Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q13523

- PRP4B_HUMAN

UniProt

Q13523 - PRP4B_HUMAN

Protein

Serine/threonine-protein kinase PRP4 homolog

Gene

PRPF4B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 162 (01 Oct 2014)
      Sequence version 3 (11 Jan 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 – 7171ATPPROSITE-ProRule annotation
    Active sitei815 – 8151Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi693 – 7019ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. protein kinase activity Source: ProtInc
    5. protein serine/threonine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. mRNA splicing, via spliceosome Source: UniProtKB
    2. protein phosphorylation Source: ProtInc
    3. RNA splicing Source: ProtInc

    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. 2681.
    SignaLinkiQ13523.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:PRPF4B
    Synonyms:KIAA0536, PRP4, PRP4H, PRP4K
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:17346. PRPF4B.

    Subcellular locationi

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. chromosome Source: Ensembl
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus, Spliceosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38447.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 10071006Serine/threonine-protein kinase PRP4 homologPRO_0000086586Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei20 – 201Phosphoserine4 Publications
    Modified residuei23 – 231Phosphoserine5 Publications
    Modified residuei32 – 321Phosphoserine5 Publications
    Modified residuei87 – 871Phosphoserine3 Publications
    Modified residuei93 – 931Phosphoserine3 Publications
    Modified residuei99 – 991N6-acetyllysineBy similarity
    Modified residuei140 – 1401Phosphotyrosine2 Publications
    Modified residuei142 – 1421Phosphoserine3 Publications
    Modified residuei144 – 1441Phosphoserine3 Publications
    Modified residuei239 – 2391Phosphoserine1 Publication
    Modified residuei241 – 2411Phosphoserine1 Publication
    Modified residuei257 – 2571Phosphoserine2 Publications
    Modified residuei277 – 2771Phosphoserine4 Publications
    Modified residuei283 – 2831Phosphoserine1 Publication
    Modified residuei294 – 2941Phosphoserine1 Publication
    Modified residuei328 – 3281Phosphoserine1 Publication
    Modified residuei354 – 3541Phosphoserine1 Publication
    Modified residuei356 – 3561Phosphoserine1 Publication
    Modified residuei366 – 3661Phosphoserine3 Publications
    Modified residuei368 – 3681Phosphoserine3 Publications
    Modified residuei385 – 3851Phosphothreonine1 Publication
    Modified residuei387 – 3871Phosphoserine1 Publication
    Modified residuei427 – 4271Phosphoserine1 Publication
    Modified residuei431 – 4311Phosphoserine3 Publications
    Modified residuei437 – 4371Phosphoserine1 Publication
    Modified residuei518 – 5181Phosphoserine3 Publications
    Modified residuei519 – 5191Phosphoserine3 Publications
    Modified residuei520 – 5201Phosphoserine3 Publications
    Modified residuei565 – 5651Phosphoserine1 Publication
    Modified residuei569 – 5691Phosphoserine1 Publication
    Modified residuei578 – 5781Phosphoserine4 Publications
    Modified residuei580 – 5801Phosphoserine4 Publications
    Modified residuei717 – 7171N6-acetyllysine1 Publication
    Modified residuei849 – 8491Phosphotyrosine3 Publications
    Modified residuei852 – 8521PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated by Clk1.5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ13523.
    PaxDbiQ13523.
    PRIDEiQ13523.

    PTM databases

    PhosphoSiteiQ13523.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ13523.
    BgeeiQ13523.
    CleanExiHS_PRPF4B.
    GenevestigatoriQ13523.

    Organism-specific databases

    HPAiHPA020638.

    Interactioni

    Subunit structurei

    Identified in the spliceosome C complex. Interacts with Clk1 C-terminus.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARRB1P494072EBI-395940,EBI-743313
    ARRB2P321213EBI-395940,EBI-714559
    gagP045906EBI-395940,EBI-780156From a different organism.
    KLF13Q9Y2Y95EBI-395940,EBI-1255893
    POLR3FQ9H1D92EBI-395940,EBI-710067

    Protein-protein interaction databases

    BioGridi114416. 39 interactions.
    IntActiQ13523. 32 interactions.
    MINTiMINT-1379795.
    STRINGi9606.ENSP00000337194.

    Structurei

    Secondary structure

    1
    1007
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi671 – 6733
    Turni684 – 6863
    Beta strandi687 – 6948
    Beta strandi697 – 6993
    Beta strandi700 – 7067
    Helixi707 – 7093
    Beta strandi713 – 7186
    Helixi724 – 74219
    Beta strandi753 – 7597
    Beta strandi762 – 7676
    Helixi774 – 7818
    Turni783 – 7853
    Helixi789 – 80820
    Helixi818 – 8203
    Beta strandi821 – 8233
    Beta strandi830 – 8323
    Beta strandi839 – 8424
    Helixi853 – 8553
    Helixi858 – 8625
    Helixi869 – 88416
    Helixi894 – 90512
    Helixi910 – 9156
    Turni920 – 9223
    Beta strandi929 – 9324
    Beta strandi943 – 9475
    Helixi955 – 9595
    Helixi967 – 98317
    Helixi988 – 9903
    Helixi994 – 9985
    Helixi1001 – 10044

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4IANX-ray2.44A/B657-1007[»]
    4IFCX-ray2.13A/B657-1007[»]
    4IIRX-ray2.00A/B657-1007[»]
    4IJPX-ray2.25A/B657-1007[»]
    ProteinModelPortaliQ13523.
    SMRiQ13523. Positions 603-1005.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini687 – 1006320Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi39 – 496458Arg/Lys-rich (basic)Add
    BLAST
    Compositional biasi40 – 7839His-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG055182.
    InParanoidiQ13523.
    KOiK08827.
    OMAiRSEIDKE.
    OrthoDBiEOG76HQ1K.
    PhylomeDBiQ13523.
    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.

