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A-kinase anchor protein 12 (AKAP-12) (Germ cell lineage protein gercelin) (Src-suppressed C kinase substrate) (SSeCKS)

 AKA12_MOUSE             Reviewed;        1684 AA.
Q9WTQ5; Q80SS4; Q810D4; Q8BPK4; Q99MP1;
02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
07-NOV-2018, entry version 117.
RecName: Full=A-kinase anchor protein 12;
Short=AKAP-12;
AltName: Full=Germ cell lineage protein gercelin;
AltName: Full=Src-suppressed C kinase substrate;
Short=SSeCKS;
Name=Akap12; Synonyms=Gag12, Ssecks;
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] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
TISSUE=Testis;
PubMed=11429284; DOI=10.1016/S0925-4773(01)00384-7;
Camus A., Mesbah K., Rallu M., Babinet C., Barra J.;
"Gene trap insertion reveals two open reading frames in the mouse
SSeCKS gene: the form predominantly detected in the nervous system is
suppressed by the insertion while the other, specific of the testis,
remains expressed.";
Mech. Dev. 105:79-91(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=BALB/cJ; TISSUE=Testis;
PubMed=11799143; DOI=10.1177/002215540205000212;
Kitamura H., Okita K., Fujikura D., Mori K., Iwanaga T., Saito M.;
"Induction of Src-suppressed C kinase substrate (SSeCKS) in vascular
endothelial cells by bacterial lipopolysaccharide.";
J. Histochem. Cytochem. 50:245-255(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Testis;
Nishina Y., Motoda Y.;
"Mouse testicular cell specific gene, GAG12.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Testis;
Tsuchida J., Tanaka H., Yomogida K., Nozaki M., Maeda N., Matsui Y.,
Nishimune Y.;
"Molecular cloning and characterization of the mouse germ cell lineage
protein cDNA, gercelin, encoding the cytoplasmic AKAP, Gercelin /
SSeCKS and the potential germ cell-specific nuclear antigen, GENA.";
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-605 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Eye;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 139-1684 (ISOFORMS 1/2).
STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
[7]
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).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-682; SER-683 AND
SER-684, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Teratocarcinoma;
PubMed=17622165; DOI=10.1021/pr070122r;
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
"A differential phosphoproteomic analysis of retinoic acid-treated P19
cells.";
J. Proteome Res. 6:3174-3186(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-353, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-22; SER-27;
SER-234; SER-270; SER-273; SER-350; SER-371; SER-467; SER-489;
SER-584; SER-631; SER-634; SER-637; SER-682; SER-733; SER-767;
SER-786; THR-871; SER-873; SER-1351 AND SER-1645, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, 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).
-!- FUNCTION: Anchoring protein that mediates the subcellular
compartmentation of protein kinase A (PKA) and protein kinase C
(PKC). {ECO:0000250}.
-!- SUBUNIT: Binds to dimeric RII-alpha regulatory subunit of PKC.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
Membrane {ECO:0000250|UniProtKB:Q02952}; Lipid-anchor
{ECO:0000250|UniProtKB:Q02952}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Alpha;
IsoId=Q9WTQ5-1; Sequence=Displayed;
Name=2; Synonyms=Gamma;
IsoId=Q9WTQ5-2; Sequence=VSP_028135;
-!- TISSUE SPECIFICITY: Isoform 1 is predominantly found in the
nervous system. Isoform 3 is testis specific.
{ECO:0000269|PubMed:11429284}.
-!- SEQUENCE CAUTION:
Sequence=BAC66465.1; Type=Frameshift; Positions=28, 43; Evidence={ECO:0000305};
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EMBL; AF326228; AAK16150.1; -; mRNA.
EMBL; AF326230; AAK16152.1; -; mRNA.
EMBL; AB020886; BAA76894.1; -; mRNA.
EMBL; AB025278; BAC66465.1; ALT_FRAME; mRNA.
EMBL; AB051563; BAB72161.1; -; mRNA.
EMBL; AB070852; BAB72164.1; -; mRNA.
EMBL; AB070853; BAB72165.1; -; mRNA.
EMBL; AK053844; BAC35553.1; -; mRNA.
EMBL; BC042461; AAH42461.1; -; mRNA.
EMBL; BC043939; AAH43939.1; -; mRNA.
CCDS; CCDS56673.1; -. [Q9WTQ5-1]
RefSeq; NP_112462.1; NM_031185.3. [Q9WTQ5-1]
UniGene; Mm.27481; -.
ProteinModelPortal; Q9WTQ5; -.
SMR; Q9WTQ5; -.
BioGrid; 219914; 11.
ELM; Q9WTQ5; -.
IntAct; Q9WTQ5; 12.
MINT; Q9WTQ5; -.
STRING; 10090.ENSMUSP00000035829; -.
iPTMnet; Q9WTQ5; -.
PhosphoSitePlus; Q9WTQ5; -.
SwissPalm; Q9WTQ5; -.
PaxDb; Q9WTQ5; -.
PeptideAtlas; Q9WTQ5; -.
PRIDE; Q9WTQ5; -.
Ensembl; ENSMUST00000045730; ENSMUSP00000035829; ENSMUSG00000038587. [Q9WTQ5-1]
Ensembl; ENSMUST00000215696; ENSMUSP00000150261; ENSMUSG00000038587. [Q9WTQ5-2]
GeneID; 83397; -.
KEGG; mmu:83397; -.
UCSC; uc007ehh.1; mouse. [Q9WTQ5-1]
CTD; 9590; -.
MGI; MGI:1932576; Akap12.
eggNOG; ENOG410IFC9; Eukaryota.
eggNOG; ENOG4110Y3C; LUCA.
GeneTree; ENSGT00730000111244; -.
HOGENOM; HOG000293190; -.
HOVERGEN; HBG050472; -.
InParanoid; Q9WTQ5; -.
KO; K16528; -.
OMA; DPQEQTS; -.
OrthoDB; EOG091G01X9; -.
PhylomeDB; Q9WTQ5; -.
TreeFam; TF105411; -.
PRO; PR:Q9WTQ5; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000038587; Expressed in 273 organ(s), highest expression level in urinary bladder.
CleanEx; MM_AKAP12; -.
ExpressionAtlas; Q9WTQ5; baseline and differential.
Genevisible; Q9WTQ5; MM.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
GO; GO:0008179; F:adenylate cyclase binding; ISO:MGI.
GO; GO:0051018; F:protein kinase A binding; IEA:InterPro.
GO; GO:0030159; F:receptor signaling complex scaffold activity; TAS:MGI.
GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISO:MGI.
GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO.
GO; GO:0010739; P:positive regulation of protein kinase A signaling; IEA:InterPro.
GO; GO:0006605; P:protein targeting; IEA:InterPro.
GO; GO:0010738; P:regulation of protein kinase A signaling; ISO:MGI.
GO; GO:0090036; P:regulation of protein kinase C signaling; IEA:InterPro.
GO; GO:0007165; P:signal transduction; ISO:MGI.
InterPro; IPR028540; AKAP12.
InterPro; IPR001573; Pkinase-A_anch_WSK-motif.
InterPro; IPR018459; RII_binding_1.
PANTHER; PTHR23209; PTHR23209; 1.
Pfam; PF10522; RII_binding_1; 1.
Pfam; PF03832; WSK; 3.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton;
Isopeptide bond; Lipoprotein; Membrane; Myristate; Phosphoprotein;
Reference proteome; Repeat; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q02952}.
CHAIN 2 1684 A-kinase anchor protein 12.
/FTId=PRO_0000304941.
DOMAIN 590 620 AKAP 1.
DOMAIN 737 767 AKAP 2.
DOMAIN 778 808 AKAP 3.
REGION 253 543 Involved in PKC-binding. {ECO:0000250}.
REGION 1501 1514 RII-binding. {ECO:0000250}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000250|UniProtKB:Q5QD51}.
MOD_RES 18 18 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 22 22 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 27 27 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 136 136 Phosphoserine.
{ECO:0000250|UniProtKB:Q02952}.
MOD_RES 234 234 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 244 244 Phosphoserine.
{ECO:0000250|UniProtKB:Q5QD51}.
MOD_RES 270 270 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 273 273 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 330 330 Phosphothreonine.
{ECO:0000250|UniProtKB:Q5QD51}.
MOD_RES 350 350 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 353 353 Phosphotyrosine.
{ECO:0000244|PubMed:19131326}.
MOD_RES 371 371 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 467 467 Phosphoserine.
{ECO:0000244|PubMed:16452087,
ECO:0000244|PubMed:21183079}.
MOD_RES 489 489 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 505 505 Phosphoserine.
{ECO:0000250|UniProtKB:Q5QD51}.
MOD_RES 507 507 Phosphoserine.
{ECO:0000250|UniProtKB:Q5QD51}.
MOD_RES 540 540 Phosphoserine.
{ECO:0000250|UniProtKB:Q5QD51}.
MOD_RES 543 543 Phosphoserine.
{ECO:0000250|UniProtKB:Q02952}.
MOD_RES 584 584 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 598 598 Phosphoserine.
{ECO:0000250|UniProtKB:Q02952}.
MOD_RES 613 613 Phosphoserine.
{ECO:0000250|UniProtKB:Q02952}.
MOD_RES 615 615 Phosphoserine.
{ECO:0000250|UniProtKB:Q02952}.
MOD_RES 628 628 Phosphothreonine.
{ECO:0000250|UniProtKB:Q5QD51}.
MOD_RES 630 630 Phosphoserine.
{ECO:0000250|UniProtKB:Q5QD51}.
MOD_RES 631 631 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 634 634 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 637 637 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 682 682 Phosphoserine.
{ECO:0000244|PubMed:17622165,
ECO:0000244|PubMed:21183079}.
MOD_RES 683 683 Phosphoserine.
{ECO:0000244|PubMed:17622165}.
MOD_RES 684 684 Phosphoserine.
{ECO:0000244|PubMed:17622165}.
MOD_RES 733 733 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 745 745 Phosphoserine.
{ECO:0000250|UniProtKB:Q02952}.
MOD_RES 767 767 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 786 786 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 871 871 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 873 873 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1059 1059 Phosphoserine.
{ECO:0000250|UniProtKB:Q5QD51}.
MOD_RES 1292 1292 Phosphoserine.
{ECO:0000250|UniProtKB:Q02952}.
MOD_RES 1351 1351 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1355 1355 Phosphoserine.
{ECO:0000250|UniProtKB:Q02952}.
MOD_RES 1357 1357 Phosphoserine.
{ECO:0000250|UniProtKB:Q5QD51}.
MOD_RES 1546 1546 Phosphoserine.
{ECO:0000250|UniProtKB:Q02952}.
MOD_RES 1645 1645 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000250|UniProtKB:Q02952}.
CROSSLNK 1030 1030 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:Q02952}.
VAR_SEQ 1 105 Missing (in isoform 2).
{ECO:0000303|PubMed:11429284,
ECO:0000303|Ref.4}.
/FTId=VSP_028135.
SEQUENCE 1684 AA; 180695 MW; E569D55762FCB19E CRC64;
MGAGSSTEQR SPEQPAESDT PSELELSGHG PAAEASGAAG DPADADPATK LPQKNGQLSA
VNGVAEQEDV HVQEESQDGQ EEEVTVEDVG QRESEDVKEK DRAKEMAASS TVVEDITKDE
QEETPEIIEQ IPASESNVEE MAQAAESQAN DVGFKKVFKF VGFKFTVKKD KNEKSDTVQL
LTVKKDEGEG AEASVGAGDH QEPGVETVGE SASKESELKQ STEKQEGTLK QAQSSTEIPL
QAESGQGTEE EAAKDGEENR EKEPTKPLES PTSPVSNETT SSFKKFFTHG WAGWRKKTSF
KKPKEDDLET SEKRKEQEAE KVDEEEGEKT EPAPAEEQEP AEGTDQARLS ADYEKVELPL
EDQVGDLEAL SEKCAPLATE VFDEKTEAHQ EVVAEVHVST VEKMTKGQGG AEVEGDVVVE
GSGESLPPEK LAETQEVPQE AEPVEELMKT KEVCVSGGDH TQLTDLSPEE KMLPKHPEGI
VSEVEMLSSQ ERIKVQGSPL KKLFSSSGLK KLSGKKQKGK RGGGGGDEEP GEYQHIQTES
PESADEQKGE SSASSPEEPE EIACLEKGPS EAPQEAEAEE GATSDGEKKR EGITPWASFK
KMVTPKKRVR RPSESDKEEE LDKVKSATLS STESTASGMQ DEVRAVGEEQ RSEEPKRRVD
TSVSWEALIC VGSSKKRARK ASSSDDEGGP RTLGGDGHRA EEASKDKEAD ALPASTQEQD
QAHGSSSPEP AGSPSEGEGV STWESFKRLV TPRKKSKSKL EERAEDSGAE QLASEIEPSR
EESWVSIKKF IPGRRKKRAD GKQEQAAVED SGPGEINEDD PDVPAVVPLS EYDAVEREKL
EAQRAQENVE LPQLKGAVYV SEELSKTLVH TVSVAVIDGT RAVTSAEERS PSWISASMTE
PLEHAEGVAT PPVGEVTEKD ITAEATPALA QTLPGGKDAH DDIVTSEVDF TSEAVTAAET
TEALRAEELT EASGAEETTD MVSAVSQLSD SPDTTEEATP VQEVEGGMLD TEEQERQTQA
VLQAVADKVK EDSQVPATQT LQRAGPKALE KVEEVEEDSE VLATEKEKDV VPEGPVQEAE
TEHLAQGSET VQATPESLEV PEVTEDVDRA TTCQVIKHQQ LMEQAVAPES SETLTDSETN
GSTPLADSDT PNGTQQDETV DSQDSNAIAA VKQSQVTEEE AAAAQTEGPS TPSSFPAQEE
HREKPGRDVL EPTQALAAGA VPILAKAEVG QEGEAGQFDG EKVKDGQCVK ELEVPVHTGP
NSQKTADLTR DSEVMEVARC QETESNEEQS ISPEKREMGT DVEKEETETK TEQASEEHEQ
ETAAPEHEGT HPKPVLTADM PHSERGKALG SLEGSPSLPD QDKADCIEVQ VQSSDTPVTQ
TTEAVKKVEE TVATSEMDES LECAGAQSLP AEKLSETGGY GTLQHGEDTV PQGPESQAES
IPIIVTPAPE SILHSDLQRE VSASQKQRSD EDNKPDAGPD AAGKESAARE KILRAEPEIL
ELESKSNKIV QSVIQTAVDQ FARTETAPET HASDLQNQVP VMQADSQGAQ QMLDKDESDL
QVSPQDGTLS AVAQEGLAVS DSSEGMSKAS EMITTLAVES ASVKESVEKL PLQCKDEKEH
AADGPQHQSL AKAEADASGN LTKESPDTNG PKLTEEGDAL KEEMNKAQTE EDDLQEPKGD
LTES


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28-476 AKAP7 encodes a member of the A-kinase anchoring protein (AKAP) family, a group of functionally related proteins that bind to a regulatory subunit (RII) of cAMP-dependent protein kinase A (PKA) and ta 0.1 mg
28-478 AKAP7 is a member of the A-kinase anchoring protein (AKAP) family, a group of functionally related proteins that bind to a regulatory subunit (RII) of cAMP-dependent protein kinase A (PKA) and target 0.05 mg
U0739m CLIA Cdk5,Cdkn5,Cell division protein kinase 5,CR6 protein kinase,CRK6,Crk6,Cyclin-dependent kinase 5,Mouse,Mus musculus,Serine_threonine-protein kinase PSSALRE,Tau protein kinase II catalytic subunit 96T
E0739m ELISA Cdk5,Cdkn5,Cell division protein kinase 5,CR6 protein kinase,CRK6,Crk6,Cyclin-dependent kinase 5,Mouse,Mus musculus,Serine_threonine-protein kinase PSSALRE,Tau protein kinase II catalytic subuni 96T
E0739m ELISA kit Cdk5,Cdkn5,Cell division protein kinase 5,CR6 protein kinase,CRK6,Crk6,Cyclin-dependent kinase 5,Mouse,Mus musculus,Serine_threonine-protein kinase PSSALRE,Tau protein kinase II catalytic s 96T
18-662-20067 Myristoylated alanine-rich C-kinase substrate - MARCKS; Protein kinase C substrate. 80 kDa protein. light chain; PKCSL; 80K-L protein Polyclonal 0.1 ml
E0739b ELISA kit Bos taurus,Bovine,CDK5,CDKN5,Cell division protein kinase 5,Cyclin-dependent kinase 5,PDPK,Proline-directed protein kinase 33 kDa subunit,Serine_threonine-protein kinase PSSALRE,Tau protein 96T
E0739b ELISA Bos taurus,Bovine,CDK5,CDKN5,Cell division protein kinase 5,Cyclin-dependent kinase 5,PDPK,Proline-directed protein kinase 33 kDa subunit,Serine_threonine-protein kinase PSSALRE,Tau protein kina 96T
U0739b CLIA Bos taurus,Bovine,CDK5,CDKN5,Cell division protein kinase 5,Cyclin-dependent kinase 5,PDPK,Proline-directed protein kinase 33 kDa subunit,Serine_threonine-protein kinase PSSALRE,Tau protein kinas 96T
EIAAB06263 CDC2L2,CDC2L3,CDK11A,Cell division cycle 2-like protein kinase 2,Cell division protein kinase 11A,Cyclin-dependent kinase 11A,Galactosyltransferase-associated protein kinase p58_GTA,Homo sapiens,Human
EIAAB06533 C-2K,CDC2L4,CDK9,Cell division cycle 2-like protein kinase 4,Cell division protein kinase 9,Cyclin-dependent kinase 9,Homo sapiens,Human,Serine_threonine-protein kinase PITALRE,TAK,Tat-associated kina
E1880h ELISA kit 39 kDa protein kinase,CAK,CAK1,CDK7,CDK-activating kinase 1,CDKN7,Cell division protein kinase 7,Cyclin-dependent kinase 7,Homo sapiens,Human,MO15,p39 Mo15,Serine_threonine-protein kinase 1 96T
U1880h CLIA kit 39 kDa protein kinase,CAK,CAK1,CDK7,CDK-activating kinase 1,CDKN7,Cell division protein kinase 7,Cyclin-dependent kinase 7,Homo sapiens,Human,MO15,p39 Mo15,Serine_threonine-protein kinase 1, 96T
E1880h ELISA 39 kDa protein kinase,CAK,CAK1,CDK7,CDK-activating kinase 1,CDKN7,Cell division protein kinase 7,Cyclin-dependent kinase 7,Homo sapiens,Human,MO15,p39 Mo15,Serine_threonine-protein kinase 1,STK1 96T


 

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