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Reviewed, UniProtKB/Swiss-Prot Q13523 (PRP4B_HUMAN)

Last modified January 19, 2010. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
    PRP4 kinase
Gene names
Name: PRPF4B
Synonyms: KIAA0536, PRP4, PRP4H, PRP4K
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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, 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

Nucleus.

Tissue specificity

Ubiquitous.

Post-translational modification

Phosphorylated by Clk1. Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22

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

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 10071006Serine/threonine-protein kinase PRP4 homolog
PRO_0000086586

Regions

Domain687 – 1006320Protein kinase
Nucleotide binding693 – 7019ATP By similarity
Compositional bias39 – 496458Arg/Lys-rich (basic)
Compositional bias40 – 7839His-rich

Sites

Active site8151Proton acceptor By similarity
Binding site7171ATP By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.18 Ref.20
Modified residue61Phosphothreonine Ref.18
Modified residue81Phosphoserine Ref.18
Modified residue201Phosphoserine Ref.10 Ref.13 Ref.19 Ref.20 Ref.22
Modified residue231Phosphoserine Ref.10 Ref.13 Ref.19 Ref.20 Ref.22
Modified residue321Phosphoserine Ref.10 Ref.13 Ref.19 Ref.20 Ref.22
Modified residue361Phosphoserine Ref.10
Modified residue871Phosphoserine Ref.13 Ref.19 Ref.20
Modified residue931Phosphoserine Ref.13 Ref.19 Ref.20
Modified residue1401Phosphotyrosine Ref.19 Ref.22
Modified residue1421Phosphoserine Ref.19 Ref.20 Ref.22
Modified residue1441Phosphoserine Ref.19 Ref.20 Ref.22
Modified residue2391Phosphoserine Ref.13
Modified residue2411Phosphoserine Ref.13
Modified residue2571Phosphoserine Ref.13 Ref.19
Modified residue2771Phosphoserine Ref.10 Ref.13 Ref.17 Ref.19
Modified residue2921Phosphoserine Ref.13 Ref.14 Ref.19
Modified residue2941Phosphoserine Ref.10 Ref.13 Ref.14 Ref.19
Modified residue3281Phosphoserine Ref.13
Modified residue3541Phosphoserine Ref.10
Modified residue3561Phosphoserine Ref.10
Modified residue3581N6-acetyllysine Ref.23
Modified residue3661Phosphoserine Ref.10 Ref.13 Ref.17
Modified residue3681Phosphoserine Ref.10 Ref.13 Ref.17
Modified residue3811Phosphoserine Ref.13
Modified residue3851Phosphothreonine Ref.13
Modified residue3871Phosphoserine Ref.10 Ref.13
Modified residue4101Phosphoserine Ref.13
Modified residue4111Phosphoserine Ref.13
Modified residue4271Phosphoserine Ref.19
Modified residue4311Phosphoserine Ref.10 Ref.13 Ref.19
Modified residue4371Phosphoserine Ref.10 Ref.13 Ref.19
Modified residue5181Phosphoserine Ref.19 Ref.22
Modified residue5191Phosphoserine Ref.19 Ref.22
Modified residue5201Phosphoserine Ref.19 Ref.22
Modified residue5691Phosphoserine Ref.10 Ref.19
Modified residue5761Phosphothreonine Ref.13
Modified residue5781Phosphoserine Ref.10 Ref.13 Ref.15 Ref.19 Ref.22
Modified residue5801Phosphoserine Ref.10 Ref.13 Ref.19 Ref.22
Modified residue7171N6-acetyllysine Ref.23
Modified residue8491Phosphotyrosine Ref.11 Ref.12 Ref.13 Ref.16 Ref.19 Ref.21
Modified residue8521Phosphoserine By similarity

Natural variations

Natural variant831V → I: dbSNP rs9503893. Ref.4 Ref.5 Ref.6
VAR_046969
Natural variant5841I → V
VAR_047798
Natural variant6581F → L in a breast cancer sample; somatic mutation. Ref.24 Ref.25
VAR_035633

Experimental info

Sequence conflict4681P → T in AAH34969. Ref.7
Sequence conflict6101K → R in BAF83933. Ref.4
Sequence conflict7541F → L in AAH34969. Ref.7
Sequence conflict8511V → F in AAH34969. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Q13523-1 [UniParc].

Last modified October 10, 2002. Version 2.
Checksum: 45ECF73ABB56D17C

FASTA1,007116,973
        10         20         30         40         50         60 
MAAAETQSLR EQPEMEDANS EKSINEENGE VSEDQSQNKH SRHKKKKHKH RSKHKKHKHS 

        70         80         90        100        110        120 
SEEDKDKKHK HKHKHKKHKR KEVIDASDKE GMSPAKRTKL DDLALLEDLE KQRALIKAEL 

       130        140        150        160        170        180 
DNELMEGKVQ SGMGLILQGY ESGSEEEGEI HEKARNGNRS STRSSSTKGK LELVDNKITT 

       190        200        210        220        230        240 
KKRSKSRSKE RTRHRSDKKK SKGGIEIVKE KTTRSKSKER KKSKSPSKRS KSQDQARKSK 

       250        260        270        280        290        300 
SPTLRRRSQE KIGKARSPTD DKVKIEDKSK SKDRKKSPII NESRSRDRGK KSRSPVDLRG 

       310        320        330        340        350        360 
KSKDRRSRSK ERKSKRSETD KEKKPIKSPS KDASSGKENR SPSRRPGRSP KRRSLSPKPR 

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

       430        440        450        460        470        480 
LSRRERSKDA SPINRWSPTR RRSRSPIRRR SRSPLRRSRS PRRRSRSPRR RDRGRRSRSR 

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

       550        560        570        580        590        600 
RRIQRQAIVQ KYKYLAEDSN MSVPSEPSSP QSSTRTRSPS PDDILERVAA DVKEYERENV 

       610        620        630        640        650        660 
DTFEASVKAK HNLMTVEQNN GSSQKKLLAP 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]"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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., 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. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., 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. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 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)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain and Lung.
[8]"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.
[9]"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
RNA 8:426-439(2002) [PubMed: 11991638] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPICEOSOMAL C COMPLEX.
[10]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; SER-32; SER-36; SER-277; SER-294; SER-354; SER-356; SER-366; SER-368; SER-387; SER-431; SER-437; SER-569; SER-578 AND SER-580, MASS SPECTROMETRY.
Tissue: Epithelium.
[11]"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules."
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.
Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-849, MASS SPECTROMETRY.
Tissue: Epithelium.
[12]"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.
[13]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; SER-32; SER-87; SER-93; SER-239; SER-241; SER-257; SER-277; SER-292; SER-294; SER-328; SER-366; SER-368; SER-381; THR-385; SER-387; SER-410; SER-411; SER-431; SER-437; THR-576; SER-578; SER-580 AND TYR-849, MASS SPECTROMETRY.
Tissue: Epithelium.
[14]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292 AND SER-294, MASS SPECTROMETRY.
Tissue: Epithelium.
[15]"Phosphoproteome analysis of the human mitotic spindle."
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578, MASS SPECTROMETRY.
Tissue: Epithelium.
[16]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-849, MASS SPECTROMETRY.
[17]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277; SER-366 AND SER-368, MASS SPECTROMETRY.
Tissue: Epithelium.
[18]"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis."
Wang B., Malik R., Nigg E.A., Korner R.
Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6 AND SER-8, ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
[19]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; SER-32; SER-87; SER-93; TYR-140; SER-142; SER-144; SER-257; SER-277; SER-292; SER-294; SER-427; SER-431; SER-437; SER-518; SER-519; SER-520; SER-569; SER-578; SER-580 AND TYR-849, MASS SPECTROMETRY.
[20]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; SER-32; SER-87; SER-93; SER-142 AND SER-144, MASS SPECTROMETRY.
[21]"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells."
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J.
J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-849, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[22]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; SER-32; TYR-140; SER-142; SER-144; SER-518; SER-519; SER-520; SER-578 AND SER-580, MASS SPECTROMETRY.
Tissue: T-cell.
[23]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-358 AND LYS-717, MASS SPECTROMETRY.
[24]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-658.
[25]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed: 17344846] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-584 AND LEU-658.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY029347 mRNA. Translation: AAK38155.1.
AF283465 mRNA. Translation: AAM19101.1.
AB011108 mRNA. Translation: BAA25462.1. Different initiation.
AK291244 mRNA. Translation: BAF83933.1.
AL138831, AL033383 Genomic DNA. Translation: CAI20480.1.
AL033383, AL138831 Genomic DNA. Translation: CAI42121.1.
CH471087 Genomic DNA. Translation: EAW55146.1.
BC009844 mRNA. Translation: AAH09844.1. Frameshift.
BC034969 mRNA. Translation: AAH34969.1.
U48736 mRNA. Translation: AAB03268.1.
IPIIPI00013721.
RefSeqNP_003904.3.
UniGeneHs.159014

3D structure databases

SMRQ13523. Positions 625-840, 669-1005.
ModBaseSearch...

Protein-protein interaction databases

IntActQ13523. 9 interactions.
STRINGQ13523.

PTM databases

PhosphoSiteQ13523.

Proteomic databases

PRIDEQ13523.

Genome annotation databases

EnsemblENST00000337659; ENSP00000337194; ENSG00000112739; Homo sapiens. [Genome view]
GeneID8899.
KEGGhsa:8899.

Organism-specific databases

CTD8899.
GeneCardsGC06P003966.
GC0XM115768.
H-InvDBHIX0005547.
HGNCHGNC:17346. PRPF4B.
HPAHPA020638.
MIM602338. gene.
PharmGKBPA38447.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG04572.
HOVERGENQ13523.
InParanoidQ13523.

Enzyme and pathway databases

BRENDA2.7.11.1. 247.

Gene expression databases

ArrayExpressQ13523.
BgeeQ13523.
CleanExHS_PRPF4B.
GenevestigatorQ13523.
GermOnlineENSG00000112739. Homo sapiens.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR002290. Ser/Thr_prot_kinase_dom.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio33431.
SOURCESearch...

Entry information

Entry namePRP4B_HUMAN
AccessionPrimary (citable) accession number: Q13523
Secondary accession number(s): A8K5C9 expand/collapse secondary AC list , Q5D0F6, Q5TAY8, Q8IVC3, Q8TDP2, Q96QT7, Q9UEE6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: October 10, 2002
Last modified: January 19, 2010
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents