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Q00839

- HNRPU_HUMAN

UniProt

Q00839 - HNRPU_HUMAN

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Protein

Heterogeneous nuclear ribonucleoprotein U

Gene

HNRNPU

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi504 – 5118ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA binding Source: ProtInc
  3. poly(A) RNA binding Source: UniProtKB
  4. RNA binding Source: ProtInc

GO - Biological processi

  1. CRD-mediated mRNA stabilization Source: UniProtKB
  2. gene expression Source: Reactome
  3. mRNA splicing, via spliceosome Source: UniProtKB
  4. osteoblast differentiation Source: UniProt
  5. RNA processing Source: ProtInc
  6. RNA splicing Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

ReactomeiREACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Heterogeneous nuclear ribonucleoprotein U
Short name:
hnRNP U
Alternative name(s):
Scaffold attachment factor A
Short name:
SAF-A
p120
pp120
Gene namesi
Name:HNRNPU
Synonyms:HNRPU, SAFA, U21.1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:5048. HNRNPU.

Subcellular locationi

Nucleus. Cytoplasm. Cell surface
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Component of ribonucleosomes. Also found associated with the cell surface.

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. CRD-mediated mRNA stability complex Source: UniProtKB
  3. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
  4. membrane Source: UniProtKB
  5. nucleoplasm Source: Reactome
  6. nucleus Source: UniProt
  7. ribonucleoprotein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162391486.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed8 Publications
Chaini2 – 825824Heterogeneous nuclear ribonucleoprotein UPRO_0000081872Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine; partial7 Publications
Modified residuei4 – 41Phosphoserine2 Publications
Modified residuei17 – 171N6-acetyllysineBy similarity
Modified residuei21 – 211N6-acetyllysineBy similarity
Modified residuei59 – 591Phosphoserine5 Publications
Modified residuei66 – 661Phosphoserine4 Publications
Modified residuei186 – 1861N6-acetyllysineBy similarity
Modified residuei255 – 2551CitrullineBy similarity
Modified residuei265 – 2651N6-acetyllysine1 Publication
Modified residuei266 – 2661PhosphotyrosineBy similarity
Modified residuei271 – 2711Phosphoserine5 Publications
Modified residuei352 – 3521N6-acetyllysine1 Publication
Modified residuei516 – 5161N6-acetyllysine1 Publication
Modified residuei524 – 5241N6-acetyllysine1 Publication
Modified residuei551 – 5511N6-acetyllysine1 Publication
Modified residuei565 – 5651N6-acetyllysine1 Publication
Modified residuei635 – 6351N6-acetyllysine1 Publication
Modified residuei739 – 7391Dimethylated arginine; in A2780 ovarian carcinoma cell line1 Publication
Modified residuei814 – 8141N6-acetyllysine1 Publication

Post-translational modificationi

Extensively phosphorylated.8 Publications
Arg-739 is dimethylated, probably to asymmetric dimethylarginine.
Citrullinated by PADI4.By similarity

Keywords - PTMi

Acetylation, Citrullination, Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ00839.
PaxDbiQ00839.
PRIDEiQ00839.

PTM databases

PhosphoSiteiQ00839.

Expressioni

Gene expression databases

BgeeiQ00839.
CleanExiHS_HNRNPU.
ExpressionAtlasiQ00839. baseline and differential.
GenevestigatoriQ00839.

Organism-specific databases

HPAiCAB011532.

Interactioni

Subunit structurei

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 CR2.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDKN2AP427712EBI-351126,EBI-375053

Protein-protein interaction databases

BioGridi109433. 286 interactions.
DIPiDIP-684N.
IntActiQ00839. 59 interactions.
MINTiMINT-1654412.
STRINGi9606.ENSP00000283179.

Structurei

Secondary structure

1
825
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni24 – 252

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZRJNMR-A23-42[»]
ProteinModelPortaliQ00839.
SMRiQ00839. Positions 3-48, 298-470.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00839.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 4235SAPPROSITE-ProRule annotationAdd
BLAST
Domaini267 – 464198B30.2/SPRYPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni714 – 73926RNA-binding RGG-boxAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 160159Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi84 – 9411Poly-GluAdd
BLAST
Compositional biasi161 – 20949Gln-richAdd
BLAST
Compositional biasi703 – 825123Gly-richAdd
BLAST
Compositional biasi740 – 75011Poly-GlyAdd
BLAST

Sequence similaritiesi

Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
Contains 1 SAP domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG297571.
GeneTreeiENSGT00390000020210.
HOGENOMiHOG000253920.
HOVERGENiHBG061101.
InParanoidiQ00839.
KOiK12888.
OMAiFKRQMAD.
OrthoDBiEOG79CZ07.
PhylomeDBiQ00839.
TreeFamiTF317301.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
IPR026745. hnRNP_U.
IPR027417. P-loop_NTPase.
IPR003034. SAP_dom.
IPR003877. SPRY_dom.
[Graphical view]
PANTHERiPTHR12381:SF11. PTHR12381:SF11. 1 hit.
PfamiPF02037. SAP. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view]
SMARTiSM00513. SAP. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50800. SAP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Long (identifier: Q00839-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSSSPVNVKK LKVSELKEEL KKRRLSDKGL KAELMERLQA ALDDEEAGGR
60 70 80 90 100
PAMEPGNGSL DLGGDSAGRS GAGLEQEAAA GGDEEEEEEE EEEEGISALD
110 120 130 140 150
GDQMELGEEN GAAGAADSGP MEEEEAASED ENGDDQGFQE GEDELGDEEE
160 170 180 190 200
GAGDENGHGE QQPQPPATQQ QQPQQQRGAA KEAAGKSSGP TSLFAVTVAP
210 220 230 240 250
PGARQGQQQA GGKKKAEGGG GGGRPGAPAA GDGKTEQKGG DKKRGVKRPR
260 270 280 290 300
EDHGRGYFEY IEENKYSRAK SPQPPVEEED EHFDDTVVCL DTYNCDLHFK
310 320 330 340 350
ISRDRLSASS LTMESFAFLW AGGRASYGVS KGKVCFEMKV TEKIPVRHLY
360 370 380 390 400
TKDIDIHEVR IGWSLTTSGM LLGEEEFSYG YSLKGIKTCN CETEDYGEKF
410 420 430 440 450
DENDVITCFA NFESDEVELS YAKNGQDLGV AFKISKEVLA GRPLFPHVLC
460 470 480 490 500
HNCAVEFNFG QKEKPYFPIP EEYTFIQNVP LEDRVRGPKG PEEKKDCEVV
510 520 530 540 550
MMIGLPGAGK TTWVTKHAAE NPGKYNILGT NTIMDKMMVA GFKKQMADTG
560 570 580 590 600
KLNTLLQRAP QCLGKFIEIA ARKKRNFILD QTNVSAAAQR RKMCLFAGFQ
610 620 630 640 650
RKAVVVCPKD EDYKQRTQKK AEVEGKDLPE HAVLKMKGNF TLPEVAECFD
660 670 680 690 700
EITYVELQKE EAQKLLEQYK EESKKALPPE KKQNTGSKKS NKNKSGKNQF
710 720 730 740 750
NRGGGHRGRG GFNMRGGNFR GGAPGNRGGY NRRGNMPQRG GGGGGSGGIG
760 770 780 790 800
YPYPRAPVFP GRGSYSNRGN YNRGGMPNRG NYNQNFRGRG NNRGYKNQSQ
810 820
GYNQWQQGQF WGQKPWSQHY HQGYY
Length:825
Mass (Da):90,584
Last modified:July 28, 2009 - v6
Checksum:i5D4EC4188436831F
GO
Isoform Short (identifier: Q00839-2) [UniParc]FASTAAdd to Basket

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

Note: Contains a N6-acetyllysine at position 215.

