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Q00839 (HNRPU_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length825 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.19

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 IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with IGF2BP1, IGF2BP2, IGF2BP3 and ERBB4. Ligand for CR2. Ref.10 Ref.11 Ref.15 Ref.19 Ref.22 Ref.28

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.15 Ref.19 Ref.22

Post-translational modification

Extensively phosphorylated. Ref.6

Arg-733 and Arg-739 are dimethylated, probably to asymmetric dimethylarginine. Ref.8

Citrullinated by PADI4 By similarity.

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 processmRNA processing
mRNA splicing
   Cellular componentCytoplasm
Nucleus
Spliceosome
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
DNA-binding
Nucleotide-binding
RNA-binding
   Molecular functionRibonucleoprotein
   PTMAcetylation
Citrullination
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processCRD-mediated mRNA stabilization

Inferred from mutant phenotype Ref.19. Source: UniProtKB

RNA processing

Traceable author statement Ref.1. Source: ProtInc

RNA splicing

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA splicing, via spliceosome

Inferred by curator Ref.11. Source: UniProtKB

osteoblast differentiation

Inferred from direct assay PubMed 16210410. Source: UniProt

   Cellular_componentCRD-mediated mRNA stability complex

Inferred from direct assay Ref.19. Source: UniProtKB

catalytic step 2 spliceosome

Inferred from direct assay Ref.11. Source: UniProtKB

cell surface

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from direct assay PubMed 16210410. Source: UniProt

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 22720776. Source: UniProt

ribonucleoprotein complex

Inferred from direct assay Ref.15. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Traceable author statement Ref.1. Source: ProtInc

RNA binding

Traceable author statement Ref.1. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.15Ref.22. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CDKN2AP427712EBI-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.
Note: Contains a N6-acetyllysine at position 215.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6 Ref.7 Ref.8
Chain2 – 825824Heterogeneous nuclear ribonucleoprotein U
PRO_0000081872

Regions

Domain8 – 4235SAP
Domain267 – 464198B30.2/SPRY
Nucleotide binding504 – 5118ATP Potential
Region714 – 73926RNA-binding RGG-box
Compositional bias2 – 160159Asp/Glu-rich (acidic)
Compositional bias84 – 9411Poly-Glu
Compositional bias161 – 20949Gln-rich
Compositional bias703 – 825123Gly-rich
Compositional bias740 – 75011Poly-Gly

Amino acid modifications

Modified residue21N-acetylserine; partial Ref.7 Ref.8 Ref.18 Ref.23 Ref.25 Ref.26 Ref.27
Modified residue41Phosphoserine Ref.23 Ref.25
Modified residue171N6-acetyllysine By similarity
Modified residue211N6-acetyllysine By similarity
Modified residue591Phosphoserine Ref.13 Ref.16 Ref.20 Ref.23 Ref.25
Modified residue661Phosphoserine Ref.16 Ref.20 Ref.23 Ref.25
Modified residue1861N6-acetyllysine By similarity
Modified residue2551Citrulline By similarity
Modified residue2651N6-acetyllysine Ref.21
Modified residue2661Phosphotyrosine By similarity
Modified residue2711Phosphoserine Ref.13 Ref.14 Ref.17 Ref.20 Ref.23
Modified residue3521N6-acetyllysine Ref.21
Modified residue5161N6-acetyllysine Ref.21
Modified residue5241N6-acetyllysine Ref.21
Modified residue5511N6-acetyllysine Ref.21
Modified residue5651N6-acetyllysine Ref.21
Modified residue6351N6-acetyllysine Ref.21
Modified residue7391Dimethylated arginine; in A2780 ovarian carcinoma cell line Ref.8
Modified residue7391Omega-N-methylated arginine Ref.8
Modified residue8141N6-acetyllysine Ref.21

Natural variations

Alternative sequence213 – 23119Missing in isoform Short.
VSP_005846
Natural variant7121F → L. Ref.1 Ref.3
Corresponds to variant rs1052660 [ dbSNP | Ensembl ].
VAR_014712

Experimental info

Sequence conflict6031A → V in AAH07950. Ref.5

Secondary structure

... 825
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified July 28, 2009. Version 6.
Checksum: 5D4EC4188436831F

FASTA82590,584
        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 

« Hide

Isoform Short [UniParc].

Checksum: BCE1AD365501EDC1
Show »

FASTA80688,980

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY 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, IDENTIFICATION BY 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[12]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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-59 AND SER-271, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Prostate cancer.
[15]"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, INTERACTION WITH IGF2BP1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[16]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 AND SER-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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-271, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, COMPONENT OF THE CRD-MEDIATED MRNA STABILIZATION COMPLEX, IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[20]"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-59; SER-66 AND SER-271, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[21]"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-265; LYS-352; LYS-516; LYS-524; LYS-551; LYS-565; LYS-635 AND LYS-814, ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-215 (ISOFORM SHORT), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ERBB4, SUBCELLULAR LOCATION.
[23]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-59; SER-66 AND SER-271, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"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].
[25]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-59 AND SER-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"Subcellular localization and RNP formation of IGF2BPs (IGF2 mRNA-binding proteins) is modulated by distinct RNA-binding domains."
Wachter K., Kohn M., Stohr N., Huttelmaier S.
Biol. Chem. 394:1077-1090(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IGF2BP1; IGF2BP2 AND IGF2BP3.
[29]"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.
CCDSCCDS31081.1. [Q00839-2]
CCDS41479.1. [Q00839-1]
PIRS22765.
RefSeqNP_004492.2. NM_004501.3. [Q00839-2]
NP_114032.2. NM_031844.2. [Q00839-1]
UniGeneHs.106212.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZRJNMR-A23-42[»]
ProteinModelPortalQ00839.
SMRQ00839. Positions 3-48, 298-470.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109433. 282 interactions.
DIPDIP-684N.
IntActQ00839. 57 interactions.
MINTMINT-1654412.
STRING9606.ENSP00000283179.

PTM databases

PhosphoSiteQ00839.

Polymorphism databases

DMDM254763463.

Proteomic databases

MaxQBQ00839.
PaxDbQ00839.
PRIDEQ00839.

Protocols and materials databases

DNASU3192.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000283179; ENSP00000283179; ENSG00000153187. [Q00839-1]
ENST00000444376; ENSP00000393151; ENSG00000153187. [Q00839-2]
GeneID3192.
KEGGhsa:3192.
UCSCuc001iaz.1. human. [Q00839-1]
uc001iba.1. human. [Q00839-2]

Organism-specific databases

CTD3192.
GeneCardsGC01M245013.
HGNCHGNC:5048. HNRNPU.
HPACAB011532.
MIM602869. gene.
neXtProtNX_Q00839.
PharmGKBPA162391486.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG297571.
HOGENOMHOG000253920.
HOVERGENHBG061101.
InParanoidQ00839.
KOK12888.
OMAFKRQMAD.
OrthoDBEOG79CZ07.
PhylomeDBQ00839.
TreeFamTF317301.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ00839.
BgeeQ00839.
CleanExHS_HNRNPU.
GenevestigatorQ00839.

Family and domain databases

Gene3D1.10.720.30. 1 hit.
3.40.50.300. 1 hit.
InterProIPR001870. B30.2/SPRY.
IPR008985. ConA-like_lec_gl_sf.
IPR026745. hnRNP_U.
IPR027417. P-loop_NTPase.
IPR003034. SAP_dom.
IPR018355. SPla/RYanodine_receptor_subgr.
IPR003877. SPRY_rcpt.
[Graphical view]
PANTHERPTHR12381:SF11. PTHR12381:SF11. 1 hit.
PfamPF02037. SAP. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view]
SMARTSM00513. SAP. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS50188. B302_SPRY. 1 hit.
PS50800. SAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHNRNPU. human.
EvolutionaryTraceQ00839.
GeneWikiHNRPU.
GenomeRNAi3192.
NextBio12700.
PROQ00839.
SOURCESearch...

Entry information

Entry nameHNRPU_HUMAN
AccessionPrimary (citable) accession number: Q00839
Secondary accession number(s): O75507 expand/collapse secondary AC list , Q8N174, Q96HY9, Q9BQ09
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: July 28, 2009
Last modified: July 9, 2014
This is version 164 of the entry and version 6 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM