Reviewed, UniProtKB/Swiss-Prot Q14103 (HNRPD_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	355 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.24
Subunit structure	Part of a complex associated with the FOS mCRD domain and consisting of PABPC1, PAIP1, CSDE1/UNR and SYNCRIP. Interacts with IGF2BP2. Ref.14
Subcellular location	Nucleus. Note: Component of ribonucleosomes.
Post-translational modification	Arg-345 is dimethylated, probably to asymmetric dimethylarginine. Ref.10 Ref.15
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: Miscellaneous discrepancy. Contaminating sequence. Sequence of unknown origin in the N-terminal part. The sequence CAA27544.1 differs from that shown. Reason: Miscellaneous discrepancy. Several sequence conflicts.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Chromosomal protein Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	DNA-binding RNA-binding
Molecular function	Ribonucleoprotein
PTM	Methylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	RNA catabolic process Traceable author statement. Source: ProtInc nuclear mRNA splicing, via spliceosome Inferred from Experiment. Source: Reactome regulation of transcription, DNA-dependent Ref.9 Non-traceable author statement. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chromosome Inferred from electronic annotation. Source: UniProtKB-KW heterogeneous nuclear ribonucleoprotein complex Non-traceable author statement. Source: UniProtKB
Molecular function	RNA binding Ref.7 Ref.11 Inferred from direct assay. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro protein binding Ref.14 Inferred from physical interaction. Source: IntAct telomeric DNA binding Ref.11 Inferred from direct assay. Source: UniProtKB transcription activator activity Ref.9 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
C1QBP	Q07021	1	EBI-432539,EBI-347528
EIF4G1	Q04637	1	EBI-432527,EBI-73711
EIF4G1	Q04637	1	EBI-432533,EBI-73711
EIF4G1	Q04637	1	EBI-432539,EBI-73711
EIF4G1	Q04637	1	EBI-432545,EBI-73711
EXOSC4	Q9NPD3	1	EBI-432539,EBI-371823
IGF2BP2	Q9Y6M1	4	EBI-432545,EBI-1024419
LDHAL6B	Q9BYZ2	2	EBI-299674,EBI-1108377
LSM5	Q9Y4Y9	1	EBI-432539,EBI-373007
PABPC1	P11940	1	EBI-432545,EBI-81531
SFN	P31947	3	EBI-432545,EBI-476295
SFN	P31947	1	EBI-432539,EBI-476295
SYNCRIP	O60506	3	EBI-432545,EBI-1024357
SYNCRIP	O60506-1	1	EBI-432545,EBI-1024377
UBE2I	P63279	2	EBI-299674,EBI-80168
UBE2I	P63279	1	EBI-432545,EBI-80168
YBX1	P67809	3	EBI-432545,EBI-354065
YBX1	P67809	2	EBI-432539,EBI-354065
YWHAH	Q04917	1	EBI-432545,EBI-306940

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

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 355

355

Heterogeneous nuclear ribonucleoprotein D0

PRO_0000081849

Regions

Domain

97 – 179

83

RRM 1

Domain

182 – 261

80

RRM 2

Compositional bias

11 – 45

35

Ala-rich

Compositional bias

270 – 347

78

Gly-rich

Compositional bias

294 – 332

39

Tyr-rich

Amino acid modifications

Modified residue

80

1

Phosphoserine Ref.19

Modified residue

82

1

Phosphoserine Ref.19 Ref.17 Ref.21

Modified residue

83

1

Phosphoserine Ref.19 Ref.21 Ref.20 Ref.22

Modified residue

87

1

Phosphoserine Ref.19

Modified residue

91

1

Phosphothreonine Ref.19

Modified residue

119

1

N6-methyllysine Ref.10

Modified residue

190

1

Phosphoserine Ref.21 Ref.16 Ref.18

Modified residue

193

1

Phosphothreonine Ref.21 Ref.20 Ref.16

Modified residue

345

1

Omega-N-methylated arginine Ref.15

Natural variations

Alternative sequence

79 – 97

19

Missing in isoform 2 and isoform 4.

VSP_005834

Alternative sequence

285 – 334

50

GPSQN…GDYSN → D in isoform 3 and isoform 4.

VSP_005835

Experimental info

Sequence conflict

150

1

S → R AA sequence Ref.11

Sequence conflict

225

1

F → L in AAA35781. Ref.9

Secondary structure

1

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355

Helix Strand Turn

Details...

