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Entry version 140 (02 Dec 2020)
Sequence version 1 (05 Jul 2004)
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Protein

Heterogeneous nuclear ribonucleoprotein U

Gene

Hnrnpu

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

DNA- and RNA-binding protein involved in several cellular processes such as nuclear chromatin organization, telomere-length regulation, transcription, mRNA alternative splicing and stability, Xist-mediated transcriptional silencing and mitotic cell progression. Plays a role in the regulation of interphase large-scale gene-rich chromatin organization through chromatin-associated RNAs (caRNAs) in a transcription-dependent manner, and thereby maintains genomic stability. Required for the localization of the long non-coding Xist RNA on the inactive chromosome X (Xi) and the subsequent initiation and maintenance of X-linked transcriptional gene silencing during X-inactivation (By similarity). Required for the topoisomerase TOP2A protein stability and activity in a RNA-dependent manner (PubMed:20554522). Plays a role as a RNA polymerase II (Pol II) holoenzyme transcription regulator. Promotes transcription initiation by direct association with the core-TFIIH basal transcription factor complex for the assembly of a functional pre-initiation complex with Pol II in a actin-dependent manner. Blocks Pol II transcription elongation activity by inhibiting the C-terminal domain (CTD) phosphorylation of Pol II and dissociates from Pol II pre-initiation complex prior to productive transcription elongation. Positively regulates CBX5-induced transcriptional gene silencing and retention of CBX5 in the nucleus. Negatively regulates glucocorticoid-mediated transcriptional activation. Key regulator of transcription initiation and elongation in embryonic stem cells upon leukemia inhibitory factor (LIF) signaling. Involved in the long non-coding RNA H19-mediated Pol II transcriptional repression. Participates in the circadian regulation of the core clock component ARNTL/BMAL1 transcription. Plays a role in the regulation of telomere length. Plays a role as a global pre-mRNA alternative splicing modulator by regulating U2 small nuclear ribonucleoprotein (snRNP) biogenesis. Plays a role in mRNA stability. Component of the CRD-mediated complex that promotes MYC mRNA stabilization. Enhances the expression of specific genes, such as tumor necrosis factor TNFA, by regulating mRNA stability, possibly through binding to the 3'-untranslated region (UTR). Plays a role in mitotic cell cycle regulation. Involved in the formation of stable mitotic spindle microtubules (MTs) attachment to kinetochore, spindle organization and chromosome congression. Phosphorylation at Ser-58 by PLK1 is required for chromosome alignement and segregation and progression through mitosis. Contributes also to the targeting of AURKA to mitotic spindle MTs (By similarity). Binds to double- and single-stranded DNA and RNA, poly(A), poly(C) and poly(G) oligoribonucleotides (PubMed:20554522). Binds to chromatin-associated RNAs (caRNAs) (By similarity). Associates with chromatin to scaffold/matrix attachment region (S/MAR) elements in DNA (PubMed:8509422). Associates with chromatin in a chromatin-associated RNAs (caRNAs)-dependent manner. Binds to the Xist RNA. Binds the long non-coding H19 RNA. Binds to SMN1/2 pre-mRNAs at G/U-rich regions. Binds to small nuclear RNAs (snRNAs). Binds to the 3'-UTR of TNFA mRNA. Binds (via RNA-binding RGG-box region) to the long non-coding Xist RNA; this binding is direct and bridges the Xist RNA and the inactive chromosome X (Xi). Also negatively regulates embryonic stem cell differentiation upon LIF signaling. Required for embryonic development (By similarity). Binds to brown fat long non-coding RNA 1 (Blnc1); facilitates the recruitment of Blnc1 by ZBTB7B required to drive brown and beige fat development and thermogenesis (By similarity).By similarity2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi478 – 485ATPSequence analysis8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, Chromatin regulator, Developmental protein, Repressor, Ribonucleoprotein
Biological processCell cycle, Cell division, Differentiation, Mitosis, mRNA processing, mRNA splicing, Transcription, Transcription regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-72163, mRNA Splicing - Major Pathway

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Heterogeneous nuclear ribonucleoprotein UImported
Short name:
hnRNP UImported
Alternative name(s):
SP1201 Publication
Scaffold-attachment factor ABy similarity
Short name:
SAF-ABy similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:HnrnpuImported
Synonyms:Hnrpu
ORF Names:rCG_20317
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 13
  • UP000234681 Componentsi: Chromosome 13, Unassembled WGS sequence

Organism-specific databases

Rat genome database

More...
RGDi
620372, Hnrnpu

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Nucleus, Spliceosome

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004422722 – 798Heterogeneous nuclear ribonucleoprotein UAdd BLAST797

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserineBy similarity1
Modified residuei4PhosphoserineBy similarity1
Modified residuei17N6-acetyllysineBy similarity1
Modified residuei21N6-acetyllysineBy similarity1
Modified residuei58PhosphoserineCombined sources1
Modified residuei179N6-acetyllysineBy similarity1
Modified residuei180ADP-ribosylserineBy similarity1
Modified residuei229CitrullineBy similarity1
Modified residuei239N6-acetyllysine; alternateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki239Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki239Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei240PhosphotyrosineBy similarity1
Modified residuei241PhosphoserineBy similarity1
Modified residuei245PhosphoserineBy similarity1
Modified residuei260PhosphothreonineBy similarity1
Modified residuei326N6-acetyllysineBy similarity1
Cross-linki469Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei490N6-acetyllysine; alternateBy similarity1
Cross-linki490Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei498N6-acetyllysine; alternateBy similarity1
Cross-linki498Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei506PhosphothreonineBy similarity1
Cross-linki510Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei525N6-acetyllysineBy similarity1
Modified residuei539N6-acetyllysine; alternateBy similarity1
Cross-linki539Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki548Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei556PhosphothreonineBy similarity1
Cross-linki583Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki600Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei609N6-acetyllysine; alternateBy similarity1
Cross-linki609Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki638Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki644Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei676Omega-N-methylarginineBy similarity1
Modified residuei689Asymmetric dimethylarginineBy similarity1
Modified residuei694Asymmetric dimethylarginineBy similarity1
Modified residuei701Asymmetric dimethylarginineBy similarity1
Modified residuei707Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei707Omega-N-methylarginine; alternateBy similarity1
Modified residuei713Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei713Omega-N-methylarginine; alternateBy similarity1
Modified residuei728Asymmetric dimethylarginineBy similarity1
Modified residuei735Asymmetric dimethylarginineBy similarity1
Modified residuei787N6-acetyllysine; alternateBy similarity1
Cross-linki787Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Cleaved at Asp-94 by CASP3 during T-cell apoptosis, resulting in a loss of DNA- and chromatin-binding activities.By similarity
Extensively phosphorylated. Phosphorylated on Ser-58 by PLK1 and dephosphorylated by protein phosphatase 2A (PP2A) in mitosis.By similarity
Arg-707 and Arg-713 are dimethylated, probably to asymmetric dimethylarginine (By similarity).By similarity
Citrullinated by PADI4.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei94 – 95Cleavage; by CASP3By similarity2

Keywords - PTMi

Acetylation, ADP-ribosylation, Citrullination, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q6IMY8

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q6IMY8

PRoteomics IDEntifications database

More...
PRIDEi
Q6IMY8

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q6IMY8

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000033790, Expressed in thymus and 21 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q6IMY8, baseline and differential

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Oligomer (via ATPase domain and RNA-binding RGG-box region); oligomerization occurs upon ATP-binding in a chromatin-associated RNAs (caRNAs)- and transcription-dependent manner and is required for chromatin decompaction. ATP hydrolysis is required to cycle from an oligomeric to monomeric state to compact chromatin.

Component of the coding region determinant (CRD)-mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. Identified in the spliceosome C complex.

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Associates with heterogeneous nuclear ribonucleoprotein (hnRNP) particles. Associates (via middle region) with the C-terminal domain (CTD) RNA polymerase II (Pol II) holoenzyme; this association occurs in a RNA-independent manner. Associates (via middle region) with the core-TFIIH basal transcription factor complex; this association inhibits the CTD phosphorylation of RNA polymerase II holoenzyme by downregulating TFIIH kinase activity. Associates with the telomerase holoenzyme complex. Associates with spindle microtubules (MTs) in a TPX2-dependent manner.

Interacts (via C-terminus) with actin; this interaction is direct and mediates association with the phosphorylated CTD of RNA polymerase II and is disrupted in presence of the long non-coding H19 RNA.

Interacts with AURKA.

Interacts (via C-terminus) with CBX5; this interaction is, at least in part, RNA-dependent.

Interacts with CR2.

Interacts with CRY1.

Interacts (via C-terminus) with EP300; this interaction enhances DNA-binding to nuclear scaffold/matrix attachment region (S/MAR) elements.

Interacts with ERBB4.

Interacts with GEMIN5.

Interacts with IGF2BP1.

Interacts with IGF2BP2 and IGF2BP3.

Interacts with NCL; this interaction occurs during mitosis.

Interacts (via C-terminus) with NR3C1 (via C-terminus).

Interacts with PLK1; this interaction induces phosphorylation of HNRNPU at Ser-58 in mitosis.

Interacts with POU3F4.

Interacts with SMARCA4; this interaction occurs in embryonic stem cells and stimulates global Pol II-mediated transcription (By similarity).

Interacts (via C-terminus) with TOP2A; this interaction protects the topoisomerase TOP2A from degradation and positively regulates the relaxation of supercoiled DNA by TOP2A in a RNA-dependent manner (PubMed:20554522).

Interacts with TPX2; this interaction recruits HNRNPU to spindle microtubules (MTs).

Interacts with UBQLN2 (By similarity).

Interacts (via RNA-binding RGG-box region) with ZBTB7B; the interaction facilitates the recruitment of long non-coding RNA Blnc1 by ZBTB7B (By similarity).

Interacts with ERCC6 (By similarity).

By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q6IMY8

Protein interaction database and analysis system

More...
IntActi
Q6IMY8, 6 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000046783

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini8 – 42SAPPROSITE-ProRule annotationBy similarityAdd BLAST35
Domaini242 – 438B30.2/SPRYPROSITE-ProRule annotationAdd BLAST197

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni462 – 646ATPase domainBy similarityAdd BLAST185
Regioni585 – 600Actin-bindingBy similarityAdd BLAST16
Regioni688 – 713RNA-binding RGG-boxBy similarityAdd BLAST26

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili624 – 651Sequence analysisAdd BLAST28

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi2 – 154Asp/Glu-rich (acidic)Add BLAST153
Compositional biasi85 – 88Poly-GluSequence analysis4
Compositional biasi116 – 119Poly-GluSequence analysis4
Compositional biasi677 – 767Gly-richPROSITE-ProRule annotationAdd BLAST91

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The SAP domain is necessary for specific binding to nuclear scaffold/matrix attachment region (S/MAR) elements in DNA. The RNA-binding RGG-box region is necessary for its association with inactive X chromosome (Xi) regions and to chromatin-associated RNAs (caRNAs). Both the DNA-binding domain SAP and the RNA-binding RGG-box region are necessary for the localization of Xist RNA on the Xi. The ATPase and RNA-binding RGG-box regions are necessary for oligomerization.By similarity

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2242, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156546

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_012140_1_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q6IMY8

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q6IMY8

TreeFam database of animal gene trees

More...
TreeFami
TF317301

Family and domain databases

Conserved Domains Database

More...
CDDi
cd12884, SPRY_hnRNP, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.720.30, 1 hit
2.60.120.920, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001870, B30.2/SPRY
IPR043136, B30.2/SPRY_sf
IPR013320, ConA-like_dom_sf
IPR026745, hnRNP_U
IPR027417, P-loop_NTPase
IPR003034, SAP_dom
IPR036361, SAP_dom_sf
IPR003877, SPRY_dom
IPR035778, SPRY_hnRNP_U

The PANTHER Classification System

More...
PANTHERi
PTHR12381:SF11, PTHR12381:SF11, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02037, SAP, 1 hit
PF00622, SPRY, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00513, SAP, 1 hit
SM00449, SPRY, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49899, SSF49899, 1 hit
SSF52540, SSF52540, 1 hit
SSF68906, SSF68906, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50188, B302_SPRY, 1 hit
PS50800, SAP, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q6IMY8-1 [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 AAAQQASQQR GPGKEAAGKS SGPTSLFAVT VAPPGARQGQ
210 220 230 240 250
QQAGGDGKTE QKAGDKKRGV KRPREDHGRG YFEYIEENKY SRAKSPQPPV
260 270 280 290 300
EEEDEHFDDT VVCLDTYNCD LHFKISRDRL SASSLTMESF AFLWAGGRAS
310 320 330 340 350
YGVSKGKVCF EMKVTEKIPV RHLYTKDIDI HEVRIGWSLT TSGMLLGEEE
360 370 380 390 400
FSYGYSLKGI KTCNCETEDY GEKFDENDVI TCFANFETDE VELSYAKNGQ
410 420 430 440 450
DLGVAFKISK EVLADRPLFP HVLCHNCAVE FNFGQKEKPY FPIPEDCTFI
460 470 480 490 500
QNVPLEDRVR GPKGPEEKKD CEVVMMIGLP GAGKTTWVTK HAAENPGKYN
510 520 530 540 550
ILGTNTIMDK MMVAGFKKQM ADTGKLNTLL QRAPQCLGKF IEIAARKKRN
560 570 580 590 600
FILDQTNVSA AAQRRKMCLF AGFQRKAVVV CPKDEDYKQR TQKKAEVEGK
610 620 630 640 650
DLPEHAVLKM KGNFTLPEVA ECFDEITYVE LQKEEAQKLL EQYKEESKKA
660 670 680 690 700
LPPEKKQNTG SKKSNKNKSG KNQFNRGGGH RGRGGFNMRG GNFRGGAPGN
710 720 730 740 750
RGGYNRRGNM PQRGGGGGSG GIGYPYPRGP VFPGRGGYSN RGNYNRGGMP
760 770 780 790
NRGNYNQNFR GRGNNRGYKN QSQGYNQWQQ GQFWGQKPWS QHYHQGYY
Length:798
Mass (Da):87,732
Last modified:July 5, 2004 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i638C059C3D602DE5
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2JZ52A0A0G2JZ52_RAT
Heterogeneous nuclear ribonucleopro...
Hnrnpu rCG_20317
803Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AABR07021872 Genomic DNA No translation available.
CH473985 Genomic DNA Translation: EDL94801.1
BC072529 mRNA Translation: AAH72529.1

NCBI Reference Sequences

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RefSeqi
NP_476480.2, NM_057139.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSRNOT00000044477; ENSRNOP00000046783; ENSRNOG00000033790

Database of genes from NCBI RefSeq genomes

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GeneIDi
117280

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:117280

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07021872 Genomic DNA No translation available.
CH473985 Genomic DNA Translation: EDL94801.1
BC072529 mRNA Translation: AAH72529.1
RefSeqiNP_476480.2, NM_057139.2

3D structure databases

Database of comparative protein structure models

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ModBasei
Search...

SWISS-MODEL Interactive Workspace

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SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

CORUMiQ6IMY8
IntActiQ6IMY8, 6 interactors
STRINGi10116.ENSRNOP00000046783

PTM databases

iPTMnetiQ6IMY8

Proteomic databases

jPOSTiQ6IMY8
PaxDbiQ6IMY8
PRIDEiQ6IMY8

Genome annotation databases

EnsembliENSRNOT00000044477; ENSRNOP00000046783; ENSRNOG00000033790
GeneIDi117280
KEGGirno:117280

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3192
RGDi620372, Hnrnpu

Phylogenomic databases

eggNOGiKOG2242, Eukaryota
GeneTreeiENSGT00940000156546
HOGENOMiCLU_012140_1_0_1
InParanoidiQ6IMY8
PhylomeDBiQ6IMY8
TreeFamiTF317301

Enzyme and pathway databases

ReactomeiR-RNO-72163, mRNA Splicing - Major Pathway

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q6IMY8

Gene expression databases

BgeeiENSRNOG00000033790, Expressed in thymus and 21 other tissues
ExpressionAtlasiQ6IMY8, baseline and differential

Family and domain databases

CDDicd12884, SPRY_hnRNP, 1 hit
Gene3Di1.10.720.30, 1 hit
2.60.120.920, 1 hit
InterProiView protein in InterPro
IPR001870, B30.2/SPRY
IPR043136, B30.2/SPRY_sf
IPR013320, ConA-like_dom_sf
IPR026745, hnRNP_U
IPR027417, P-loop_NTPase
IPR003034, SAP_dom
IPR036361, SAP_dom_sf
IPR003877, SPRY_dom
IPR035778, SPRY_hnRNP_U
PANTHERiPTHR12381:SF11, PTHR12381:SF11, 1 hit
PfamiView protein in Pfam
PF02037, SAP, 1 hit
PF00622, SPRY, 1 hit
SMARTiView protein in SMART
SM00513, SAP, 1 hit
SM00449, SPRY, 1 hit
SUPFAMiSSF49899, SSF49899, 1 hit
SSF52540, SSF52540, 1 hit
SSF68906, SSF68906, 1 hit
PROSITEiView protein in PROSITE
PS50188, B302_SPRY, 1 hit
PS50800, SAP, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHNRPU_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q6IMY8
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 22, 2017
Last sequence update: July 5, 2004
Last modified: December 2, 2020
This is version 140 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome
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