heterogeneous nuclear ribonucleoprotein K, isoform D [Drosophila melanogaster]
Protein Classification
KH domain-containing protein( domain architecture ID 16910669)
K homology (KH) domain-containing protein may bind single-stranded RNA or DNA
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| KH-I_HNRNPK_rpt3 | cd22434 | third type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ... |
242-315 | 1.80e-26 | ||
third type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ribonucleoprotein K (hnRNP K) and similar proteins; hnRNP K, also called transformation up-regulated nuclear protein (TUNP), is a pre-mRNA binding protein that binds tenaciously to poly(C) sequences. It may be involved in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. It can also bind poly(C) single-stranded DNA. hnRNP K plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. hnRNP K contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one. : Pssm-ID: 411862 [Multi-domain] Cd Length: 74 Bit Score: 99.32 E-value: 1.80e-26
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| Name | Accession | Description | Interval | E-value | ||
| KH-I_HNRNPK_rpt3 | cd22434 | third type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ... |
242-315 | 1.80e-26 | ||
third type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ribonucleoprotein K (hnRNP K) and similar proteins; hnRNP K, also called transformation up-regulated nuclear protein (TUNP), is a pre-mRNA binding protein that binds tenaciously to poly(C) sequences. It may be involved in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. It can also bind poly(C) single-stranded DNA. hnRNP K plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. hnRNP K contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one. Pssm-ID: 411862 [Multi-domain] Cd Length: 74 Bit Score: 99.32 E-value: 1.80e-26
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| KH_1 | pfam00013 | KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ... |
244-308 | 7.77e-05 | ||
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia. Pssm-ID: 459630 [Multi-domain] Cd Length: 65 Bit Score: 39.96 E-value: 7.77e-05
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| Name | Accession | Description | Interval | E-value | ||
| KH-I_HNRNPK_rpt3 | cd22434 | third type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ... |
242-315 | 1.80e-26 | ||
third type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ribonucleoprotein K (hnRNP K) and similar proteins; hnRNP K, also called transformation up-regulated nuclear protein (TUNP), is a pre-mRNA binding protein that binds tenaciously to poly(C) sequences. It may be involved in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. It can also bind poly(C) single-stranded DNA. hnRNP K plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. hnRNP K contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one. Pssm-ID: 411862 [Multi-domain] Cd Length: 74 Bit Score: 99.32 E-value: 1.80e-26
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| KH-I_PCBP_rpt3 | cd22439 | third type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ... |
244-309 | 1.39e-07 | ||
third type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding proteins (PCBPs); The PCBP family, also known as hnRNP E family, comprises four members, PCBP1-4, which are RNA-binding proteins that interact in a sequence-specific manner with single-stranded poly(C) sequences. They are mainly involved in various posttranscriptional regulations, including mRNA stabilization or translational activation/silencing. Besides, PCBPs may share iron chaperone activity. PCBPs contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one. Pssm-ID: 411867 [Multi-domain] Cd Length: 68 Bit Score: 48.00 E-value: 1.39e-07
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| KH-I_PCBP1_2_rpt3 | cd22521 | third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 1 (PCBP1) ... |
244-314 | 1.10e-06 | ||
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 1 (PCBP1) and similar proteins; The family includes PCBP1 (also called alpha-CP1, or heterogeneous nuclear ribonucleoprotein E1, or hnRNP E1, or nucleic acid-binding protein SUB2.3) and PCBP2 (also called alpha-CP2, or heterogeneous nuclear ribonucleoprotein E2, or hnRNP E2). They are single-stranded nucleic acid binding proteins that bind preferentially to oligo dC. They act as iron chaperones for ferritin. In case of infection by poliovirus, PCBP1 plays a role in initiation of viral RNA replication in concert with the viral protein 3CD. PCBP2 is a major cellular poly(rC)-binding protein. It also binds poly(rU). PCBP2 negatively regulates cellular antiviral responses mediated by MAVS signaling. It acts as an adapter between MAVS and the E3 ubiquitin ligase ITCH, therefore triggering MAVS ubiquitination and degradation. PCBP2 forms a metabolon with the heme oxygenase 1/cytochrome P450 reductase complex for heme catabolism and iron transfer. Both PCBP1 and PCBP2 contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one. Pssm-ID: 411949 Cd Length: 76 Bit Score: 45.82 E-value: 1.10e-06
