Serine/threonine-protein kinase PRP4 homolog

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
    Pre-mRNA protein kinase

Gene names

Name:	Prpf4b
Synonyms:	Cbp143, Prp4h, Prp4k, Prp4m, Prpk

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length	1007 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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 By similarity. Interacts with Clk1 C-terminus.
Subcellular location	Nucleus.
Post-translational modification	Phosphorylated by Clk1. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. Contains 1 protein kinase domain.

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Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Nucleus Spliceosome
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	RNA splicing Inferred from electronic annotation. Source: UniProtKB-KW mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	chromosome Ref.3 Inferred from direct assay. Source: MGI spliceosome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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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_0000086587

Regions

Domain

687 – 1006

320

Protein kinase

Nucleotide binding

693 – 701

9

ATP By similarity

Compositional bias

40 – 497

458

Arg/Lys-rich (basic)

Compositional bias

41 – 79

39

His-rich

Sites

Active site

815

1

Proton acceptor By similarity

Binding site

717

1

ATP By similarity

Amino acid modifications

Modified residue

21

1

Phosphoserine By similarity

Modified residue

24

1

Phosphoserine By similarity

Modified residue

33

1

Phosphoserine By similarity

Modified residue

37

1

Phosphoserine By similarity

Modified residue

88

1

Phosphoserine

Modified residue

94

1

Phosphoserine

Modified residue

141

1

Phosphotyrosine By similarity

Modified residue

143

1

Phosphoserine By similarity

Modified residue

145

1

Phosphoserine By similarity

Modified residue

240

1

Phosphoserine By similarity

Modified residue

242

1

Phosphoserine By similarity

Modified residue

258

1

Phosphoserine By similarity

Modified residue

278

1

Phosphoserine By similarity

Modified residue

292

1

Phosphoserine By similarity

Modified residue

294

1

Phosphoserine By similarity

Modified residue

328

1

Phosphoserine By similarity

Modified residue

354

1

Phosphoserine By similarity

Modified residue

356

1

Phosphoserine By similarity

Modified residue

366

1

Phosphoserine By similarity

Modified residue

368

1

Phosphoserine By similarity

Modified residue

381

1

Phosphoserine By similarity

Modified residue

385

1

Phosphothreonine By similarity

Modified residue

387

1

Phosphoserine By similarity

Modified residue

410

1

Phosphoserine By similarity

Modified residue

411

1

Phosphoserine By similarity

Modified residue

427

1

Phosphoserine Ref.10

Modified residue

431

1

Phosphoserine Ref.10

Modified residue

437

1

Phosphoserine Ref.10

Modified residue

518

1

Phosphoserine By similarity

Modified residue

519

1

Phosphoserine By similarity

Modified residue

520

1

Phosphoserine By similarity

Modified residue

569

1

Phosphoserine By similarity

Modified residue

576

1

Phosphoserine Ref.7

Modified residue

578

1

Phosphoserine Ref.7

Modified residue

580

1

Phosphoserine Ref.7 Ref.10

Modified residue

849

1

Phosphotyrosine Ref.5 Ref.6 Ref.8 Ref.9 Ref.10

Modified residue

852

1

Phosphoserine Ref.10

Experimental info

Sequence conflict

185 – 187

3

SKS → IPG in AAC32042. Ref.3

Sequence conflict

223

1

K → I in AAC32042. Ref.3

Sequence conflict

478

1

K → R in BAC39069. Ref.2

Sequence conflict

633

1

F → L in AAB03269. Ref.4

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Sequences

Sequence

Length

Mass (Da)

Tools

Q61136-1 [UniParc].

Last modified October 10, 2002. Version 2.
Checksum: 18E6C3C43BE7AB4C
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FASTA

1,007

116,948

        10         20         30         40         50         60 
MAATEPPSLR EQAEMDDADN SEKSVNEENG EVSEDQSQNK HSRHKKKKHK HRSKHKKHKH 

        70         80         90        100        110        120 
SSEEDRDKKH KHKHKHKKHK RKEVIEASDK EGLSPAKRTK LDDLALLEDL EKQRALIKAE 

       130        140        150        160        170        180 
LDNELMEGKV QSGMGLILQG YESGSEEEGE IHEKARNGNR SSTRSSSTRG KLEITDNKNS 

       190        200        210        220        230        240 
AKKRSKSRSK ERTRHRSDKR KSKGAGEMLR EKANRSKSKE RRKSKSPSKR SKSQDQARKS 

       250        260        270        280        290        300 
KSPPLRRRSQ EKVGKARSPA EEKMKSEEKG KIKDRKKSPI VNERSRDRSK KSKSPVDLRD 

       310        320        330        340        350        360 
KSKDRRSRSK ERKSKRSEID KEKKPIKSPS KDASSGKENR SPSRRPGRSP KRRSLSPKLR 

