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Q13523 (PRP4B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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 kinase
PRP4 pre-mRNA-processing factor 4 homolog
Gene names
Name:PRPF4B
Synonyms:KIAA0536, PRP4, PRP4H, PRP4K
OrganismHomo sapiens (Human) [Reference 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. Interacts with Clk1 C-terminus. Ref.9

Subcellular location

Nucleus.

Tissue specificity

Ubiquitous.

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 caution

The sequence AAH09844.1 differs from that shown. Reason: Frameshift at position 432.

The sequence BAA25462.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.13
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.13 Ref.19 Ref.20
Modified residue201Phosphoserine Ref.12 Ref.14 Ref.16 Ref.18
Modified residue231Phosphoserine Ref.11 Ref.12 Ref.14 Ref.16 Ref.18
Modified residue321Phosphoserine Ref.11 Ref.12 Ref.14 Ref.16 Ref.18
Modified residue871Phosphoserine Ref.11 Ref.16 Ref.18
Modified residue931Phosphoserine Ref.11 Ref.16 Ref.18
Modified residue991N6-acetyllysine By similarity
Modified residue1401Phosphotyrosine Ref.12 Ref.14
Modified residue1421Phosphoserine Ref.12 Ref.14 Ref.18
Modified residue1441Phosphoserine Ref.12 Ref.14 Ref.18
Modified residue2391Phosphoserine Ref.16
Modified residue2411Phosphoserine Ref.16
Modified residue2571Phosphoserine Ref.12 Ref.16
Modified residue2771Phosphoserine Ref.11 Ref.12 Ref.16 Ref.18
Modified residue2831Phosphoserine Ref.16
Modified residue2941Phosphoserine Ref.18
Modified residue3281Phosphoserine Ref.18
Modified residue3541Phosphoserine Ref.18
Modified residue3561Phosphoserine Ref.18
Modified residue3661Phosphoserine Ref.11 Ref.16 Ref.18
Modified residue3681Phosphoserine Ref.11 Ref.16 Ref.18
Modified residue3851Phosphothreonine Ref.18
Modified residue3871Phosphoserine Ref.18
Modified residue4271Phosphoserine Ref.12
Modified residue4311Phosphoserine Ref.12 Ref.16 Ref.18
Modified residue4371Phosphoserine Ref.12
Modified residue5181Phosphoserine Ref.14 Ref.16 Ref.18
Modified residue5191Phosphoserine Ref.14 Ref.16 Ref.18
Modified residue5201Phosphoserine Ref.14 Ref.16 Ref.18
Modified residue5651Phosphoserine Ref.16
Modified residue5691Phosphoserine Ref.12
Modified residue5781Phosphoserine Ref.12 Ref.14 Ref.16 Ref.18
Modified residue5801Phosphoserine Ref.12 Ref.14 Ref.16 Ref.18
Modified residue7171N6-acetyllysine Ref.15
Modified residue8491Phosphotyrosine Ref.12 Ref.16 Ref.18
Modified residue8521Phosphoserine By similarity

Natural variations

Natural variant831I → V. Ref.1 Ref.2 Ref.3 Ref.4 Ref.11 Ref.12 Ref.13 Ref.16 Ref.18
Corresponds to variant rs9503893 [ dbSNP | Ensembl ].
VAR_046969
Natural variant5841I → V. Ref.22
VAR_047798
Natural variant6581F → L in a breast cancer sample; somatic mutation. Ref.21 Ref.22
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

Secondary structure

......................................................... 1007
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q13523 [UniParc].

Last modified January 11, 2011. Version 3.
Checksum: EC8C1538A61EDA78

FASTA1,007116,987
        10         20         30         40         50         60 
MAAAETQSLR EQPEMEDANS EKSINEENGE VSEDQSQNKH SRHKKKKHKH RSKHKKHKHS 

        70         80         90        100        110        120 
SEEDKDKKHK HKHKHKKHKR KEIIDASDKE 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, VARIANT VAL-83.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-83.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-83.
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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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].
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[10]"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].
[11]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-32; SER-87; SER-93; SER-277; SER-366 AND SER-368, VARIANT [LARGE SCALE ANALYSIS] VAL-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; SER-32; TYR-140; SER-142; SER-144; SER-257; SER-277; SER-427; SER-431; SER-437; SER-569; SER-578; SER-580 AND TYR-849, VARIANT [LARGE SCALE ANALYSIS] VAL-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, VARIANT [LARGE SCALE ANALYSIS] VAL-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[14]"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] [Europe PMC] [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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-717, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [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-283; SER-366; SER-368; SER-431; SER-518; SER-519; SER-520; SER-565; SER-578; SER-580 AND TYR-849, VARIANT [LARGE SCALE ANALYSIS] VAL-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; SER-32; SER-87; SER-93; SER-142; SER-144; SER-277; SER-294; SER-328; SER-354; SER-356; SER-366; SER-368; THR-385; SER-387; SER-431; SER-518; SER-519; SER-520; SER-578; SER-580 AND TYR-849, VARIANT [LARGE SCALE ANALYSIS] VAL-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"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] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-658.
[22]"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] [Europe PMC] [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.
RefSeqNP_003904.3. NM_003913.4.
UniGeneHs.159014.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4IANX-ray2.44A/B657-1007[»]
4IFCX-ray2.13A/B657-1007[»]
4IIRX-ray2.00A/B657-1007[»]
4IJPX-ray2.25A/B657-1007[»]
ProteinModelPortalQ13523.
SMRQ13523. Positions 603-1005.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114416. 36 interactions.
IntActQ13523. 32 interactions.
MINTMINT-1379795.
STRING9606.ENSP00000337194.

Chemistry

BindingDBQ13523.
ChEMBLCHEMBL1908382.
GuidetoPHARMACOLOGY2177.

PTM databases

PhosphoSiteQ13523.

Polymorphism databases

DMDM317373526.

Proteomic databases

PaxDbQ13523.
PRIDEQ13523.

Protocols and materials databases

DNASU8899.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000337659; ENSP00000337194; ENSG00000112739.
ENST00000480058; ENSP00000433547; ENSG00000112739.
GeneID8899.
KEGGhsa:8899.
UCSCuc003mvv.3. human.

Organism-specific databases

CTD8899.
GeneCardsGC06P004021.
H-InvDBHIX0005547.
HGNCHGNC:17346. PRPF4B.
HPAHPA020638.
MIM602338. gene.
neXtProtNX_Q13523.
PharmGKBPA38447.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG055182.
InParanoidQ13523.
KOK08827.
OMARSEIDKE.
OrthoDBEOG76HQ1K.
PhylomeDBQ13523.
TreeFamTF315246.

Enzyme and pathway databases

BRENDA2.7.11.1. 2681.
SignaLinkQ13523.

Gene expression databases

ArrayExpressQ13523.
BgeeQ13523.
CleanExHS_PRPF4B.
GenevestigatorQ13523.

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

ChiTaRSPRPF4B. human.
GeneWikiPRPF4B.
GenomeRNAi8899.
NextBio33431.
PROQ13523.
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: January 11, 2011
Last modified: April 16, 2014
This is version 157 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM