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UniProtKB/Swiss-Prot entry Q14103


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HNRPD_HUMAN
Primary accession number Q14103
Secondary accession numbers A8K9J2 P07029 Q01858 Q14100 Q14101 Q14102 Q4W5A1 Q9UCE8 Q9UCE9
Integrated into Swiss-Prot on February 21, 2001
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 107)
Name and origin of the protein
Protein name Heterogeneous nuclear ribonucleoprotein D0
Synonyms hnRNP D0
AU-rich element RNA-binding protein 1
Gene name
Name: HNRNPD
Synonyms: AUF1, HNRPD
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), AND NUCLEOTIDE SEQUENCE [MRNA] OF 70-355 (ISOFORM 2).
TISSUE=Cervix carcinoma;
DOI=10.1074/jbc.270.38.22167; PubMed=7673195 [NCBI, ExPASy, EBI, Israel, Japan]
Kajita Y., Nakayama J., Aizawa M., Ishikawa F.;
"The UUAG-specific RNA binding protein, heterogeneous nuclear ribonucleoprotein D0. Common modular structure and binding properties of the 2xRBD-Gly family.";
J. Biol. Chem. 270:22167-22175(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
DOI=10.1006/geno.1998.5237; PubMed=9615222 [NCBI, ExPASy, EBI, Israel, Japan]
Dempsey L.A., Li M.-J., DePace A., Bray-Ward P., Maizels N.;
"The human HNRPD locus maps to 4q21 and encodes a highly conserved protein.";
Genomics 49:378-384(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Thymus;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03466; PubMed=15815621 [NCBI, ExPASy, EBI, Israel, Japan]
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and 4.";
Nature 434:724-731(2005).
[5]
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 6-235.
DOI=10.1093/nar/14.10.4077; PubMed=3754960 [NCBI, ExPASy, EBI, Israel, Japan]
Lahiri D.K., Thomas J.O.;
"A cDNA clone of the hnRNP C proteins and its homology with the single-stranded DNA binding protein UP2.";
Nucleic Acids Res. 14:4077-4094(1986).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 9-355 (ISOFORM 3), AND CHARACTERIZATION.
TISSUE=Blood;
DOI=10.1042/0264-6021:3380417; PubMed=10024518 [NCBI, ExPASy, EBI, Israel, Japan]
Tolnay M., Vereshchagina L.A., Tsokos G.C.;
"Heterogeneous nuclear ribonucleoprotein D0B is a sequence-specific DNA-binding protein.";
Biochem. J. 338:417-425(1999).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 23-355 (ISOFORM 3).
PubMed=1433497 [NCBI, ExPASy, EBI, Israel, Japan]
Tay N., Chan S.-H., Ren E.-C.;
"Identification and cloning of a novel heterogeneous nuclear ribonucleoprotein C-like protein that functions as a transcriptional activator of the hepatitis B virus enhancer II.";
J. Virol. 66:6841-6848(1992).
[10]
PROTEIN SEQUENCE OF 139-157; 184-203 AND 224-237, AND NUCLEOTIDE-BINDING.
TISSUE=Cervix carcinoma;
PubMed=8321232 [NCBI, ExPASy, EBI, Israel, Japan]
Ishikawa F., Matunis M.J., Dreyfuss G., Cech T.R.;
"Nuclear proteins that bind the pre-mRNA 3' splice site sequence r(UUAG/G) and the human telomeric DNA sequence d(TTAGGG)n.";
Mol. Cell. Biol. 13:4301-4310(1993).
[11]
ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3 AND 4).
DOI=10.1006/geno.1997.5142; PubMed=9521873 [NCBI, ExPASy, EBI, Israel, Japan]
Wagner B.J., DeMaria C.T., Sun Y., Wilson G.M., Brewer G.;
"Structure and genomic organization of the human AUF1 gene: alternative pre-mRNA splicing generates four protein isoforms.";
Genomics 48:195-202(1998).
[12]
FUNCTION IN TRANSLATIONALLY COUPLED MRNA TURNOVER, AND IDENTIFICATION IN A COMPLEX WITH SYNCRIP; PABPC1; PAIP1 AND CSDE1.
TISSUE=Placenta;
DOI=10.1016/S0092-8674(00)00102-1; PubMed=11051545 [NCBI, ExPASy, EBI, Israel, Japan]
Grosset C., Chen C.-Y.A., Xu N., Sonenberg N., Jacquemin-Sablon H., Shyu A.-B.;
"A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex.";
Cell 103:29-40(2000).
[13]
INTERACTION WITH IGF2BP2.
DOI=10.1515/BC.2003.004; PubMed=12674497 [NCBI, ExPASy, EBI, Israel, Japan]
Moraes K.C., Quaresma A.J., Maehnss K., Kobarg J.;
"Identification and characterization of proteins that selectively interact with isoforms of the mRNA binding protein AUF1 (hnRNP D).";
Biol. Chem. 384:25-37(2003).
[14]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-345, AND MASS SPECTROMETRY.
DOI=10.1038/nmeth715; PubMed=15782174 [NCBI, ExPASy, EBI, Israel, Japan]
Ong S.E., Mittler G., Mann M.;
"Identifying and quantifying in vivo methylation sites by heavy methyl SILAC.";
Nat. Methods 1:119-126(2004).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190 AND THR-193, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND MASS SPECTROMETRY.
TISSUE=T-cell;
DOI=10.1038/nmeth776; PubMed=16094384 [NCBI, ExPASy, EBI, Israel, Japan]
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry.";
Nat. Methods 2:591-598(2005).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-82; SER-83; SER-87 AND THR-91, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND THR-193, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-83; SER-190 AND THR-193, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1002/pmic.200700884; PubMed=18318008 [NCBI, ExPASy, EBI, Israel, Japan]
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.";
Proteomics 8:1346-1361(2008).
[22]
STRUCTURE BY NMR OF 98-172, AND FUNCTION.
DOI=10.1006/jmbi.1999.2616; PubMed=10080887 [NCBI, ExPASy, EBI, Israel, Japan]
Nagata T., Kurihara Y., Matsuda G., Saeki J., Kohno T., Yanagida Y., Ishikawa F., Uesugi S., Katahira M.;
"Structure and interactions with RNA of the N-terminal UUAG-specific RNA-binding domain of hnRNP D0.";
J. Mol. Biol. 287:221-237(1999).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D55671; BAA09522.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D55672; BAA09523.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D55673; BAA09524.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D55674; BAA09525.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF026126; AAC23474.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF026126; AAC23475.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF026126; AAC23476.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK292707; BAF85396.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC124016; AAY40913.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471057; EAX05874.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002401; AAH02401.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC023977; AAH23977.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC026015; AAH26015.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X03910; CAA27544.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF039575; AAB96683.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M94630; AAA35781.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A24016; A24016.
A44192; A44192.
B48138; B48138.
RefSeq NP_001003810.1; -.
NP_002129.2; -.
NP_112737.1; -.
NP_112738.1; -.
UniGene Hs.480073
3D structure databases
PDB
1HD0; NMR; -; A=98-172.[ExPASy / RCSB / EBI]
1HD1; NMR; -; A=98-172.[ExPASy / RCSB / EBI]
1IQT; NMR; -; A=183-257.[ExPASy / RCSB / EBI]
1WTB; NMR; -; A=181-259.[ExPASy / RCSB / EBI]
1X0F; NMR; -; A=181-259.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1HD0; -.
1HD1; -.
1IQT; -.
1WTB; -.
1X0F; -.
ModBase Q14103.
Protein-protein interaction databases
IntAct Q14103; 4.
PTM databases
PhosphoSite Q14103; -.
Enzyme and pathway databases
Reactome REACT_1675; mRNA Processing.
REACT_6167; Influenza Infection.
REACT_71; Gene Expression.
2D gel databases
SWISS-2DPAGE Q14103; -.
Organism-specific databases
GeneCards GC04M083494; -.
H-InvDB HIX0004333; -.
HGNC HGNC:5036; HNRNPD.
GenAtlas HNRNPD.
HPA HPA004911; -.
MIM 601324; gene. [NCBI / EBI]
PharmGKB PA29361; -.
GeneCards Q14103.
Gene expression databases
ArrayExpress Q14103; -.
CleanEx HS_HNRNPD; -.
GermOnline ENSG00000138668; Homo sapiens.
Ontologies
GO
GO:0005694; Cellular component: chromosome (inferred from electronic annotation from UniProtKB-KW).
GO:0030530; Cellular component: heterogeneous nuclear ribonucleoprotein complex (non-traceable author statement from UniProtKB).
GO:0000166; Molecular function: nucleotide binding (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0003723; Molecular function: RNA binding (inferred from direct assay from UniProtKB).
GO:0042162; Molecular function: telomeric DNA binding (inferred from direct assay from UniProtKB).
GO:0016563; Molecular function: transcription activator activity (non-traceable author statement from UniProtKB).
GO:0000398; Biological process: nuclear mRNA splicing, via spliceosome (inferred from experiment from Reactome).
GO:0006355; Biological process: regulation of transcription, DNA-dependent (non-traceable author statement from UniProtKB).
GO:0006401; Biological process: RNA catabolic process (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR012677; a_b_plait_nuc_bd.
IPR000504; RRM_RNP1.
Graphical view of domain structure.
Gene3D G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
Pfam PF00076; RRM_1; 2.
Pfam graphical view of domain structure.
SMART SM00360; RRM; 2.
SMART graphical view of domain structure.
PROSITE PS50102; RRM; 2.
PROSITE graphical view of domain structure (profiles).
Proteomics databases
PRIDE Q14103; -.
Genome annotation databases
Ensembl ENSG00000138668; Homo sapiens. [Contig view]
GeneID 3184; -.
KEGG hsa:3184; -.
Phylogenomic databases
HOVERGEN Q14103; -.
Other
LinkHub Q14103; -.
NextBio 12644; -.
SOURCE HNRNPD; Homo sapiens.
ProtoNet Q14103.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Chromosomal protein; Direct protein sequencing; DNA-binding; Methylation; Nucleus; Phosphoprotein; Repeat; Ribonucleoprotein; RNA-binding; Transcription; Transcription regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   355  355     Heterogeneous nuclear ribonucleoprotein D0. PRO_0000081849
DOMAIN   97   179  83     RRM 1. 
DOMAIN   182   261  80     RRM 2. 
COMPBIAS   11    45  35     Ala-rich. 
COMPBIAS   270   347  78     Gly-rich. 
COMPBIAS   294   332  39     Tyr-rich. 
MOD_RES   80    80        Phosphoserine. 
MOD_RES   82    82        Phosphoserine. 
MOD_RES   83    83        Phosphoserine. 
MOD_RES   87    87        Phosphoserine. 
MOD_RES   91    91        Phosphothreonine. 
MOD_RES   190   190        Phosphoserine. 
MOD_RES   193   193        Phosphothreonine. 
MOD_RES   345   345        Omega-N-methylated arginine. 
VAR_SEQ   79    97        Missing (in isoform 2 and isoform 4). VSP_005834
VAR_SEQ   285   334        GPSQNWNQGYSNYWNQGYGNYGYNSQGYGGYGGYDYTGYN NYYGYGDYSN -> D (in isoform 3 and isoform 4). VSP_005835
CONFLICT   150   150