Product: hnRNP U Antibody
Catalog: AF6626
Description: Rabbit polyclonal antibody to hnRNP U
Application: WB ELISA(peptide)
Reactivity: Human, Mouse
Mol.Wt.: 91kD(Calculated).
Uniprot: Q00839
RRID: AB_2847349

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Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, ELISA(peptide) 1:20000-1:40000
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse
Clonality:
Polyclonal
Specificity:
hnRNP U Antibody detects endogenous levels of total hnRNP U.
RRID:
AB_2847349
Cite Format: Affinity Biosciences Cat# AF6626, RRID:AB_2847349.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

Heterogeneous nuclear ribonucleoprotein U; hnRNP U; hnRNP U protein; HNRNPU; hnRNPU protein; HNRPU; HNRPU_HUMAN; p120; p120 nuclear protein; pp120; SAF A; SAF-A; SAFA; Scaffold attachment factor A; U21.1;

Immunogens

Immunogen:

A synthesized peptide derived from human hnRNP U.

Uniprot:
Gene(ID):
Expression:
Q00839 HNRPU_HUMAN:

Widely expressed.

Sequence:
MSSSPVNVKKLKVSELKEELKKRRLSDKGLKAELMERLQAALDDEEAGGRPAMEPGNGSLDLGGDSAGRSGAGLEQEAAAGGDEEEEEEEEEEEGISALDGDQMELGEENGAAGAADSGPMEEEEAASEDENGDDQGFQEGEDELGDEEEGAGDENGHGEQQPQPPATQQQQPQQQRGAAKEAAGKSSGPTSLFAVTVAPPGARQGQQQAGGKKKAEGGGGGGRPGAPAAGDGKTEQKGGDKKRGVKRPREDHGRGYFEYIEENKYSRAKSPQPPVEEEDEHFDDTVVCLDTYNCDLHFKISRDRLSASSLTMESFAFLWAGGRASYGVSKGKVCFEMKVTEKIPVRHLYTKDIDIHEVRIGWSLTTSGMLLGEEEFSYGYSLKGIKTCNCETEDYGEKFDENDVITCFANFESDEVELSYAKNGQDLGVAFKISKEVLAGRPLFPHVLCHNCAVEFNFGQKEKPYFPIPEEYTFIQNVPLEDRVRGPKGPEEKKDCEVVMMIGLPGAGKTTWVTKHAAENPGKYNILGTNTIMDKMMVAGFKKQMADTGKLNTLLQRAPQCLGKFIEIAARKKRNFILDQTNVSAAAQRRKMCLFAGFQRKAVVVCPKDEDYKQRTQKKAEVEGKDLPEHAVLKMKGNFTLPEVAECFDEITYVELQKEEAQKLLEQYKEESKKALPPEKKQNTGSKKSNKNKSGKNQFNRGGGHRGRGGFNMRGGNFRGGAPGNRGGYNRRGNMPQRGGGGGGSGGIGYPYPRAPVFPGRGSYSNRGNYNRGGMPNRGNYNQNFRGRGNNRGYKNQSQGYNQWQQGQFWGQKPWSQHYHQGYY

PTMs - Q00839 As Substrate

Site PTM Type Enzyme
S2 Acetylation
S2 Phosphorylation
S3 Phosphorylation
S4 Phosphorylation
K9 Acetylation
K12 Ubiquitination
S14 Phosphorylation
K17 Acetylation
K17 Sumoylation
K17 Ubiquitination
K21 Acetylation
S26 Phosphorylation
K28 Acetylation
K28 Ubiquitination
K31 Acetylation
K31 Ubiquitination
R50 Methylation
S59 Phosphorylation P78527 (PRKDC) , P53350 (PLK1)
S66 Phosphorylation
K181 Acetylation
K181 Ubiquitination
K186 Acetylation
K186 Ubiquitination
S187 Phosphorylation
S188 Phosphorylation
T191 Phosphorylation
S192 Phosphorylation
K213 Acetylation
K215 Methylation
R224 Methylation
K234 Acetylation
K234 Ubiquitination
R255 Methylation
Y257 Phosphorylation
Y260 Phosphorylation
K265 Acetylation
K265 Sumoylation
K265 Ubiquitination
Y266 Phosphorylation
S267 Phosphorylation
S271 Phosphorylation
T286 Phosphorylation
T292 Phosphorylation
Y293 Phosphorylation
Y327 Phosphorylation
S330 Phosphorylation
K333 Ubiquitination
K339 Acetylation
K339 Ubiquitination
K343 Acetylation
K343 Ubiquitination
K352 Acetylation
K352 Ubiquitination
K387 Ubiquitination
C389 S-Nitrosylation
C391 S-Nitrosylation
K423 Ubiquitination
K433 Ubiquitination
S435 Phosphorylation
K436 Ubiquitination
K464 Acetylation
K464 Ubiquitination
Y466 Phosphorylation
Y473 Phosphorylation
T474 Phosphorylation
K489 Ubiquitination
C497 S-Nitrosylation
K510 Ubiquitination
K516 Acetylation
K516 Methylation
K516 Ubiquitination
K524 Acetylation
K524 Sumoylation
K524 Ubiquitination
Y525 Phosphorylation
T532 Phosphorylation
K536 Ubiquitination
K543 Acetylation
K543 Methylation
K543 Ubiquitination
K544 Acetylation
K544 Methylation
K544 Ubiquitination
T549 Phosphorylation
K551 Acetylation
K551 Ubiquitination
T554 Phosphorylation
C562 S-Nitrosylation
K565 Acetylation
K565 Ubiquitination
R572 Methylation
R575 Methylation
T582 Phosphorylation
S585 Phosphorylation
K592 Ubiquitination
C594 S-Nitrosylation
K602 Ubiquitination
C607 S-Nitrosylation
K609 Acetylation
K609 Sumoylation
K609 Ubiquitination
Y613 Phosphorylation
K614 Acetylation
K614 Ubiquitination
K619 Ubiquitination
K626 Acetylation
K626 Ubiquitination
K635 Acetylation
K635 Sumoylation
K635 Ubiquitination
K637 Ubiquitination
T653 Phosphorylation
Y654 Phosphorylation
K659 Ubiquitination
K664 Sumoylation
K664 Ubiquitination
Y669 Phosphorylation
K670 Acetylation
K670 Methylation
K670 Sumoylation
K670 Ubiquitination
S673 Phosphorylation
K674 Acetylation
K674 Ubiquitination
K675 Ubiquitination
S690 Phosphorylation
R702 Methylation
R707 Methylation
R709 Methylation
R715 Methylation
R720 Methylation
R727 Methylation
Y730 Phosphorylation
R732 Methylation
R733 Methylation
R739 Methylation
Y753 Phosphorylation
R755 Methylation
R762 Methylation
R768 Methylation
R773 Methylation
R779 Methylation
R787 Methylation
R789 Methylation
R793 Methylation
S799 Phosphorylation
Y802 Phosphorylation
K814 Acetylation
K814 Ubiquitination
S817 Phosphorylation
Y820 Phosphorylation
Y824 Phosphorylation
Y825 Phosphorylation

Research Backgrounds

Function:

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). 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 (By similarity). 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 (By similarity). 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-59 by PLK1 is required for chromosome alignement and segregation and progression through mitosis. Contributes also to the targeting of AURKA to mitotic spindle MTs. Binds to double- and single-stranded DNA and RNA, poly(A), poly(C) and poly(G) oligoribonucleotides. Binds to chromatin-associated RNAs (caRNAs). Associates with chromatin to scaffold/matrix attachment region (S/MAR) elements 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) (By similarity). Also negatively regulates embryonic stem cell differentiation upon LIF signaling (By similarity). 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).

(Microbial infection) Negatively regulates immunodeficiency virus type 1 (HIV-1) replication by preventing the accumulation of viral mRNA transcripts in the cytoplasm.

PTMs:

Cleaved at Asp-100 by CASP3 during T-cell apoptosis, resulting in a loss of DNA- and chromatin-binding activities.

Extensively phosphorylated. Phosphorylated on Ser-59 by PLK1 and dephosphorylated by protein phosphatase 2A (PP2A) in mitosis.

Arg-739 is dimethylated, probably to asymmetric dimethylarginine (Ref.8). Arg-733 is dimethylated, probably to asymmetric dimethylarginine (By similarity).

Citrullinated by PADI4.

Subcellular Location:

Nucleus. Nucleus matrix. Chromosome. Nucleus speckle. Cytoplasm>Cytoskeleton>Microtubule organizing center>Centrosome. Chromosome>Centromere>Kinetochore. Cytoplasm>Cytoskeleton>Spindle. Cytoplasm>Cytoskeleton>Spindle pole. Midbody. Cytoplasm. Cell surface. Cytoplasmic granule.
Note: Localizes at inactive X chromosome (Xi) regions (PubMed:11003645, PubMed:14608463, PubMed:15563465). Localizes in the nucleus during interphase (PubMed:21242313). At metaphase, localizes with mitotic spindle microtubules (MTs) (PubMed:21242313). At anaphase, localizes in the mitotic spindle midzone (PubMed:21242313). Localizes in spindle MTs proximal to spindle poles in a TPX2- and AURKA-dependent manner (PubMed:21242313). The Ser-59 phosphorylated form localizes to centrosomes during prophase and metaphase, to mitotic spindles in anaphase and to the midbody during cytokinesis (PubMed:25986610). Colocalizes with SMARCA4 in the nucleus (By similarity). Colocalizes with CBX5 in the nucleus (PubMed:19617346). Colocalizes with NR3C1 in nuclear speckles (PubMed:9353307). Localized in cytoplasmic ribonucleoprotein (RNP) granules containing untranslated mRNAs (PubMed:17289661).

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Widely expressed.

Subunit Structure:

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 (By similarity). 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-59 in mitosis. Interacts with POU3F4. Interacts with SMARCA4; this interaction occurs in embryonic stem cells and stimulates global Pol II-mediated transcription. 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 (By similarity). Interacts with TPX2; this interaction recruits HNRNPU to spindle microtubules (MTs). Interacts with UBQLN2. 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.

(Microbial infection) Interacts with HIV-1 protein Rev.

Family&Domains:

The SAP domain is necessary for specific binding to nuclear scaffold/matrix attachment region (S/MAR) elements in DNA (PubMed:9405365, PubMed:11003645). The RNA-binding RGG-box region is necessary for its association with inactive X chromosome (Xi) regions and to chromatin-associated RNAs (caRNAs) (PubMed:14608463, PubMed:28622508). Both the DNA-binding domain SAP and the RNA-binding RGG-box region are necessary for the localization of Xist RNA on the Xi (By similarity). The ATPase and RNA-binding RGG-box regions are necessary for oligomerization (PubMed:28622508).

Research Fields

· Genetic Information Processing > Transcription > Spliceosome.

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