Beta strand

99 – 102

4

Helix

110 – 118

9

Beta strand

123 – 127

5

Turn

132 – 135

4

Beta strand

139 – 147

9

Helix

148 – 156

9

Beta strand

183 – 186

4

Helix

195 – 203

9

Beta strand

208 – 212

5

Beta strand

226 – 233

8

Helix

234 – 241

8

Beta strand

244 – 247

4

Beta strand

250 – 253

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (p45) (Dx9) [UniParc]. Last modified November 1, 1996. Version 1. Checksum: D0B6EA177BEF789E	FASTA	355	38,434
	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
	Isoform 2 (p42) (Dx4). Checksum: FEE18D61B7714B51	FASTA	336	36,272
	10 20 30 40 50 60 MSEEQFGGDG AAAAATAAVG GSAGEQEGAM VAATQGAAAA AGSGAGTGGG TASGGTEGGS 70 80 90 100 110 120 AESEGAKIDA SKNEEDEGKM FIGGLSWDTT KKDLKDYFSK FGEVVDCTLK LDPITGRSRG 130 140 150 160 170 180 FGFVLFKESE SVDKVMDQKE HKLNGKVIDP KRAKAMKTKE PVKKIFVGGL SPDTPEEKIR 190 200 210 220 230 240 EYFGGFGEVE SIELPMDNKT NKRRGFCFIT FKEEEPVKKI MEKKYHNVGL SKCEIKVAMS 250 260 270 280 290 300 KEQYQQQQQW GSRGGFAGRA RGRGGGPSQN WNQGYSNYWN QGYGNYGYNS QGYGGYGGYD 310 320 330 YTGYNNYYGY GDYSNQQSGY GKVSRRGGHQ NSYKPY
	Isoform 3 (p40) (Dx7). Checksum: ABCDD6ACF812F647	FASTA	306	32,835
	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 GRGGDQQSGY GKVSRRGGHQ NSYKPY
	Isoform 4 (p37). Checksum: 98DF6E78EAF3BBC1	FASTA	287	30,672
	10 20 30 40 50 60 MSEEQFGGDG AAAAATAAVG GSAGEQEGAM VAATQGAAAA AGSGAGTGGG TASGGTEGGS 70 80 90 100 110 120 AESEGAKIDA SKNEEDEGKM FIGGLSWDTT KKDLKDYFSK FGEVVDCTLK LDPITGRSRG 130 140 150 160 170 180 FGFVLFKESE SVDKVMDQKE HKLNGKVIDP KRAKAMKTKE PVKKIFVGGL SPDTPEEKIR 190 200 210 220 230 240 EYFGGFGEVE SIELPMDNKT NKRRGFCFIT FKEEEPVKKI MEKKYHNVGL SKCEIKVAMS 250 260 270 280 KEQYQQQQQW GSRGGFAGRA RGRGGDQQSG YGKVSRRGGH QNSYKPY

References

	« Hide 'large scale' referencesShow '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: 7673195] [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: 9615222] [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. , 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: 14702039] [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. , 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: 15815621] [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. , 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: 15489334] [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: 3754960] [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: 10024518] [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: 1433497] [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: 8321232] [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: 9521873] [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: 11051545] [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: 12674497] [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: 15782174] [Abstract] Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-345, MASS SPECTROMETRY.
[16]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190 AND THR-193, MASS SPECTROMETRY. Tissue: Epithelium.
[17]	"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry." Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R. Nat. Methods 2:591-598(2005) [PubMed: 16094384] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, MASS SPECTROMETRY. Tissue: T-cell.
[18]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, MASS SPECTROMETRY. Tissue: Epithelium.
[19]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-82; SER-83; SER-87 AND THR-91, MASS SPECTROMETRY.
[20]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND THR-193, MASS SPECTROMETRY.
[21]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-83; SER-190 AND THR-193, MASS SPECTROMETRY.
[22]	"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: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, MASS SPECTROMETRY. Tissue: Liver.
[23]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[24]	"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: 10080887] [Abstract] Cited for: STRUCTURE BY NMR OF 98-172, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

IPI

IPI00028888.
IPI00220683.
IPI00220684.
IPI00220685.

PIR

A24016.
A44192.
B48138.

RefSeq

NP_001003810.1.
NP_002129.2.
NP_112737.1.
NP_112738.1.

UniGene

Hs.480073

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HD0	NMR	-	A	98-172	[»]
1HD1	NMR	-	A	98-172	[»]
1IQT	NMR	-	A	183-257	[»]
1WTB	NMR	-	A	181-259	[»]
1X0F	NMR	-	A	181-259	[»]
2Z5N	X-ray	3.20	B	332-355	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q14103. 41 interactions.

PTM databases

PhosphoSite

Q14103.

2-D gel databases

SWISS-2DPAGE

Q14103.

Proteomic databases

PRIDE

Q14103.

Genome annotation databases

Ensembl

ENSG00000138668. Homo sapiens. [Contig view]

GeneID

3184.

KEGG

hsa:3184.

Organism-specific databases

GeneCards

GC04M083494.

H-InvDB

HIX0004333.

HGNC

HGNC:5036. HNRNPD.

HPA

HPA004911.

MIM

601324. gene.

PharmGKB

PA29361.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q14103.

OMA

Q14103. PRHTEAA.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_6167. Influenza Infection.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q14103.

Bgee

Q14103.

GermOnline

ENSG00000138668. Homo sapiens.

Family and domain databases

InterPro

IPR012677. a_b_plait_nuc_bd.
IPR012956. CARG-binding_factor_N.
IPR000504. RRM_RNP1.
[Graphical view]

Gene3D

G3DSA:3.30.70.330. a_b_plait_nuc_bd. 2 hits.

Pfam

PF08143. CBFNT. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view]

SMART

SM00360. RRM. 2 hits.
[Graphical view]

PROSITE

PS50102. RRM. 2 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

12644.

PMAP-CutDB

Q14103.

SOURCE

Search...

Entry information

Entry name

HNRPD_HUMAN

Accession

Primary (citable) accession number: Q14103
Secondary accession number(s): A8K9J2 , 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:	June 16, 2009
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)