECO:0000244|PDB:5IXQ}.
STRAND 311 313 {ECO:0000244|PDB:5IXO}.
HELIX 325 329 {ECO:0000244|PDB:5IXO}.
STRAND 335 337 {ECO:0000244|PDB:5IXO}.
STRAND 340 346 {ECO:0000244|PDB:5IXO}.
TURN 349 354 {ECO:0000244|PDB:5IXO}.
STRAND 359 361 {ECO:0000244|PDB:5IXO}.
STRAND 364 369 {ECO:0000244|PDB:5IXO}.
TURN 373 378 {ECO:0000244|PDB:5IXO}.
STRAND 383 385 {ECO:0000244|PDB:5IXO}.
STRAND 388 393 {ECO:0000244|PDB:5IXO}.
HELIX 397 401 {ECO:0000244|PDB:5IXO}.
STRAND 407 409 {ECO:0000244|PDB:5IXO}.
STRAND 412 418 {ECO:0000244|PDB:5IXO}.
HELIX 421 423 {ECO:0000244|PDB:5IXO}.
STRAND 431 433 {ECO:0000244|PDB:5IXO}.
STRAND 436 441 {ECO:0000244|PDB:5IXO}.
HELIX 445 449 {ECO:0000244|PDB:5IXO}.
STRAND 455 457 {ECO:0000244|PDB:5IXO}.
STRAND 460 465 {ECO:0000244|PDB:5IXO}.
HELIX 469 473 {ECO:0000244|PDB:5IXO}.
STRAND 479 481 {ECO:0000244|PDB:5IXO}.
STRAND 484 490 {ECO:0000244|PDB:5IXO}.
HELIX 493 497 {ECO:0000244|PDB:5IXO}.
STRAND 503 505 {ECO:0000244|PDB:5IXO}.
STRAND 508 513 {ECO:0000244|PDB:5IXO}.
STRAND 527 529 {ECO:0000244|PDB:5IXO}.
STRAND 532 535 {ECO:0000244|PDB:5IXO}.
HELIX 541 545 {ECO:0000244|PDB:5IXO}.
STRAND 551 553 {ECO:0000244|PDB:5IXO}.
STRAND 560 562 {ECO:0000244|PDB:5IXO}.
HELIX 565 569 {ECO:0000244|PDB:5IXO}.
STRAND 573 576 {ECO:0000244|PDB:5IXO}.
STRAND 579 585 {ECO:0000244|PDB:5IXO}.
HELIX 588 590 {ECO:0000244|PDB:5IXO}.
HELIX 593 598 {ECO:0000244|PDB:5IXO}.
STRAND 605 609 {ECO:0000244|PDB:5IXO}.
STRAND 612 614 {ECO:0000244|PDB:5IXO}.
SEQUENCE 999 AA; 109096 MW; F5793D899EA0C6A7 CRC64;
MLYCLILLLC LSSTYLPSLS LNQDATILRQ AKLGLSDPAQ SLSSWSDNND VTPCKWLGVS
CDATSNVVSV DLSSFMLVGP FPSILCHLPS LHSLSLYNNS INGSLSADDF DTCHNLISLD
LSENLLVGSI PKSLPFNLPN LKFLEISGNN LSDTIPSSFG EFRKLESLNL AGNFLSGTIP
ASLGNVTTLK ELKLAYNLFS PSQIPSQLGN LTELQVLWLA GCNLVGPIPP SLSRLTSLVN
LDLTFNQLTG SIPSWITQLK TVEQIELFNN SFSGELPESM GNMTTLKRFD ASMNKLTGKI
PDNLNLLNLE SLNLFENMLE GPLPESITRS KTLSELKLFN NRLTGVLPSQ LGANSPLQYV
DLSYNRFSGE IPANVCGEGK LEYLILIDNS FSGEISNNLG KCKSLTRVRL SNNKLSGQIP
HGFWGLPRLS LLELSDNSFT GSIPKTIIGA KNLSNLRISK NRFSGSIPNE IGSLNGIIEI
SGAENDFSGE IPESLVKLKQ LSRLDLSKNQ LSGEIPRELR GWKNLNELNL ANNHLSGEIP
KEVGILPVLN YLDLSSNQFS GEIPLELQNL KLNVLNLSYN HLSGKIPPLY ANKIYAHDFI
GNPGLCVDLD GLCRKITRSK NIGYVWILLT IFLLAGLVFV VGIVMFIAKC RKLRALKSST
LAASKWRSFH KLHFSEHEIA DCLDEKNVIG FGSSGKVYKV ELRGGEVVAV KKLNKSVKGG
DDEYSSDSLN RDVFAAEVET LGTIRHKSIV RLWCCCSSGD CKLLVYEYMP NGSLADVLHG
DRKGGVVLGW PERLRIALDA AEGLSYLHHD CVPPIVHRDV KSSNILLDSD YGAKVADFGI
AKVGQMSGSK TPEAMSGIAG SCGYIAPEYV YTLRVNEKSD IYSFGVVLLE LVTGKQPTDS
ELGDKDMAKW VCTALDKCGL EPVIDPKLDL KFKEEISKVI HIGLLCTSPL PLNRPSMRKV
VIMLQEVSGA VPCSSPNTSK RSKTGGKLSP YYTEDLNSV


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EIAAB13074 Eck,Epha2,Ephrin type-A receptor 2,Epithelial cell kinase,Mouse,Mus musculus,Myk2,Sek2,Tyrosine-protein kinase receptor ECK,Tyrosine-protein kinase receptor MPK-5,Tyrosine-protein kinase receptor SEK-
EIAAB34873 Ankrd3,Ankyrin repeat domain-containing protein 3,Mouse,Mus musculus,PKC-associated protein kinase,PKC-regulated protein kinase,Pkk,Receptor-interacting serine_threonine-protein kinase 4,Ripk4
EIAAB13105 Ephb2,Ephrin type-B receptor 2,Epth3,Mouse,Mus musculus,Neural kinase,Nuk,Nuk receptor tyrosine kinase,Sek3,Tyrosine-protein kinase receptor EPH-3,Tyrosine-protein kinase receptor SEK-3
EIAAB42378 Angiopoietin-1 receptor,Homo sapiens,hTIE2,Human,p140 TEK,TEK,TIE2,Tunica interna endothelial cell kinase,Tyrosine-protein kinase receptor TEK,Tyrosine-protein kinase receptor TIE-2
EIAAB42377 Angiopoietin-1 receptor,HYK,Hyk,Mouse,mTIE2,Mus musculus,p140 TEK,STK1,Tek,Tie2,Tie-2,Tunica interna endothelial cell kinase,Tyrosine-protein kinase receptor TEK,Tyrosine-protein kinase receptor TIE-2
EIAAB31334 Bos taurus,Bovine,PKN,PKN1,PRK1,PRKCL1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein kinase PKN-alpha,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine
EIAAB34871 Homocysteine respondent protein HCYP2,Rat,Rattus norvegicus,Receptor-interacting protein 3,Receptor-interacting serine_threonine-protein kinase 3,Rip3,RIP-3,Ripk3,RIP-like protein kinase 3
EIAAB31332 Mouse,Mus musculus,Pkn,Pkn1,Prk1,Prkcl1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine protein kinase N
31-354 TGFBR2 is a member of the Ser_Thr protein kinase family and the TGFB receptor subfamily. The protein is a transmembrane protein that has a protein kinase domain, forms a heterodimeric complex with ano 0.1 mg
30-884 GRK4 is a member of the guanine nucleotide-binding protein (G protein)-coupled receptor kinase subfamily of the Ser_Thr protein kinase family. The protein phosphorylates the activated forms of G prote 0.05 mg
EIAAB33008 CCK4,CCK-4,Colon carcinoma kinase 4,Homo sapiens,Human,Inactive tyrosine-protein kinase 7,Protein-tyrosine kinase 7,Pseudo tyrosine kinase receptor 7,PTK7,Tyrosine-protein kinase-like 7
E0015h ELISA kit Activin receptor-like kinase 3,ACVRLK3,ALK3,ALK-3,BMP type-1A receptor,BMPR1A,BMPR-1A,Bone morphogenetic protein receptor type-1A,Homo sapiens,Human,Serine_threonine-protein kinase receptor 96T
E0015h ELISA Activin receptor-like kinase 3,ACVRLK3,ALK3,ALK-3,BMP type-1A receptor,BMPR1A,BMPR-1A,Bone morphogenetic protein receptor type-1A,Homo sapiens,Human,Serine_threonine-protein kinase receptor R5,S 96T
U0015h CLIA Activin receptor-like kinase 3,ACVRLK3,ALK3,ALK-3,BMP type-1A receptor,BMPR1A,BMPR-1A,Bone morphogenetic protein receptor type-1A,Homo sapiens,Human,Serine_threonine-protein kinase receptor R5,SK 96T
EIAAB31333 Homo sapiens,Human,PAK1,PAK-1,PKN,PKN1,PRK1,PRKCL1,Protease-activated kinase 1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein kinase PKN-alpha,Protein-kinase C-related kinase 1,Serine_threo
EIAAB31331 PAK-1,Pkn,Pkn1,Prk1,Prkcl1,Protease-activated kinase 1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein-kinase C-related kinase 1,Rat,Rattus norvegicus,Serine_threonine-protein kinase N1,Seri
U0039m CLIA Fetal liver kinase 2,FL cytokine receptor,FLK-2,Flk-2,Flt3,FLT-3,Flt-3,Fms-like tyrosine kinase 3,Mouse,Mus musculus,Receptor-type tyrosine-protein kinase FLT3,Tyrosine-protein kinase receptor fl 96T
E0039m ELISA Fetal liver kinase 2,FL cytokine receptor,FLK-2,Flk-2,Flt3,FLT-3,Flt-3,Fms-like tyrosine kinase 3,Mouse,Mus musculus,Receptor-type tyrosine-protein kinase FLT3,Tyrosine-protein kinase receptor f 96T
EIAAB33010 Inactive tyrosine-protein kinase 7,Mouse,Mus musculus,Protein chuzhoi,Protein-tyrosine kinase 7,Pseudo tyrosine kinase receptor 7,Ptk7,Tyrosine-protein kinase-like 7
EIAAB34868 Cell death protein RIP,Homo sapiens,Human,Receptor-interacting protein 1,Receptor-interacting serine_threonine-protein kinase 1,RIP,RIP1,RIP-1,RIPK1,Serine_threonine-protein kinase RIP
EIAAB34867 Cell death protein RIP,Mouse,Mus musculus,Receptor-interacting protein 1,Receptor-interacting serine_threonine-protein kinase 1,Rinp,Rip,RIP-1,Ripk1,Serine_threonine-protein kinase RIP
EIAAB34869 Homo sapiens,Human,Receptor-interacting protein 3,Receptor-interacting serine_threonine-protein kinase 3,RIP3,RIP-3,RIPK3,RIP-like protein kinase 3
EIAAB34870 Mouse,mRIP3,Mus musculus,Receptor-interacting protein 3,Receptor-interacting serine_threonine-protein kinase 3,Rip3,RIP-3,Ripk3,RIP-like protein kinase 3
E0039m ELISA kit Fetal liver kinase 2,FL cytokine receptor,FLK-2,Flk-2,Flt3,FLT-3,Flt-3,Fms-like tyrosine kinase 3,Mouse,Mus musculus,Receptor-type tyrosine-protein kinase FLT3,Tyrosine-protein kinase recep 96T
EIAAB42160 Activin A receptor type II-like protein kinase of 53kD,Activin receptor-like kinase 5,ALK5,ALK5,ALK-5,Homo sapiens,Human,Serine_threonine-protein kinase receptor R4,SKR4,SKR4,TbetaR-I,TGF-beta recepto


 

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