Heterogeneous nuclear ribonucleoprotein U

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Relevant documents

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Relevant documents

Preferred order of sections

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Preferred order of sections

With

Entry

#Exp.

IntAct

Notes

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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

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.18
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.11 Ref.15 Ref.18 Ref.21
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.18 Ref.21
Post-translational modification	Extensively phosphorylated. Ref.6 Arg-733 and Arg-739 are dimethylated, probably to asymmetric dimethylarginine. Ref.8
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.

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.18. Source: UniProtKB mRNA splicing, via spliceosome Inferred by curator Ref.11. Source: UniProtKB
Cellular_component	CRD-mediated mRNA stability complex Inferred from direct assay Ref.18. Source: UniProtKB catalytic step 2 spliceosome Inferred from direct assay Ref.11. Source: UniProtKB cell surface Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	ATP 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
Complete GO annotation...

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

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Initiator methionine

1

Removed Ref.6 Ref.7 Ref.8

Chain

2 – 825

824

Heterogeneous nuclear ribonucleoprotein U

PRO_0000081872

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

Modified residue

2

1

N-acetylserine; partial Ref.7 Ref.8 Ref.22 Ref.24

Modified residue

4

1

Phosphoserine Ref.22 Ref.24

Modified residue

59

1

Phosphoserine Ref.13 Ref.16 Ref.19 Ref.22 Ref.24

Modified residue

66

1

Phosphoserine Ref.16 Ref.19 Ref.22 Ref.24

Modified residue

265

1

N6-acetyllysine Ref.20

Modified residue

271

1

Phosphoserine Ref.13 Ref.14 Ref.17 Ref.19 Ref.22

Modified residue

352

1

N6-acetyllysine Ref.20

Modified residue

516

1

N6-acetyllysine Ref.20

Modified residue

524

1

N6-acetyllysine Ref.20

Modified residue

551

1

N6-acetyllysine Ref.20

Modified residue

565

1

N6-acetyllysine Ref.20

Modified residue

635

1

N6-acetyllysine Ref.20

Modified residue

739

1

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

Modified residue

739

1

Omega-N-methylated arginine Ref.8

Modified residue

814

1

N6-acetyllysine Ref.20

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

Sequence conflict

603

1

A → V in AAH07950. Ref.5

1

.

825

Helix Strand Turn

Details...

Sequence		Length	Mass (Da)
Isoform Long [UniParc]. Last modified July 28, 2009. Version 6. Checksum: 5D4EC4188436831F Show »	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 « Hide
Isoform Short [UniParc]. Checksum: BCE1AD365501EDC1 Show »	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 « Hide

	« 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] [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. 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, 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] [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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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.
[19]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[20]	"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), MASS SPECTROMETRY.
[21]	"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.
[22]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"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].
[24]	"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, MASS SPECTROMETRY.
[25]	"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.

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.

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

Q00839.

ModBase

Search...

DIP

DIP-684N.

IntAct

Q00839. 40 interactions.

MINT

MINT-1654412.

STRING

9606.ENSP00000283179.

PhosphoSite

Q00839.

DMDM

254763463.

PaxDb

Q00839.

PRIDE

Q00839.

DNASU

3192.

StructuralBiologyKnowledgebase

Search...

Ensembl

ENST00000283179; ENSP00000283179; ENSG00000153187.
ENST00000444376; ENSP00000393151; ENSG00000153187.

GeneID

3192.

KEGG

hsa:3192.

UCSC

uc001iaz.1. human.
uc001iba.1. human.

CTD

3192.

GeneCards

GC01M245013.

HGNC

HGNC:5048. HNRNPU.

HPA

CAB011532.

MIM

602869. gene.

neXtProt

NX_Q00839.

PharmGKB

PA162391486.

GenAtlas

Search...

eggNOG

NOG297571.

HOGENOM

HOG000253920.

HOVERGEN

HBG061101.

InParanoid

Q00839.

KO

K12888.

OMA

PYPRAPV.

Reactome

REACT_1675. mRNA Processing.
REACT_71. Gene Expression.

ArrayExpress

Q00839.

Bgee

Q00839.

CleanEx

HS_HNRNPU.

Genevestigator

Q00839.

GermOnline

ENSG00000153187. Homo sapiens.

Gene3D

1.10.720.30. 1 hit.

InterPro

IPR001870. B30.2/SPRY.
IPR008985. ConA-like_lec_gl_sf.
IPR026745. hnRNP_U.
IPR003034. SAP_dom.
IPR018355. SPla/RYanodine_receptor_subgr.
IPR003877. SPRY_rcpt.
[Graphical view]

PANTHER

PTHR12381:SF11. PTHR12381:SF11. 1 hit.

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...

ChiTaRS

HNRNPU. human.

EvolutionaryTrace

Q00839.

GenomeRNAi

3192.

NextBio

12700.

SOURCE

Search...

Entry name

HNRPU_HUMAN

Accession

Primary (citable) accession number: Q00839
Secondary accession number(s): O75507

Q9BQ09

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	July 28, 2009
Last modified:	May 1, 2013
This is version 151 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.

Human chromosome 1

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

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

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.