       370        380        390        400        410        420 
DKSRRSRSPL LNDRRSKQSK SPSRTLSPGR RAKSRSLERK RREPERRRLS SPRTRPRDDI 

       430        440        450        460        470        480 
LGRCERSKDA SPINRWSPTR RRSRSPIRRR SRSPLRRSRS PRRRSRSPRR RDRSRRSKSR 

       490        500        510        520        530        540 
LRRRSRSRGG HRRRSRSKVK EDKFKGSLSE GMKVEQESSS DDNLEDFDVE EEDEEALIEQ 

       550        560        570        580        590        600 
RRIQRQAIVQ KYKYLAEDSN ISVPSEPSSP QSSTRSRSPS PDDILERVAA DVKEYERENV 

       610        620        630        640        650        660 
DTFEASVKAK HNLMTVEQNN GSSQKKILAP DMFTESDDMF AAYFDSARLR AAGIGKDFKE 

       670        680        690        700        710        720 
NPNLRDNWTD AEGYYRVNIG EVLDKRYNVY GYTGQGVFSN VVRARDNARA NQEVAVKIIR 

       730        740        750        760        770        780 
NNELMQKTGL KELEFLKKLN DADPDDKFHC LRLFRHFYHK QHLCLVFEPL SMNLREVLKK 

       790        800        810        820        830        840 
YGKDVGLHIK AVRSYSQQLF LALKLLKRCN ILHADIKPDN ILVNESKTIL KLCDFGSASH 

       850        860        870        880        890        900 
VADNDITPYL VSRFYRAPEI IIGKSYDYGI DMWSVGCTLY ELYTGKILFP GKTNNHMLKL 

       910        920        930        940        950        960 
AMDLKGKMPN KMIRKGVFKD QHFDQNLNFM YIEVDKVTER EKVTVMSTIN PTKDLLADLI 

       970        980        990       1000 
GCQRLPEDQR KKVHQLKDLL DQILMLDPAK RISINQALQH AFIQEKI

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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].
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Hippocampus, Spinal ganglion and Urinary bladder.
[3]	"Capturing novel mouse genes encoding chromosomal and other nuclear proteins." Tate P., Lee M., Tweedie S., Skarnes W.C., Bickmore W.A. J. Cell Sci. 111:2575-2585(1998) [PubMed: 9701556] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 185-1007.
[4]	"Functional analysis of the fission yeast Prp4 protein kinase involved in pre-mRNA splicing and isolation of a putative mammalian homologue." Gross T., Lutzelberger M., Wiegmann H., Klingenhoff A., Shenoy S., Kaeufer N.F. Nucleic Acids Res. 25:1028-1035(1997) [PubMed: 9102632] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 512-1007.
[5]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-849, MASS SPECTROMETRY.
[6]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed: 17947660] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-849, MASS SPECTROMETRY. Tissue: Mast cell.
[7]	"A differential phosphoproteomic analysis of retinoic acid-treated P19 cells." Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D. J. Proteome Res. 6:3174-3186(2007) [PubMed: 17622165] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576; SER-578 AND SER-580, MASS SPECTROMETRY.
[8]	"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks." Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M. Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-849, MASS SPECTROMETRY.
[9]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-849, MASS SPECTROMETRY. Tissue: Brain.
[10]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427; SER-431; SER-437; SER-580; TYR-849 AND SER-852, MASS SPECTROMETRY. Tissue: Liver.
[11]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed: 19131326] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-94; SER-431; SER-437 AND TYR-849, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	AF283466 mRNA. Translation: AAM19102.1. AK020579 mRNA. Translation: BAB32137.3. AK021274 mRNA. Translation: BAB32358.3. AK083926 mRNA. Translation: BAC39069.1. AF033663 mRNA. Translation: AAC32042.1. U48737 mRNA. Translation: AAB03269.1.
IPI	IPI00320690.
UniGene	Mm.10027 Mm.475929
3D structure databases
HSSP	HSSP built from PDB template 1JOW based on UniProtKB Q00534.
ModBase	Search...
PTM databases
PhosphoSite	Q61136.
Proteomic databases
PRIDE	Q61136.
Genome annotation databases
Ensembl	ENSMUSG00000021413. Mus musculus. [Contig view]
Organism-specific databases
MGI	MGI:109584. Prpf4b.
Phylogenomic databases
HOGENOM	Q61136.
HOVERGEN	Q61136.
Enzyme and pathway databases
BRENDA	2.7.11.1. 244.
Gene expression databases
ArrayExpress	Q61136.
Bgee	Q61136.
GermOnline	ENSMUSG00000021413. Mus musculus.
Family and domain databases
InterPro	IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

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Entry information

Entry name

PRP4B_MOUSE

Accession

Primary (citable) accession number: Q61136
Secondary accession number(s): O88378

Q9CTT0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	October 10, 2002
Last modified:	June 16, 2009
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents