产品: | hnRNP U 抗体 |
货号: | AF6626 |
描述: | Rabbit polyclonal antibody to hnRNP U |
应用: | WB ELISA(peptide) |
反应: | Human, Mouse |
分子量: | 91kD(Calculated). |
蛋白号: | Q00839 |
RRID: | AB_2847349 |
产品描述
*The optimal dilutions should be determined by the end user.
*Tips:
WB: 适用于变性蛋白样本的免疫印迹检测. IHC: 适用于组织样本的石蜡(IHC-p)或冰冻(IHC-f)切片样本的免疫组化/荧光检测. IF/ICC: 适用于细胞样本的荧光检测. ELISA(peptide): 适用于抗原肽的ELISA检测.
引用格式: Affinity Biosciences Cat# AF6626, RRID:AB_2847349.
展开/折叠
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;
抗原和靶标
A synthesized peptide derived from human hnRNP U.
- Q00839 HNRPU_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MSSSPVNVKKLKVSELKEELKKRRLSDKGLKAELMERLQAALDDEEAGGRPAMEPGNGSLDLGGDSAGRSGAGLEQEAAAGGDEEEEEEEEEEEGISALDGDQMELGEENGAAGAADSGPMEEEEAASEDENGDDQGFQEGEDELGDEEEGAGDENGHGEQQPQPPATQQQQPQQQRGAAKEAAGKSSGPTSLFAVTVAPPGARQGQQQAGGKKKAEGGGGGGRPGAPAAGDGKTEQKGGDKKRGVKRPREDHGRGYFEYIEENKYSRAKSPQPPVEEEDEHFDDTVVCLDTYNCDLHFKISRDRLSASSLTMESFAFLWAGGRASYGVSKGKVCFEMKVTEKIPVRHLYTKDIDIHEVRIGWSLTTSGMLLGEEEFSYGYSLKGIKTCNCETEDYGEKFDENDVITCFANFESDEVELSYAKNGQDLGVAFKISKEVLAGRPLFPHVLCHNCAVEFNFGQKEKPYFPIPEEYTFIQNVPLEDRVRGPKGPEEKKDCEVVMMIGLPGAGKTTWVTKHAAENPGKYNILGTNTIMDKMMVAGFKKQMADTGKLNTLLQRAPQCLGKFIEIAARKKRNFILDQTNVSAAAQRRKMCLFAGFQRKAVVVCPKDEDYKQRTQKKAEVEGKDLPEHAVLKMKGNFTLPEVAECFDEITYVELQKEEAQKLLEQYKEESKKALPPEKKQNTGSKKSNKNKSGKNQFNRGGGHRGRGGFNMRGGNFRGGAPGNRGGYNRRGNMPQRGGGGGGSGGIGYPYPRAPVFPGRGSYSNRGNYNRGGMPNRGNYNQNFRGRGNNRGYKNQSQGYNQWQQGQFWGQKPWSQHYHQGYY
翻译修饰 - Q00839 作为底物
Site | PTM Type | Enzyme | Source |
---|---|---|---|
S2 | Acetylation | Uniprot | |
S2 | Phosphorylation | Uniprot | |
S3 | Phosphorylation | Uniprot | |
S4 | Phosphorylation | Uniprot | |
K9 | Acetylation | Uniprot | |
K12 | Ubiquitination | Uniprot | |
S14 | Phosphorylation | Uniprot | |
K17 | Acetylation | Uniprot | |
K17 | Sumoylation | Uniprot | |
K17 | Ubiquitination | Uniprot | |
K21 | Acetylation | Uniprot | |
S26 | Phosphorylation | Uniprot | |
K28 | Acetylation | Uniprot | |
K28 | Ubiquitination | Uniprot | |
K31 | Acetylation | Uniprot | |
K31 | Ubiquitination | Uniprot | |
R50 | Methylation | Uniprot | |
S59 | Phosphorylation | P78527 (PRKDC) , P53350 (PLK1) | Uniprot |
S66 | Phosphorylation | Uniprot | |
K181 | Acetylation | Uniprot | |
K181 | Ubiquitination | Uniprot | |
K186 | Acetylation | Uniprot | |
K186 | Ubiquitination | Uniprot | |
S187 | Phosphorylation | Uniprot | |
S188 | Phosphorylation | Uniprot | |
T191 | Phosphorylation | Uniprot | |
S192 | Phosphorylation | Uniprot | |
K213 | Acetylation | Uniprot | |
K215 | Methylation | Uniprot | |
R224 | Methylation | Uniprot | |
K234 | Acetylation | Uniprot | |
K234 | Ubiquitination | Uniprot | |
R255 | Methylation | Uniprot | |
Y257 | Phosphorylation | Uniprot | |
Y260 | Phosphorylation | Uniprot | |
K265 | Acetylation | Uniprot | |
K265 | Sumoylation | Uniprot | |
K265 | Ubiquitination | Uniprot | |
Y266 | Phosphorylation | Uniprot | |
S267 | Phosphorylation | Uniprot | |
S271 | Phosphorylation | Uniprot | |
T286 | Phosphorylation | Uniprot | |
T292 | Phosphorylation | Uniprot | |
Y293 | Phosphorylation | Uniprot | |
Y327 | Phosphorylation | Uniprot | |
S330 | Phosphorylation | Uniprot | |
K333 | Ubiquitination | Uniprot | |
K339 | Acetylation | Uniprot | |
K339 | Ubiquitination | Uniprot | |
K343 | Acetylation | Uniprot | |
K343 | Ubiquitination | Uniprot | |
K352 | Acetylation | Uniprot | |
K352 | Ubiquitination | Uniprot | |
K387 | Ubiquitination | Uniprot | |
C389 | S-Nitrosylation | Uniprot | |
C391 | S-Nitrosylation | Uniprot | |
K423 | Ubiquitination | Uniprot | |
K433 | Ubiquitination | Uniprot | |
S435 | Phosphorylation | Uniprot | |
K436 | Ubiquitination | Uniprot | |
K464 | Acetylation | Uniprot | |
K464 | Ubiquitination | Uniprot | |
Y466 | Phosphorylation | Uniprot | |
Y473 | Phosphorylation | Uniprot | |
T474 | Phosphorylation | Uniprot | |
K489 | Ubiquitination | Uniprot | |
C497 | S-Nitrosylation | Uniprot | |
K510 | Ubiquitination | Uniprot | |
K516 | Acetylation | Uniprot | |
K516 | Methylation | Uniprot | |
K516 | Ubiquitination | Uniprot | |
K524 | Acetylation | Uniprot | |
K524 | Sumoylation | Uniprot | |
K524 | Ubiquitination | Uniprot | |
Y525 | Phosphorylation | Uniprot | |
T532 | Phosphorylation | Uniprot | |
K536 | Ubiquitination | Uniprot | |
K543 | Acetylation | Uniprot | |
K543 | Methylation | Uniprot | |
K543 | Ubiquitination | Uniprot | |
K544 | Acetylation | Uniprot | |
K544 | Methylation | Uniprot | |
K544 | Ubiquitination | Uniprot | |
T549 | Phosphorylation | Uniprot | |
K551 | Acetylation | Uniprot | |
K551 | Ubiquitination | Uniprot | |
T554 | Phosphorylation | Uniprot | |
C562 | S-Nitrosylation | Uniprot | |
K565 | Acetylation | Uniprot | |
K565 | Ubiquitination | Uniprot | |
R572 | Methylation | Uniprot | |
R575 | Methylation | Uniprot | |
T582 | Phosphorylation | Uniprot | |
S585 | Phosphorylation | Uniprot | |
K592 | Ubiquitination | Uniprot | |
C594 | S-Nitrosylation | Uniprot | |
K602 | Ubiquitination | Uniprot | |
C607 | S-Nitrosylation | Uniprot | |
K609 | Acetylation | Uniprot | |
K609 | Sumoylation | Uniprot | |
K609 | Ubiquitination | Uniprot | |
Y613 | Phosphorylation | Uniprot | |
K614 | Acetylation | Uniprot | |
K614 | Ubiquitination | Uniprot | |
K619 | Ubiquitination | Uniprot | |
K626 | Acetylation | Uniprot | |
K626 | Ubiquitination | Uniprot | |
K635 | Acetylation | Uniprot | |
K635 | Sumoylation | Uniprot | |
K635 | Ubiquitination | Uniprot | |
K637 | Ubiquitination | Uniprot | |
T653 | Phosphorylation | Uniprot | |
Y654 | Phosphorylation | Uniprot | |
K659 | Ubiquitination | Uniprot | |
K664 | Sumoylation | Uniprot | |
K664 | Ubiquitination | Uniprot | |
Y669 | Phosphorylation | Uniprot | |
K670 | Acetylation | Uniprot | |
K670 | Methylation | Uniprot | |
K670 | Sumoylation | Uniprot | |
K670 | Ubiquitination | Uniprot | |
S673 | Phosphorylation | Uniprot | |
K674 | Acetylation | Uniprot | |
K674 | Ubiquitination | Uniprot | |
K675 | Ubiquitination | Uniprot | |
S690 | Phosphorylation | Uniprot | |
R702 | Methylation | Uniprot | |
R707 | Methylation | Uniprot | |
R709 | Methylation | Uniprot | |
R715 | Methylation | Uniprot | |
R720 | Methylation | Uniprot | |
R727 | Methylation | Uniprot | |
Y730 | Phosphorylation | Uniprot | |
R732 | Methylation | Uniprot | |
R733 | Methylation | Uniprot | |
R739 | Methylation | Uniprot | |
Y753 | Phosphorylation | Uniprot | |
R755 | Methylation | Uniprot | |
R762 | Methylation | Uniprot | |
R768 | Methylation | Uniprot | |
R773 | Methylation | Uniprot | |
R779 | Methylation | Uniprot | |
R787 | Methylation | Uniprot | |
R789 | Methylation | Uniprot | |
R793 | Methylation | Uniprot | |
S799 | Phosphorylation | Uniprot | |
Y802 | Phosphorylation | Uniprot | |
K814 | Acetylation | Uniprot | |
K814 | Ubiquitination | Uniprot | |
S817 | Phosphorylation | Uniprot | |
Y820 | Phosphorylation | Uniprot | |
Y824 | Phosphorylation | Uniprot | |
Y825 | Phosphorylation | Uniprot |
研究背景
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.
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.
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).
Widely expressed.
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.
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).
研究领域
· Genetic Information Processing > Transcription > Spliceosome.
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