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Acidic leucine-rich nuclear phosphoprotein 32 family member A (Acidic nuclear phosphoprotein pp32) (pp32) (Leucine-rich acidic nuclear protein) (LANP) (Mapmodulin) (Potent heat-stable protein phosphatase 2A inhibitor I1PP2A) (Putative HLA-DR-associated protein I) (PHAPI)

 AN32A_HUMAN             Reviewed;         249 AA.
P39687; B2R6T4; Q53FK4; Q5J8L8; Q7M4N6;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
22-NOV-2017, entry version 180.
RecName: Full=Acidic leucine-rich nuclear phosphoprotein 32 family member A;
AltName: Full=Acidic nuclear phosphoprotein pp32;
Short=pp32;
AltName: Full=Leucine-rich acidic nuclear protein;
Short=LANP;
AltName: Full=Mapmodulin;
AltName: Full=Potent heat-stable protein phosphatase 2A inhibitor I1PP2A;
AltName: Full=Putative HLA-DR-associated protein I;
Short=PHAPI;
Name=ANP32A; Synonyms=C15orf1, LANP, MAPM, PHAP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-26; 29-47; 71-97
AND 100-161.
TISSUE=B-cell lymphoma;
PubMed=8192856; DOI=10.1515/bchm3.1994.375.2.113;
Vaesen M., Barnikol-Watanabe S., Goetz H., Adil Awni L., Cole T.,
Zimmermann B., Kratzin H.D., Hilschmann N.;
"Purification and characterization of two putative HLA class II
associated proteins: PHAPI and PHAPII.";
Biol. Chem. Hoppe-Seyler 375:113-126(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 7-12 AND 29-44.
TISSUE=Kidney;
PubMed=8679524; DOI=10.1021/bi960581y;
Li M., Makkinje A., Damuni Z.;
"Molecular identification of I1PP2A, a novel potent heat-stable
inhibitor protein of protein phosphatase 2A.";
Biochemistry 35:6998-7002(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8970164; DOI=10.1091/mbc.7.12.2045;
Chen T.-H., Brody J.R., Romantsev F.E., Yu J.-G., Kayler A.E.,
Voneiff E., Kuhajda F.P., Pasternack G.R.;
"Structure of pp32, an acidic nuclear protein which inhibits oncogene-
induced formation of transformed foci.";
Mol. Biol. Cell 7:2045-2056(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9353121; DOI=10.1038/40159;
Matilla A., Koshy B.T., Cummings C.J., Isobe T., Orr H.T.,
Zoghbi H.Y.;
"The cerebellar leucine-rich acidic nuclear protein interacts with
ataxin-1.";
Nature 389:974-978(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Brain;
PubMed=15642345; DOI=10.1016/j.febslet.2004.11.097;
Tsujio I., Zaidi T., Xu J., Kotula L., Grundke-Iqbal I., Iqbal K.;
"Inhibitors of protein phosphatase-2A from human brain structures,
immunocytological localization and activities towards
dephosphorylation of the Alzheimer type hyperphosphorylated tau.";
FEBS Lett. 579:363-372(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Synovium;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lymph;
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).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10400610; DOI=10.1074/jbc.274.29.20053;
Brody J.R., Kadkol S.S., Mahmoud M.A., Rebel J.M., Pasternack G.R.;
"Identification of sequences required for inhibition of oncogene-
mediated transformation by pp32.";
J. Biol. Chem. 274:20053-20055(1999).
[12]
INTERACTION WITH THE INHAT COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=11163245; DOI=10.1016/S0092-8674(01)00196-9;
Seo S.-B., McNamara P., Heo S., Turner A., Lane W.S., Chakravarti D.;
"Regulation of histone acetylation and transcription by INHAT, a human
cellular complex containing the Set oncoprotein.";
Cell 104:119-130(2001).
[13]
INTERACTION WITH SET.
PubMed=11555662; DOI=10.1074/jbc.M108137200;
Beresford P.J., Zhang D., Oh D.Y., Fan Z., Greer E.L., Russo M.L.,
Jaju M., Lieberman J.;
"Granzyme A activates an endoplasmic reticulum-associated caspase-
independent nuclease to induce single-stranded DNA nicks.";
J. Biol. Chem. 276:43285-43293(2001).
[14]
FUNCTION.
PubMed=11360199; DOI=10.1038/sj.onc.1204294;
Bai J., Brody J.R., Kadkol S.S., Pasternack G.R.;
"Tumor suppression and potentiation by manipulation of pp32
expression.";
Oncogene 20:2153-2160(2001).
[15]
INTERACTION WITH ELAVL1, AND SUBCELLULAR LOCATION.
PubMed=11729309; DOI=10.1126/science.1064693;
Gallouzi I.-E., Steitz J.A.;
"Delineation of mRNA export pathways by the use of cell-permeable
peptides.";
Science 294:1895-1901(2001).
[16]
IDENTIFICATION IN THE SET COMPLEX.
PubMed=12628186; DOI=10.1016/S0092-8674(03)00150-8;
Fan Z., Beresford P.J., Oh D.Y., Zhang D., Lieberman J.;
"Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-
mediated apoptosis, and the nucleosome assembly protein SET is its
inhibitor.";
Cell 112:659-672(2003).
[17]
SUBCELLULAR LOCATION.
PubMed=12524539; DOI=10.1038/ni885;
Fan Z., Beresford P.J., Zhang D., Xu Z., Novina C.D., Yoshida A.,
Pommier Y., Lieberman J.;
"Cleaving the oxidative repair protein Ape1 enhances cell death
mediated by granzyme A.";
Nat. Immunol. 4:145-153(2003).
[18]
GENE FAMILY, AND NOMENCLATURE.
PubMed=15895553; DOI=10.1080/14734220410019020;
Matilla A., Radrizzani M.;
"The Anp32 family of proteins containing leucine-rich repeats.";
Cerebellum 4:7-18(2005).
[19]
IDENTIFICATION IN THE SET COMPLEX.
PubMed=16818237; DOI=10.1016/j.molcel.2006.06.005;
Chowdhury D., Beresford P.J., Zhu P., Zhang D., Sung J.S., Demple B.,
Perrino F.W., Lieberman J.;
"The exonuclease TREX1 is in the SET complex and acts in concert with
NM23-H1 to degrade DNA during granzyme A-mediated cell death.";
Mol. Cell 23:133-142(2006).
[20]
FUNCTION, AND INTERACTION WITH E4F1.
PubMed=17557114; DOI=10.1038/sj.embor.7400983;
Cvetanovic M., Rooney R.J., Garcia J.J., Toporovskaya N., Zoghbi H.Y.,
Opal P.;
"The role of LANP and ataxin 1 in E4F-mediated transcriptional
repression.";
EMBO Rep. 8:671-677(2007).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15 AND SER-17, 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).
[22]
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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15 AND SER-17, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
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).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158, 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).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[26]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-149, AND LEUCINE-RICH
REPEATS.
PubMed=17567741; DOI=10.1110/ps.072803507;
Huyton T., Wolberger C.;
"The crystal structure of the tumor suppressor protein pp32 (Anp32a):
structural insights into Anp32 family of proteins.";
Protein Sci. 16:1308-1315(2007).
-!- FUNCTION: Implicated in a number of cellular processes, including
proliferation, differentiation, caspase-dependent and caspase-
independent apoptosis, suppression of transformation (tumor
suppressor), inhibition of protein phosphatase 2A, regulation of
mRNA trafficking and stability in association with ELAVL1, and
inhibition of acetyltransferases as part of the INHAT (inhibitor
of histone acetyltransferases) complex. Plays a role in E4F1-
mediated transcriptional repression. {ECO:0000269|PubMed:10400610,
ECO:0000269|PubMed:11360199, ECO:0000269|PubMed:15642345,
ECO:0000269|PubMed:17557114}.
-!- SUBUNIT: Component of the SET complex, composed of at least
ANP32A, APEX1, HMGB2, NME1, SET and TREX1. Directly interacts with
SET. Interacts with ATXN1/SCA1. Interacts with MAP1B. Interacts
with ELAVL1. Part of the INHAT (inhibitor of histone
acetyltransferases) complex. Interacts with E4F1.
{ECO:0000269|PubMed:11163245, ECO:0000269|PubMed:11555662,
ECO:0000269|PubMed:11729309, ECO:0000269|PubMed:12628186,
ECO:0000269|PubMed:16818237, ECO:0000269|PubMed:17557114}.
-!- INTERACTION:
O15169:AXIN1; NbExp=2; IntAct=EBI-359234, EBI-710484;
Q66K89:E4F1; NbExp=3; IntAct=EBI-359234, EBI-1227043;
P67775:PPP2CA; NbExp=2; IntAct=EBI-359234, EBI-712311;
P63331:Ppp2ca (xeno); NbExp=2; IntAct=EBI-359234, EBI-7050205;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Endoplasmic reticulum.
Note=Translocates to the cytoplasm during the process of
neuritogenesis (By similarity). Shuttles between nucleus and
cytoplasm. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in all tissues tested. Highly
expressed in kidney and skeletal muscle, moderate levels of
expression in brain, placenta and pancreas, and weakly expressed
in lung. Found in all regions of the brain examined (amygdala,
caudate nucleus, corpus callosum, hippocampus and thalamus), with
highest levels in amygdala. {ECO:0000269|PubMed:15642345}.
-!- PTM: Phosphorylated on serine residues.
-!- PTM: The N-terminus is blocked.
-!- PTM: Some glutamate residues are glycylated by TTLL8. This
modification occurs exclusively on glutamate residues and results
in a glycine chain on the gamma-carboxyl group (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the ANP32 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD97000.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; X75090; CAA52981.1; -; mRNA.
EMBL; U60823; AAC50570.1; -; mRNA.
EMBL; U73477; AAB39706.1; -; mRNA.
EMBL; AF025684; AAB91548.1; -; mRNA.
EMBL; AY349171; AAQ79832.1; -; mRNA.
EMBL; BT007436; AAP36104.1; -; mRNA.
EMBL; AK223280; BAD97000.1; ALT_INIT; mRNA.
EMBL; AK312703; BAG35581.1; -; mRNA.
EMBL; CH471082; EAW77824.1; -; Genomic_DNA.
EMBL; BC007200; AAH07200.1; -; mRNA.
CCDS; CCDS45292.1; -.
PIR; S36375; S36375.
PIR; S43309; S43309.
RefSeq; NP_006296.1; NM_006305.3.
UniGene; Hs.458747; -.
PDB; 2JE0; X-ray; 2.40 A; A/B/C/D/E/F=1-149.
PDB; 2JE1; X-ray; 2.69 A; A/B/C/D=1-149.
PDB; 4XOS; X-ray; 1.56 A; A/B=1-149.
PDBsum; 2JE0; -.
PDBsum; 2JE1; -.
PDBsum; 4XOS; -.
ProteinModelPortal; P39687; -.
SMR; P39687; -.
BioGrid; 113791; 57.
CORUM; P39687; -.
IntAct; P39687; 19.
MINT; MINT-4999627; -.
STRING; 9606.ENSP00000417864; -.
iPTMnet; P39687; -.
PhosphoSitePlus; P39687; -.
SwissPalm; P39687; -.
BioMuta; ANP32A; -.
DMDM; 730318; -.
SWISS-2DPAGE; P39687; -.
EPD; P39687; -.
MaxQB; P39687; -.
PaxDb; P39687; -.
PeptideAtlas; P39687; -.
PRIDE; P39687; -.
TopDownProteomics; P39687; -.
DNASU; 8125; -.
Ensembl; ENST00000465139; ENSP00000417864; ENSG00000140350.
GeneID; 8125; -.
KEGG; hsa:8125; -.
UCSC; uc002arl.4; human.
CTD; 8125; -.
DisGeNET; 8125; -.
EuPathDB; HostDB:ENSG00000140350.15; -.
GeneCards; ANP32A; -.
HGNC; HGNC:13233; ANP32A.
HPA; CAB005231; -.
HPA; HPA063133; -.
HPA; HPA067561; -.
MIM; 600832; gene.
neXtProt; NX_P39687; -.
OpenTargets; ENSG00000140350; -.
PharmGKB; PA24811; -.
eggNOG; KOG2739; Eukaryota.
eggNOG; ENOG4111HZT; LUCA.
GeneTree; ENSGT00560000077130; -.
HOGENOM; HOG000007361; -.
HOVERGEN; HBG053102; -.
InParanoid; P39687; -.
KO; K18646; -.
OMA; DCNDEEA; -.
OrthoDB; EOG091G0R8Z; -.
PhylomeDB; P39687; -.
TreeFam; TF317206; -.
Reactome; R-HSA-450520; HuR (ELAVL1) binds and stabilizes mRNA.
ChiTaRS; ANP32A; human.
EvolutionaryTrace; P39687; -.
GenomeRNAi; 8125; -.
PMAP-CutDB; P39687; -.
PRO; PR:P39687; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000140350; -.
CleanEx; HS_ANP32A; -.
ExpressionAtlas; P39687; baseline and differential.
Genevisible; P39687; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0042393; F:histone binding; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
GO; GO:0006913; P:nucleocytoplasmic transport; IDA:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR003603; U2A'_phosphoprotein32A_C.
SMART; SM00446; LRRcap; 1.
SUPFAM; SSF52058; SSF52058; 1.
PROSITE; PS51450; LRR; 4.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
Endoplasmic reticulum; Leucine-rich repeat; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation.
CHAIN 1 249 Acidic leucine-rich nuclear
phosphoprotein 32 family member A.
/FTId=PRO_0000137592.
REPEAT 18 38 LRR 1. {ECO:0000269|PubMed:17567741}.
REPEAT 43 64 LRR 2. {ECO:0000269|PubMed:17567741}.
REPEAT 65 87 LRR 3. {ECO:0000269|PubMed:17567741}.
REPEAT 89 110 LRR 4. {ECO:0000269|PubMed:17567741}.
DOMAIN 123 161 LRRCT.
REGION 150 174 Necessary for tumor-suppressive function.
REGION 165 249 Interaction with E4F1. {ECO:0000250}.
COMPBIAS 168 249 Asp/Glu-rich (highly acidic).
MOD_RES 15 15 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 17 17 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 158 158 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
CONFLICT 186 186 V -> A (in Ref. 8; BAD97000).
{ECO:0000305}.
HELIX 3 10 {ECO:0000244|PDB:4XOS}.
TURN 11 13 {ECO:0000244|PDB:4XOS}.
HELIX 16 18 {ECO:0000244|PDB:4XOS}.
STRAND 20 23 {ECO:0000244|PDB:4XOS}.
STRAND 46 48 {ECO:0000244|PDB:4XOS}.
STRAND 68 70 {ECO:0000244|PDB:4XOS}.
HELIX 81 86 {ECO:0000244|PDB:4XOS}.
STRAND 92 94 {ECO:0000244|PDB:4XOS}.
HELIX 103 106 {ECO:0000244|PDB:4XOS}.
HELIX 107 111 {ECO:0000244|PDB:4XOS}.
STRAND 117 119 {ECO:0000244|PDB:4XOS}.
HELIX 124 127 {ECO:0000244|PDB:4XOS}.
HELIX 131 138 {ECO:0000244|PDB:4XOS}.
SEQUENCE 249 AA; 28585 MW; CA2D1A756FBAEA04 CRC64;
MEMGRRIHLE LRNRTPSDVK ELVLDNSRSN EGKLEGLTDE FEELEFLSTI NVGLTSIANL
PKLNKLKKLE LSDNRVSGGL EVLAEKCPNL THLNLSGNKI KDLSTIEPLK KLENLKSLDL
FNCEVTNLND YRENVFKLLP QLTYLDGYDR DDKEAPDSDA EGYVEGLDDE EEDEDEEEYD
EDAQVVEDEE DEDEEEEGEE EDVSGEEEED EEGYNDGEVD DEEDEEELGE EERGQKRKRE
PEDEGEDDD


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18-661-15153 Putative HLA-DR-associated protein I - Potent heat-stable protein phosphatase 2A inhibitor I1PP2A; Acidic nuclear phosphoprotein pp32; Leucine-rich acidic nuclear protein; Lanp; Putative HLA-DR-associ 0.1 mg
18-661-15154 Putative HLA-DR-associated protein I - Potent heat-stable protein phosphatase 2A inhibitor I1PP2A; Acidic nuclear phosphoprotein pp32; Leucine-rich acidic nuclear protein; Lanp; Putative HLA-DR-associ 0.1 mg
18-661-15152 Putative HLA-DR-associated protein - Potent heat-stable protein phosphatase 2A inhibitor I1PP2A; Acidic nuclear phosphoprotein pp32; Leucine-rich acidic nuclear protein; Lanp; Putative HLA-DR-associat 0.1 mg
18-661-15150 Putative HLA-DR-associated protein I - Potent heat-stable protein phosphatase 2A inhibitor I1PP2A; Acidic nuclear phosphoprotein pp32; Leucine-rich acidic nuclear protein; Lanp; Putative HLA-DR-associ 0.1 mg
AN32C_MOUSE ELISA Kit FOR Putative acidic leucine-rich nuclear phosphoprotein 32 family member C; organism: Mouse; gene name: Anp32c 96T
CSB-EL001823RA Rat Acidic leucine-rich nuclear phosphoprotein 32 family member B(ANP32B) ELISA kit 96T
AN32D_HUMAN Human ELISA Kit FOR Acidic leucine-rich nuclear phosphoprotein 32 family member D 96T
CSB-EL001826RA Rat Acidic leucine-rich nuclear phosphoprotein 32 family member E(ANP32E) ELISA kit 96T
CSB-EL001822RA Rat Acidic leucine-rich nuclear phosphoprotein 32 family member A(ANP32A) ELISA kit 96T
ANP32F ANP32D Gene acidic (leucine-rich) nuclear phosphoprotein 32 family, member D
E1990h Human ELISA Kit FOR Acidic leucine-rich nuclear phosphoprotein 32 family member C 96T
E1092c Chicken ELISA Kit FOR Acidic leucine-rich nuclear phosphoprotein 32 family member E 96T
15-288-21207 Acidic (Leucine-rich) nuclear phosphoprotein 32 family. member E variant - Polyclonal 0.1 mg
ANPEP ANP32E Gene acidic (leucine-rich) nuclear phosphoprotein 32 family, member E
15-288-21207 Acidic (Leucine-rich) nuclear phosphoprotein 32 family. member E variant - Polyclonal 0.05 mg
E1075b Human ELISA Kit FOR Acidic leucine-rich nuclear phosphoprotein 32 family member E 96T
CSB-EL001822DO Dog Acidic leucine-rich nuclear phosphoprotein 32 family member A(ANP32A) ELISA kit 96T
ANP32E ANP32C Gene acidic (leucine-rich) nuclear phosphoprotein 32 family, member C
201-20-0333 ANP32B{acidic (leucine-rich) nuclear phosphoprotein 32 family, member B}rabbit.pAb 0.1ml
ANP32C ANP32A Gene acidic (leucine-rich) nuclear phosphoprotein 32 family, member A
201-20-0332 ANP32A{acidic (leucine-rich) nuclear phosphoprotein 32 family, member A}rabbit.pAb 0.1ml
E1483p Mouse ELISA Kit FOR Acidic leucine-rich nuclear phosphoprotein 32 family member B 96T
ANP32D ANP32B Gene acidic (leucine-rich) nuclear phosphoprotein 32 family, member B
CSB-EL001822RA Rat Acidic leucine-rich nuclear phosphoprotein 32 family member A(ANP32A) ELISA kit SpeciesRat 96T
CSB-EL001822DO Dog Acidic leucine-rich nuclear phosphoprotein 32 family member A(ANP32A) ELISA kit SpeciesDog 96T


 

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