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Q14103 (HNRPD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heterogeneous nuclear ribonucleoprotein D0
Short name=hnRNP D0
Alternative name(s):
AU-rich element RNA-binding protein 1
Gene names
Name:HNRNPD
Synonyms:AUF1, HNRPD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length355 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds with high affinity to RNA molecules that contain AU-rich elements (AREs) found within the 3'-UTR of many proto-oncogenes and cytokine mRNAs. Also binds to double- and single-stranded DNA sequences in a specific manner and functions a transcription factor. Each of the RNA-binding domains specifically can bind solely to a single-stranded non-monotonous 5'-UUAG-3' sequence and also weaker to the single-stranded 5'-TTAGGG-3' telomeric DNA repeat. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats. Binding of RRM1 to DNA inhibits the formation of DNA quadruplex structure which may play a role in telomere elongation. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Ref.13 Ref.29

Subunit structure

Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Part of a complex associated with the FOS mCRD domain and consisting of PABPC1, PAIP1, CSDE1/UNR and SYNCRIP. Interacts with IGF2BP2. Interacts with GTPBP1. Ref.13 Ref.14 Ref.17 Ref.27

Subcellular location

Nucleus. Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Component of ribonucleosomes. Ref.17

Post-translational modification

Arg-345 is dimethylated, probably to asymmetric dimethylarginine. Ref.10

Methylated by PRMT1, in an insulin-dependent manner. The PRMT1-mediated methylation regulates tyrosine phosphorylation By similarity. Ref.10

Sequence similarities

Contains 2 RRM (RNA recognition motif) domains.

Sequence caution

The sequence AAA35781.1 differs from that shown. Reason: Frameshift at positions 45, 59 and 355.

The sequence AAA35781.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.

The sequence CAA27544.1 differs from that shown. Reason: Several sequence conflicts.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14103-1)

Also known as: p45; Dx9;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q14103-2)

Also known as: p42; Dx4;

The sequence of this isoform differs from the canonical sequence as follows:
     79-97: Missing.
Isoform 3 (identifier: Q14103-3)

Also known as: p40; Dx7;

The sequence of this isoform differs from the canonical sequence as follows:
     285-334: GPSQNWNQGYSNYWNQGYGNYGYNSQGYGGYGGYDYTGYNNYYGYGDYSN → D
Note: Contains a N6-acetyllysine at position 292.
Isoform 4 (identifier: Q14103-4)

Also known as: p37;

The sequence of this isoform differs from the canonical sequence as follows:
     79-97: Missing.
     285-334: GPSQNWNQGYSNYWNQGYGNYGYNSQGYGGYGGYDYTGYNNYYGYGDYSN → D
Note: Contains a N6-acetyllysine at position 273.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 355355Heterogeneous nuclear ribonucleoprotein D0
PRO_0000081849

Regions

Domain97 – 17983RRM 1
Domain182 – 26180RRM 2
Compositional bias11 – 4535Ala-rich
Compositional bias270 – 34778Gly-rich
Compositional bias294 – 33239Tyr-rich

Amino acid modifications

Modified residue711Phosphoserine Ref.25
Modified residue801Phosphoserine Ref.25 Ref.28
Modified residue821Phosphoserine Ref.20 Ref.23
Modified residue831Phosphoserine Ref.20 Ref.25 Ref.28
Modified residue1191N6-methyllysine Ref.10
Modified residue1651N6-acetyllysine Ref.24
Modified residue1901Phosphoserine Ref.16 Ref.20 Ref.23 Ref.25 Ref.28
Modified residue1931Phosphothreonine Ref.19 Ref.20 Ref.23 Ref.25
Modified residue2511N6-acetyllysine Ref.24
Modified residue3451Dimethylated arginine Ref.15

Natural variations

Alternative sequence79 – 9719Missing in isoform 2 and isoform 4.
VSP_005834
Alternative sequence285 – 33450GPSQN…GDYSN → D in isoform 3 and isoform 4.
VSP_005835

Experimental info

Sequence conflict1501S → R AA sequence Ref.11
Sequence conflict2251F → L in AAA35781. Ref.9

Secondary structure

1 ................................... 355
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (p45) (Dx9) [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: D0B6EA177BEF789E

FASTA35538,434
        10         20         30         40         50         60 
MSEEQFGGDG AAAAATAAVG GSAGEQEGAM VAATQGAAAA AGSGAGTGGG TASGGTEGGS 

        70         80         90        100        110        120 
AESEGAKIDA SKNEEDEGHS NSSPRHSEAA TAQREEWKMF IGGLSWDTTK KDLKDYFSKF 

       130        140        150        160        170        180 
GEVVDCTLKL DPITGRSRGF GFVLFKESES VDKVMDQKEH KLNGKVIDPK RAKAMKTKEP 

       190        200        210        220        230        240 
VKKIFVGGLS PDTPEEKIRE YFGGFGEVES IELPMDNKTN KRRGFCFITF KEEEPVKKIM 

       250        260        270        280        290        300 
EKKYHNVGLS KCEIKVAMSK EQYQQQQQWG SRGGFAGRAR GRGGGPSQNW NQGYSNYWNQ 

       310        320        330        340        350 
GYGNYGYNSQ GYGGYGGYDY TGYNNYYGYG DYSNQQSGYG KVSRRGGHQN SYKPY

« Hide

Isoform 2 (p42) (Dx4) [UniParc].

Checksum: FEE18D61B7714B51
Show »

FASTA33636,272
Isoform 3 (p40) (Dx7) [UniParc].

Checksum: ABCDD6ACF812F647
Show »

FASTA30632,835
Isoform 4 (p37) [UniParc].

Checksum: 98DF6E78EAF3BBC1
Show »

FASTA28730,672

References

« Hide 'large scale' references
[1]"The UUAG-specific RNA binding protein, heterogeneous nuclear ribonucleoprotein D0. Common modular structure and binding properties of the 2xRBD-Gly family."
Kajita Y., Nakayama J., Aizawa M., Ishikawa F.
J. Biol. Chem. 270:22167-22175(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), NUCLEOTIDE SEQUENCE [MRNA] OF 70-355 (ISOFORM 2).
Tissue: Cervix carcinoma.
[2]"The human HNRPD locus maps to 4q21 and encodes a highly conserved protein."
Dempsey L.A., Li M.-J., DePace A., Bray-Ward P., Maizels N.
Genomics 49:378-384(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Thymus.
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
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. expand/collapse author list , 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.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Tissue: Lung.
[7]"A cDNA clone of the hnRNP C proteins and its homology with the single-stranded DNA binding protein UP2."
Lahiri D.K., Thomas J.O.
Nucleic Acids Res. 14:4077-4094(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-235.
[8]"Heterogeneous nuclear ribonucleoprotein D0B is a sequence-specific DNA-binding protein."
Tolnay M., Vereshchagina L.A., Tsokos G.C.
Biochem. J. 338:417-425(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-355 (ISOFORM 3), CHARACTERIZATION.
Tissue: Blood.
[9]"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."
Tay N., Chan S.-H., Ren E.-C.
J. Virol. 66:6841-6848(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 23-355 (ISOFORM 3).
[10]Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 68-85; 99-110; 112-129; 139-158; 184-218; 224-231 AND 261-272, METHYLATION AT LYS-119, MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[11]"Nuclear proteins that bind the pre-mRNA 3' splice site sequence r(UUAG/G) and the human telomeric DNA sequence d(TTAGGG)n."
Ishikawa F., Matunis M.J., Dreyfuss G., Cech T.R.
Mol. Cell. Biol. 13:4301-4310(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 139-157; 184-203 AND 224-237, NUCLEOTIDE-BINDING.
Tissue: Cervix carcinoma.
[12]"Structure and genomic organization of the human AUF1 gene: alternative pre-mRNA splicing generates four protein isoforms."
Wagner B.J., DeMaria C.T., Sun Y., Wilson G.M., Brewer G.
Genomics 48:195-202(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3 AND 4).
[13]"A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex."
Grosset C., Chen C.-Y.A., Xu N., Sonenberg N., Jacquemin-Sablon H., Shyu A.-B.
Cell 103:29-40(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRANSLATIONALLY COUPLED MRNA TURNOVER, IDENTIFICATION IN A COMPLEX WITH SYNCRIP; PABPC1; PAIP1 AND CSDE1.
Tissue: Placenta.
[14]"Identification and characterization of proteins that selectively interact with isoforms of the mRNA binding protein AUF1 (hnRNP D)."
Moraes K.C., Quaresma A.J., Maehnss K., Kobarg J.
Biol. Chem. 384:25-37(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IGF2BP2.
[15]"Identifying and quantifying in vivo methylation sites by heavy methyl SILAC."
Ong S.E., Mittler G., Mann M.
Nat. Methods 1:119-126(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-345, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[16]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[17]"Molecular composition of IMP1 ribonucleoprotein granules."
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C.
Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[18]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[19]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-193, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[20]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-83; SER-190 AND THR-193, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[21]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[22]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-190 AND THR-193, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[24]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-165 AND LYS-251, ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-292 (ISOFORM 3), ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-273 (ISOFORM 4), MASS SPECTROMETRY.
[25]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-80; SER-83; SER-190 AND THR-193, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[26]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"Modulation of exosome-mediated mRNA turnover by interaction of GTP-binding protein 1 (GTPBP1) with its target mRNAs."
Woo K.C., Kim T.D., Lee K.H., Kim D.Y., Kim S., Lee H.R., Kang H.J., Chung S.J., Senju S., Nishimura Y., Kim K.T.
FASEB J. 25:2757-2769(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GTPBP1.
[28]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-83 AND SER-190, MASS SPECTROMETRY.
[29]"Structure and interactions with RNA of the N-terminal UUAG-specific RNA-binding domain of hnRNP D0."
Nagata T., Kurihara Y., Matsuda G., Saeki J., Kohno T., Yanagida Y., Ishikawa F., Uesugi S., Katahira M.
J. Mol. Biol. 287:221-237(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 98-172, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D55671 mRNA. Translation: BAA09522.1.
D55672 mRNA. Translation: BAA09523.1.
D55673 mRNA. Translation: BAA09524.1.
D55674 mRNA. Translation: BAA09525.1.
AF026126 Genomic DNA. Translation: AAC23474.1.
AF026126 Genomic DNA. Translation: AAC23475.1.
AF026126 Genomic DNA. Translation: AAC23476.1.
AK292707 mRNA. Translation: BAF85396.1.
AC124016 Genomic DNA. Translation: AAY40913.1.
CH471057 Genomic DNA. Translation: EAX05874.1.
BC002401 mRNA. Translation: AAH02401.1.
BC023977 mRNA. Translation: AAH23977.1.
BC026015 mRNA. Translation: AAH26015.1.
X03910 mRNA. Translation: CAA27544.1. Sequence problems.
AF039575 mRNA. Translation: AAB96683.1.
M94630 mRNA. Translation: AAA35781.1. Sequence problems.
IPIIPI00028888.
IPI00220683.
IPI00220684.
IPI00220685.
PIRA24016.
A44192.
B48138.
RefSeqNP_001003810.1. NM_001003810.1.
NP_002129.2. NM_002138.3.
NP_112737.1. NM_031369.2.
NP_112738.1. NM_031370.2.
UniGeneHs.480073.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HD0NMR-A98-172[»]
1HD1NMR-A98-172[»]
1IQTNMR-A183-257[»]
1WTBNMR-A181-259[»]
1X0FNMR-A181-259[»]
2Z5NX-ray3.20B332-355[»]
ProteinModelPortalQ14103.
ModBaseSearch...

Protein-protein interaction databases

IntActQ14103. 35 interactions.
MINTMINT-5001251.

PTM databases

PhosphoSiteQ14103.

Polymorphism databases

DMDM13124489.

2D gel databases

SWISS-2DPAGEQ14103.

Proteomic databases

PaxDbQ14103.
PRIDEQ14103.

Protocols and materials databases

DNASU3184.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000313899; ENSP00000313199; ENSG00000138668.
ENST00000352301; ENSP00000305860; ENSG00000138668.
ENST00000353341; ENSP00000313327; ENSG00000138668.
GeneID3184.
KEGGhsa:3184.
UCSCuc003hmm.1. human.
uc003hmn.1. human.
uc003hmo.1. human.
uc003hmp.1. human.

Organism-specific databases

CTD3184.
GeneCardsGC04M083274.
HGNCHGNC:5036. HNRNPD.
HPAHPA004911.
MIM601324. gene.
neXtProtNX_Q14103.
PharmGKBPA29361.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0724.
HOVERGENHBG002295.
InParanoidQ14103.
KOK13044.
OMAPNQNWNQ.
OrthoDBEOG49W2FZ.
PhylomeDBQ14103.

Enzyme and pathway databases

ReactomeREACT_1675. mRNA Processing.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ14103.
BgeeQ14103.
GenevestigatorQ14103.
GermOnlineENSG00000138668. Homo sapiens.

Family and domain databases

Gene3D3.30.70.330. 2 hits.
InterProIPR012956. CARG-binding_factor_N.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF08143. CBFNT. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view]
SMARTSM00360. RRM. 2 hits.
[Graphical view]
PROSITEPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHNRNPD. human.
EvolutionaryTraceQ14103.
GenomeRNAi3184.
NextBio12644.
PMAP-CutDBQ14103.
SOURCESearch...

Entry information

Entry nameHNRPD_HUMAN
AccessionPrimary (citable) accession number: Q14103
Secondary accession number(s): A8K9J2 expand/collapse secondary AC list , P07029, Q01858, Q14100, Q14101, Q14102, Q4W5A1, Q9UCE8, Q9UCE9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1996
Last modified: May 29, 2013
This is version 159 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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