Q00839 (HNRPU_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Heterogeneous nuclear ribonucleoprotein U
Short name=hnRNP U

Alternative name(s):
Scaffold attachment factor A
Short name=SAF-A
p120
pp120

Gene names

Name:	HNRNPU
Synonyms:	HNRPU, SAFA, U21.1

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	825 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the CRD-mediated complex that promotes MYC mRNA stabilization. Binds to pre-mRNA. Has high affinity for scaffold-attached region (SAR) DNA. Binds to double- and single-stranded DNA and RNA. Ref.23
Subunit structure	Identified in the spliceosome C complex. Component of the coding region determinant (CRD)-mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. 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. Interacts with IGF2BP1 and ERBB4. Ligand for CR2. Ref.10 Ref.17 Ref.26
Subcellular location	Nucleus. Cytoplasm. Cell surface. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Component of ribonucleosomes. Also found associated with the cell surface. Ref.6 Ref.17 Ref.23 Ref.26
Post-translational modification	Extensively phosphorylated. Ref.6 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.24 Arg-733 and Arg-739 are dimethylated, probably to asymmetric dimethylarginine. Ref.8 Ref.12
Sequence similarities	Contains 1 B30.2/SPRY domain. Contains 1 SAP domain.
Sequence caution	The sequence AAC19382.1 differs from that shown. Reason: Aberrant splicing.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus Spliceosome
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding DNA-binding Nucleotide-binding RNA-binding
Molecular function	Ribonucleoprotein
PTM	Acetylation Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	CRD-mediated mRNA stabilization Inferred from mutant phenotype Ref.23. Source: UniProtKB nuclear mRNA splicing, via spliceosome Inferred by curator Ref.11. Source: UniProtKB
Cellular component	CRD-mediated mRNA stability complex Inferred from direct assay Ref.23. Source: UniProtKB catalytic step 2 spliceosome Inferred from direct assay Ref.11. Source: UniProtKB cell surface Inferred from electronic annotation. Source: UniProtKB-SubCell heterogeneous nuclear ribonucleoprotein complex Traceable author statement. Source: ProtInc nucleoplasm Traceable author statement. Source: Reactome
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Traceable author statement. Source: ProtInc RNA binding Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction Ref.17Ref.26. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDKN2A	P42771	2	EBI-351126,EBI-375053

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: Q00839-1)

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 Short (identifier: Q00839-2)

The sequence of this isoform differs from the canonical sequence as follows:
     213-231: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6 Ref.7 Ref.8

Chain

2 – 825

824

Heterogeneous nuclear ribonucleoprotein U

PRO_0000081872

Regions

Domain

8 – 42

35

SAP

Domain

267 – 464

198

B30.2/SPRY

Nucleotide binding

504 – 511

8

ATP Potential

Region

714 – 739

26

RNA-binding RGG-box

Compositional bias

2 – 160

159

Asp/Glu-rich (acidic)

