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Pinin (140 kDa nuclear and cell adhesion-related phosphoprotein) (Desmosome-associated protein) (Domain-rich serine protein) (DRS protein) (DRSP) (Melanoma metastasis clone A protein) (Nuclear protein SDK3) (SR-like protein)

 PININ_HUMAN             Reviewed;         717 AA.
Q9H307; B4DZX8; O60899; Q53EM7; Q6P5X4; Q7KYL1; Q99738; Q9UHZ9;
Q9UQR9;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
28-MAR-2018, sequence version 5.
23-MAY-2018, entry version 144.
RecName: Full=Pinin;
AltName: Full=140 kDa nuclear and cell adhesion-related phosphoprotein;
AltName: Full=Desmosome-associated protein;
AltName: Full=Domain-rich serine protein;
Short=DRS protein;
Short=DRSP;
AltName: Full=Melanoma metastasis clone A protein;
AltName: Full=Nuclear protein SDK3;
AltName: Full=SR-like protein;
Name=PNN; Synonyms=DRS, MEMA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 44-50; 213-228 AND
537-553, PUTATIVE FUNCTION IN EPITHELIA MAINTENANCE, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Placenta;
PubMed=8922384; DOI=10.1083/jcb.135.4.1027;
Ouyang P., Sugrue S.P.;
"Characterization of pinin, a novel protein associated with the
desmosome-intermediate filament complex.";
J. Cell Biol. 135:1027-1042(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PUTATIVE FUNCTION.
PubMed=10645008; DOI=10.1038/sj.onc.1203328;
Shi Y., Ouyang P., Sugrue S.P.;
"Characterization of the gene encoding pinin/DRS/memA and evidence for
its potential tumor suppressor function.";
Oncogene 19:289-297(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Adrenal gland;
PubMed=10931946; DOI=10.1073/pnas.160270997;
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
"Gene expression profiling in the human hypothalamus-pituitary-adrenal
axis and full-length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-671.
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
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).
[6]
PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=T-cell;
Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
Submitted (MAY-2006) to UniProtKB.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-717, VARIANT GLY-671, AND TISSUE
SPECIFICITY.
TISSUE=Melanoma;
PubMed=10095061; DOI=10.1016/S0167-4781(99)00012-3;
Degen W.G.J., Agterbos M.A., Muyrers J.P.P., Bloemers H.P.J.,
Swart G.W.M.;
"memA/DRS, a putative mediator of multiprotein complexes, is
overexpressed in the metastasizing human melanoma cell lines BLM and
MV3.";
Biochim. Biophys. Acta 1444:384-394(1999).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 7-717, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Keratinocyte;
PubMed=9447706; DOI=10.1046/j.1432-0436.1997.6230119.x;
Brandner J., Reidenbach S., Franke W.W.;
"Evidence that 'pinin', reportedly a differentiation-specific
desmosomal protein, is actually a widespread nuclear protein.";
Differentiation 62:119-127(1997).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 105-717.
TISSUE=Thymus;
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]
SUBCELLULAR LOCATION.
PubMed=10486276; DOI=10.1006/bbrc.1999.1353;
Ouyang P.;
"Antibodies differentiate desmosome-form and nucleus-form pinin:
evidence that pinin is a moonlighting protein with dual location at
the desmosome and within the nucleus.";
Biochem. Biophys. Res. Commun. 263:192-200(1999).
[11]
INTERACTION WITH KRT8; KRT18 AND KRT19, AND MUTAGENESIS OF LEU-8 AND
LEU-19.
PubMed=10809736; DOI=10.1074/jbc.275.20.14910;
Shi J., Sugrue S.P.;
"Dissection of protein linkage between keratins and pinin, a protein
with dual location at desmosome-intermediate filament complex and in
the nucleus.";
J. Biol. Chem. 275:14910-14915(2000).
[12]
FUNCTION IN PRE-MRNA SPLICING, AND SUBCELLULAR LOCATION.
PubMed=12051732; DOI=10.1016/S0006-291X(02)00495-3;
Wang P., Lou P.-J., Leu S., Ouyang P.;
"Modulation of alternative pre-mRNA splicing in vivo by pinin.";
Biochem. Biophys. Res. Commun. 294:448-455(2002).
[13]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
SPLICEOSOMAL C COMPLEX.
PubMed=11991638; DOI=10.1017/S1355838202021088;
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
"Purification and characterization of native spliceosomes suitable for
three-dimensional structural analysis.";
RNA 8:426-439(2002).
[14]
INTERACTION WITH PS1D/PNO40.
PubMed=12893261; DOI=10.1016/S0006-291X(03)01208-7;
Chang W.-L., Lee D.-C., Leu S., Huang Y.-M., Lu M.-C., Ouyang P.;
"Molecular characterization of a novel nucleolar protein, pNO40.";
Biochem. Biophys. Res. Commun. 307:569-577(2003).
[15]
IDENTIFICATION IN A COMPLEX WITH SR PROTEINS, INTERACTION WITH PNISR;
SFRS4 AND SRRM2, AND SUBCELLULAR LOCATION.
PubMed=14578391; DOI=10.1167/iovs.03-0240;
Zimowska G., Shi J., Munguba G., Jackson M.R., Alpatov R.,
Simmons M.N., Shi Y., Sugrue S.P.;
"Pinin/DRS/memA interacts with SRp75, SRm300 and SRrp130 in corneal
epithelial cells.";
Invest. Ophthalmol. Vis. Sci. 44:4715-4723(2003).
[16]
FUNCTION IN PRE-MRNA SPLICING, IDENTIFICATION IN A MRNP COMPLEX WITH
RNPS1, INTERACTION WITH RNPS1, AND SUBCELLULAR LOCATION.
PubMed=14517304; DOI=10.1128/MCB.23.20.7363-7376.2003;
Li C., Lin R.-I., Lai M.-C., Ouyang P., Tarn W.-Y.;
"Nuclear Pnn/DRS protein binds to spliced mRNPs and participates in
mRNA processing and export via interaction with RNPS1.";
Mol. Cell. Biol. 23:7363-7376(2003).
[17]
INTERACTION WITH PPIG, AND SUBCELLULAR LOCATION.
PubMed=15358154; DOI=10.1016/j.bbrc.2004.07.013;
Lin C.L., Leu S., Lu M.C., Ouyang P.;
"Over-expression of SR-cyclophilin, an interaction partner of nuclear
pinin, releases SR family splicing factors from nuclear speckles.";
Biochem. Biophys. Res. Commun. 321:638-647(2004).
[18]
INTERACTION WITH RNPS1.
PubMed=14729963; DOI=10.1128/MCB.24.3.1174-1187.2004;
Sakashita E., Tatsumi S., Werner D., Endo H., Mayeda A.;
"Human RNPS1 and its associated factors: a versatile alternative pre-
mRNA splicing regulator in vivo.";
Mol. Cell. Biol. 24:1174-1187(2004).
[19]
FUNCTION IN TRANSCRIPTIONAL ACTIVATION, DNA-BINDING, INTERACTION WITH
CTBP1 AND CTBP2, AND MUTAGENESIS OF 502-PRO-GLU-503.
PubMed=15542832; DOI=10.1128/MCB.24.23.10223-10235.2004;
Alpatov R., Munguba G.C., Caton P., Joo J.H., Shi Y., Shi Y.,
Hunt M.E., Sugrue S.P.;
"Nuclear speckle-associated protein Pnn/DRS binds to the
transcriptional corepressor CtBP and relieves CtBP-mediated repression
of the E-cadherin gene.";
Mol. Cell. Biol. 24:10223-10235(2004).
[20]
FUNCTION IN CELL-CELL ADHESION, AND SUBCELLULAR LOCATION.
PubMed=15735603; DOI=1v11/a15;
Joo J.-H., Alpatov R., Munguba G.C., Jackson M.R., Hunt M.E.,
Sugrue S.P.;
"Reduction of Pnn by RNAi induces loss of cell-cell adhesion between
human corneal epithelial cells.";
Mol. Vis. 11:133-142(2005).
[21]
IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16314458; DOI=10.1261/rna.2155905;
Tange T.O., Shibuya T., Jurica M.S., Moore M.J.;
"Biochemical analysis of the EJC reveals two new factors and a stable
tetrameric protein core.";
RNA 11:1869-1883(2005).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100; SER-347 AND
SER-381, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-100; SER-375;
SER-443; SER-450 AND SER-552, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[26]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381 AND SER-443, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[28]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-238, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-96; SER-100;
SER-114; SER-115; THR-124; SER-347; SER-381; SER-443; SER-450 AND
SER-552, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[30]
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).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-66; SER-100;
SER-347; SER-450; SER-658; SER-692 AND SER-695, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[32]
IDENTIFICATION IN THE PSAP COMPLEX, AND FUNCTION OF THE PSAP COMPLEX.
PubMed=22388736; DOI=10.1038/nsmb.2242;
Murachelli A.G., Ebert J., Basquin C., Le Hir H., Conti E.;
"The structure of the ASAP core complex reveals the existence of a
Pinin-containing PSAP complex.";
Nat. Struct. Mol. Biol. 19:378-386(2012).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-66; SER-100;
SER-347; SER-381; SER-443; SER-450 AND SER-552, 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).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-100 AND SER-347,
AND 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).
[35]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-109 AND LYS-157, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[36]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-157, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[37]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-157, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[38]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-109; LYS-157; LYS-304;
LYS-528 AND LYS-553, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[39]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-109; LYS-121; LYS-137;
LYS-155; LYS-157; LYS-228; LYS-280; LYS-304; LYS-311; LYS-359;
LYS-365; LYS-446; LYS-528; LYS-536 AND LYS-553, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Transcriptional activator binding to the E-box 1 core
sequence of the E-cadherin promoter gene; the core-binding
sequence is 5'CAGGTG-3'. Capable of reversing CTBP1-mediated
transcription repression. Auxiliary component of the splicing-
dependent multiprotein exon junction complex (EJC) deposited at
splice junction on mRNAs. The EJC is a dynamic structure
consisting of core proteins and several peripheral nuclear and
cytoplasmic associated factors that join the complex only
transiently either during EJC assembly or during subsequent mRNA
metabolism. Participates in the regulation of alternative pre-mRNA
splicing. Associates to spliced mRNA within 60 nt upstream of the
5'-splice sites. Component of the PSAP complex which binds RNA in
a sequence-independent manner and is proposed to be recruited to
the EJC prior to or during the splicing process and to regulate
specific excision of introns in specific transcription subsets.
Involved in the establishment and maintenance of epithelia cell-
cell adhesion. Potential tumor suppressor for renal cell
carcinoma. {ECO:0000269|PubMed:12051732,
ECO:0000269|PubMed:14517304, ECO:0000269|PubMed:15542832,
ECO:0000269|PubMed:15735603, ECO:0000269|PubMed:22388736}.
-!- SUBUNIT: Found in a mRNA splicing-dependent exon junction complex
(EJC). Found in a complex with SR proteins. Found in a mRNP
complex with RNPS1. Component of the PSAP complex consisting of
RNPS1, SAP18 and PNN. Interacts with PNISR, CTBP1, CTBP2, KRT8,
KRT18, KRT19, PS1D/PNO40, PPIG, RNPS1, SFRS4 and SRRM2. Identified
in the spliceosome C complex. {ECO:0000269|PubMed:10809736,
ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:12893261,
ECO:0000269|PubMed:14517304, ECO:0000269|PubMed:14578391,
ECO:0000269|PubMed:14729963, ECO:0000269|PubMed:15358154,
ECO:0000269|PubMed:15542832, ECO:0000269|PubMed:16314458,
ECO:0000269|PubMed:22388736}.
-!- INTERACTION:
Q15287-1:RNPS1; NbExp=3; IntAct=EBI-681904, EBI-15972541;
O00422:SAP18; NbExp=2; IntAct=EBI-681904, EBI-1044156;
-!- SUBCELLULAR LOCATION: Nucleus speckle. Cell junction, desmosome.
Note=Cell-cell contact area, predominantly desmosome of
intercellular adherens junction. Not a nucleocytoplasmic shuttling
protein.
-!- TISSUE SPECIFICITY: Expressed in placenta, lung, liver, kidney,
pancreas, spleen, thymus, prostate, testis, ovary, small
intestine, colon, heart, epidermis, esophagus, brain and smooth
and skeletal muscle. Expressed strongly in melanoma metastasis
lesions and advanced primary tumors. {ECO:0000269|PubMed:10095061,
ECO:0000269|PubMed:8922384, ECO:0000269|PubMed:9447706}.
-!- SIMILARITY: Belongs to the pinin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA70874.1; Type=Frameshift; Positions=104; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U77718; AAB48304.1; -; mRNA.
EMBL; AF195139; AAG33941.1; -; Genomic_DNA.
EMBL; AF112222; AAF17209.1; -; mRNA.
EMBL; AK223612; BAD97332.1; -; mRNA.
EMBL; BC062602; AAH62602.1; -; mRNA.
EMBL; Y09703; CAA70874.1; ALT_FRAME; mRNA.
EMBL; Y10351; CAA71377.1; -; mRNA.
EMBL; AK303136; BAG64240.1; -; mRNA.
CCDS; CCDS9671.1; -.
RefSeq; NP_002678.2; NM_002687.3.
UniGene; Hs.409965; -.
ProteinModelPortal; Q9H307; -.
BioGrid; 111412; 121.
CORUM; Q9H307; -.
DIP; DIP-32950N; -.
IntAct; Q9H307; 37.
MINT; Q9H307; -.
STRING; 9606.ENSP00000216832; -.
MoonProt; Q9H307; -.
TCDB; 3.A.18.1.1; the nuclear mrna exporter (mrna-e) family.
iPTMnet; Q9H307; -.
PhosphoSitePlus; Q9H307; -.
SwissPalm; Q9H307; -.
BioMuta; PNN; -.
DMDM; 73921750; -.
EPD; Q9H307; -.
MaxQB; Q9H307; -.
PaxDb; Q9H307; -.
PeptideAtlas; Q9H307; -.
PRIDE; Q9H307; -.
Ensembl; ENST00000216832; ENSP00000216832; ENSG00000100941.
GeneID; 5411; -.
KEGG; hsa:5411; -.
UCSC; uc001wuw.5; human.
CTD; 5411; -.
DisGeNET; 5411; -.
EuPathDB; HostDB:ENSG00000100941.8; -.
GeneCards; PNN; -.
H-InvDB; HIX0037750; -.
HGNC; HGNC:9162; PNN.
HPA; HPA001378; -.
MIM; 603154; gene.
neXtProt; NX_Q9H307; -.
OpenTargets; ENSG00000100941; -.
PharmGKB; PA33484; -.
eggNOG; KOG3756; Eukaryota.
eggNOG; ENOG4110W63; LUCA.
GeneTree; ENSGT00730000111160; -.
HOVERGEN; HBG053104; -.
InParanoid; Q9H307; -.
KO; K13114; -.
OrthoDB; EOG091G0S2R; -.
PhylomeDB; Q9H307; -.
TreeFam; TF331859; -.
ChiTaRS; PNN; human.
GeneWiki; Pinin; -.
GenomeRNAi; 5411; -.
PRO; PR:Q9H307; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000100941; -.
CleanEx; HS_PNN; -.
ExpressionAtlas; Q9H307; baseline and differential.
Genevisible; Q9H307; HS.
GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
GO; GO:0005911; C:cell-cell junction; TAS:ProtInc.
GO; GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
GO; GO:0005882; C:intermediate filament; TAS:ProtInc.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0005198; F:structural molecule activity; NAS:ProtInc.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR006786; Pinin_SDK_MemA.
InterPro; IPR006787; Pinin_SDK_N.
Pfam; PF04696; Pinin_SDK_memA; 1.
Pfam; PF04697; Pinin_SDK_N; 1.
ProDom; PD011048; Pinin_SDK_N; 1.
1: Evidence at protein level;
Acetylation; Activator; Cell junction; Coiled coil; Complete proteome;
Direct protein sequencing; DNA-binding; Isopeptide bond; Methylation;
mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Spliceosome; Transcription;
Transcription regulation; Tumor suppressor; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000269|Ref.6}.
CHAIN 2 717 Pinin.
/FTId=PRO_0000190242.
REGION 2 284 Necessary for interaction with RNPS1.
REGION 2 167 Necessary for mediating alternative 5'
splicing.
REGION 2 98 Necessary for interactions with KRT8,
KRT18 and KRT19.
REGION 221 284 Sufficient for PSAP complex assembly.
REGION 606 717 Necessary for interaction with PPIG.
{ECO:0000269|PubMed:15358154}.
COILED 2 32 {ECO:0000255}.
COILED 163 234 {ECO:0000255}.
COILED 287 379 {ECO:0000255}.
COILED 446 467 {ECO:0000255}.
COMPBIAS 172 471 Glu-rich.
COMPBIAS 469 520 Gln-rich.
COMPBIAS 552 704 Ser-rich.
COMPBIAS 632 717 Arg-rich.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000269|Ref.6}.
MOD_RES 48 48 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 54 54 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:O35691}.
MOD_RES 58 58 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 66 66 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 96 96 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 100 100 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 114 114 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 115 115 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 124 124 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 238 238 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 238 238 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:O35691}.
MOD_RES 347 347 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 375 375 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 381 381 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 443 443 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 450 450 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 552 552 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 658 658 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 692 692 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 695 695 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
CROSSLNK 109 109 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 121 121 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 137 137 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 155 155 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 157 157 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 157 157 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 228 228 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 280 280 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 304 304 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 311 311 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 359 359 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 365 365 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 446 446 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 528 528 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 536 536 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 553 553 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
VARIANT 671 671 S -> G (in dbSNP:rs13021).
{ECO:0000269|PubMed:10095061,
ECO:0000269|Ref.4}.
/FTId=VAR_023368.
MUTAGEN 8 8 L->P: Abolishes interaction with KRT18.
{ECO:0000269|PubMed:10809736}.
MUTAGEN 19 19 L->P: Abolishes interaction with KRT18.
{ECO:0000269|PubMed:10809736}.
MUTAGEN 502 503 PE->AA: Abolishes interaction with CTBP1
and shows moderate relief of CTBP1-
mediated repression.
{ECO:0000269|PubMed:15542832}.
CONFLICT 69 69 Missing (in Ref. 1; AAB48304).
{ECO:0000305}.
CONFLICT 168 168 K -> N (in Ref. 1; AAB48304).
{ECO:0000305}.
CONFLICT 268 268 E -> D (in Ref. 1; AAB48304).
{ECO:0000305}.
CONFLICT 303 303 Q -> H (in Ref. 1; AAB48304).
{ECO:0000305}.
CONFLICT 320 320 E -> V (in Ref. 1; AAB48304).
{ECO:0000305}.
CONFLICT 343 343 A -> G (in Ref. 1; AAB48304).
{ECO:0000305}.
CONFLICT 402 403 DQ -> EE (in Ref. 2; AAG33941).
{ECO:0000305}.
CONFLICT 441 441 T -> S (in Ref. 9; BAG64240 and 7;
CAA70874). {ECO:0000305}.
CONFLICT 459 459 E -> D (in Ref. 1; AAB48304).
{ECO:0000305}.
CONFLICT 478 478 P -> A (in Ref. 1; AAB48304).
{ECO:0000305}.
CONFLICT 491 492 QP -> EPQPQLQPEPAQPQLQSQPQLQLQSQCHA (in
Ref. 1; AA sequence). {ECO:0000305}.
CONFLICT 497 497 Q -> H (in Ref. 1; AAB48304).
{ECO:0000305}.
CONFLICT 520 520 Q -> H (in Ref. 1; AAB48304).
{ECO:0000305}.
CONFLICT 523 523 L -> F (in Ref. 1; AAB48304).
{ECO:0000305}.
CONFLICT 541 541 P -> T (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 543 543 E -> D (in Ref. 1; AAB48304).
{ECO:0000305}.
CONFLICT 547 547 T -> I (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 550 550 P -> S (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 551 551 E -> D (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 553 557 KSKTK -> ESETN (in Ref. 1; AAB48304).
{ECO:0000305}.
CONFLICT 566 566 A -> T (in Ref. 1; AAB48304).
{ECO:0000305}.
CONFLICT 569 571 KTS -> RTT (in Ref. 1; AAB48304).
{ECO:0000305}.
CONFLICT 618 618 S -> G (in Ref. 3; AAF17209 and 8;
CAA71377). {ECO:0000305}.
CONFLICT 623 623 S -> SST (in Ref. 7; CAA70874).
{ECO:0000305}.
CONFLICT 664 664 H -> P (in Ref. 2; AAG33941).
{ECO:0000305}.
SEQUENCE 717 AA; 81628 MW; 1F24D3F12E053C8F CRC64;
MAVAVRTLQE QLEKAKESLK NVDENIRKLT GRDPNDVRPI QARLLALSGP GGGRGRGSLL
LRRGFSDSGG GPPAKQRDLE GAVSRLGGER RTRRESRQES DPEDDDVKKP ALQSSVVATS
KERTRRDLIQ DQNMDEKGKQ RNRRIFGLLM GTLQKFKQES TVATERQKRR QEIEQKLEVQ
AEEERKQVEN ERRELFEERR AKQTELRLLE QKVELAQLQE EWNEHNAKII KYIRTKTKPH
LFYIPGRMCP ATQKLIEESQ RKMNALFEGR RIEFAEQINK MEARPRRQSM KEKEHQVVRN
EEQKAEQEEG KVAQREEELE ETGNQHNDVE IEEAGEEEEK EIAIVHSDAE KEQEEEEQKQ
EMEVKMEEET EVRESEKQQD SQPEEVMDVL EMVENVKHVI ADQEVMETNR VESVEPSENE
ASKELEPEME FEIEPDKECK TLSPGKENVS ALDMEKESEE KEEKESEPQP EPVAQPQPQS
QPQLQLQSQS QPVLQSQPPS QPEDLSLAVL QPTPQVTQEQ GHLLPERKDF PVESVKLTEV
PVEPVLTVHP ESKSKTKTRS RSRGRARNKT SKSRSRSSSS SSSSSSSTSS SSGSSSSSGS
SSSRSSSSSS SSTSGSSSRD SSSSTSSSSE SRSRSRGRGH NRDRKHRRSV DRKRRDTSGL
ERSHKSSKGG SSRDTKGSKD KNSRSDRKRS ISESSRSGKR SSRSERDRKS DRKDKRR


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