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

C-Jun-amino-terminal kinase-interacting protein 4 (JIP-4) (JNK-interacting protein 4) (JNK-associated leucine-zipper protein) (JLP) (JNK/SAPK-associated protein 2) (JSAP2) (Mitogen-activated protein kinase 8-interacting protein 4) (Sperm-associated antigen 9)

 JIP4_MOUSE              Reviewed;        1321 AA.
Q58A65; Q3UH77; Q3UHF0; Q58VQ4; Q5NC70; Q5NC78; Q6A057; Q6PAS3;
Q8CJC2;
02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
02-MAY-2006, sequence version 2.
18-JUL-2018, entry version 129.
RecName: Full=C-Jun-amino-terminal kinase-interacting protein 4;
Short=JIP-4;
Short=JNK-interacting protein 4;
AltName: Full=JNK-associated leucine-zipper protein;
Short=JLP;
AltName: Full=JNK/SAPK-associated protein 2;
Short=JSAP2;
AltName: Full=Mitogen-activated protein kinase 8-interacting protein 4;
AltName: Full=Sperm-associated antigen 9;
Name=Spag9; Synonyms=Jip4, Jsap2, Kiaa0516, Mapk8ip4;
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 2), FUNCTION, INTERACTION WITH
MAX; MAPK8; MAPK14; MAP3K3; MYC AND MAP2K4, AND SUBCELLULAR LOCATION.
PubMed=12391307; DOI=10.1073/pnas.232310199;
Lee C.M., Onesime D., Reddy C.D., Dhanasekaran N., Reddy E.P.;
"JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules
and transcription factors.";
Proc. Natl. Acad. Sci. U.S.A. 99:14189-14194(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), FUNCTION, INTERACTION WITH
KNS2 AND MAPK8, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
PHOSPHORYLATION.
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=15767678; DOI=10.1128/MCB.25.7.2733-2743.2005;
Kelkar N., Standen C.L., Davis R.J.;
"Role of the JIP4 scaffold protein in the regulation of mitogen-
activated protein kinase signaling pathways.";
Mol. Cell. Biol. 25:2733-2743(2005).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Testis;
Takamatsu N., Tochigi M., Ito M., Odama Y., Xu P., Nakabeppu Y.,
Yoshioka K., Shiba T.;
"JSAP2, a novel member of the JSAP1 JNK scaffold protein family.";
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain;
PubMed=15368895; DOI=10.1093/dnares/11.3.205;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 11:205-218(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
STRAIN=C57BL/6J;
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 GENOMIC DNA], AND ALTERNATIVE
SPLICING.
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
STRAIN=C57BL/6J; TISSUE=Brain, and Olfactory epithelium;
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).
[8]
INTERACTION WITH KNS2, AND INDUCTION.
PubMed=15987681; DOI=10.1074/jbc.M505499200;
Nguyen Q., Lee C.M., Le A., Reddy E.P.;
"JLP associates with kinesin light chain 1 through a novel leucine
zipper-like domain.";
J. Biol. Chem. 280:30185-30191(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-733, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-217 AND THR-365, 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-203; THR-217; THR-292
AND SER-733, 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: The JNK-interacting protein (JIP) group of scaffold
proteins selectively mediates JNK signaling by aggregating
specific components of the MAPK cascade to form a functional JNK
signaling module. {ECO:0000269|PubMed:12391307,
ECO:0000269|PubMed:15767678}.
-!- SUBUNIT: Homodimer. The homodimer interacts with ARF6, forming a
heterotetramer (By similarity). Homooligomer. Interacts with MAX,
MAPK8, MAPK14, MAPK10, MAPK14, MAP3K3, MYC, KNS2, and MAP2K4.
Interaction with KNS2 is important in the formation of ternary
complex with MAPK8. {ECO:0000250, ECO:0000269|PubMed:12391307,
ECO:0000269|PubMed:15767678, ECO:0000269|PubMed:15987681}.
-!- INTERACTION:
P62331:Arf6; NbExp=10; IntAct=EBI-6530207, EBI-988682;
O88447:Klc1; NbExp=6; IntAct=EBI-6530207, EBI-301550;
Q5S007:LRRK2 (xeno); NbExp=2; IntAct=EBI-6530207, EBI-5323863;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
Note=Perinuclear distribution in response to stress signals such
as UV radiation.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=Q58A65-1; Sequence=Displayed;
Name=2;
IsoId=Q58A65-2; Sequence=VSP_018228;
Name=3;
IsoId=Q58A65-3; Sequence=VSP_018226, VSP_018227, VSP_018228,
VSP_018229;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q58A65-4; Sequence=VSP_018226, VSP_018227, VSP_018228,
VSP_018230;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q58A65-5; Sequence=VSP_018227, VSP_018228;
Note=No experimental confirmation available.;
Name=6;
IsoId=Q58A65-6; Sequence=VSP_018225, VSP_018228;
-!- TISSUE SPECIFICITY: Isoform 6 is highly expressed in brain,
kidney, liver, heart. {ECO:0000269|PubMed:15767678}.
-!- INDUCTION: Up-regulated during neuronal differentiation.
{ECO:0000269|PubMed:15987681}.
-!- PTM: Phosphorylated by MAPK8 and MAPK14.
{ECO:0000269|PubMed:15767678}.
-!- SIMILARITY: Belongs to the JIP scaffold family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD32239.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAI35376.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF327451; AAN61564.1; -; mRNA.
EMBL; AY823270; AAX19462.1; -; mRNA.
EMBL; AB047782; BAD93176.1; -; mRNA.
EMBL; AK172961; BAD32239.1; ALT_INIT; mRNA.
EMBL; AK147431; BAE27907.1; -; mRNA.
EMBL; AK147537; BAE27980.1; -; mRNA.
EMBL; AL662838; CAI35367.1; -; Genomic_DNA.
EMBL; AL662838; CAI35375.1; -; Genomic_DNA.
EMBL; AL662838; CAI35376.1; ALT_SEQ; Genomic_DNA.
EMBL; BC060100; AAH60100.1; -; mRNA.
EMBL; BC094670; AAH94670.1; -; mRNA.
CCDS; CCDS25248.1; -. [Q58A65-2]
CCDS; CCDS56797.1; -. [Q58A65-3]
RefSeq; NP_001020599.1; NM_001025428.1.
RefSeq; NP_001020600.1; NM_001025429.1. [Q58A65-3]
RefSeq; NP_001020601.1; NM_001025430.1.
RefSeq; NP_001186132.1; NM_001199203.1.
RefSeq; NP_001186133.1; NM_001199204.1.
RefSeq; NP_001186134.1; NM_001199205.1. [Q58A65-4]
RefSeq; NP_081845.2; NM_027569.2. [Q58A65-2]
RefSeq; XP_006534282.1; XM_006534219.2. [Q58A65-6]
UniGene; Mm.260737; -.
UniGene; Mm.479010; -.
ProteinModelPortal; Q58A65; -.
SMR; Q58A65; -.
BioGrid; 214283; 5.
IntAct; Q58A65; 4.
MINT; Q58A65; -.
STRING; 10090.ENSMUSP00000042271; -.
iPTMnet; Q58A65; -.
PhosphoSitePlus; Q58A65; -.
PaxDb; Q58A65; -.
PeptideAtlas; Q58A65; -.
PRIDE; Q58A65; -.
Ensembl; ENSMUST00000041956; ENSMUSP00000042271; ENSMUSG00000020859. [Q58A65-2]
Ensembl; ENSMUST00000075695; ENSMUSP00000075115; ENSMUSG00000020859. [Q58A65-3]
GeneID; 70834; -.
KEGG; mmu:70834; -.
UCSC; uc007kxx.1; mouse. [Q58A65-2]
UCSC; uc007kxy.1; mouse. [Q58A65-1]
UCSC; uc007kxz.1; mouse. [Q58A65-6]
UCSC; uc007kya.1; mouse. [Q58A65-3]
UCSC; uc007kyc.1; mouse. [Q58A65-5]
UCSC; uc007kyd.1; mouse. [Q58A65-4]
CTD; 9043; -.
MGI; MGI:1918084; Spag9.
eggNOG; KOG2077; Eukaryota.
eggNOG; ENOG410XQ19; LUCA.
GeneTree; ENSGT00670000097546; -.
HOVERGEN; HBG024110; -.
InParanoid; Q58A65; -.
KO; K20317; -.
OMA; RENPAMQ; -.
OrthoDB; EOG091G016S; -.
PhylomeDB; Q58A65; -.
TreeFam; TF313096; -.
Reactome; R-MMU-375170; CDO in myogenesis.
ChiTaRS; Spag9; mouse.
PRO; PR:Q58A65; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020859; -.
CleanEx; MM_SPAG9; -.
ExpressionAtlas; Q58A65; baseline and differential.
Genevisible; Q58A65; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005815; C:microtubule organizing center; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
GO; GO:0008432; F:JUN kinase binding; IDA:MGI.
GO; GO:0019894; F:kinesin binding; IDA:MGI.
GO; GO:0005078; F:MAP-kinase scaffold activity; IBA:GO_Central.
GO; GO:0048273; F:mitogen-activated protein kinase p38 binding; IDA:MGI.
GO; GO:0030159; F:receptor signaling complex scaffold activity; IBA:GO_Central.
GO; GO:0007257; P:activation of JUN kinase activity; IDA:MGI.
GO; GO:0000187; P:activation of MAPK activity; IDA:MGI.
GO; GO:0090074; P:negative regulation of protein homodimerization activity; IDA:MGI.
GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
GO; GO:0043410; P:positive regulation of MAPK cascade; IGI:MGI.
GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:MGI.
GO; GO:0051260; P:protein homooligomerization; IDA:MGI.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:MGI.
GO; GO:0051146; P:striated muscle cell differentiation; IGI:MGI.
GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR032486; JIP_LZII.
InterPro; IPR019143; JNK/Rab-associated_protein-1_N.
InterPro; IPR034743; RH1.
InterPro; IPR034744; RH2.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF16471; JIP_LZII; 1.
Pfam; PF09744; Jnk-SapK_ap_N; 1.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS51776; RH1; 1.
PROSITE; PS51777; RH2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Coiled coil; Complete proteome;
Cytoplasm; Phosphoprotein; Reference proteome.
CHAIN 1 1321 C-Jun-amino-terminal kinase-interacting
protein 4.
/FTId=PRO_0000234077.
DOMAIN 7 95 RH1. {ECO:0000255|PROSITE-
ProRule:PRU01112}.
DOMAIN 500 604 RH2. {ECO:0000255|PROSITE-
ProRule:PRU01113}.
COILED 66 166 {ECO:0000255}.
COILED 408 534 {ECO:0000250}.
COILED 724 758 {ECO:0000255}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:O60271}.
MOD_RES 109 109 Phosphoserine.
{ECO:0000250|UniProtKB:O60271}.
MOD_RES 183 183 Phosphoserine.
{ECO:0000250|UniProtKB:O60271}.
MOD_RES 185 185 Phosphoserine.
{ECO:0000250|UniProtKB:O60271}.
MOD_RES 194 194 Phosphoserine.
{ECO:0000250|UniProtKB:O60271}.
MOD_RES 203 203 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 217 217 Phosphothreonine.
{ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 238 238 Phosphoserine.
{ECO:0000250|UniProtKB:O60271}.
MOD_RES 251 251 Phosphoserine.
{ECO:0000250|UniProtKB:O60271}.
MOD_RES 265 265 Phosphoserine.
{ECO:0000250|UniProtKB:O60271}.
MOD_RES 268 268 Phosphoserine.
{ECO:0000250|UniProtKB:O60271}.
MOD_RES 272 272 Phosphoserine.
{ECO:0000250|UniProtKB:O60271}.
MOD_RES 292 292 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 311 311 Phosphoserine.
{ECO:0000250|UniProtKB:O60271}.
MOD_RES 329 329 Phosphoserine.
{ECO:0000250|UniProtKB:O60271}.
MOD_RES 332 332 Phosphoserine.
{ECO:0000250|UniProtKB:O60271}.
MOD_RES 347 347 Phosphoserine.
{ECO:0000250|UniProtKB:O60271}.
MOD_RES 348 348 Phosphothreonine.
{ECO:0000250|UniProtKB:O60271}.
MOD_RES 365 365 Phosphothreonine.
{ECO:0000244|PubMed:19131326}.
MOD_RES 418 418 Phosphothreonine.
{ECO:0000250|UniProtKB:O60271}.
MOD_RES 586 586 Phosphothreonine.
{ECO:0000250|UniProtKB:O60271}.
MOD_RES 588 588 Phosphoserine.
{ECO:0000250|UniProtKB:O60271}.
MOD_RES 595 595 Phosphothreonine.
{ECO:0000250|UniProtKB:O60271}.
MOD_RES 705 705 Phosphoserine.
{ECO:0000250|UniProtKB:O60271}.
MOD_RES 728 728 Phosphoserine.
{ECO:0000250|UniProtKB:O60271}.
MOD_RES 730 730 Phosphoserine.
{ECO:0000250|UniProtKB:O60271}.
MOD_RES 732 732 Phosphoserine.
{ECO:0000250|UniProtKB:O60271}.
MOD_RES 733 733 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 1188 1188 Phosphoserine.
{ECO:0000250|UniProtKB:O60271}.
MOD_RES 1264 1264 Phosphothreonine.
{ECO:0000250|UniProtKB:O60271}.
VAR_SEQ 1 165 Missing (in isoform 6).
{ECO:0000303|PubMed:15767678}.
/FTId=VSP_018225.
VAR_SEQ 1 143 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:15368895,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_018226.
VAR_SEQ 144 196 RLEEREAELKKEYNALHQRHTEMIHNYMEHLERTKLHQLSG
SDQLEATAHSRI -> MNPGCMLLFVFGFVGGAVVINSAIL
VSLSVLLLVHFSISTGVPALTQNLPRIL (in isoform
3, isoform 4 and isoform 5).
{ECO:0000303|PubMed:15368895,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_018227.
VAR_SEQ 248 261 Missing (in isoform 2, isoform 3, isoform
4, isoform 5 and isoform 6).
{ECO:0000303|PubMed:12391307,
ECO:0000303|PubMed:15368895,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:15767678,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_018228.
VAR_SEQ 405 405 G -> GEYSG (in isoform 3).
{ECO:0000303|PubMed:15368895}.
/FTId=VSP_018229.
VAR_SEQ 1175 1175 T -> TVILHQGRLLGLRA (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_018230.
CONFLICT 241 241 R -> C (in Ref. 1; AAN61564).
{ECO:0000305}.
CONFLICT 453 453 E -> A (in Ref. 1; AAN61564).
{ECO:0000305}.
CONFLICT 468 468 E -> G (in Ref. 5; BAE27980).
{ECO:0000305}.
CONFLICT 705 705 S -> T (in Ref. 3; BAD93176).
{ECO:0000305}.
CONFLICT 1114 1114 L -> P (in Ref. 5; BAE27907).
{ECO:0000305}.
