Reviewed, UniProtKB/Swiss-Prot Q13523 (PRP4B_HUMAN)

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

Name:	PRPF4B
Synonyms:	KIAA0536, PRP4, PRP4H, PRP4K

Organism

Homo sapiens (Human) [Complete proteome]

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 further processed into a mature form.
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	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

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	Acetylation Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	RNA splicing Ref.8 Traceable author statement. Source: ProtInc mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW protein amino acid phosphorylation Ref.8 Traceable author statement. Source: ProtInc
Cellular component	spliceosomal complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
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
	Initiator methionine	1	1	Removed
	Chain	2 – 1007	1006	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	2	1	N-acetylalanine Ref.18 Ref.20
	Modified residue	6	1	Phosphothreonine Ref.18
	Modified residue	8	1	Phosphoserine Ref.18
	Modified residue	20	1	Phosphoserine Ref.10 Ref.13 Ref.19 Ref.20 Ref.22
	Modified residue	23	1	Phosphoserine Ref.10 Ref.13 Ref.19 Ref.20 Ref.22
	Modified residue	32	1	Phosphoserine Ref.10 Ref.13 Ref.19 Ref.20 Ref.22
	Modified residue	36	1	Phosphoserine Ref.10
	Modified residue	87	1	Phosphoserine Ref.13 Ref.19 Ref.20
	Modified residue	93	1	Phosphoserine Ref.13 Ref.19 Ref.20
	Modified residue	140	1	Phosphotyrosine Ref.19 Ref.22
	Modified residue	142	1	Phosphoserine Ref.19 Ref.20 Ref.22
	Modified residue	144	1	Phosphoserine Ref.19 Ref.20 Ref.22
	Modified residue	239	1	Phosphoserine Ref.13
	Modified residue	241	1	Phosphoserine Ref.13
	Modified residue	257	1	Phosphoserine Ref.13 Ref.19
	Modified residue	277	1	Phosphoserine Ref.10 Ref.13 Ref.17 Ref.19
	Modified residue	292	1	Phosphoserine Ref.13 Ref.14 Ref.19
	Modified residue	294	1	Phosphoserine Ref.10 Ref.13 Ref.14 Ref.19
	Modified residue	328	1	Phosphoserine Ref.13
	Modified residue	354	1	Phosphoserine Ref.10
	Modified residue	356	1	Phosphoserine Ref.10
	Modified residue	358	1	N6-acetyllysine Ref.23
	Modified residue	366	1	Phosphoserine Ref.10 Ref.13 Ref.17
	Modified residue	368	1	Phosphoserine Ref.10 Ref.13 Ref.17
	Modified residue	381	1	Phosphoserine Ref.13
	Modified residue	385	1	Phosphothreonine Ref.13
	Modified residue	387	1	Phosphoserine Ref.10 Ref.13
	Modified residue	410	1	Phosphoserine Ref.13
	Modified residue	411	1	Phosphoserine Ref.13
	Modified residue	427	1	Phosphoserine Ref.19
	Modified residue	431	1	Phosphoserine Ref.10 Ref.13 Ref.19
	Modified residue	437	1	Phosphoserine Ref.10 Ref.13 Ref.19
	Modified residue	518	1	Phosphoserine Ref.19 Ref.22
	Modified residue	519	1	Phosphoserine Ref.19 Ref.22
	Modified residue	520	1	Phosphoserine Ref.19 Ref.22
	Modified residue	569	1	Phosphoserine Ref.10 Ref.19
	Modified residue	576	1	Phosphothreonine Ref.13
	Modified residue	578	1	Phosphoserine Ref.10 Ref.13 Ref.15 Ref.19 Ref.22
	Modified residue	580	1	Phosphoserine Ref.10 Ref.13 Ref.19 Ref.22
	Modified residue	717	1	N6-acetyllysine Ref.23
	Modified residue	849	1	Phosphotyrosine Ref.11 Ref.12 Ref.13 Ref.16 Ref.19 Ref.21
	Modified residue	852	1	Phosphoserine By similarity
Natural variations
	Natural variant	83	1	V → I: dbSNP rs9503893. Ref.4 Ref.5 Ref.6		VAR_046969
	Natural variant	584	1	I → V		VAR_047798
	Natural variant	658	1	F → L in a breast cancer sample; somatic mutation. Ref.24 Ref.25		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

	Sequence		Length	Mass (Da)
	Q13523-1 [UniParc]. Last modified October 10, 2002. Version 2. Checksum: 45ECF73ABB56D17C	FASTA	1,007	116,973
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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. , 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. , 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.
IPI	IPI00013721.
RefSeq	NP_003904.3.
UniGene	Hs.159014
3D structure databases
SMR	Q13523. Positions 625-840, 669-1005.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13523. 9 interactions.
STRING	Q13523.
PTM databases
PhosphoSite	Q13523.
Proteomic databases
PRIDE	Q13523.
Genome annotation databases
Ensembl	ENST00000337659; ENSP00000337194; ENSG00000112739; Homo sapiens. [Genome view]
GeneID	8899.
KEGG	hsa:8899.
Organism-specific databases
CTD	8899.
GeneCards	GC06P003966. GC0XM115768.
H-InvDB	HIX0005547.
HGNC	HGNC:17346. PRPF4B.
HPA	HPA020638.
MIM	602338. gene.
PharmGKB	PA38447.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG04572.
HOVERGEN	Q13523.
InParanoid	Q13523.
Enzyme and pathway databases
BRENDA	2.7.11.1. 247.
Gene expression databases
ArrayExpress	Q13523.
Bgee	Q13523.
CleanEx	HS_PRPF4B.
Genevestigator	Q13523.
GermOnline	ENSG00000112739. Homo sapiens.
Family and domain databases
InterPro	IPR011009. 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]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
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
NextBio	33431.
SOURCE	Search...

Entry information

Entry name

PRP4B_HUMAN

Accession

Primary (citable) accession number: Q13523
Secondary accession number(s): A8K5C9 , 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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.