Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q61136 (PRP4B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1007 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 By similarity. Interacts with Clk1 C-terminus.

Subcellular location

Nucleus.

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 10071006Serine/threonine-protein kinase PRP4 homolog
PRO_0000086587

Regions

Domain687 – 1006320Protein kinase
Nucleotide binding693 – 7019ATP By similarity
Compositional bias40 – 497458Arg/Lys-rich (basic)
Compositional bias41 – 7939His-rich

Sites

Active site8151Proton acceptor By similarity
Binding site7171ATP By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue211Phosphoserine By similarity
Modified residue241Phosphoserine By similarity
Modified residue331Phosphoserine By similarity
Modified residue881Phosphoserine Ref.11
Modified residue941Phosphoserine Ref.11
Modified residue1001N6-acetyllysine
Modified residue1411Phosphotyrosine By similarity
Modified residue1431Phosphoserine By similarity
Modified residue1451Phosphoserine By similarity
Modified residue2401Phosphoserine By similarity
Modified residue2421Phosphoserine By similarity
Modified residue2581Phosphoserine By similarity
Modified residue2781Phosphoserine By similarity
Modified residue2941Phosphoserine By similarity
Modified residue3281Phosphoserine By similarity
Modified residue3541Phosphoserine By similarity
Modified residue3561Phosphoserine By similarity
Modified residue3661Phosphoserine By similarity
Modified residue3681Phosphoserine By similarity
Modified residue3851Phosphothreonine By similarity
Modified residue3871Phosphoserine By similarity
Modified residue4271Phosphoserine By similarity
Modified residue4311Phosphoserine Ref.11
Modified residue4371Phosphoserine Ref.11
Modified residue5181Phosphoserine By similarity
Modified residue5191Phosphoserine By similarity
Modified residue5201Phosphoserine By similarity
Modified residue5651Phosphoserine By similarity
Modified residue5691Phosphoserine By similarity
Modified residue5761Phosphoserine Ref.9
Modified residue5781Phosphoserine Ref.9
Modified residue5801Phosphoserine Ref.9
Modified residue7171N6-acetyllysine By similarity
Modified residue8491Phosphotyrosine Ref.8 Ref.11
Modified residue8521Phosphoserine By similarity

Experimental info

Sequence conflict185 – 1873SKS → IPG in AAC32042. Ref.5
Sequence conflict2231K → I in AAC32042. Ref.5
Sequence conflict4781R → K in AAM19102. Ref.1
Sequence conflict4781R → K in AAC32042. Ref.5
Sequence conflict6331F → L in AAB03269. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q61136 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 18E1B7371E17AB4C

FASTA1,007116,976
        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 RDRSRRSRSR 

       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 

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Hippocampus, Spinal ganglion and Urinary bladder.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 185-1007.
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 512-1007.
[7]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-849, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Mast cell.
[9]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576; SER-578 AND SER-580, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[10]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-94; SER-431; SER-437 AND TYR-849, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[12]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF283466 mRNA. Translation: AAM19102.1.
AK020579 mRNA. Translation: BAB32137.3.
AK021274 mRNA. Translation: BAB32358.3.
AK083926 mRNA. Translation: BAC39069.1.
CH466546 Genomic DNA. Translation: EDL40895.1.
BC141272 mRNA. Translation: AAI41273.1.
BC141273 mRNA. Translation: AAI41274.1.
AF033663 mRNA. Translation: AAC32042.1.
U48737 mRNA. Translation: AAB03269.1.
RefSeqNP_038858.2. NM_013830.2.
UniGeneMm.10027.
Mm.482253.

3D structure databases

ProteinModelPortalQ61136.
SMRQ61136. Positions 603-1005.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202400. 2 interactions.
IntActQ61136. 3 interactions.
MINTMINT-1751441.

PTM databases

PhosphoSiteQ61136.

Proteomic databases

PaxDbQ61136.
PRIDEQ61136.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000077853; ENSMUSP00000077019; ENSMUSG00000021413.
GeneID19134.
KEGGmmu:19134.
UCSCuc007qbp.2. mouse.

Organism-specific databases

CTD8899.
MGIMGI:109584. Prpf4b.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00740000115319.
HOVERGENHBG055182.
InParanoidB2RUN6.
KOK08827.
OMARSEIDKE.
OrthoDBEOG76HQ1K.
TreeFamTF315246.

Enzyme and pathway databases

BRENDA2.7.11.1. 3474.

Gene expression databases

ArrayExpressQ61136.
BgeeQ61136.
GenevestigatorQ61136.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio295762.
PROQ61136.
SOURCESearch...

Entry information

Entry namePRP4B_MOUSE
AccessionPrimary (citable) accession number: Q61136
Secondary accession number(s): B2RUN6 expand/collapse secondary AC list , O88378, Q8BND8, Q8R4Y5, Q9CTL9, Q9CTT0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 27, 2011
Last modified: March 19, 2014
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

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