Reviewed,
UniProtKB/Swiss-Prot Q13523 (PRP4B_HUMAN)
Last modified
November 25, 2008.
Version 101.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Serine/threonine-protein kinase PRP4 homolog EC=2.7.11.1 Alternative name(s): PRP4 pre-mRNA-processing factor 4 homolog PRP4 kinase | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 1007 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Has a role in pre-mRNA splicing. Phosphorylates SF2/ASF. |
| Catalytic activity | ATP + a protein = ADP + a phosphoprotein. |
| Subunit structure | Identified in the spliceosome C complex, at least composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23, DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1, GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRPH1, HNRPK, HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2, SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8. Interacts with Clk1 C-terminus. |
| Subcellular location | |
| Tissue specificity | Ubiquitous. |
| Post-translational modification | Phosphorylated by Clk1. |
| Sequence similarities | Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. Contains 1 protein kinase domain. |
| Sequence caution | The sequence AAH09844.1 differs from that shown. Reason: Frameshift at position 432. |
Ontologies
Keywords | |
|---|---|
| Biological process | mRNA processing mRNA splicing |
| Cellular component | Nucleus Spliceosome |
| Coding sequence diversity | Polymorphism |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Serine/threonine-protein kinase Transferase |
| PTM | Phosphoprotein |
Gene Ontology (GO) | |
| Biological process | RNA splicing Ref.8 Traceable author statement. Source: ProtInc mRNA processingInferred from electronic annotation. Source: UniProtKB-KW protein amino acid phosphorylation Ref.8Traceable author statement. Source: ProtInc |
| Cellular component | spliceosome Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | ATP binding Inferred from electronic annotation. Source: InterPro protein bindingInferred from physical interaction. Source: IntAct protein serine/threonine kinase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| ARRB1 | P49407 | 1 | EBI-395940,EBI-743313 | |
| ARRB2 | P32121 | 1 | EBI-395940,EBI-714559 | |
| gag | P04590 | 3 | EBI-395940,EBI-780156 | From a different organism. |
| KLF13 | Q9Y2Y9 | 3 | EBI-395940,EBI-1255893 | |
| POLR3F | Q9H1D9 | 1 | EBI-395940,EBI-710067 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1007 | 1007 | Serine/threonine-protein kinase PRP4 homolog | PRO_0000086586 | |||||
Regions | |||||||||
| Domain | 687 – 1006 | 320 | Protein kinase | ||||||
| Nucleotide binding | 693 – 701 | 9 | ATP By similarity | ||||||
| Compositional bias | 39 – 496 | 458 | Arg/Lys-rich (basic) | ||||||
| Compositional bias | 40 – 78 | 39 | His-rich | ||||||
Sites | |||||||||
| Active site | 815 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 717 | 1 | ATP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 20 | 1 | Phosphoserine | ||||||
| Modified residue | 23 | 1 | Phosphoserine | ||||||
| Modified residue | 32 | 1 | Phosphoserine | ||||||
| Modified residue | 36 | 1 | Phosphoserine | ||||||
| Modified residue | 87 | 1 | Phosphoserine | ||||||
| Modified residue | 93 | 1 | Phosphoserine | ||||||
| Modified residue | 140 | 1 | Phosphotyrosine | ||||||
| Modified residue | 142 | 1 | Phosphoserine | ||||||
| Modified residue | 144 | 1 | Phosphoserine | ||||||
| Modified residue | 239 | 1 | Phosphoserine | ||||||
| Modified residue | 241 | 1 | Phosphoserine | ||||||
| Modified residue | 257 | 1 | Phosphoserine | ||||||
| Modified residue | 277 | 1 | Phosphoserine | ||||||
| Modified residue | 292 | 1 | Phosphoserine | ||||||
| Modified residue | 294 | 1 | Phosphoserine | ||||||
| Modified residue | 328 | 1 | Phosphoserine | ||||||
| Modified residue | 354 | 1 | Phosphoserine | ||||||
| Modified residue | 356 | 1 | Phosphoserine | ||||||
| Modified residue | 366 | 1 | Phosphoserine | ||||||
| Modified residue | 368 | 1 | Phosphoserine | ||||||
| Modified residue | 381 | 1 | Phosphoserine | ||||||
| Modified residue | 385 | 1 | Phosphothreonine | ||||||
| Modified residue | 387 | 1 | Phosphoserine | ||||||
| Modified residue | 410 | 1 | Phosphoserine | ||||||
| Modified residue | 411 | 1 | Phosphoserine | ||||||
| Modified residue | 427 | 1 | Phosphoserine | ||||||
| Modified residue | 431 | 1 | Phosphoserine | ||||||
| Modified residue | 437 | 1 | Phosphoserine | ||||||
| Modified residue | 518 | 1 | Phosphoserine | ||||||
| Modified residue | 519 | 1 | Phosphoserine | ||||||
| Modified residue | 520 | 1 | Phosphoserine | ||||||
| Modified residue | 569 | 1 | Phosphoserine | ||||||
| Modified residue | 576 | 1 | Phosphothreonine | ||||||
| Modified residue | 578 | 1 | Phosphoserine | ||||||
| Modified residue | 580 | 1 | Phosphoserine | ||||||
| Modified residue | 849 | 1 | Phosphotyrosine | ||||||
| Modified residue | 852 | 1 | Phosphoserine By similarity | ||||||
Natural variations | |||||||||
| Natural variant | 83 | 1 | V → I: dbSNP rs9503893. | VAR_046969 | |||||
| Natural variant | 584 | 1 | I → V | VAR_047798 | |||||
| Natural variant | 658 | 1 | F → L in a breast cancer sample; somatic mutation. | VAR_035633 | |||||
Experimental info | |||||||||
| Sequence conflict | 468 | 1 | P → T in AAH34969. Ref.7 | ||||||
| Sequence conflict | 610 | 1 | K → R in BAF83933. Ref.4 | ||||||
| Sequence conflict | 754 | 1 | F → L in AAH34969. Ref.7 | ||||||
| Sequence conflict | 851 | 1 | V → F in AAH34969. Ref.7 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning of human PRP4 reveals interaction with Clk1." Kojima T., Zama T., Wada K., Onogi H., Hagiwara M. J. Biol. Chem. 276:32247-32256(2001) [PubMed: 11418604] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION. |
| [2] | "Mammalian PRP4 kinase copurifies and interacts with components of both the U5 snRNP and the N-CoR deacetylase complexes." Dellaire G., Makarov E.M., Cowger J.J.M., Longman D., Sutherland H.G.E., Luehrmann R., Torchia J., Bickmore W.A. Mol. Cell. Biol. 22:5141-5156(2002) [PubMed: 12077342] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [3] | "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro." Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:31-39(1998) [PubMed: 9628581] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain. |
| [4] | "Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-83. |
| [5] | "The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. Beck S.Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ILE-83. |
| [6] | Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ILE-83. |
| [7] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." Th |

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