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NCK-interacting protein with SH3 domain (54 kDa VacA-interacting protein) (54 kDa vimentin-interacting protein) (VIP54) (90 kDa SH3 protein interacting with Nck) (AF3p21) (Dia-interacting protein 1) (DIP-1) (Diaphanous protein-interacting protein) (SH3 adapter protein SPIN90) (WASP-interacting SH3-domain protein) (WISH) (Wiskott-Aldrich syndrome protein-interacting protein)

 SPN90_HUMAN             Reviewed;         722 AA.
Q9NZQ3; B4DFL5; Q6GU34; Q6SPF3; Q8TC10; Q9UGM8;
05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
30-AUG-2017, entry version 156.
RecName: Full=NCK-interacting protein with SH3 domain;
AltName: Full=54 kDa VacA-interacting protein;
AltName: Full=54 kDa vimentin-interacting protein;
Short=VIP54;
AltName: Full=90 kDa SH3 protein interacting with Nck;
AltName: Full=AF3p21;
AltName: Full=Dia-interacting protein 1;
Short=DIP-1;
AltName: Full=Diaphanous protein-interacting protein;
AltName: Full=SH3 adapter protein SPIN90;
AltName: Full=WASP-interacting SH3-domain protein;
Short=WISH;
AltName: Full=Wiskott-Aldrich syndrome protein-interacting protein;
Name=NCKIPSD; Synonyms=AF3P21, SPIN90;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHROMOSOMAL TRANSLOCATION
WITH KMT2A/MLL1.
TISSUE=Leukemia;
PubMed=10648423;
Sano K., Hayakawa A., Piao J.-H., Kosaka Y., Nakamura H.;
"Novel SH3 protein encoded by the AF3p21 gene is fused to the mixed
lineage leukemia protein in a therapy-related leukemia with
t(3;11)(p21;q23).";
Blood 95:1066-1068(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH VACA, AND
TISSUE SPECIFICITY.
TISSUE=Cervix carcinoma;
PubMed=10619843; DOI=10.1093/emboj/19.1.48;
de Bernard M., Moschioni M., Napolitani G., Rappuoli R.,
Montecucco C.;
"The VacA toxin of Helicobacter pylori identifies a new intermediate
filament-interacting protein.";
EMBO J. 19:48-56(2000).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
TISSUE=Cervix carcinoma;
PubMed=11241789; DOI=10.1002/gcc.1102;
Hayakawa A., Matsuda Y., Daibata M., Nakamura H., Sano K.;
"Genomic organization, tissue expression and cellular localization of
AF3p21, a fusion partner of MLL in therapy-related leukemia.";
Genes Chromosomes Cancer 30:364-374(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Heart;
PubMed=11278500; DOI=10.1074/jbc.M009411200;
Lim C.S., Park E.S., Kim D.J., Song Y.H., Eom S.H., Chun J.-S.,
Kim J.H., Kim J.-K., Park D., Song W.K.;
"SPIN90 (SH3 protein interacting with Nck, 90 kDa), an adapter protein
that is developmentally regulated during cardiac myocyte
differentiation.";
J. Biol. Chem. 276:12871-12878(2001).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS
1 AND 2).
TISSUE=Brain, and Placenta;
PubMed=11509578; DOI=10.1074/jbc.M107026200;
Satoh S., Tominaga T.;
"mDia-interacting protein acts downstream of rho-mDia and modifies src
activation and stress fiber formation.";
J. Biol. Chem. 276:39290-39294(2001).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND INTERACTION WITH FHOD1.
TISSUE=Bone marrow;
PubMed=15095401; DOI=10.1002/jcb.20031;
Westendorf J.J., Koka S.;
"Identification of FHOD1-binding proteins and mechanisms of FHOD1-
regulated actin dynamics.";
J. Cell. Biochem. 92:29-41(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
SER-660.
TISSUE=Placenta, and Skin;
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).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 448-722 (ISOFORM 5).
TISSUE=Brain cortex;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[11]
INTERACTION WITH FASLG.
PubMed=19807924; DOI=10.1186/1471-2172-10-53;
Voss M., Lettau M., Janssen O.;
"Identification of SH3 domain interaction partners of human FasL
(CD178) by phage display screening.";
BMC Immunol. 10:53-53(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
FUNCTION IN ANGIOGENESIS, AND INTERACTION WITH TMIGD2.
PubMed=22419821; DOI=10.1091/mbc.E11-11-0934;
Rahimi N., Rezazadeh K., Mahoney J.E., Hartsough E., Meyer R.D.;
"Identification of IGPR-1 as a novel adhesion molecule involved in
angiogenesis.";
Mol. Biol. Cell 23:1646-1656(2012).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-181, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Has an important role in stress fiber formation induced
by active diaphanous protein homolog 1 (DRF1). Induces microspike
formation, in vivo (By similarity). In vitro, stimulates N-WASP-
induced ARP2/3 complex activation in the absence of CDC42 (By
similarity). May play an important role in the maintenance of
sarcomeres and/or in the assembly of myofibrils into sarcomeres.
Implicated in regulation of actin polymerization and cell
adhesion. Plays a role in angiogenesis. {ECO:0000250,
ECO:0000269|PubMed:22419821}.
-!- SUBUNIT: Associates with the intermediate filaments, vimentin and
desmin. Binds the first and third SH3 domains of NCK. Binds the
proline-rich domains of N-WASP through its SH3 domain (By
similarity). Similarly, binds diaphanous protein homolog 1 (DRF1).
Binds the SH3 domains of GRB2 through its proline-rich domains.
Interacts with Helicobacter pylori toxin vacA. Isoform 4 interacts
with FHOD1. Interacts with FASLG. Interacts with TMIGD2.
{ECO:0000250, ECO:0000269|PubMed:10619843,
ECO:0000269|PubMed:15095401, ECO:0000269|PubMed:19807924,
ECO:0000269|PubMed:22419821}.
-!- INTERACTION:
Q60437:BAIAP2 (xeno); NbExp=3; IntAct=EBI-745080, EBI-7010040;
Q9UQB8:BAIAP2; NbExp=2; IntAct=EBI-745080, EBI-525456;
Q96FN4:CPNE2; NbExp=4; IntAct=EBI-10963850, EBI-7097057;
P06241:FYN; NbExp=2; IntAct=EBI-745080, EBI-515315;
Q9Z0W5:Pacsin1 (xeno); NbExp=6; IntAct=EBI-745080, EBI-1550185;
Q9QY17:Pacsin2 (xeno); NbExp=2; IntAct=EBI-745080, EBI-491201;
O00233:PSMD9; NbExp=3; IntAct=EBI-745080, EBI-750973;
O60504:SORBS3; NbExp=3; IntAct=EBI-745080, EBI-741237;
-!- SUBCELLULAR LOCATION: Nucleus. Note=Colocalizes with DRF1 at
membrane ruffles, and with Nck at Z-disks in mature cardiac
myocytes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q9NZQ3-1; Sequence=Displayed;
Name=2;
IsoId=Q9NZQ3-2; Sequence=VSP_003971;
Name=3;
IsoId=Q9NZQ3-3; Sequence=VSP_039422;
Note=No experimental confirmation available.;
Name=4; Synonyms=WISH-B;
IsoId=Q9NZQ3-4; Sequence=VSP_039422, VSP_039425, VSP_039426;
Name=5;
IsoId=Q9NZQ3-5; Sequence=VSP_039423, VSP_039424;
Note=Found in a brain affected by Alzheimer disease. May be due
to intron retention. No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highest expression in heart, brain, skeletal
muscle, kidney and liver. Lower levels in placenta, lung, small
intestine and leukocytes. Weak expression in colon, thymus and
spleen. {ECO:0000269|PubMed:10619843}.
-!- DISEASE: Note=A chromosomal aberration involving NCKIPSD/AF3p21 is
found in therapy-related leukemia. Translocation t(3;11)(p21;q23)
with KMT2A/MLL1. {ECO:0000269|PubMed:10648423}.
-!- SEQUENCE CAUTION:
Sequence=BAG57476.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/AF3p21ID228.html";
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EMBL; AF178432; AAF35985.1; -; mRNA.
EMBL; AJ242655; CAB65089.2; -; mRNA.
EMBL; AF303581; AAK09094.1; -; mRNA.
EMBL; AB069981; BAB63204.1; -; Genomic_DNA.
EMBL; AB069982; BAB63205.1; -; Genomic_DNA.
EMBL; AY453794; AAR83735.1; -; mRNA.
EMBL; AC141002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC016052; AAH16052.1; -; mRNA.
EMBL; BC026280; AAH26280.1; -; mRNA.
EMBL; AK294151; BAG57476.1; ALT_INIT; mRNA.
CCDS; CCDS2776.1; -. [Q9NZQ3-1]
CCDS; CCDS46827.1; -. [Q9NZQ3-3]
RefSeq; NP_057537.1; NM_016453.3. [Q9NZQ3-1]
RefSeq; NP_909119.1; NM_184231.2. [Q9NZQ3-3]
UniGene; Hs.655006; -.
ProteinModelPortal; Q9NZQ3; -.
SMR; Q9NZQ3; -.
BioGrid; 119583; 54.
IntAct; Q9NZQ3; 52.
MINT; MINT-1438080; -.
STRING; 9606.ENSP00000294129; -.
iPTMnet; Q9NZQ3; -.
PhosphoSitePlus; Q9NZQ3; -.
BioMuta; NCKIPSD; -.
DMDM; 17433253; -.
EPD; Q9NZQ3; -.
MaxQB; Q9NZQ3; -.
PaxDb; Q9NZQ3; -.
PeptideAtlas; Q9NZQ3; -.
PRIDE; Q9NZQ3; -.
DNASU; 51517; -.
Ensembl; ENST00000294129; ENSP00000294129; ENSG00000213672. [Q9NZQ3-1]
Ensembl; ENST00000416649; ENSP00000389059; ENSG00000213672. [Q9NZQ3-3]
GeneID; 51517; -.
KEGG; hsa:51517; -.
UCSC; uc003cum.5; human. [Q9NZQ3-1]
CTD; 51517; -.
DisGeNET; 51517; -.
GeneCards; NCKIPSD; -.
HGNC; HGNC:15486; NCKIPSD.
HPA; CAB019267; -.
HPA; HPA050005; -.
MIM; 606671; gene.
neXtProt; NX_Q9NZQ3; -.
OpenTargets; ENSG00000213672; -.
PharmGKB; PA134872724; -.
eggNOG; KOG4035; Eukaryota.
eggNOG; ENOG410Y8WT; LUCA.
GeneTree; ENSGT00390000015725; -.
HOGENOM; HOG000008184; -.
HOVERGEN; HBG061630; -.
InParanoid; Q9NZQ3; -.
OMA; YHTDMMA; -.
OrthoDB; EOG091G0D4N; -.
PhylomeDB; Q9NZQ3; -.
TreeFam; TF324522; -.
Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs.
SignaLink; Q9NZQ3; -.
SIGNOR; Q9NZQ3; -.
ChiTaRS; NCKIPSD; human.
GeneWiki; NCKIPSD; -.
GenomeRNAi; 51517; -.
PRO; PR:Q9NZQ3; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000213672; -.
CleanEx; HS_NCKIPSD; -.
ExpressionAtlas; Q9NZQ3; baseline and differential.
Genevisible; Q9NZQ3; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005882; C:intermediate filament; NAS:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0008092; F:cytoskeletal protein binding; NAS:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0007010; P:cytoskeleton organization; NAS:UniProtKB.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0006607; P:NLS-bearing protein import into nucleus; TAS:ProtInc.
GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd11849; SH3_SPIN90; 1.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR018556; DUF2013.
InterPro; IPR001452; SH3_domain.
InterPro; IPR035514; SPIN90_SH3.
Pfam; PF09431; DUF2013; 1.