SEQUENCE 1321 AA; 146219 MW; 93A6E97A62E0E92C CRC64;
MELEDGVVYQ EEPGGSGAVM SERVSGLAGS IYREFERLIG RYDEEVVKEL MPLVVAVLEN
LDSVFAQDQE HQVELELLRD DNEQLITQYE REKALRKHAE EKFIEFEDSQ EQEKKDLQTR
VESLESQTRQ LELKAKNYAD QISRLEEREA ELKKEYNALH QRHTEMIHNY MEHLERTKLH
QLSGSDQLEA TAHSRIRKER PISLGIFPLP AGDGLLTPDT QKGGETPGSE QWKFQELSQP
RSHTSLKVSH SPEPPKAVEQ EDELSDISQG GSKATTPAST ANSDVSAIPP DTPSKEDNEG
FVKGTDTSNK SEISKHIEVQ VAQETRNVST ESGENEEKSE VQAIIESTPE LDMDKDLSGY
KGSSTPTKGI ENKAFDRNTE SLFEELSSAG SGLIGDVDEG ADLLGMGREV ENLILENTQL
LETKNALNVV KNDLIAKVDE LTCEKDVLQG ELEAVKQAKL KLEDKNRELE EELRKARAEA
EDARQKAKDD DDSDIPTAQR KRFTRVEMAR VLMERNQYKE RLMELQEAVR WTEMIRASRE
NPAMQEKKRS SIWQFFSRLF SSSSNATKKP EPPVNLKYNA PTSHVTPSVK KRSSTLSQLP
GDKSKAFDFL SEETEASLAS RREQKREQYR QVKAHVQKED GRVQAFGWSL PQKYKQVANG
QGETKMKNLP VPVYLRPLDE KDASMKLWCA VGVNLSGGKT RDGGSVVGAS VFYKDIAGLD
TEGSKQRSAS QSSLDKLDQE LKEQQKEFKN QEELSSQVWI CTSTHSTTKV IIIDAVQPGN
ILDSFTVCNS HVLCIASVPG ARETDYPAGE ELSESGQVDK ASLCGSMTSN SSAEMDSLLG
GITVVGCSTE GLTGAATSPS TNGASPVIEK PPEMETENSE VDENIPTAEE ATEATEGNAG
STEDTVDISQ PGVYTEHVFT DPLGVQIPED LSPVFQSSND SDVYKDQISV LPNEQDLARE
EAQKMSSLLP TMWLGAQNGC LYVHSSVAQW RKCLHSIKLK DSILSIVHVK GIVLVALADG
TLAIFHRGVD GQWDLSNYHL LDLGRPHHSI RCMTVVHDKV WCGYRNKIYV VQPKAMKIEK
SFDAHPRKES QVRQLAWVGD GVWVSIRLDS TLRLYHAHTY QHLQDVDIEP YVSKMLGTGK
LGFSFVRITA LMVSCNRLWV GTGNGVIISI PLTETNKTSG TPGNRPGSVI RVYGDENSDK
VTPGTFIPYC SMAHAQLCFH GHRDAVKFFV AVPGQVISPQ SSSGGADLTA DKAGSSAQEP
SSQTPLKSML VISGGEGYID FRMGDEGGES ELLGEDLPLE PSVTKAERSH LIVWQVMCGN
E


Related products :

Catalog number Product name Quantity
EIAAB38485 Homo sapiens,Human,MAPKAP1,MIP1,Mitogen-activated protein kinase 2-associated protein 1,mSIN1,SAPK-interacting protein 1,SIN1,Stress-activated map kinase-interacting protein 1,Target of rapamycin comp
EIAAB38486 Mapkap1,Mip1,Mitogen-activated protein kinase 2-associated protein 1,Mouse,Mus musculus,SAPK-interacting protein 1,Sin1,Stress-activated map kinase-interacting protein 1,Target of rapamycin complex 2
EIAAB38489 Bos taurus,Bovine,MAPKAP1,Mitogen-activated protein kinase 2-associated protein 1,SAPK-interacting protein 1,SIN1,Stress-activated map kinase-interacting protein 1,Target of rapamycin complex 2 subuni
EIAAB38487 Mapkap1,Mip1,Mitogen-activated protein kinase 2-associated protein 1,Rat,Rattus norvegicus,SAPK-interacting protein 1,Sin1,Stress-activated map kinase-interacting protein 1,Target of rapamycin complex
EIAAB38488 Chicken,Gallus gallus,MAPKAP1,Mitogen-activated protein kinase 2-associated protein 1,SAPK-interacting protein 1,SIN1,Stress-activated map kinase-interacting protein 1,Target of rapamycin complex 2 su
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
EIAAB24831 Mapk1ip1l,MAPK-interacting and spindle-stabilizing protein-like,Mitogen-activated protein kinase 1-interacting protein 1-like,Mouse,Mus musculus
EIAAB24833 Bos taurus,Bovine,MAPK1IP1L,MAPK-interacting and spindle-stabilizing protein-like,Mitogen-activated protein kinase 1-interacting protein 1-like
EIAAB24830 Mapk1ip1,MAPK-interacting and spindle-stabilizing protein,Miss,Mitogen-activated protein kinase 1-interacting protein 1,Mouse,Mus musculus
EIAAB24832 C14orf32,Homo sapiens,Human,MAPK1IP1L,MAPK-interacting and spindle-stabilizing protein-like,Mitogen-activated protein kinase 1-interacting protein 1-like
EIAAB41234 Homo sapiens,Human,MAP3K7IP3,Mitogen-activated protein kinase kinase kinase 7-interacting protein 3,NF-kappa-B-activating protein 1,TAB3,TAB-3,TAK1-binding protein 3,TGF-beta-activated kinase 1 and MA
EIAAB41230 Homo sapiens,Human,KIAA0733,MAP3K7IP2,Mitogen-activated protein kinase kinase kinase 7-interacting protein 2,TAB2,TAB-2,TAK1-binding protein 2,TGF-beta-activated kinase 1 and MAP3K7-binding protein 2,
EIAAB41233 Kiaa4135,Map3k7ip3,Mitogen-activated protein kinase kinase kinase 7-interacting protein 3,Mouse,Mus musculus,Tab3,TAB-3,TAK1-binding protein 3,TGF-beta-activated kinase 1 and MAP3K7-binding protein 3,
EIAAB41231 Kiaa0733,Map3k7ip2,Mitogen-activated protein kinase kinase kinase 7-interacting protein 2,Mouse,Mus musculus,Tab2,TAB-2,TAK1-binding protein 2,TGF-beta-activated kinase 1 and MAP3K7-binding protein 2,
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
EIAAB41228 Homo sapiens,Human,MAP3K7IP1,Mitogen-activated protein kinase kinase kinase 7-interacting protein 1,TAB1,TAK1-binding protein 1,TGF-beta-activated kinase 1 and MAP3K7-binding protein 1,TGF-beta-activa
EIAAB41229 Map3k7ip1,Mitogen-activated protein kinase kinase kinase 7-interacting protein 1,Mouse,Mus musculus,Tab1,TAK1-binding protein 1,TGF-beta-activated kinase 1 and MAP3K7-binding protein 1,TGF-beta-activa
18-003-42203 Mitogen-activated protein kinase kinase kinase 7-interacting protein 2 - TAK1-binding protein 2 Polyclonal 0.05 mg Aff Pur
10-288-21983F Calcium and integrin-binding protein 1 - Calmyrin; DNA-PKcs-interacting protein; Kinase-interacting protein; KIP; CIB; SNK-interacting protein 2-28; SIP2-28 0.05 mg
10-288-21983F Calcium and integrin-binding protein 1 - Calmyrin; DNA-PKcs-interacting protein; Kinase-interacting protein; KIP; CIB; SNK-interacting protein 2-28; SIP2-28 0.1 mg
EIAAB31219 Mouse,Mus musculus,p21-activated protein kinase-interacting protein 1,PAK1-interacting protein 1,Pak1ip1,Putative PAK inhibitor Skb15
18-661-15208 Mitogen-activated protein kinase kinase kinase 7-interacting protein 1 - TGF-beta-activated kinase 1-binding protein 1; TAK1-binding protein 1 Polyclonal 0.1 mg
EIAAB29564 52 kDa repressor of the inhibitor of the protein kinase,58 kDa interferon-induced protein kinase-interacting protein,Mouse,Mus musculus,p52rIPK,p58IPK-interacting protein,Prkrir,THAP domain-containing
EIAAB31221 Bos taurus,Bovine,p21-activated protein kinase-interacting protein 1,PAK1-interacting protein 1,PAK1IP1


 

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