Show »
Length:806
Mass (Da):88,980
Checksum:iBCE1AD365501EDC1
GO

Sequence cautioni

The sequence AAC19382.1 differs from that shown. Reason: Aberrant splicing.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti603 – 6031A → V in AAH07950. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti712 – 7121F → L.2 Publications
Corresponds to variant rs1052660 [ dbSNP | Ensembl ].
VAR_014712

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei213 – 23119Missing in isoform Short. 3 PublicationsVSP_005846Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS31081.1. [Q00839-2]
CCDS41479.1. [Q00839-1]
PIRiS22765.
RefSeqiNP_004492.2. NM_004501.3. [Q00839-2]
NP_114032.2. NM_031844.2. [Q00839-1]
UniGeneiHs.106212.

Genome annotation databases

EnsembliENST00000283179; ENSP00000283179; ENSG00000153187. [Q00839-1]
ENST00000444376; ENSP00000393151; ENSG00000153187. [Q00839-2]
GeneIDi3192.
KEGGihsa:3192.
UCSCiuc001iaz.1. human. [Q00839-1]
uc001iba.1. human. [Q00839-2]

Polymorphism databases

DMDMi254763463.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS31081.1. [Q00839-2 ]
CCDS41479.1. [Q00839-1 ]
PIRi S22765.
RefSeqi NP_004492.2. NM_004501.3. [Q00839-2 ]
NP_114032.2. NM_031844.2. [Q00839-1 ]
UniGenei Hs.106212.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ZRJ NMR - A 23-42 [» ]
ProteinModelPortali Q00839.
SMRi Q00839. Positions 3-48, 298-470.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109433. 286 interactions.
DIPi DIP-684N.
IntActi Q00839. 59 interactions.
MINTi MINT-1654412.
STRINGi 9606.ENSP00000283179.

PTM databases

PhosphoSitei Q00839.

Polymorphism databases

DMDMi 254763463.

Proteomic databases

MaxQBi Q00839.
PaxDbi Q00839.
PRIDEi Q00839.

Protocols and materials databases

DNASUi 3192.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000283179 ; ENSP00000283179 ; ENSG00000153187 . [Q00839-1 ]
ENST00000444376 ; ENSP00000393151 ; ENSG00000153187 . [Q00839-2 ]
GeneIDi 3192.
KEGGi hsa:3192.
UCSCi uc001iaz.1. human. [Q00839-1 ]
uc001iba.1. human. [Q00839-2 ]

Organism-specific databases

CTDi 3192.
GeneCardsi GC01M245013.
HGNCi HGNC:5048. HNRNPU.
HPAi CAB011532.
MIMi 602869. gene.
neXtProti NX_Q00839.
PharmGKBi PA162391486.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG297571.
GeneTreei ENSGT00390000020210.
HOGENOMi HOG000253920.
HOVERGENi HBG061101.
InParanoidi Q00839.
KOi K12888.
OMAi FKRQMAD.
OrthoDBi EOG79CZ07.
PhylomeDBi Q00839.
TreeFami TF317301.

Enzyme and pathway databases

Reactomei REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSi HNRNPU. human.
EvolutionaryTracei Q00839.
GeneWikii HNRPU.
GenomeRNAii 3192.
NextBioi 12700.
PROi Q00839.
SOURCEi Search...

Gene expression databases

Bgeei Q00839.
CleanExi HS_HNRNPU.
ExpressionAtlasi Q00839. baseline and differential.
Genevestigatori Q00839.

Family and domain databases

Gene3Di 1.10.720.30. 1 hit.
3.40.50.300. 1 hit.
InterProi IPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
IPR026745. hnRNP_U.
IPR027417. P-loop_NTPase.
IPR003034. SAP_dom.
IPR003877. SPRY_dom.
[Graphical view ]
PANTHERi PTHR12381:SF11. PTHR12381:SF11. 1 hit.
Pfami PF02037. SAP. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view ]
SMARTi SM00513. SAP. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEi PS50188. B302_SPRY. 1 hit.
PS50800. SAP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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. 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.

Entry informationi

Entry nameiHNRPU_HUMAN
AccessioniPrimary (citable) accession number: Q00839
Secondary accession number(s): O75507
, Q8N174, Q96HY9, Q9BQ09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: July 28, 2009
Last modified: November 26, 2014
This is version 168 of the entry and version 6 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3