HNRNPU
entrez
3192
canonical
uniprot
Q00839
canonical
ensembl
ENSG00000153187
resolver
ensp
ENSP00000393151
resolver
ensp
ENSP00000491215
resolver
genesymbol
HNRNPU
resolver
genesymbol_syn
C1orf199
resolver
genesymbol_syn
HNRPU
resolver
genesymbol_syn
SAFA
resolver
genesymbol_syn
U21.1
resolver
hgnc
HGNC:5048
resolver
uniprot
O75507
resolver
uniprot
Q8N174
resolver
uniprot
Q96BA7
resolver
uniprot
Q96HY9
resolver
uniprot
Q9BQ09
resolver
uniprot_entry
HNRPU_HUMAN
resolver
uniprot_entry
Q96BA7_HUMAN
resolver
uniprot_sec
O75507
resolver
uniprot_sec
Q8N174
resolver
uniprot_sec
Q96HY9
resolver
uniprot_sec
Q9BQ09
resolver
amino_acid_sequence
MSSSPVNVKKLKVSELKEELKKRRLSDKGLKAELMERLQAALDDEEAGGRPAMEPGNGSLDLGGDSAGRSGAGLEQEAAAGGDEEEEEEEEEEEGISALDGDQMELGEENGAAGAADSGPMEEEEAASEDENGDDQGFQEGEDELGDEEEGAGDENGHGEQQPQPPATQQQQPQQQRGAAKEAAGKSSGPTSLFAVTVAPPGARQGQQQAGGKKKAEGGGGGGRPGAPAAGDGKTEQKGGDKKRGVKRPREDHGRGYFEYIEENKYSRAKSPQPPVEEEDEHFDDTVVCLDTYNCDLHFKISRDRLSASSLTMESFAFLWAGGRASYGVSKGKVCFEMKVTEKIPVRHLYTKDIDIHEVRIGWSLTTSGMLLGEEEFSYGYSLKGIKTCNCETEDYGEKFDENDVITCFANFESDEVELSYAKNGQDLGVAFKISKEVLAGRPLFPHVLCHNCAVEFNFGQKEKPYFPIPEEYTFIQNVPLEDRVRGPKGPEEKKDCEVVMMIGLPGAGKTTWVTKHAAENPGKYNILGTNTIMDKMMVAGFKKQMADTGKLNTLLQRAPQCLGKFIEIAARKKRNFILDQTNVSAAAQRRKMCLFAGFQRKAVVVCPKDEDYKQRTQKKAEVEGKDLPEHAVLKMKGNFTLPEVAECFDEITYVELQKEEAQKLLEQYKEESKKALPPEKKQNTGSKKSNKNKSGKNQFNRGGGHRGRGGFNMRGGNFRGGAPGNRGGYNRRGNMPQRGGGGGGSGGIGYPYPRAPVFPGRGSYSNRGNYNRGGMPNRGNYNQNFRGRGNNRGYKNQSQGYNQWQQGQFWGQKPWSQHYHQGYY
uniprot
proteins
disease_involvement
DISEASE: Developmental and epileptic encephalopathy 54 (DEE54) [MIM:617391]: A form of epileptic encephalopathy, a heterogeneous group of severe early-onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. {ECO:0000269|PubMed:23708187, ECO:0000269|PubMed:25356899}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
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). {ECO:0000250|UniProtKB:Q8VEK3, ECO:0000269|PubMed:10490622, ECO:0000269|PubMed:10671544, ECO:0000269|PubMed:11003645, ECO:0000269|PubMed:11909954, ECO:0000269|PubMed:1324173, ECO:0000269|PubMed:15711563, ECO:0000269|PubMed:1628625, ECO:0000269|PubMed:17174306, ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:18082603, ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:19617346, ECO:0000269|PubMed:21242313, ECO:0000269|PubMed:22325991, ECO:0000269|PubMed:23811339, ECO:0000269|PubMed:25986610, ECO:0000269|PubMed:26244333, ECO:0000269|PubMed:28622508, ECO:0000269|PubMed:7509195, ECO:0000269|PubMed:8068679, ECO:0000269|PubMed:8174554, ECO:0000269|PubMed:9204873, ECO:0000269|PubMed:9353307, ECO:0000269|PubMed:9405365}.; FUNCTION: (Microbial infection) Negatively regulates immunodeficiency virus type 1 (HIV-1) replication by preventing the accumulation of viral mRNA transcripts in the cytoplasm. {ECO:0000269|PubMed:16916646}.
uniprot
proteins
mass_dalton
90584
uniprot
proteins
mutagenesis
MUTAGEN 59; /note="S->A: No change in interaction with AURKA, PLK1 and TPX2. Increases mitotic chromosome misalignment and chromosome segregation defects and time required to progress through mitosis."; /evidence="ECO:0000269|PubMed:17081983"; MUTAGEN 59; /note="S->E: Increases mitotic chromosome misalignment and chromosome segregation defects and decreases time required to progress through mitosis."; /evidence="ECO:0000269|PubMed:17081983"; MUTAGEN 100; /note="D->A: No cleavage by caspases during apoptosis. Inhibits CASP3-induced cleavage in vitro."; /evidence="ECO:0000269|PubMed:10671544"; MUTAGEN 616..620; /note="RTQKK->ATQAA: Loss of actin-binding."; /evidence="ECO:0000269|PubMed:15711563
uniprot
proteins
post_translational_modification
PTM: Cleaved at Asp-100 by CASP3 during T-cell apoptosis, resulting in a loss of DNA- and chromatin-binding activities (PubMed:10671544, PubMed:9405365). {ECO:0000269|PubMed:10671544, ECO:0000269|PubMed:9405365}.; PTM: Extensively phosphorylated (PubMed:7993898). Phosphorylated on Ser-59 by PLK1 and dephosphorylated by protein phosphatase 2A (PP2A) in mitosis (PubMed:25986610). {ECO:0000269|PubMed:25986610, ECO:0000269|PubMed:7993898}.; PTM: Arg-739 is dimethylated, probably to asymmetric dimethylarginine (Ref.8). Arg-733 is dimethylated, probably to asymmetric dimethylarginine (By similarity). {ECO:0000250|UniProtKB:Q8VEK3, ECO:0000269|Ref.8}.; PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q8VEK3}.
uniprot
proteins
pubmed
10490622
uniprot
proteins
pubmed
10671544
uniprot
proteins
pubmed
11003645
uniprot
proteins
pubmed
11909954
uniprot
proteins
pubmed
11991638
uniprot
proteins
pubmed
1324173
uniprot
proteins
pubmed
14608463
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15563465
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
15711563
uniprot
proteins
pubmed
1628625
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16916646
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17174306
uniprot
proteins
pubmed
17289661
uniprot
proteins
pubmed
17487921
uniprot
proteins
pubmed
18082603
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19029303
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19617346
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19808671
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20858735
uniprot
proteins
pubmed
21242313
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22325991
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23640942
uniprot
proteins
pubmed
23708187
uniprot
proteins
pubmed
23811339
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25356899
uniprot
proteins
pubmed
25616961
uniprot
proteins
pubmed
25911097
uniprot
proteins
pubmed
25986610
uniprot
proteins
pubmed
26030138
uniprot
proteins
pubmed
26244333
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28190768
uniprot
proteins
pubmed
28622508
uniprot
proteins
pubmed
7509195
uniprot
proteins
pubmed
7753047
uniprot
proteins
pubmed
7993898
uniprot
proteins
pubmed
8068679
uniprot
proteins
pubmed
8174554
uniprot
proteins
pubmed
9105675
uniprot
proteins
pubmed
9204873
uniprot
proteins
pubmed
9353307
uniprot
proteins
pubmed
9405365
uniprot
proteins
sequence_length
825
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10671544, ECO:0000269|PubMed:11003645, ECO:0000269|PubMed:1324173, ECO:0000269|PubMed:14608463, ECO:0000269|PubMed:15563465, ECO:0000269|PubMed:19617346, ECO:0000269|PubMed:21242313, ECO:0000269|PubMed:8174554, ECO:0000269|PubMed:9353307, ECO:0000269|PubMed:9405365}. Nucleus matrix {ECO:0000269|PubMed:1324173, ECO:0000269|PubMed:14608463, ECO:0000269|PubMed:8174554}. Chromosome {ECO:0000269|PubMed:11003645, ECO:0000269|PubMed:14608463, ECO:0000269|PubMed:15563465}. Nucleus speckle {ECO:0000269|PubMed:9353307}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:25986610}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:21242313}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:21242313, ECO:0000269|PubMed:25986610}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:21242313}. Midbody {ECO:0000269|PubMed:25986610}. Cytoplasm {ECO:0000269|PubMed:19029303}. Cell surface {ECO:0000269|PubMed:7993898}. Cytoplasmic granule {ECO:0000269|PubMed:17289661}. 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). {ECO:0000250|UniProtKB:Q8VEK3, ECO:0000269|PubMed:11003645, ECO:0000269|PubMed:14608463, ECO:0000269|PubMed:15563465, ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:19617346, ECO:0000269|PubMed:21242313, ECO:0000269|PubMed:25986610, ECO:0000269|PubMed:9353307}.
uniprot
proteins