Search Results

Overview

Uniprot ID	Q00839
Protein Name	Heterogeneous nuclear ribonucleoprotein U
Gene Name	HNRNPU
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
12	PVNVKKLKVSELKEE
17	KLKVSELKEELKKRR
181	QQQRGAAKEAAGKSS
186	AAKEAAGKSSGPTSL
21	SELKEELKKRRLSDK
213	GQQQAGGKKKAEGGG
215	QQAGGKKKAEGGGGG
22	ELKEELKKRRLSDKG
234	APAAGDGKTEQKGGD
265	FEYIEENKYSRAKSP
28	KKRRLSDKGLKAELM
31	RLSDKGLKAELMERL
333	SYGVSKGKVCFEMKV
343	FEMKVTEKIPVRHLY
352	PVRHLYTKDIDIHEV
436	GVAFKISKEVLAGRP
489	EDRVRGPKGPEEKKD
495	PKGPEEKKDCEVVMM
516	GKTTWVTKHAAENPG
543	KMMVAGFKKQMADTG
544	MMVAGFKKQMADTGK
565	RAPQCLGKFIEIAAR
592	SAAAQRRKMCLFAGF
602	LFAGFQRKAVVVCPK
609	KAVVVCPKDEDYKQR
626	KKAEVEGKDLPEHAV
635	LPEHAVLKMKGNFTL
637	EHAVLKMKGNFTLPE
670	QKLLEQYKEESKKAL
682	KALPPEKKQNTGSKK
9	SSSPVNVKKLKVSEL

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 (PubMed:10490622, PubMed:18082603, PubMed:19029303, PubMed:22325991, PubMed:25986610, PubMed:28622508). 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 (PubMed:1324173, PubMed:28622508, PubMed:8174554). 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 (PubMed:10490622, PubMed:15711563, PubMed:19617346, PubMed:23811339, PubMed:8174554, PubMed:9353307). 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 (PubMed:10490622, PubMed:15711563). 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 (PubMed:10490622). Positively regulates CBX5-induced transcriptional gene silencing and retention of CBX5 in the nucleus (PubMed:19617346). Negatively regulates glucocorticoid-mediated transcriptional activation (PubMed:9353307). 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 (PubMed:23811339). Participates in the circadian regulation of the core clock component BMAL1 transcription (By similarity). Plays a role in the regulation of telomere length (PubMed:18082603). Plays a role as a global pre-mRNA alternative splicing modulator by regulating U2 small nuclear ribonucleoprotein (snRNP) biogenesis (PubMed:22325991). Plays a role in mRNA stability (PubMed:17174306, PubMed:17289661, PubMed:19029303). Component of the CRD-mediated complex that promotes MYC mRNA stabilization (PubMed:19029303). 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) (PubMed:17174306). Plays a role in mitotic cell cycle regulation (PubMed:21242313, PubMed:25986610). Involved in the formation of stable mitotic spindle microtubules (MTs) attachment to kinetochore, spindle organization and chromosome congression (PubMed:21242313). Phosphorylation at Ser-59 by PLK1 is required for chromosome alignement and segregation and progression through mitosis (PubMed:25986610). Also contributes to the targeting of AURKA to mitotic spindle MTs (PubMed:21242313). Binds to double- and single-stranded DNA and RNA, poly(A), poly(C) and poly(G) oligoribonucleotides (PubMed:1628625, PubMed:8068679, PubMed:8174554, PubMed:9204873, PubMed:9405365). Binds to chromatin-associated RNAs (caRNAs) (PubMed:28622508). Associates with chromatin to scaffold/matrix attachment region (S/MAR) elements in a chromatin-associated RNAs (caRNAs)-dependent manner (PubMed:10671544, PubMed:11003645, PubMed:11909954, PubMed:1324173, PubMed:28622508, PubMed:7509195, PubMed:9204873, PubMed:9405365). Binds to the Xist RNA (PubMed:26244333). Binds the long non-coding H19 RNA (PubMed:23811339). Binds to SMN1/2 pre-mRNAs at G/U-rich regions (PubMed:22325991). Binds to small nuclear RNAs (snRNAs) (PubMed:22325991). Binds to the 3'-UTR of TNFA mRNA (PubMed:17174306). 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)

Protein Sequence

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

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0071013	catalytic step 2 spliceosome
Cellular Component	GO:0009986	cell surface
Cellular Component	GO:0005813	centrosome
Cellular Component	GO:0070937	CRD-mediated mRNA stability complex
Cellular Component	GO:0036464	cytoplasmic ribonucleoprotein granule
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0030425	dendrite
Cellular Component	GO:0098577	inactive sex chromosome
Cellular Component	GO:0000776	kinetochore
Cellular Component	GO:0016020	membrane
Cellular Component	GO:0030496	midbody
Cellular Component	GO:0072686	mitotic spindle
Cellular Component	GO:1990498	mitotic spindle microtubule
Cellular Component	GO:1990023	mitotic spindle midzone
Cellular Component	GO:0000228	nuclear chromosome
Cellular Component	GO:0016363	nuclear matrix
Cellular Component	GO:0016607	nuclear speck
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0005634	nucleus
Cellular Component	GO:0032991	protein-containing complex
Cellular Component	GO:1990904	ribonucleoprotein complex
Cellular Component	GO:0000922	spindle pole
Cellular Component	GO:0005697	telomerase holoenzyme complex
Molecular Function	GO:0003779	actin binding
Molecular Function	GO:0005524	ATP binding
Molecular Function	GO:0003682	chromatin binding
Molecular Function	GO:0031490	chromatin DNA binding
Molecular Function	GO:0003677	DNA binding
Molecular Function	GO:0003690	double-stranded DNA binding
Molecular Function	GO:0003725	double-stranded RNA binding
Molecular Function	GO:0042802	identical protein binding
Molecular Function	GO:0106222	lncRNA binding
Molecular Function	GO:0003730	mRNA 3'-UTR binding
Molecular Function	GO:0034584	piRNA binding
Molecular Function	GO:0008143	poly(A) binding
Molecular Function	GO:0017130	poly(C) RNA binding
Molecular Function	GO:0034046	poly(G) binding
Molecular Function	GO:0036002	pre-mRNA binding
Molecular Function	GO:1990841	promoter-specific chromatin binding
Molecular Function	GO:0044877	protein-containing complex binding
Molecular Function	GO:0043021	ribonucleoprotein complex binding
Molecular Function	GO:0003723	RNA binding
Molecular Function	GO:0099122	RNA polymerase II C-terminal domain binding
Molecular Function	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding
Molecular Function	GO:0000993	RNA polymerase II complex binding
Molecular Function	GO:1990837	sequence-specific double-stranded DNA binding
Molecular Function	GO:0003697	single-stranded DNA binding
Molecular Function	GO:0003727	single-stranded RNA binding
Molecular Function	GO:0017069	snRNA binding
Molecular Function	GO:0070034	telomerase RNA binding
Molecular Function	GO:0001097	TFIIH-class transcription factor complex binding
Molecular Function	GO:0003714	transcription corepressor activity
Biological Process	GO:1990845	adaptive thermogenesis
Biological Process	GO:0000380	alternative mRNA splicing, via spliceosome
Biological Process	GO:0051301	cell division
Biological Process	GO:0071385	cellular response to glucocorticoid stimulus
Biological Process	GO:1990830	cellular response to leukemia inhibitory factor
Biological Process	GO:0006325	chromatin organization
Biological Process	GO:0032922	circadian regulation of gene expression
Biological Process	GO:0070934	CRD-mediated mRNA stabilization
Biological Process	GO:0098963	dendritic transport of messenger ribonucleoprotein complex
Biological Process	GO:0006351	DNA-templated transcription
Biological Process	GO:0009048	dosage compensation by inactivation of X chromosome
Biological Process	GO:0051457	maintenance of protein location in nucleus
Biological Process	GO:0000398	mRNA splicing, via spliceosome
Biological Process	GO:0048255	mRNA stabilization
Biological Process	GO:0033673	negative regulation of kinase activity
Biological Process	GO:1900152	negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay
Biological Process	GO:2000737	negative regulation of stem cell differentiation
Biological Process	GO:0032211	negative regulation of telomere maintenance via telomerase
Biological Process	GO:0000122	negative regulation of transcription by RNA polymerase II
Biological Process	GO:0034244	negative regulation of transcription elongation by RNA polymerase II
Biological Process	GO:0001649	osteoblast differentiation
Biological Process	GO:1902425	positive regulation of attachment of mitotic spindle microtubules to kinetochore
Biological Process	GO:0090336	positive regulation of brown fat cell differentiation
Biological Process	GO:2000767	positive regulation of cytoplasmic translation
Biological Process	GO:2000373	positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity
Biological Process	GO:2000648	positive regulation of stem cell proliferation
Biological Process	GO:0045944	positive regulation of transcription by RNA polymerase II
Biological Process	GO:1902889	protein localization to spindle microtubule
Biological Process	GO:0060816	random inactivation of X chromosome
Biological Process	GO:0000381	regulation of alternative mRNA splicing, via spliceosome
Biological Process	GO:1902275	regulation of chromatin organization
Biological Process	GO:0007346	regulation of mitotic cell cycle
Biological Process	GO:1901673	regulation of mitotic spindle assembly
Biological Process	GO:0031048	regulatory ncRNA-mediated heterochromatin formation
Biological Process	GO:1990280	RNA localization to chromatin
Biological Process	GO:0006396	RNA processing

Reference

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[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[4] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[5] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[6] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[7] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[8] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[9] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[10] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[11] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.