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Protein

Heterogeneous nuclear ribonucleoprotein U

Gene

Hnrnpu

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 (By similarity). Plays a role in the circadian regulation of the core clock component ARNTL/BMAL1 transcription (PubMed:18332112).By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi480 – 4878ATPSequence analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • core promoter binding Source: UniProtKB
  • poly(A) RNA binding Source: MGI
  • telomerase RNA binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

Biological rhythms, mRNA processing, mRNA splicing

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiR-MMU-72163. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Heterogeneous nuclear ribonucleoprotein UImported
Short name:
hnRNP U1 Publication
Alternative name(s):
Scaffold attachment factor A1 Publication
Short name:
SAF-A1 Publication
Gene namesi
Name:HnrnpuImported
Synonyms:HnrpuImported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1858195. Hnrnpu.

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasm By similarity
  • Cell surface By similarity

  • Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Component of ribonucleosomes.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 800799Heterogeneous nuclear ribonucleoprotein UPRO_0000387947Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei4 – 41PhosphoserineBy similarity
Modified residuei58 – 581PhosphoserineBy similarity
Modified residuei231 – 2311Citrulline1 Publication
Modified residuei241 – 2411N6-acetyllysine; alternateBy similarity
Cross-linki241 – 241Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei247 – 2471PhosphoserineBy similarity
Modified residuei262 – 2621PhosphothreonineBy similarity
Modified residuei328 – 3281N6-acetyllysineBy similarity
Modified residuei492 – 4921N6-acetyllysineBy similarity
Modified residuei500 – 5001N6-acetyllysineBy similarity
Modified residuei527 – 5271N6-acetyllysineBy similarity
Modified residuei541 – 5411N6-acetyllysineBy similarity
Cross-linki585 – 585Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei611 – 6111N6-acetyllysineBy similarity
Cross-linki646 – 646Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei709 – 7091Omega-N-methylated arginineBy similarity
Modified residuei715 – 7151Dimethylated arginine; alternateBy similarity
Modified residuei715 – 7151Omega-N-methylated arginine; alternateBy similarity
Modified residuei789 – 7891N6-acetyllysineBy similarity

Post-translational modificationi

Extensively phosphorylated.By similarity
Arg-709 and Arg-715 are dimethylated, probably to asymmetric dimethylarginine.By similarity
Citrullinated by PADI4.1 Publication

Keywords - PTMi

Acetylation, Citrullination, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8VEK3.
MaxQBiQ8VEK3.
PaxDbiQ8VEK3.
PRIDEiQ8VEK3.

PTM databases

iPTMnetiQ8VEK3.
PhosphoSiteiQ8VEK3.
SwissPalmiQ8VEK3.

Expressioni

Gene expression databases

BgeeiQ8VEK3.
GenevisibleiQ8VEK3. MM.

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 (By similarity). Interacts with CRY1. Interacts with UBQLN2 (By similarity).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Smarca4Q3TKT43EBI-529674,EBI-1210244

Protein-protein interaction databases

BioGridi206185. 10 interactions.
DIPiDIP-34257N.
IntActiQ8VEK3. 5 interactions.
STRINGi10090.ENSMUSP00000047571.

Structurei

3D structure databases

ProteinModelPortaliQ8VEK3.
SMRiQ8VEK3. Positions 262-470.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 4235SAPPROSITE-ProRule annotationAdd
BLAST
Domaini244 – 440197B30.2/SPRYPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni690 – 71526RNA-binding RGG-boxBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili626 – 65328Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 154153Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi679 – 76991Gly-richAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2242. Eukaryota.
ENOG410Y1WQ. LUCA.
GeneTreeiENSGT00390000020210.
HOGENOMiHOG000253920.
InParanoidiQ8VEK3.
KOiK12888.
OMAiFKRQMAD.
PhylomeDBiQ8VEK3.
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. 2 hits.
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]

Sequencei

Sequence statusi: Complete.

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

Q8VEK3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSPVNVKK LKVSELKEEL KKRRLSDKGL KADLMDRLQA ALDNEAGGRP
60 70 80 90 100
AMEPGNGSLD LGGDAAGRSG AGLEQEAAAG AEDDEEEEGI AALDGDQMEL
110 120 130 140 150
GEENGAAGAA DAGAMEEEEA ASEDENGDDQ GFQEGEDELG DEEEGAGDEN
160 170 180 190 200
GHGEQQSQPP AAAAQQQPSQ QRGAGKEAAG KSSGPTSLFA VTVAPPGARQ
210 220 230 240 250
GQQQAGGDGK TEQKGGDKKR GVKRPREDHG RGYFEYIEEN KYSRAKSPQP
260 270 280 290 300
PVEEEDEHFD DTVVCLDTYN CDLHFKISRD RLSASSLTME SFAFLWAGGR
310 320 330 340 350
ASYGVSKGKV CFEMKVTEKI PVRHLYTKDI DIHEVRIGWS LTTSGMLLGE
360 370 380 390 400
EEFSYGYSLK GIKTCNCETE DYGEKFDEND VITCFANFET DEVELSYAKN
410 420 430 440 450
GQDLGVAFKI SKEVLADRPL FPHVLCHNCA VEFNFGQKEK PYFPIPEDCT
460 470 480 490 500
FIQNVPLEDR VRGPKGPEEK KDCEVVMMIG LPGAGKTTWV TKHAAENPGK
510 520 530 540 550
YNILGTNTIM DKMMVAGFKK QMADTGKLNT LLQRAPQCLG KFIEIAARKK
560 570 580 590 600
RNFILDQTNV SAAAQRRKMC LFAGFQRKAV VVCPKDEDYK QRTQKKAEVE
610 620 630 640 650
GKDLPEHAVL KMKGNFTLPE VAECFDEITY VELQKEEAQK LLEQYKEESK
660 670 680 690 700
KALPPEKKQN TGSKKSNKNK SGKNQFNRGG GHRGRGGFNM RGGNFRGGAP
710 720 730 740 750
GNRGGYNRRG NMPQRGGGGG SGGIGYPYPR GPVFPGRGGY SNRGNYNRGG
760 770 780 790 800
MPNRGNYNQN FRGRGNNRGY KNQSQGYNQW QQGQFWGQKP WSQHYHQGYY
Length:800
Mass (Da):87,918
Last modified:March 1, 2002 - v1
Checksum:i2BA7C73043F847B2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK165844 mRNA. Translation: BAE38409.1.
CH466555 Genomic DNA. Translation: EDL13176.1.
BC018353 mRNA. Translation: AAH18353.1.
AF073991 Genomic DNA. Translation: AAD29847.1.
CCDSiCCDS35804.1.
RefSeqiNP_058085.2. NM_016805.2.
UniGeneiMm.482674.
Mm.86589.

Genome annotation databases

EnsembliENSMUST00000037748; ENSMUSP00000047571; ENSMUSG00000039630.
GeneIDi51810.
KEGGimmu:51810.
UCSCiuc011wxl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK165844 mRNA. Translation: BAE38409.1.
CH466555 Genomic DNA. Translation: EDL13176.1.
BC018353 mRNA. Translation: AAH18353.1.
AF073991 Genomic DNA. Translation: AAD29847.1.
CCDSiCCDS35804.1.
RefSeqiNP_058085.2. NM_016805.2.
UniGeneiMm.482674.
Mm.86589.

3D structure databases

ProteinModelPortaliQ8VEK3.
SMRiQ8VEK3. Positions 262-470.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi206185. 10 interactions.
DIPiDIP-34257N.
IntActiQ8VEK3. 5 interactions.
STRINGi10090.ENSMUSP00000047571.

PTM databases

iPTMnetiQ8VEK3.
PhosphoSiteiQ8VEK3.
SwissPalmiQ8VEK3.

Proteomic databases

EPDiQ8VEK3.
MaxQBiQ8VEK3.
PaxDbiQ8VEK3.
PRIDEiQ8VEK3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000037748; ENSMUSP00000047571; ENSMUSG00000039630.
GeneIDi51810.
KEGGimmu:51810.
UCSCiuc011wxl.1. mouse.

Organism-specific databases

CTDi3192.
MGIiMGI:1858195. Hnrnpu.

Phylogenomic databases

eggNOGiKOG2242. Eukaryota.
ENOG410Y1WQ. LUCA.
GeneTreeiENSGT00390000020210.
HOGENOMiHOG000253920.
InParanoidiQ8VEK3.
KOiK12888.
OMAiFKRQMAD.
PhylomeDBiQ8VEK3.
TreeFamiTF317301.

Enzyme and pathway databases

ReactomeiR-MMU-72163. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSiHnrnpu. mouse.
PROiQ8VEK3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VEK3.
GenevisibleiQ8VEK3. MM.

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. 2 hits.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. "hnRNP U is required for early embryonic development."
    Roshon M.J., DeGregori J., Ruley H.E.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 208-268.
  5. "Rhythmic SAF-A binding underlies circadian transcription of the Bmal1 gene."
    Onishi Y., Hanai S., Ohno T., Hara Y., Ishida N.
    Mol. Cell. Biol. 28:3477-3488(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. "Molecular characterization of Mybbp1a as a co-repressor on the Period2 promoter."
    Hara Y., Onishi Y., Oishi K., Miyazaki K., Fukamizu A., Ishida N.
    Nucleic Acids Res. 37:1115-1126(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CRY1.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Liver, Lung, Pancreas, Spleen and Testis.
  8. Cited for: CITRULLINATION AT ARG-231.

Entry informationi

Entry nameiHNRPU_MOUSE
AccessioniPrimary (citable) accession number: Q8VEK3
Secondary accession number(s): Q9R205
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: March 1, 2002
Last modified: June 8, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.