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| KH-I_BTR1_rpt3 | cd22514 | third type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 and ... |
244-310 | 1.27e-06 | ||
third type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 and similar proteins; BTR1, also called Binding to ToMV RNA 1, is a negative regulator of tomato mosaic virus (ToMV) multiplication but has no effect on the multiplication of cucumber mosaic virus (CMV). BTR1 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one. Pssm-ID: 411942 [Multi-domain] Cd Length: 71 Bit Score: 45.49 E-value: 1.27e-06
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| KH-I_HEN4_like_rpt5 | cd22462 | fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana KH ... |
245-308 | 6.08e-06 | ||
fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana KH domain-containing protein HEN4 and similar protein; HEN4, also called protein HUA ENHANCER 4, plays a role in floral reproductive organ identity in the third whorl and floral determinacy specification by specifically promoting the processing of AGAMOUS (AG) pre-mRNA. It functions in association with HUA1 and HUA2. HEN4 contains five K-homology (KH) RNA-binding domains. The model corresponds to the KH5 domain of HEN4. Pssm-ID: 411890 [Multi-domain] Cd Length: 66 Bit Score: 43.39 E-value: 6.08e-06
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| KH-I_NOVA_rpt3 | cd09031 | third type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ... |
282-310 | 8.19e-06 | ||
third type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ventral antigen (Nova); The family includes two related neuronal RNA-binding proteins, Nova-1 and Nova-2. Nova-1, also called onconeural ventral antigen 1, or paraneoplastic Ri antigen, or ventral neuron-specific protein 1, may regulate RNA splicing or metabolism in a specific subset of developing neurons. It interacts with RNA containing repeats of the YCAY sequence. It is a brain-enriched splicing factor regulating neuronal alternative splicing. Nova-1 is involved in neurological disorders and carcinogenesis. Nova-2, also called astrocytic NOVA1-like RNA-binding protein, is a neuronal RNA-binding protein expressed in a broader central nervous system (CNS) distribution than Nova-1. It functions in neuronal RNA metabolism. NOVA family proteins contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one. Pssm-ID: 411807 [Multi-domain] Cd Length: 71 Bit Score: 42.95 E-value: 8.19e-06
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| KH-I_PCBP3_rpt3 | cd22522 | third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 3 (PCBP3) ... |
241-309 | 2.61e-05 | ||
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 3 (PCBP3) and similar proteins; PCBP3, also called alpha-CP3, or PCBP3-overlapping transcript, or PCBP3-overlapping transcript 1, or heterogeneous nuclear ribonucleoprotein E3, or hnRNP E3, is a single-stranded nucleic acid binding protein that binds preferentially to oligo dC. It can function as a repressor dependent on binding to single-strand and double-stranded poly(C) sequences. PCBP3 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one. Pssm-ID: 411950 [Multi-domain] Cd Length: 75 Bit Score: 41.64 E-value: 2.61e-05
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| KH-I_FUBP_rpt1 | cd22396 | first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ... |
270-308 | 2.64e-05 | ||
first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding proteins; The far upstream element-binding protein (FUBP) family includes FUBP1-3. FUBP1, also called FBP, or FUSE-binding protein 1, or DNA helicase V, or DH V, binds RNA and single-stranded DNA (ssDNA) and may act both as activator and repressor of transcription. It regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP proteins contain four K-homology (KH) RNA-binding domains. The model corresponds to the first one. Pssm-ID: 411824 [Multi-domain] Cd Length: 68 Bit Score: 41.47 E-value: 2.64e-05
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| KH-I | cd00105 | K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ... |
246-307 | 4.02e-05 | ||
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found in a wide variety of proteins including ribosomal proteins, transcription factors and post-transcriptional modifiers of mRNA. There are two different KH domains that belong to different protein folds, but they share a single KH motif. The KH motif is folded into a beta alpha alpha beta unit. In addition to the core, type II KH domains (e.g. ribosomal protein S3) include an N-terminal extension and type I KH domains (e.g. hnRNP K) contain a C-terminal extension. Some KH-I superfamily members contain a divergent KH domain that lacks the RNA-binding GXXG motif. Some others have a mutated GXXG motif which may or may not have nucleic acid binding ability. Pssm-ID: 411802 [Multi-domain] Cd Length: 63 Bit Score: 40.74 E-value: 4.02e-05
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| KH_1 | pfam00013 | KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ... |
244-308 | 7.77e-05 | ||
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia. Pssm-ID: 459630 [Multi-domain] Cd Length: 65 Bit Score: 39.96 E-value: 7.77e-05
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| KH-I_PCBP4_rpt3 | cd22523 | third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 4 (PCBP4) ... |
244-306 | 6.29e-04 | ||
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 4 (PCBP4) and similar proteins; PCBP4, also called alpha-CP4, or heterogeneous nuclear ribonucleoprotein E4, or hnRNP E4, is a single-stranded nucleic acid binding protein that binds preferentially to oligo dC. It regulates both basal and stress-induced p21 expression through binding p21 3'-UTR and modulating p21 mRNA stability. It also plays a role in the cell cycle and is implicated in lung tumor suppression. PCBP4 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one. Pssm-ID: 411951 Cd Length: 68 Bit Score: 37.57 E-value: 6.29e-04
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| KH-I_RCF3_like_rpt5 | cd22463 | fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ... |
246-307 | 2.01e-03 | ||
fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH domain-containing protein RCF3 and similar protein; RCF3, also called protein ENHANCED STRESS RESPONSE 1 (ESR1), or protein HIGH OSMOTIC STRESS GENE EXPRESSION 5 (HOS5), or protein REGULATOR OF CBF GENE EXPRESSION 3, or protein SHINY 1 (SHI1), acts as negative regulator of osmotic stress-induced gene expression. It is involved in the regulation of thermotolerance responses under heat stress. It functions as an upstream regulator of heat stress transcription factor (HSF) genes. HEN4, also called protein HUA ENHANCER 4, plays a role in floral reproductive organ identity in the third whorl and floral determinacy specification by specifically promoting the processing of AGAMOUS (AG) pre-mRNA. It functions in association with HUA1 and HUA2. RCF3 contains five K-homology (KH) RNA-binding domains. The model corresponds to the KH5 domain of RCF3. Pssm-ID: 411891 [Multi-domain] Cd Length: 71 Bit Score: 36.26 E-value: 2.01e-03
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| KH-I_FUBP_rpt4 | cd22399 | fourth type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ... |
244-309 | 2.76e-03 | ||
fourth type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding proteins; The far upstream element-binding protein (FUBP) family includes FUBP1-3. FUBP1, also called FBP, or FUSE-binding protein 1, or DNA helicase V, or DH V, binds RNA and single-stranded DNA (ssDNA) and may act both as activator and repressor of transcription. It regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP proteins contain four K-homology (KH) RNA-binding domains. The model corresponds to the fourth one. Pssm-ID: 411827 [Multi-domain] Cd Length: 67 Bit Score: 35.66 E-value: 2.76e-03
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| KH-I_PCBP_rpt2 | cd02396 | second type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ... |
280-310 | 4.95e-03 | ||
second type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding proteins (PCBPs); The PCBP family, also known as hnRNP E family, comprises four members, PCBP1-4, which are RNA-binding proteins that interact in a sequence-specific manner with single-stranded poly(C) sequences. They are mainly involved in various posttranscriptional regulations, including mRNA stabilization or translational activation/silencing. Besides, PCBPs may share iron chaperone activity. PCBPs contain three K-homology (KH) RNA-binding domains. The model corresponds to the second one. Pssm-ID: 411806 [Multi-domain] Cd Length: 72 Bit Score: 35.32 E-value: 4.95e-03
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