Pfam; PF00018; SH3_1; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF50044; SSF50044; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
Alternative splicing; Chromosomal rearrangement; Complete proteome;
Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene;
Reference proteome; SH3 domain; SH3-binding.
CHAIN 1 722 NCK-interacting protein with SH3 domain.
/FTId=PRO_0000072130.
DOMAIN 1 58 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
MOTIF 175 192 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 171 275 Pro-rich.
COMPBIAS 197 240 Ser/Thr-rich.
COMPBIAS 442 487 Leu-rich.
COMPBIAS 534 601 Leu-rich.
SITE 57 58 Breakpoint for translocation to form
KMT2A/MLL1-AF3P21 oncogene.
MOD_RES 120 120 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ESJ4}.
MOD_RES 181 181 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 294 294 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ESJ4}.
VAR_SEQ 165 171 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:15095401,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_039422.
VAR_SEQ 567 596 AADQNVIMAALSKHANVKIFSEKLLLLLNR -> GGVGPGW
AVAEHMVALRLSTLSIPMSFLSC (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_039423.
VAR_SEQ 597 722 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_039424.
VAR_SEQ 656 722 LRMEYLSLMHAIVRTTPYLQHRHRLPDLQAILRRILNEEET
SPQCQMDRMIVREMCKEFLVLGEAPS -> GPFGAGQRPWP
GVPRLLEPGSTPSREPHPVERSGVPALTSSWASGCPRPLHP
ALQLVIDSAFGGRSV (in isoform 2).
{ECO:0000303|PubMed:10619843}.
/FTId=VSP_003971.
VAR_SEQ 656 658 LRM -> GVH (in isoform 4).
{ECO:0000303|PubMed:15095401}.
/FTId=VSP_039425.
VAR_SEQ 659 722 Missing (in isoform 4).
{ECO:0000303|PubMed:15095401}.
/FTId=VSP_039426.
VARIANT 324 324 T -> S (in dbSNP:rs6785620).
/FTId=VAR_051378.
VARIANT 660 660 Y -> S (in dbSNP:rs17855516).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_063400.
SEQUENCE 722 AA; 78960 MW; 7683046B94647332 CRC64;
MYRALYAFRS AEPNALAFAA GETFLVLERS SAHWWLAARA RSGETGYVPP AYLRRLQGLE
QDVLQAIDRA IEAVHNTAMR DGGKYSLEQR GVLQKLIHHR KETLSRRGPS ASSVAVMTSS
TSDHHLDAAA ARQPNGVCRA GFERQHSLPS SEHLGADGGL YQIPLPSSQI PPQPRRAAPT
TPPPPVKRRD REALMASGSG GHNTMPSGGN SVSSGSSVSS TSLDTLYTSS SPSEPGSSCS
PTPPPVPRRG THTTVSQVQP PPSKASAPEP PAEEEVATGT TSASDDLEAL GTLSLGTTEE
KAAAEAAVPR TIGAELMELV RRNTGLSHEL CRVAIGIIVG HIQASVPASS PVMEQVLLSL
VEGKDLSMAL PSGQVCHDQQ RLEVIFADLA RRKDDAQQRS WALYEDEGVI RCYLEELLHI
LTDADPEVCK KMCKRNEFES VLALVAYYQM EHRASLRLLL LKCFGAMCSL DAAIISTLVS
SVLPVELARD MQTDTQDHQK LCYSALILAM VFSMGEAVPY AHYEHLGTPF AQFLLNIVED
GLPLDTTEQL PDLCVNLLLA LNLHLPAADQ NVIMAALSKH ANVKIFSEKL LLLLNRGDDP
VRIFKHEPQP PHSVLKFLQD VFGSPATAAI FYHTDMMALI DITVRHIADL SPGDKLRMEY
LSLMHAIVRT TPYLQHRHRL PDLQAILRRI LNEEETSPQC QMDRMIVREM CKEFLVLGEA
PS


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EIAAB46350 Mouse,Mus musculus,WAS_WASL-interacting protein family member 1,WASP-interacting protein,Waspip,Wip,Wipf1,Wiskott-Aldrich syndrome protein-interacting protein
EIAAB46351 Rat,Rattus norvegicus,WAS_WASL-interacting protein family member 1,WASP-interacting protein,Waspip,Wip,Wipf1,Wiskott-Aldrich syndrome protein-interacting protein
EIAAB39603 54 kDa VacA-interacting protein,90 kDa N-WASP-interacting protein,90 kDa SH3 protein interacting with Nck,Mouse,Mus musculus,NCK-interacting protein with SH3 domain,Nckipsd,N-WASP-binding protein,SH3
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
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
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
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
EIAAB31034 Androgen receptor-interacting protein 3,ARIP3,DAB2-interacting protein,DIP,E3 SUMO-protein ligase PIAS2,Homo sapiens,Human,Miz1,Msx-interacting zinc finger protein,PIAS2,PIAS-NY protein,PIASX,Protein
EIAAB32252 Addicsin,ADP-ribosylation factor-like protein 6-interacting protein 5,Aip5,Aip-5,ARL-6-interacting protein 5,Arl6ip5,Glutamate transporter EAAC1-interacting protein,GTRAP3-18,Jwa,Mouse,Mus musculus,PR
EIAAB30253 Aip1,ALG-2-interacting protein 1,ALG-2-interacting protein X,Alix,E2F1-inducible protein,Eig2,Mouse,Mus musculus,Pdcd6ip,Programmed cell death 6-interacting protein
EIAAB07421 Cdc42-interacting protein 4,Cip4,Rat,Rattus norvegicus,Salt tolerant protein,Stp,Thyroid receptor-interacting protein 10,TR-interacting protein 10,Trip10,TRIP-10
EIAAB44012 Homo sapiens,Human,OIP1,OIP-1,Opa-interacting protein 1,Thyroid receptor-interacting protein 6,TR-interacting protein 6,TRIP6,TRIP-6,ZRP-1,Zyxin-related protein 1
15-288-22308F GIPC PDZ domain-containing protein 1 - RGS19-interacting protein 1; GAIP C-terminus-interacting protein; RGS-GAIP-interacting protein; Tax interaction protein 2; TIP-2 Polyclonal 0.1 mg
15-288-22308F GIPC PDZ domain-containing protein 1 - RGS19-interacting protein 1; GAIP C-terminus-interacting protein; RGS-GAIP-interacting protein; Tax interaction protein 2; TIP-2 Polyclonal 0.05 mg
18-003-44197 PDZ domain-containing protein GIPC1 - RGS19-interacting protein 1; GAIP C-terminus-interacting protein; RGS-GAIP-interacting protein; Tax interaction protein 2; TIP-2 Polyclonal 0.05 mg Aff Pur
EIAAB31033 Androgen receptor-interacting protein 3,ARIP3,DAB2-interacting protein,DIP,E3 SUMO-protein ligase PIAS2,Miz1,Mouse,Msx-interacting zinc finger protein,Mus musculus,Pias2,Piasx,Protein inhibitor of act
EIAAB31032 Androgen receptor-interacting protein 3,ARIP3,DAB2-interacting protein,DIP,E3 SUMO-protein ligase PIAS2,Miz1,Msx-interacting-zinc finger protein,Pias2,Piasx,Protein inhibitor of activated STAT x,Prote
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
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
10-288-22308F GIPC PDZ domain-containing protein 1 - RGS19-interacting protein 1; GAIP C-terminus-interacting protein; RGS-GAIP-interacting protein; Tax interaction protein 2; TIP-2 0.05 mg
10-288-22308F GIPC PDZ domain-containing protein 1 - RGS19-interacting protein 1; GAIP C-terminus-interacting protein; RGS-GAIP-interacting protein; Tax interaction protein 2; TIP-2 0.1 mg
EIAAB29754 Homo sapiens,HSPC218,Human,PABP-interacting protein 2,PAIP2,PAIP-2,PAIP2A,Poly(A)-binding protein-interacting protein 2,Polyadenylate-binding protein-interacting protein 2


 

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