Full text data of HNRNPAB
HNRNPAB
(ABBP1, HNRPAB)
[Confidence: low (only semi-automatic identification from reviews)]
Heterogeneous nuclear ribonucleoprotein A/B; hnRNP A/B (APOBEC1-binding protein 1; ABBP-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Heterogeneous nuclear ribonucleoprotein A/B; hnRNP A/B (APOBEC1-binding protein 1; ABBP-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q99729
ID ROAA_HUMAN Reviewed; 332 AA.
AC Q99729; B3KNN5; D3DWP7; Q04150; Q8N7U3; Q9BQ99;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-SEP-2007, sequence version 2.
DT 22-JAN-2014, entry version 128.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein A/B;
DE Short=hnRNP A/B;
DE AltName: Full=APOBEC1-binding protein 1;
DE Short=ABBP-1;
GN Name=HNRNPAB; Synonyms=ABBP1, HNRPAB;
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 4).
RX PubMed=1717314; DOI=10.1016/0014-5793(91)81249-8;
RA Khan F., Jaiswal A.K., Szer W.;
RT "Cloning and sequence analysis of a human type A/B hnRNP protein.";
RL FEBS Lett. 290:159-161(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=8999813; DOI=10.1074/jbc.272.3.1452;
RA Lau P.P., Zhu H.J., Nakamuta M., Chan L.;
RT "Cloning of an Apobec-1-binding protein that also interacts with
RT apolipoprotein B mRNA and evidence for its involvement in RNA
RT editing.";
RL J. Biol. Chem. 272:1452-1455(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Testis;
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 [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Placenta, Skin, and Uterus;
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 [6]
RP PROTEIN SEQUENCE OF 71-101; 111-118; 170-190; 196-203 AND 233-248,
RP METHYLATION AT ARG-245, AND MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-322, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=15782174; DOI=10.1038/nmeth715;
RA Ong S.E., Mittler G., Mann M.;
RT "Identifying and quantifying in vivo methylation sites by heavy methyl
RT SILAC.";
RL Nat. Methods 1:119-126(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-271 (ISOFORM 3), ACETYLATION
RP [LARGE SCALE ANALYSIS] AT LYS-272 (ISOFORM 4), 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-255 (ISOFORM 3), PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-256 (ISOFORM 4), AND MASS 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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-255 (ISOFORM 3), PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-256 (ISOFORM 4), AND MASS 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).
CC -!- FUNCTION: Binds single-stranded RNA. Has a high affinity for G-
CC rich and U-rich regions of hnRNA. Also binds to APOB mRNA
CC transcripts around the RNA editing site.
CC -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. Interacts with APOBEC1.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Localized in
CC cytoplasmic mRNP granules containing untranslated mRNAs.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q99729-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99729-2; Sequence=VSP_007826, VSP_007828;
CC Name=3;
CC IsoId=Q99729-3; Sequence=VSP_007826, VSP_007828, VSP_007829;
CC Note=Contains a N6-acetyllysine at position 271. Contains a
CC phosphoserine at position 255;
CC Name=4;
CC IsoId=Q99729-4; Sequence=VSP_007826, VSP_007829;
CC Note=Ref.1 (AAA36575) sequence differs from that shown due to
CC several frameshifts. Contains a N6-acetyllysine at position 272.
CC Contains a phosphoserine at position 256;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Dimethylation at Arg-322 is probably asymmetric.
CC -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50956.1; Type=Frameshift; Positions=296, 307, 330;
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DR EMBL; M65028; AAA36575.1; ALT_FRAME; mRNA.
DR EMBL; U76713; AAC50956.1; ALT_FRAME; mRNA.
DR EMBL; AK054600; BAG51397.1; -; mRNA.
DR EMBL; AK097657; BAC05134.1; -; mRNA.
DR EMBL; CH471165; EAW53843.1; -; Genomic_DNA.
DR EMBL; CH471165; EAW53844.1; -; Genomic_DNA.
DR EMBL; CH471165; EAW53845.1; -; Genomic_DNA.
DR EMBL; BC001616; AAH01616.1; -; mRNA.
DR EMBL; BC002625; AAH02625.1; -; mRNA.
DR EMBL; BC004561; AAH04561.1; -; mRNA.
DR EMBL; BC009359; AAH09359.1; -; mRNA.
DR EMBL; BC036708; AAH36708.1; -; mRNA.
DR PIR; S17563; S17563.
DR RefSeq; NP_004490.2; NM_004499.3.
DR RefSeq; NP_112556.2; NM_031266.2.
DR UniGene; Hs.591731; -.
DR UniGene; Hs.715055; -.
DR PDB; 3S7R; X-ray; 2.15 A; A/B=59-144.
DR PDBsum; 3S7R; -.
DR ProteinModelPortal; Q99729; -.
DR SMR; Q99729; 24-232.
DR IntAct; Q99729; 32.
DR MINT; MINT-4537784; -.
DR STRING; 9606.ENSP00000351108; -.
DR PhosphoSite; Q99729; -.
DR DMDM; 158523286; -.
DR SWISS-2DPAGE; Q99729; -.
DR PaxDb; Q99729; -.
DR PRIDE; Q99729; -.
DR Ensembl; ENST00000355836; ENSP00000348093; ENSG00000197451.
DR Ensembl; ENST00000358344; ENSP00000351108; ENSG00000197451.
DR Ensembl; ENST00000504898; ENSP00000425031; ENSG00000197451.
DR Ensembl; ENST00000506259; ENSP00000427465; ENSG00000197451.
DR GeneID; 3182; -.
DR KEGG; hsa:3182; -.
DR CTD; 3182; -.
DR GeneCards; GC05P177631; -.
DR HGNC; HGNC:5034; HNRNPAB.
DR HPA; HPA046688; -.
DR MIM; 602688; gene.
DR neXtProt; NX_Q99729; -.
DR PharmGKB; PA162391196; -.
DR eggNOG; COG0724; -.
DR HOGENOM; HOG000234441; -.
DR HOVERGEN; HBG002295; -.
DR InParanoid; Q99729; -.
DR KO; K13044; -.
DR OMA; FIFITYK; -.
DR OrthoDB; EOG715Q6V; -.
DR ChiTaRS; HNRNPAB; human.
DR EvolutionaryTrace; Q99729; -.
DR GeneWiki; HNRPAB; -.
DR GenomeRNAi; 3182; -.
DR NextBio; 12628; -.
DR PRO; PR:Q99729; -.
DR ArrayExpress; Q99729; -.
DR Bgee; Q99729; -.
DR CleanEx; HS_HNRNPAB; -.
DR Genevestigator; Q99729; -.
DR GO; GO:0005737; C:cytoplasm; ISS:HGNC.
DR GO; GO:0005634; C:nucleus; ISS:HGNC.
DR GO; GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; TAS:ProtInc.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:HGNC.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; ISS:HGNC.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012956; CARG-binding_factor_N.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF08143; CBFNT; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1 332 Heterogeneous nuclear ribonucleoprotein
FT A/B.
FT /FTId=PRO_0000081492.
FT DOMAIN 69 154 RRM 1.
FT DOMAIN 153 233 RRM 2.
FT COMPBIAS 241 324 Gly-rich.
FT MOD_RES 242 242 Phosphoserine.
FT MOD_RES 245 245 Dimethylated arginine; alternate.
FT MOD_RES 245 245 Omega-N-methylarginine; alternate.
FT MOD_RES 322 322 Dimethylated arginine.
FT VAR_SEQ 26 32 ASRGRGW -> GESPAGAG (in isoform 2,
FT isoform 3 and isoform 4).
FT /FTId=VSP_007826.
FT VAR_SEQ 164 165 SP -> A (in isoform 2 and isoform 3).
FT /FTId=VSP_007828.
FT VAR_SEQ 264 310 Missing (in isoform 3 and isoform 4).
FT /FTId=VSP_007829.
FT STRAND 70 74
FT HELIX 82 89
FT TURN 90 92
FT STRAND 95 102
FT TURN 104 106
FT STRAND 109 119
FT HELIX 121 128
FT STRAND 132 134
FT STRAND 137 143
SQ SEQUENCE 332 AA; 36225 MW; F824A7E08D15268A CRC64;
MSEAGEEQPM ETTGATENGH EAVPEASRGR GWTGAAAGAG GATAAPPSGN QNGAEGDQIN
ASKNEEDAGK MFVGGLSWDT SKKDLKDYFT KFGEVVDCTI KMDPNTGRSR GFGFILFKDA
ASVEKVLDQK EHRLDGRVID PKKAMAMKKD PVKKIFVGGL NPESPTEEKI REYFGEFGEI
EAIELPMDPK LNKRRGFVFI TFKEEEPVKK VLEKKFHTVS GSKCEIKVAQ PKEVYQQQQY
GSGGRGNRNR GNRGSGGGGG GGGQSQSWNQ GYGNYWNQGY GYQQGYGPGY GGYDYSPYGY
YGYGPGYDYS QGSTNYGKSQ RRGGHQNNYK PY
//
ID ROAA_HUMAN Reviewed; 332 AA.
AC Q99729; B3KNN5; D3DWP7; Q04150; Q8N7U3; Q9BQ99;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-SEP-2007, sequence version 2.
DT 22-JAN-2014, entry version 128.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein A/B;
DE Short=hnRNP A/B;
DE AltName: Full=APOBEC1-binding protein 1;
DE Short=ABBP-1;
GN Name=HNRNPAB; Synonyms=ABBP1, HNRPAB;
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 4).
RX PubMed=1717314; DOI=10.1016/0014-5793(91)81249-8;
RA Khan F., Jaiswal A.K., Szer W.;
RT "Cloning and sequence analysis of a human type A/B hnRNP protein.";
RL FEBS Lett. 290:159-161(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=8999813; DOI=10.1074/jbc.272.3.1452;
RA Lau P.P., Zhu H.J., Nakamuta M., Chan L.;
RT "Cloning of an Apobec-1-binding protein that also interacts with
RT apolipoprotein B mRNA and evidence for its involvement in RNA
RT editing.";
RL J. Biol. Chem. 272:1452-1455(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Testis;
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 [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Placenta, Skin, and Uterus;
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 [6]
RP PROTEIN SEQUENCE OF 71-101; 111-118; 170-190; 196-203 AND 233-248,
RP METHYLATION AT ARG-245, AND MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-322, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=15782174; DOI=10.1038/nmeth715;
RA Ong S.E., Mittler G., Mann M.;
RT "Identifying and quantifying in vivo methylation sites by heavy methyl
RT SILAC.";
RL Nat. Methods 1:119-126(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-271 (ISOFORM 3), ACETYLATION
RP [LARGE SCALE ANALYSIS] AT LYS-272 (ISOFORM 4), 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-255 (ISOFORM 3), PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-256 (ISOFORM 4), AND MASS 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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-255 (ISOFORM 3), PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-256 (ISOFORM 4), AND MASS 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).
CC -!- FUNCTION: Binds single-stranded RNA. Has a high affinity for G-
CC rich and U-rich regions of hnRNA. Also binds to APOB mRNA
CC transcripts around the RNA editing site.
CC -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. Interacts with APOBEC1.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Localized in
CC cytoplasmic mRNP granules containing untranslated mRNAs.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q99729-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99729-2; Sequence=VSP_007826, VSP_007828;
CC Name=3;
CC IsoId=Q99729-3; Sequence=VSP_007826, VSP_007828, VSP_007829;
CC Note=Contains a N6-acetyllysine at position 271. Contains a
CC phosphoserine at position 255;
CC Name=4;
CC IsoId=Q99729-4; Sequence=VSP_007826, VSP_007829;
CC Note=Ref.1 (AAA36575) sequence differs from that shown due to
CC several frameshifts. Contains a N6-acetyllysine at position 272.
CC Contains a phosphoserine at position 256;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Dimethylation at Arg-322 is probably asymmetric.
CC -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50956.1; Type=Frameshift; Positions=296, 307, 330;
CC -----------------------------------------------------------------------
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DR EMBL; M65028; AAA36575.1; ALT_FRAME; mRNA.
DR EMBL; U76713; AAC50956.1; ALT_FRAME; mRNA.
DR EMBL; AK054600; BAG51397.1; -; mRNA.
DR EMBL; AK097657; BAC05134.1; -; mRNA.
DR EMBL; CH471165; EAW53843.1; -; Genomic_DNA.
DR EMBL; CH471165; EAW53844.1; -; Genomic_DNA.
DR EMBL; CH471165; EAW53845.1; -; Genomic_DNA.
DR EMBL; BC001616; AAH01616.1; -; mRNA.
DR EMBL; BC002625; AAH02625.1; -; mRNA.
DR EMBL; BC004561; AAH04561.1; -; mRNA.
DR EMBL; BC009359; AAH09359.1; -; mRNA.
DR EMBL; BC036708; AAH36708.1; -; mRNA.
DR PIR; S17563; S17563.
DR RefSeq; NP_004490.2; NM_004499.3.
DR RefSeq; NP_112556.2; NM_031266.2.
DR UniGene; Hs.591731; -.
DR UniGene; Hs.715055; -.
DR PDB; 3S7R; X-ray; 2.15 A; A/B=59-144.
DR PDBsum; 3S7R; -.
DR ProteinModelPortal; Q99729; -.
DR SMR; Q99729; 24-232.
DR IntAct; Q99729; 32.
DR MINT; MINT-4537784; -.
DR STRING; 9606.ENSP00000351108; -.
DR PhosphoSite; Q99729; -.
DR DMDM; 158523286; -.
DR SWISS-2DPAGE; Q99729; -.
DR PaxDb; Q99729; -.
DR PRIDE; Q99729; -.
DR Ensembl; ENST00000355836; ENSP00000348093; ENSG00000197451.
DR Ensembl; ENST00000358344; ENSP00000351108; ENSG00000197451.
DR Ensembl; ENST00000504898; ENSP00000425031; ENSG00000197451.
DR Ensembl; ENST00000506259; ENSP00000427465; ENSG00000197451.
DR GeneID; 3182; -.
DR KEGG; hsa:3182; -.
DR CTD; 3182; -.
DR GeneCards; GC05P177631; -.
DR HGNC; HGNC:5034; HNRNPAB.
DR HPA; HPA046688; -.
DR MIM; 602688; gene.
DR neXtProt; NX_Q99729; -.
DR PharmGKB; PA162391196; -.
DR eggNOG; COG0724; -.
DR HOGENOM; HOG000234441; -.
DR HOVERGEN; HBG002295; -.
DR InParanoid; Q99729; -.
DR KO; K13044; -.
DR OMA; FIFITYK; -.
DR OrthoDB; EOG715Q6V; -.
DR ChiTaRS; HNRNPAB; human.
DR EvolutionaryTrace; Q99729; -.
DR GeneWiki; HNRPAB; -.
DR GenomeRNAi; 3182; -.
DR NextBio; 12628; -.
DR PRO; PR:Q99729; -.
DR ArrayExpress; Q99729; -.
DR Bgee; Q99729; -.
DR CleanEx; HS_HNRNPAB; -.
DR Genevestigator; Q99729; -.
DR GO; GO:0005737; C:cytoplasm; ISS:HGNC.
DR GO; GO:0005634; C:nucleus; ISS:HGNC.
DR GO; GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; TAS:ProtInc.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:HGNC.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; ISS:HGNC.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012956; CARG-binding_factor_N.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF08143; CBFNT; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1 332 Heterogeneous nuclear ribonucleoprotein
FT A/B.
FT /FTId=PRO_0000081492.
FT DOMAIN 69 154 RRM 1.
FT DOMAIN 153 233 RRM 2.
FT COMPBIAS 241 324 Gly-rich.
FT MOD_RES 242 242 Phosphoserine.
FT MOD_RES 245 245 Dimethylated arginine; alternate.
FT MOD_RES 245 245 Omega-N-methylarginine; alternate.
FT MOD_RES 322 322 Dimethylated arginine.
FT VAR_SEQ 26 32 ASRGRGW -> GESPAGAG (in isoform 2,
FT isoform 3 and isoform 4).
FT /FTId=VSP_007826.
FT VAR_SEQ 164 165 SP -> A (in isoform 2 and isoform 3).
FT /FTId=VSP_007828.
FT VAR_SEQ 264 310 Missing (in isoform 3 and isoform 4).
FT /FTId=VSP_007829.
FT STRAND 70 74
FT HELIX 82 89
FT TURN 90 92
FT STRAND 95 102
FT TURN 104 106
FT STRAND 109 119
FT HELIX 121 128
FT STRAND 132 134
FT STRAND 137 143
SQ SEQUENCE 332 AA; 36225 MW; F824A7E08D15268A CRC64;
MSEAGEEQPM ETTGATENGH EAVPEASRGR GWTGAAAGAG GATAAPPSGN QNGAEGDQIN
ASKNEEDAGK MFVGGLSWDT SKKDLKDYFT KFGEVVDCTI KMDPNTGRSR GFGFILFKDA
ASVEKVLDQK EHRLDGRVID PKKAMAMKKD PVKKIFVGGL NPESPTEEKI REYFGEFGEI
EAIELPMDPK LNKRRGFVFI TFKEEEPVKK VLEKKFHTVS GSKCEIKVAQ PKEVYQQQQY
GSGGRGNRNR GNRGSGGGGG GGGQSQSWNQ GYGNYWNQGY GYQQGYGPGY GGYDYSPYGY
YGYGPGYDYS QGSTNYGKSQ RRGGHQNNYK PY
//
MIM
602688
*RECORD*
*FIELD* NO
602688
*FIELD* TI
*602688 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A/B; HNRNPAB
;;APOLIPOPROTEIN B mRNA-EDITING ENZYME, CATALYTIC POLYPEPTIDE 1-BINDING
read morePROTEIN 1;;
APOBEC1-BINDING PROTEIN 1; ABBP1;;
HNRPAB
*FIELD* TX
CLONING
Apolipoprotein B (APOB; 107730) mRNA editing is an intranuclear function
and is mediated by a multiprotein editosome complex (see APOBEC1;
600130). Using the yeast 2-hybrid system, Lau et al. (1997) identified
an APOBEC1-binding protein (ABBP1) that interacts with APOB mRNA. The
ABBP1 cDNA encodes a 331-amino acid protein that is identical to the
human type A/B heterogeneous nuclear ribonucleoprotein (hnRNP) reported
by Khan et al. (1991), except for a 47-residue insertion in its
C-terminal region. Khan et al. (1991) identified the type A/B hnRNP as
an RNA-binding protein of unknown function in HeLa cells. Northern blot
analysis indicated that ABBP1 mRNA is distributed in multiple human
tissues as an approximately 2-kb transcript. The 47-amino acid insertion
of ABBP1 is encoded by an alternatively spliced exon.
GENE FUNCTION
Lau et al. (1997) found that ABBP1 contains typical RNP-type RNA-binding
motifs in its N-terminal half and glycine-rich motifs, which house the
APOBEC1-binding region, in its C-terminal region. ABBP1 binds to APOB
mRNA transcripts around the editing site and can be UV-crosslinked to
them. Editing is inhibited by ABBP1 immunodepletion or antisense ABBP1
cDNA transfection.
*FIELD* RF
1. Khan, F. A.; Jaiswal, A. K.; Szer, W.: Cloning and sequence analysis
of a human type A/B hnRNP protein. FEBS Lett. 290: 159-161, 1991.
2. Lau, P. P.; Zhu, H.-J.; Nakamuta, M.; Chan, L.: Cloning of an
apobec-1-binding protein that also interacts with apolipoprotein B
mRNA and evidence for its involvement in RNA editing. J. Biol. Chem. 272:
1452-1455, 1997.
*FIELD* CD
Ethylin Wang Jabs: 6/4/1998
*FIELD* ED
carol: 06/11/2012
wwang: 8/27/2008
mgross: 5/5/2003
alopez: 2/12/2001
psherman: 6/5/1998
psherman: 6/4/1998
*RECORD*
*FIELD* NO
602688
*FIELD* TI
*602688 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A/B; HNRNPAB
;;APOLIPOPROTEIN B mRNA-EDITING ENZYME, CATALYTIC POLYPEPTIDE 1-BINDING
read morePROTEIN 1;;
APOBEC1-BINDING PROTEIN 1; ABBP1;;
HNRPAB
*FIELD* TX
CLONING
Apolipoprotein B (APOB; 107730) mRNA editing is an intranuclear function
and is mediated by a multiprotein editosome complex (see APOBEC1;
600130). Using the yeast 2-hybrid system, Lau et al. (1997) identified
an APOBEC1-binding protein (ABBP1) that interacts with APOB mRNA. The
ABBP1 cDNA encodes a 331-amino acid protein that is identical to the
human type A/B heterogeneous nuclear ribonucleoprotein (hnRNP) reported
by Khan et al. (1991), except for a 47-residue insertion in its
C-terminal region. Khan et al. (1991) identified the type A/B hnRNP as
an RNA-binding protein of unknown function in HeLa cells. Northern blot
analysis indicated that ABBP1 mRNA is distributed in multiple human
tissues as an approximately 2-kb transcript. The 47-amino acid insertion
of ABBP1 is encoded by an alternatively spliced exon.
GENE FUNCTION
Lau et al. (1997) found that ABBP1 contains typical RNP-type RNA-binding
motifs in its N-terminal half and glycine-rich motifs, which house the
APOBEC1-binding region, in its C-terminal region. ABBP1 binds to APOB
mRNA transcripts around the editing site and can be UV-crosslinked to
them. Editing is inhibited by ABBP1 immunodepletion or antisense ABBP1
cDNA transfection.
*FIELD* RF
1. Khan, F. A.; Jaiswal, A. K.; Szer, W.: Cloning and sequence analysis
of a human type A/B hnRNP protein. FEBS Lett. 290: 159-161, 1991.
2. Lau, P. P.; Zhu, H.-J.; Nakamuta, M.; Chan, L.: Cloning of an
apobec-1-binding protein that also interacts with apolipoprotein B
mRNA and evidence for its involvement in RNA editing. J. Biol. Chem. 272:
1452-1455, 1997.
*FIELD* CD
Ethylin Wang Jabs: 6/4/1998
*FIELD* ED
carol: 06/11/2012
wwang: 8/27/2008
mgross: 5/5/2003
alopez: 2/12/2001
psherman: 6/5/1998
psherman: 6/4/1998