Compositional bias

84 – 94

11

Poly-Glu

Compositional bias

161 – 209

49

Gln-rich

Compositional bias

703 – 825

123

Gly-rich

Compositional bias

740 – 750

11

Poly-Gly

Amino acid modifications

Modified residue

2

1

N-acetylserine; partial Ref.7 Ref.8

Modified residue

4

1

Phosphoserine Ref.14 Ref.22

Modified residue

26

1

Phosphoserine Ref.18

Modified residue

50

1

Omega-N-methylarginine Ref.12

Modified residue

59

1

Phosphoserine Ref.14 Ref.19 Ref.21 Ref.24

Modified residue

66

1

Phosphoserine Ref.19 Ref.21 Ref.24

Modified residue

188

1

Phosphoserine Ref.19

Modified residue

234

1

N6-acetyllysine Ref.25

Modified residue

265

1

N6-acetyllysine Ref.25

Modified residue

271

1

Phosphoserine Ref.14 Ref.15 Ref.16 Ref.20 Ref.21 Ref.22 Ref.24

Modified residue

286

1

Phosphothreonine Ref.22

Modified residue

352

1

N6-acetyllysine Ref.25

Modified residue

464

1

N6-acetyllysine Ref.25

Modified residue

473

1

Phosphotyrosine Ref.13

Modified residue

516

1

N6-acetyllysine Ref.25

Modified residue

524

1

N6-acetyllysine Ref.25

Modified residue

551

1

N6-acetyllysine Ref.25

Modified residue

565

1

N6-acetyllysine Ref.25

Modified residue

626

1

N6-acetyllysine Ref.25

Modified residue

635

1

N6-acetyllysine Ref.25

Modified residue

670

1

N6-acetyllysine Ref.25

Modified residue

733

1

Omega-N-methylated arginine Ref.12

Modified residue

739

1

Dimethylated arginine; in A2780 ovarian carcinoma cell line Ref.8 Ref.12

Modified residue

739

1

Omega-N-methylated arginine Ref.8 Ref.12

Modified residue

814

1

N6-acetyllysine Ref.25

Natural variations

Alternative sequence

213 – 231

19

Missing in isoform Short.

VSP_005846

Natural variant

712

1

F → L. Ref.1 Ref.3
Corresponds to variant rs1052660 [ dbSNP | Ensembl ].

VAR_014712

Experimental info

Sequence conflict

603

1

A → V in AAH07950. Ref.5

Secondary structure

1

.

.

.

825

Helix Strand Turn

Details...

Turn

24 – 25

2

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified July 28, 2009. Version 6. Checksum: 5D4EC4188436831F	FASTA	825	90,584
	10 20 30 40 50 60 MSSSPVNVKK LKVSELKEEL KKRRLSDKGL KAELMERLQA ALDDEEAGGR PAMEPGNGSL 70 80 90 100 110 120 DLGGDSAGRS GAGLEQEAAA GGDEEEEEEE EEEEGISALD GDQMELGEEN GAAGAADSGP 130 140 150 160 170 180 MEEEEAASED ENGDDQGFQE GEDELGDEEE GAGDENGHGE QQPQPPATQQ QQPQQQRGAA 190 200 210 220 230 240 KEAAGKSSGP TSLFAVTVAP PGARQGQQQA GGKKKAEGGG GGGRPGAPAA GDGKTEQKGG 250 260 270 280 290 300 DKKRGVKRPR EDHGRGYFEY IEENKYSRAK SPQPPVEEED EHFDDTVVCL DTYNCDLHFK 310 320 330 340 350 360 ISRDRLSASS LTMESFAFLW AGGRASYGVS KGKVCFEMKV TEKIPVRHLY TKDIDIHEVR 370 380 390 400 410 420 IGWSLTTSGM LLGEEEFSYG YSLKGIKTCN CETEDYGEKF DENDVITCFA NFESDEVELS 430 440 450 460 470 480 YAKNGQDLGV AFKISKEVLA GRPLFPHVLC HNCAVEFNFG QKEKPYFPIP EEYTFIQNVP 490 500 510 520 530 540 LEDRVRGPKG PEEKKDCEVV MMIGLPGAGK TTWVTKHAAE NPGKYNILGT NTIMDKMMVA 550 560 570 580 590 600 GFKKQMADTG KLNTLLQRAP QCLGKFIEIA ARKKRNFILD QTNVSAAAQR RKMCLFAGFQ 610 620 630 640 650 660 RKAVVVCPKD EDYKQRTQKK AEVEGKDLPE HAVLKMKGNF TLPEVAECFD EITYVELQKE 670 680 690 700 710 720 EAQKLLEQYK EESKKALPPE KKQNTGSKKS NKNKSGKNQF NRGGGHRGRG GFNMRGGNFR 730 740 750 760 770 780 GGAPGNRGGY NRRGNMPQRG GGGGGSGGIG YPYPRAPVFP GRGSYSNRGN YNRGGMPNRG 790 800 810 820 NYNQNFRGRG NNRGYKNQSQ GYNQWQQGQF WGQKPWSQHY HQGYY
	Isoform Short [UniParc]. Checksum: BCE1AD365501EDC1	FASTA	806	88,980
	10 20 30 40 50 60 MSSSPVNVKK LKVSELKEEL KKRRLSDKGL KAELMERLQA ALDDEEAGGR PAMEPGNGSL 70 80 90 100 110 120 DLGGDSAGRS GAGLEQEAAA GGDEEEEEEE EEEEGISALD GDQMELGEEN GAAGAADSGP 130 140 150 160 170 180 MEEEEAASED ENGDDQGFQE GEDELGDEEE GAGDENGHGE QQPQPPATQQ QQPQQQRGAA 190 200 210 220 230 240 KEAAGKSSGP TSLFAVTVAP PGARQGQQQA GGDGKTEQKG GDKKRGVKRP REDHGRGYFE 250 260 270 280 290 300 YIEENKYSRA KSPQPPVEEE DEHFDDTVVC LDTYNCDLHF KISRDRLSAS SLTMESFAFL 310 320 330 340 350 360 WAGGRASYGV SKGKVCFEMK VTEKIPVRHL YTKDIDIHEV RIGWSLTTSG MLLGEEEFSY 370 380 390 400 410 420 GYSLKGIKTC NCETEDYGEK FDENDVITCF ANFESDEVEL SYAKNGQDLG VAFKISKEVL 430 440 450 460 470 480 AGRPLFPHVL CHNCAVEFNF GQKEKPYFPI PEEYTFIQNV PLEDRVRGPK GPEEKKDCEV 490 500 510 520 530 540 VMMIGLPGAG KTTWVTKHAA ENPGKYNILG TNTIMDKMMV AGFKKQMADT GKLNTLLQRA 550 560 570 580 590 600 PQCLGKFIEI AARKKRNFIL DQTNVSAAAQ RRKMCLFAGF QRKAVVVCPK DEDYKQRTQK 610 620 630 640 650 660 KAEVEGKDLP EHAVLKMKGN FTLPEVAECF DEITYVELQK EEAQKLLEQY KEESKKALPP 670 680 690 700 710 720 EKKQNTGSKK SNKNKSGKNQ FNRGGGHRGR GGFNMRGGNF RGGAPGNRGG YNRRGNMPQR 730 740 750 760 770 780 GGGGGGSGGI GYPYPRAPVF PGRGSYSNRG NYNRGGMPNR GNYNQNFRGR GNNRGYKNQS 790 800 QGYNQWQQGQ FWGQKPWSQH YHQGYY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure and binding activity of the hnRNP U protein: binding RNA through RGG box." Kiledjian M., Dreyfuss G. EMBO J. 11:2655-2664(1992) [PubMed: 1628625] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), RNA-BINDING DOMAIN, VARIANT LEU-712.
[2]	"hnRNP-U/SAF-A is encoded by two differentially polyadenylated mRNAs in human cells." Fackelmayer F.O., Richter A. Biochim. Biophys. Acta 1217:232-234(1994) [PubMed: 7509195] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
[3]	"A variant of human scaffold attachment factor A (SAF-A), also known as heterogeneous nuclear ribonucleoprotein U (hnRNP-U)." Fackelmayer F.O. Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANT LEU-712.
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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] (ISOFORM SHORT). Tissue: Eye, Lymph, Placenta and Skin.
[6]	"Major cell surface-located protein substrates of an ecto-protein kinase are homologs of known nuclear proteins." Jordan P., Heid H., Kinzel V., Kubler D. Biochemistry 33:14696-14706(1994) [PubMed: 7993898] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-7; 256-265 AND 463-476, PHOSPHORYLATION, SUBCELLULAR LOCATION.
[7]	Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M. Submitted (MAY-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-9; 186-194; 319-330; 399-409; 423-432; 452-461; 464-475 AND 524-535, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY. Tissue: T-cell.
[8]	Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-9; 13-21; 38-69; 187-204; 256-268; 306-324; 353-360; 424-433; 463-484; 495-510; 525-543; 552-558; 566-572; 576-590; 592-601; 627-635; 665-674 AND 734-755, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, METHYLATION AT ARG-739, MASS SPECTROMETRY. Tissue: Ovarian carcinoma.
[9]	"Purification of two isoforms of hnRNP-U and characterization of their nucleic acid binding activity." Fackelmayer F.O., Richter A. Biochemistry 33:10416-10422(1994) [PubMed: 8068679] [Abstract] Cited for: CHARACTERIZATION.
[10]	"Binding sites of the Epstein-Barr virus and C3d receptor (CR2, CD21) for its three intracellular ligands, the p53 anti-oncoprotein, the p68 calcium binding protein and the nuclear p120 ribonucleoprotein." Barel M., Balbo M., Gauffre A., Frade R. Mol. Immunol. 32:389-397(1995) [PubMed: 7753047] [Abstract] Cited for: INTERACTION WITH CR2.
[11]	"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis." Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J. RNA 8:426-439(2002) [PubMed: 11991638] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[12]	"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-50; ARG-733 AND ARG-739, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-473, MASS SPECTROMETRY.
[14]	"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-4; SER-59 AND SER-271, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line." Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S. Electrophoresis 28:2027-2034(2007) [PubMed: 17487921] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271, MASS SPECTROMETRY. Tissue: Prostate cancer.
[16]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271, 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: 17289661] [Abstract] Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[18]	"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-26, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[19]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59; SER-66 AND SER-188, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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-271, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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-59; SER-66 AND SER-271, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-271 AND THR-286, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[23]	"Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs." Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S. RNA 15:104-115(2009) [PubMed: 19029303] [Abstract] Cited for: FUNCTION, COMPONENT OF THE CRD-MEDIATED MRNA STABILIZATION COMPLEX, IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[24]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59; SER-66 AND SER-271, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[25]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-234; LYS-265; LYS-352; LYS-464; LYS-516; LYS-524; LYS-551; LYS-565; LYS-626; LYS-635; LYS-670 AND LYS-814, MASS SPECTROMETRY.
[26]	"Interactions of ErbB4 and Kap1 connect the growth factor and DNA damage response pathways." Gilmore-Hebert M., Ramabhadran R., Stern D.F. Mol. Cancer Res. 8:1388-1398(2010) [PubMed: 20858735] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ERBB4, SUBCELLULAR LOCATION.
[27]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]	"Solution structure of the SAP domain of human E1B-55kDa-associated protein 5 isoform C." RIKEN structural genomics initiative (RSGI) Submitted (JAN-2008) to the PDB data bank Cited for: STRUCTURE BY NMR OF 23-42.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X65488 mRNA. Translation: CAA46472.1.
AF068846 mRNA. Translation: AAC19382.1. Sequence problems.
BX323046 Genomic DNA. Translation: CAI11058.1.
BC003367 mRNA. Translation: AAH03367.1.
BC003621 mRNA. Translation: AAH03621.1.
BC007950 mRNA. Translation: AAH07950.2.
BC024767 mRNA. Translation: AAH24767.1.
BC034925 mRNA. Translation: AAH34925.1.

IPI

IPI00479217.
IPI00883857.

PIR

S22765.

RefSeq

NP_004492.2. NM_004501.3.
NP_114032.2. NM_031844.2.

UniGene

Hs.106212.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZRJ	NMR	-	A	23-42	[»]

ProteinModelPortal

Q00839.

SMR

Q00839. Positions 2-47, 498-617.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-684N.

IntAct

Q00839. 25 interactions.

MINT

MINT-1654412.

STRING

Q00839.

PTM databases

PhosphoSite

Q00839.

Polymorphism databases

DMDM

254763463.

Proteomic databases

PRIDE

Q00839.

Protocols and materials databases

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000283179; ENSP00000283179; ENSG00000153187.

GeneID

3192.

KEGG

hsa:3192.

UCSC

uc001iba.1. human.

Organism-specific databases

CTD

3192.

GeneCards

GC01M245013.

HGNC

HGNC:5048. HNRNPU.

HPA

CAB011532.

MIM

602869. gene.

neXtProt

NX_Q00839.

PharmGKB

PA162391486.

GenAtlas

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Phylogenomic databases

eggNOG

prNOG13042.

HOGENOM

HBG446506.

HOVERGEN

HBG061101.

InParanoid

Q00839.

OMA

SKKSLPP.

PhylomeDB

Q00839.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q00839.

Bgee

Q00839.

CleanEx

HS_HNRNPU.

Genevestigator

Q00839.

GermOnline

ENSG00000153187. Homo sapiens.

Family and domain databases

InterPro

IPR001870. B30.2/SPRY.
IPR008985. ConA-like_lec_gl.
IPR003034. SAP_DNA-bd.
IPR018355. SPla/RYanodine_receptor_subgr.
IPR003877. SPRY_rcpt.
[Graphical view]

Gene3D

G3DSA:1.10.720.30. G3DSA:1.10.720.30. 1 hit.

KO

K12888.

Pfam

PF02037. SAP. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view]

SMART

SM00513. SAP. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]

SUPFAM

SSF49899. ConA_like_lec_gl. 1 hit.

PROSITE

PS50188. B302_SPRY. 1 hit.
PS50800. SAP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

12700.

SOURCE

Search...

Entry information

Entry name

HNRPU_HUMAN

Accession

Primary (citable) accession number: Q00839
Secondary accession number(s): O75507 , Q8N174, Q96HY9, Q9BQ09

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	July 28, 2009
Last modified:	January 25, 2012
This is version 137 of the entry and version 6 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.