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Q61136

- PRP4B_MOUSE

UniProt

Q61136 - PRP4B_MOUSE

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Protein
Serine/threonine-protein kinase PRP4 homolog
Gene
Prpf4b, Cbp143, Prp4h, Prp4k, Prp4m, Prpk
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Has a role in pre-mRNA splicing. Phosphorylates SF2/ASF.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei717 – 7171ATP By similarity
Active sitei815 – 8151Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi693 – 7019ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein kinase activity Source: MGI
  3. protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

  1. RNA splicing Source: UniProtKB-KW
  2. mRNA processing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 3474.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Prpf4b
Synonyms:Cbp143, Prp4h, Prp4k, Prp4m, Prpk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:109584. Prpf4b.

Subcellular locationi

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: Ensembl
  2. chromosome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 10071006Serine/threonine-protein kinase PRP4 homolog
PRO_0000086587Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei21 – 211Phosphoserine By similarity
Modified residuei24 – 241Phosphoserine By similarity
Modified residuei33 – 331Phosphoserine By similarity
Modified residuei88 – 881Phosphoserine1 Publication
Modified residuei94 – 941Phosphoserine1 Publication
Modified residuei100 – 1001N6-acetyllysine1 Publication
Modified residuei141 – 1411Phosphotyrosine By similarity
Modified residuei143 – 1431Phosphoserine By similarity
Modified residuei145 – 1451Phosphoserine By similarity
Modified residuei240 – 2401Phosphoserine By similarity
Modified residuei242 – 2421Phosphoserine By similarity
Modified residuei258 – 2581Phosphoserine By similarity
Modified residuei278 – 2781Phosphoserine By similarity
Modified residuei294 – 2941Phosphoserine By similarity
Modified residuei328 – 3281Phosphoserine By similarity
Modified residuei354 – 3541Phosphoserine By similarity
Modified residuei356 – 3561Phosphoserine By similarity
Modified residuei366 – 3661Phosphoserine By similarity
Modified residuei368 – 3681Phosphoserine By similarity
Modified residuei385 – 3851Phosphothreonine By similarity
Modified residuei387 – 3871Phosphoserine By similarity
Modified residuei427 – 4271Phosphoserine By similarity
Modified residuei431 – 4311Phosphoserine1 Publication
Modified residuei437 – 4371Phosphoserine1 Publication
Modified residuei518 – 5181Phosphoserine By similarity
Modified residuei519 – 5191Phosphoserine By similarity
Modified residuei520 – 5201Phosphoserine By similarity
Modified residuei565 – 5651Phosphoserine By similarity
Modified residuei569 – 5691Phosphoserine By similarity
Modified residuei576 – 5761Phosphoserine1 Publication
Modified residuei578 – 5781Phosphoserine1 Publication
Modified residuei580 – 5801Phosphoserine1 Publication
Modified residuei717 – 7171N6-acetyllysine By similarity
Modified residuei849 – 8491Phosphotyrosine2 Publications
Modified residuei852 – 8521Phosphoserine By similarity

Post-translational modificationi

Phosphorylated by Clk1.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ61136.
PaxDbiQ61136.
PRIDEiQ61136.

PTM databases

PhosphoSiteiQ61136.

Expressioni

Gene expression databases

ArrayExpressiQ61136.
BgeeiQ61136.
GenevestigatoriQ61136.

Interactioni

Subunit structurei

Identified in the spliceosome C complex By similarity. Interacts with Clk1 C-terminus.

Protein-protein interaction databases

BioGridi202400. 2 interactions.
IntActiQ61136. 3 interactions.
MINTiMINT-1751441.

Structurei

3D structure databases

ProteinModelPortaliQ61136.
SMRiQ61136. Positions 603-1005.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini687 – 1006320Protein kinase
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi40 – 497458Arg/Lys-rich (basic)
Add
BLAST
Compositional biasi41 – 7939His-rich
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00580000081366.
HOVERGENiHBG055182.
InParanoidiB2RUN6.
KOiK08827.
OMAiRSEIDKE.
OrthoDBiEOG76HQ1K.
TreeFamiTF315246.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q61136-1 [UniParc]FASTAAdd to Basket

« Hide

MAATEPPSLR EQAEMDDADN SEKSVNEENG EVSEDQSQNK HSRHKKKKHK     50
HRSKHKKHKH SSEEDRDKKH KHKHKHKKHK RKEVIEASDK EGLSPAKRTK 100
LDDLALLEDL EKQRALIKAE LDNELMEGKV QSGMGLILQG YESGSEEEGE 150
IHEKARNGNR SSTRSSSTRG KLEITDNKNS AKKRSKSRSK ERTRHRSDKR 200
KSKGAGEMLR EKANRSKSKE RRKSKSPSKR SKSQDQARKS KSPPLRRRSQ 250
EKVGKARSPA EEKMKSEEKG KIKDRKKSPI VNERSRDRSK KSKSPVDLRD 300
KSKDRRSRSK ERKSKRSEID KEKKPIKSPS KDASSGKENR SPSRRPGRSP 350
KRRSLSPKLR DKSRRSRSPL LNDRRSKQSK SPSRTLSPGR RAKSRSLERK 400
RREPERRRLS SPRTRPRDDI LGRCERSKDA SPINRWSPTR RRSRSPIRRR 450
SRSPLRRSRS PRRRSRSPRR RDRSRRSRSR LRRRSRSRGG HRRRSRSKVK 500
EDKFKGSLSE GMKVEQESSS DDNLEDFDVE EEDEEALIEQ RRIQRQAIVQ 550
KYKYLAEDSN ISVPSEPSSP QSSTRSRSPS PDDILERVAA DVKEYERENV 600
DTFEASVKAK HNLMTVEQNN GSSQKKILAP DMFTESDDMF AAYFDSARLR 650
AAGIGKDFKE NPNLRDNWTD AEGYYRVNIG EVLDKRYNVY GYTGQGVFSN 700
VVRARDNARA NQEVAVKIIR NNELMQKTGL KELEFLKKLN DADPDDKFHC 750
LRLFRHFYHK QHLCLVFEPL SMNLREVLKK YGKDVGLHIK AVRSYSQQLF 800
LALKLLKRCN ILHADIKPDN ILVNESKTIL KLCDFGSASH VADNDITPYL 850
VSRFYRAPEI IIGKSYDYGI DMWSVGCTLY ELYTGKILFP GKTNNHMLKL 900
AMDLKGKMPN KMIRKGVFKD QHFDQNLNFM YIEVDKVTER EKVTVMSTIN 950
PTKDLLADLI GCQRLPEDQR KKVHQLKDLL DQILMLDPAK RISINQALQH 1000
AFIQEKI 1007
Length:1,007
Mass (Da):116,976
Last modified:July 27, 2011 - v3
Checksum:i18E1B7371E17AB4C
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti185 – 1873SKS → IPG in AAC32042. 1 Publication
Sequence conflicti223 – 2231K → I in AAC32042. 1 Publication
Sequence conflicti478 – 4781R → K in AAM19102. 1 Publication
Sequence conflicti478 – 4781R → K in AAC32042. 1 Publication
Sequence conflicti633 – 6331F → L in AAB03269. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS26448.1.
RefSeqiNP_038858.2. NM_013830.2.
UniGeneiMm.10027.
Mm.482253.

Genome annotation databases

EnsembliENSMUST00000077853; ENSMUSP00000077019; ENSMUSG00000021413.
GeneIDi19134.
KEGGimmu:19134.
UCSCiuc007qbp.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS26448.1.
RefSeqi NP_038858.2. NM_013830.2.
UniGenei Mm.10027.
Mm.482253.

3D structure databases

ProteinModelPortali Q61136.
SMRi Q61136. Positions 603-1005.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202400. 2 interactions.
IntActi Q61136. 3 interactions.
MINTi MINT-1751441.

PTM databases

PhosphoSitei Q61136.

Proteomic databases

MaxQBi Q61136.
PaxDbi Q61136.
PRIDEi Q61136.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000077853 ; ENSMUSP00000077019 ; ENSMUSG00000021413 .
GeneIDi 19134.
KEGGi mmu:19134.
UCSCi uc007qbp.2. mouse.

Organism-specific databases

CTDi 8899.
MGIi MGI:109584. Prpf4b.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00580000081366.
HOVERGENi HBG055182.
InParanoidi B2RUN6.
KOi K08827.
OMAi RSEIDKE.
OrthoDBi EOG76HQ1K.
TreeFami TF315246.

Enzyme and pathway databases

BRENDAi 2.7.11.1. 3474.

Miscellaneous databases

NextBioi 295762.
PROi Q61136.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q61136.
Bgeei Q61136.
Genevestigatori Q61136.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiPRP4B_MOUSE
AccessioniPrimary (citable) accession number: Q61136
Secondary accession number(s): B2RUN6
, O88378, Q8BND8, Q8R4Y5, Q9CTL9, Q9CTT0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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