Full text data of ANP32B
ANP32B
(APRIL, PHAPI2)
[Confidence: low (only semi-automatic identification from reviews)]
Acidic leucine-rich nuclear phosphoprotein 32 family member B (Acidic protein rich in leucines; Putative HLA-DR-associated protein I-2; PHAPI2; Silver-stainable protein SSP29)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Acidic leucine-rich nuclear phosphoprotein 32 family member B (Acidic protein rich in leucines; Putative HLA-DR-associated protein I-2; PHAPI2; Silver-stainable protein SSP29)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q92688
ID AN32B_HUMAN Reviewed; 251 AA.
AC Q92688; B2R9C7; O00655; P78458; P78459;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1997, sequence version 1.
DT 22-JAN-2014, entry version 125.
DE RecName: Full=Acidic leucine-rich nuclear phosphoprotein 32 family member B;
DE AltName: Full=Acidic protein rich in leucines;
DE AltName: Full=Putative HLA-DR-associated protein I-2;
DE Short=PHAPI2;
DE AltName: Full=Silver-stainable protein SSP29;
GN Name=ANP32B; Synonyms=APRIL, PHAPI2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Vaesen M., Barnikol-Watanabe S., Kratzin H.D., Hilschmann N.;
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zhu L., Henning D., Valdez B.C.;
RT "Molecular cloning and partial characterization of a new silver-
RT stainable protein.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC TISSUE=Pancreas;
RX PubMed=9473664; DOI=10.1016/S0167-4781(97)00165-6;
RA Mencinger M., Panagopoulos I., Contreras J.A., Mitelman F., Aman P.;
RT "Expression analysis and chromosomal mapping of a novel human gene,
RT APRIL, encoding an acidic protein rich in leucines.";
RL Biochim. Biophys. Acta 1395:176-180(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15895553; DOI=10.1080/14734220410019020;
RA Matilla A., Radrizzani M.;
RT "The Anp32 family of proteins containing leucine-rich repeats.";
RL Cerebellum 4:7-18(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-86, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP STRUCTURE BY NMR OF 1-161, FUNCTION, SUBUNIT, INTERACTION WITH
RP HISTONES H3 AND H4, AND LEUCINE-RICH REPEATS.
RX PubMed=20538007; DOI=10.1016/j.jmb.2010.06.005;
RA Tochio N., Umehara T., Munemasa Y., Suzuki T., Sato S., Tsuda K.,
RA Koshiba S., Kigawa T., Nagai R., Yokoyama S.;
RT "Solution structure of histone chaperone ANP32B: interaction with core
RT histones H3-H4 through its acidic concave domain.";
RL J. Mol. Biol. 401:97-114(2010).
CC -!- FUNCTION: Multifunctional protein working as a cell cycle
CC progression factor as well as a cell survival factor. Required for
CC the progression from the G1 to the S phase. Anti-apoptotic protein
CC which functions as a caspase-3 inhibitor. Has no phosphatase 2A
CC (PP2A) inhibitor activity (By similarity). Exhibits histone
CC chaperone properties, stimulating core histones to assemble into a
CC nucleosome.
CC -!- SUBUNIT: Monomer. Interacts with histones H3 and H4.
CC -!- SUBCELLULAR LOCATION: Isoform 1: Nucleus. Note=Accumulates in the
CC nuclei at the S phase (By similarity).
CC -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Note=Lacks a nuclear
CC localization signal.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Anp32b1, PHAPI2b;
CC IsoId=Q92688-1; Sequence=Displayed;
CC Name=2; Synonyms=Anp32b2, PHAPI2b;
CC IsoId=Q92688-2; Sequence=VSP_019304;
CC Note=No canonical donor splice site;
CC -!- TISSUE SPECIFICITY: Expressed in heart, lung, pancreas, prostate
CC and in spleen, thymus and placenta.
CC -!- DOMAIN: Histone binding is mediated by the concave surface of the
CC LRR region.
CC -!- PTM: Some glutamate residues are glycylated by TTLL8. This
CC modification occurs exclusively on glutamate residues and results
CC in a glycine chain on the gamma-carboxyl group (By similarity).
CC -!- SIMILARITY: Belongs to the ANP32 family.
CC -!- SIMILARITY: Contains 4 LRR (leucine-rich) repeats.
CC -!- SIMILARITY: Contains 1 LRRCT domain.
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DR EMBL; Y07569; CAA68855.1; -; mRNA.
DR EMBL; U70439; AAB37579.1; -; mRNA.
DR EMBL; Y07969; CAA69265.1; -; mRNA.
DR EMBL; Y07570; CAA68856.1; -; mRNA.
DR EMBL; AK313733; BAG36474.1; -; mRNA.
DR EMBL; AL354726; CAI15260.1; -; Genomic_DNA.
DR EMBL; CH471105; EAW58865.1; -; Genomic_DNA.
DR EMBL; BC013003; AAH13003.1; -; mRNA.
DR EMBL; BC019658; AAH19658.1; -; mRNA.
DR RefSeq; NP_006392.1; NM_006401.2.
DR UniGene; Hs.730654; -.
DR PDB; 2ELL; NMR; -; A=1-161.
DR PDB; 2RR6; NMR; -; A=1-161.
DR PDBsum; 2ELL; -.
DR PDBsum; 2RR6; -.
DR ProteinModelPortal; Q92688; -.
DR SMR; Q92688; 1-161.
DR IntAct; Q92688; 13.
DR STRING; 9606.ENSP00000345848; -.
DR PhosphoSite; Q92688; -.
DR DMDM; 26390818; -.
DR PaxDb; Q92688; -.
DR PRIDE; Q92688; -.
DR Ensembl; ENST00000339399; ENSP00000345848; ENSG00000136938.
DR GeneID; 10541; -.
DR KEGG; hsa:10541; -.
DR UCSC; uc004aya.3; human.
DR CTD; 10541; -.
DR GeneCards; GC09P100745; -.
DR HGNC; HGNC:16677; ANP32B.
DR neXtProt; NX_Q92688; -.
DR PharmGKB; PA24812; -.
DR eggNOG; NOG322008; -.
DR HOGENOM; HOG000007361; -.
DR HOVERGEN; HBG053102; -.
DR InParanoid; Q92688; -.
DR OMA; DEVSGEX; -.
DR OrthoDB; EOG7TJ3KH; -.
DR ChiTaRS; ANP32B; human.
DR EvolutionaryTrace; Q92688; -.
DR GeneWiki; ANP32B; -.
DR GenomeRNAi; 10541; -.
DR NextBio; 39993; -.
DR PMAP-CutDB; Q92688; -.
DR PRO; PR:Q92688; -.
DR ArrayExpress; Q92688; -.
DR Bgee; Q92688; -.
DR CleanEx; HS_ANP32B; -.
DR Genevestigator; Q92688; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003603; U2A'_phosphoprotein32A_C.
DR SMART; SM00446; LRRcap; 1.
DR PROSITE; PS51450; LRR; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chaperone;
KW Complete proteome; Cytoplasm; Leucine-rich repeat; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1 251 Acidic leucine-rich nuclear
FT phosphoprotein 32 family member B.
FT /FTId=PRO_0000137595.
FT REPEAT 16 40 LRR 1.
FT REPEAT 43 64 LRR 2.
FT REPEAT 65 84 LRR 3.
FT REPEAT 89 110 LRR 4.
FT DOMAIN 123 161 LRRCT.
FT COMPBIAS 146 251 Asp/Glu-rich (highly acidic).
FT MOD_RES 86 86 N6-acetyllysine.
FT MOD_RES 244 244 Phosphothreonine.
FT VAR_SEQ 196 251 Missing (in isoform 2).
FT /FTId=VSP_019304.
FT CONFLICT 1 2 Missing (in Ref. 3; CAA69265).
FT HELIX 3 11
FT HELIX 16 18
FT STRAND 20 23
FT HELIX 39 43
FT STRAND 46 52
FT STRAND 68 73
FT HELIX 82 86
FT STRAND 92 94
FT STRAND 96 99
FT HELIX 104 109
FT STRAND 117 119
FT HELIX 124 126
FT HELIX 131 136
FT STRAND 157 159
SQ SEQUENCE 251 AA; 28788 MW; 93A1AADF8EDE7D53 CRC64;
MDMKRRIHLE LRNRTPAAVR ELVLDNCKSN DGKIEGLTAE FVNLEFLSLI NVGLISVSNL
PKLPKLKKLE LSENRIFGGL DMLAEKLPNL THLNLSGNKL KDISTLEPLK KLECLKSLDL
FNCEVTNLND YRESVFKLLP QLTYLDGYDR EDQEAPDSDA EVDGVDEEEE DEEGEDEEDE
DDEDGEEEEF DEEDDEDEDV EGDEDDDEVS EEEEEFGLDE EDEDEDEDEE EEEGGKGEKR
KRETDDEGED D
//
ID AN32B_HUMAN Reviewed; 251 AA.
AC Q92688; B2R9C7; O00655; P78458; P78459;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1997, sequence version 1.
DT 22-JAN-2014, entry version 125.
DE RecName: Full=Acidic leucine-rich nuclear phosphoprotein 32 family member B;
DE AltName: Full=Acidic protein rich in leucines;
DE AltName: Full=Putative HLA-DR-associated protein I-2;
DE Short=PHAPI2;
DE AltName: Full=Silver-stainable protein SSP29;
GN Name=ANP32B; Synonyms=APRIL, PHAPI2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Vaesen M., Barnikol-Watanabe S., Kratzin H.D., Hilschmann N.;
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zhu L., Henning D., Valdez B.C.;
RT "Molecular cloning and partial characterization of a new silver-
RT stainable protein.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC TISSUE=Pancreas;
RX PubMed=9473664; DOI=10.1016/S0167-4781(97)00165-6;
RA Mencinger M., Panagopoulos I., Contreras J.A., Mitelman F., Aman P.;
RT "Expression analysis and chromosomal mapping of a novel human gene,
RT APRIL, encoding an acidic protein rich in leucines.";
RL Biochim. Biophys. Acta 1395:176-180(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15895553; DOI=10.1080/14734220410019020;
RA Matilla A., Radrizzani M.;
RT "The Anp32 family of proteins containing leucine-rich repeats.";
RL Cerebellum 4:7-18(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-86, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP STRUCTURE BY NMR OF 1-161, FUNCTION, SUBUNIT, INTERACTION WITH
RP HISTONES H3 AND H4, AND LEUCINE-RICH REPEATS.
RX PubMed=20538007; DOI=10.1016/j.jmb.2010.06.005;
RA Tochio N., Umehara T., Munemasa Y., Suzuki T., Sato S., Tsuda K.,
RA Koshiba S., Kigawa T., Nagai R., Yokoyama S.;
RT "Solution structure of histone chaperone ANP32B: interaction with core
RT histones H3-H4 through its acidic concave domain.";
RL J. Mol. Biol. 401:97-114(2010).
CC -!- FUNCTION: Multifunctional protein working as a cell cycle
CC progression factor as well as a cell survival factor. Required for
CC the progression from the G1 to the S phase. Anti-apoptotic protein
CC which functions as a caspase-3 inhibitor. Has no phosphatase 2A
CC (PP2A) inhibitor activity (By similarity). Exhibits histone
CC chaperone properties, stimulating core histones to assemble into a
CC nucleosome.
CC -!- SUBUNIT: Monomer. Interacts with histones H3 and H4.
CC -!- SUBCELLULAR LOCATION: Isoform 1: Nucleus. Note=Accumulates in the
CC nuclei at the S phase (By similarity).
CC -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Note=Lacks a nuclear
CC localization signal.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Anp32b1, PHAPI2b;
CC IsoId=Q92688-1; Sequence=Displayed;
CC Name=2; Synonyms=Anp32b2, PHAPI2b;
CC IsoId=Q92688-2; Sequence=VSP_019304;
CC Note=No canonical donor splice site;
CC -!- TISSUE SPECIFICITY: Expressed in heart, lung, pancreas, prostate
CC and in spleen, thymus and placenta.
CC -!- DOMAIN: Histone binding is mediated by the concave surface of the
CC LRR region.
CC -!- PTM: Some glutamate residues are glycylated by TTLL8. This
CC modification occurs exclusively on glutamate residues and results
CC in a glycine chain on the gamma-carboxyl group (By similarity).
CC -!- SIMILARITY: Belongs to the ANP32 family.
CC -!- SIMILARITY: Contains 4 LRR (leucine-rich) repeats.
CC -!- SIMILARITY: Contains 1 LRRCT domain.
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DR EMBL; Y07569; CAA68855.1; -; mRNA.
DR EMBL; U70439; AAB37579.1; -; mRNA.
DR EMBL; Y07969; CAA69265.1; -; mRNA.
DR EMBL; Y07570; CAA68856.1; -; mRNA.
DR EMBL; AK313733; BAG36474.1; -; mRNA.
DR EMBL; AL354726; CAI15260.1; -; Genomic_DNA.
DR EMBL; CH471105; EAW58865.1; -; Genomic_DNA.
DR EMBL; BC013003; AAH13003.1; -; mRNA.
DR EMBL; BC019658; AAH19658.1; -; mRNA.
DR RefSeq; NP_006392.1; NM_006401.2.
DR UniGene; Hs.730654; -.
DR PDB; 2ELL; NMR; -; A=1-161.
DR PDB; 2RR6; NMR; -; A=1-161.
DR PDBsum; 2ELL; -.
DR PDBsum; 2RR6; -.
DR ProteinModelPortal; Q92688; -.
DR SMR; Q92688; 1-161.
DR IntAct; Q92688; 13.
DR STRING; 9606.ENSP00000345848; -.
DR PhosphoSite; Q92688; -.
DR DMDM; 26390818; -.
DR PaxDb; Q92688; -.
DR PRIDE; Q92688; -.
DR Ensembl; ENST00000339399; ENSP00000345848; ENSG00000136938.
DR GeneID; 10541; -.
DR KEGG; hsa:10541; -.
DR UCSC; uc004aya.3; human.
DR CTD; 10541; -.
DR GeneCards; GC09P100745; -.
DR HGNC; HGNC:16677; ANP32B.
DR neXtProt; NX_Q92688; -.
DR PharmGKB; PA24812; -.
DR eggNOG; NOG322008; -.
DR HOGENOM; HOG000007361; -.
DR HOVERGEN; HBG053102; -.
DR InParanoid; Q92688; -.
DR OMA; DEVSGEX; -.
DR OrthoDB; EOG7TJ3KH; -.
DR ChiTaRS; ANP32B; human.
DR EvolutionaryTrace; Q92688; -.
DR GeneWiki; ANP32B; -.
DR GenomeRNAi; 10541; -.
DR NextBio; 39993; -.
DR PMAP-CutDB; Q92688; -.
DR PRO; PR:Q92688; -.
DR ArrayExpress; Q92688; -.
DR Bgee; Q92688; -.
DR CleanEx; HS_ANP32B; -.
DR Genevestigator; Q92688; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003603; U2A'_phosphoprotein32A_C.
DR SMART; SM00446; LRRcap; 1.
DR PROSITE; PS51450; LRR; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chaperone;
KW Complete proteome; Cytoplasm; Leucine-rich repeat; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1 251 Acidic leucine-rich nuclear
FT phosphoprotein 32 family member B.
FT /FTId=PRO_0000137595.
FT REPEAT 16 40 LRR 1.
FT REPEAT 43 64 LRR 2.
FT REPEAT 65 84 LRR 3.
FT REPEAT 89 110 LRR 4.
FT DOMAIN 123 161 LRRCT.
FT COMPBIAS 146 251 Asp/Glu-rich (highly acidic).
FT MOD_RES 86 86 N6-acetyllysine.
FT MOD_RES 244 244 Phosphothreonine.
FT VAR_SEQ 196 251 Missing (in isoform 2).
FT /FTId=VSP_019304.
FT CONFLICT 1 2 Missing (in Ref. 3; CAA69265).
FT HELIX 3 11
FT HELIX 16 18
FT STRAND 20 23
FT HELIX 39 43
FT STRAND 46 52
FT STRAND 68 73
FT HELIX 82 86
FT STRAND 92 94
FT STRAND 96 99
FT HELIX 104 109
FT STRAND 117 119
FT HELIX 124 126
FT HELIX 131 136
FT STRAND 157 159
SQ SEQUENCE 251 AA; 28788 MW; 93A1AADF8EDE7D53 CRC64;
MDMKRRIHLE LRNRTPAAVR ELVLDNCKSN DGKIEGLTAE FVNLEFLSLI NVGLISVSNL
PKLPKLKKLE LSENRIFGGL DMLAEKLPNL THLNLSGNKL KDISTLEPLK KLECLKSLDL
FNCEVTNLND YRESVFKLLP QLTYLDGYDR EDQEAPDSDA EVDGVDEEEE DEEGEDEEDE
DDEDGEEEEF DEEDDEDEDV EGDEDDDEVS EEEEEFGLDE EDEDEDEDEE EEEGGKGEKR
KRETDDEGED D
//