    Q13523-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAAETQSLR EQPEMEDANS EKSINEENGE VSEDQSQNKH SRHKKKKHKH     50
    RSKHKKHKHS SEEDKDKKHK HKHKHKKHKR KEIIDASDKE GMSPAKRTKL 100
    DDLALLEDLE KQRALIKAEL DNELMEGKVQ SGMGLILQGY ESGSEEEGEI 150
    HEKARNGNRS STRSSSTKGK LELVDNKITT KKRSKSRSKE RTRHRSDKKK 200
    SKGGIEIVKE KTTRSKSKER KKSKSPSKRS KSQDQARKSK SPTLRRRSQE 250
    KIGKARSPTD DKVKIEDKSK SKDRKKSPII NESRSRDRGK KSRSPVDLRG 300
    KSKDRRSRSK ERKSKRSETD KEKKPIKSPS KDASSGKENR SPSRRPGRSP 350
    KRRSLSPKPR DKSRRSRSPL LNDRRSKQSK SPSRTLSPGR RAKSRSLERK 400
    RREPERRRLS SPRTRPRDDI LSRRERSKDA SPINRWSPTR RRSRSPIRRR 450
    SRSPLRRSRS PRRRSRSPRR RDRGRRSRSR LRRRSRSRGG RRRRSRSKVK 500
    EDKFKGSLSE GMKVEQESSS DDNLEDFDVE EEDEEALIEQ RRIQRQAIVQ 550
    KYKYLAEDSN MSVPSEPSSP QSSTRTRSPS PDDILERVAA DVKEYERENV 600
    DTFEASVKAK HNLMTVEQNN GSSQKKLLAP 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):116,987
    Last modified:January 11, 2011 - v3
    Checksum:iEC8C1538A61EDA78
    GO

    Sequence cautioni

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti468 – 4681P → T in AAH34969. (PubMed:15489334)Curated
    Sequence conflicti610 – 6101K → R in BAF83933. (PubMed:14702039)Curated
    Sequence conflicti754 – 7541F → L in AAH34969. (PubMed:15489334)Curated
    Sequence conflicti851 – 8511V → F in AAH34969. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti83 – 831I → V.9 Publications
    Corresponds to variant rs9503893 [ dbSNP | Ensembl ].
    VAR_046969
    Natural varianti584 – 5841I → V.1 Publication
    VAR_047798
    Natural varianti658 – 6581F → L in a breast cancer sample; somatic mutation. 2 Publications
    VAR_035633

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS4488.1.
    RefSeqiNP_003904.3. NM_003913.4.
    UniGeneiHs.159014.

    Genome annotation databases

    EnsembliENST00000337659; ENSP00000337194; ENSG00000112739.
    ENST00000480058; ENSP00000433547; ENSG00000112739.
    GeneIDi8899.
    KEGGihsa:8899.
    UCSCiuc003mvv.3. human.

    Polymorphism databases

    DMDMi317373526.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS4488.1.
    RefSeqi NP_003904.3. NM_003913.4.
    UniGenei Hs.159014.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4IAN X-ray 2.44 A/B 657-1007 [» ]
    4IFC X-ray 2.13 A/B 657-1007 [» ]
    4IIR X-ray 2.00 A/B 657-1007 [» ]
    4IJP X-ray 2.25 A/B 657-1007 [» ]
    ProteinModelPortali Q13523.
    SMRi Q13523. Positions 603-1005.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114416. 39 interactions.
    IntActi Q13523. 32 interactions.
    MINTi MINT-1379795.
    STRINGi 9606.ENSP00000337194.

    Chemistry

    BindingDBi Q13523.
    ChEMBLi CHEMBL1908382.
    GuidetoPHARMACOLOGYi 2177.

    PTM databases

    PhosphoSitei Q13523.

    Polymorphism databases

    DMDMi 317373526.

    Proteomic databases

    MaxQBi Q13523.
    PaxDbi Q13523.
    PRIDEi Q13523.

    Protocols and materials databases

    DNASUi 8899.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000337659 ; ENSP00000337194 ; ENSG00000112739 .
    ENST00000480058 ; ENSP00000433547 ; ENSG00000112739 .
    GeneIDi 8899.
    KEGGi hsa:8899.
    UCSCi uc003mvv.3. human.

    Organism-specific databases

    CTDi 8899.
    GeneCardsi GC06P004021.
    H-InvDB HIX0005547.
    HGNCi HGNC:17346. PRPF4B.
    HPAi HPA020638.
    MIMi 602338. gene.
    neXtProti NX_Q13523.
    PharmGKBi PA38447.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG055182.
    InParanoidi Q13523.
    KOi K08827.
    OMAi RSEIDKE.
    OrthoDBi EOG76HQ1K.
    PhylomeDBi Q13523.
    TreeFami TF315246.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 2681.
    SignaLinki Q13523.

    Miscellaneous databases

    ChiTaRSi PRPF4B. human.
    GeneWikii PRPF4B.
    GenomeRNAii 8899.
    NextBioi 33431.
    PROi Q13523.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13523.
    Bgeei Q13523.
    CleanExi HS_PRPF4B.
    Genevestigatori Q13523.

    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

    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.
      , 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.
      , 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. 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. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. 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.
      , 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.

    Entry informationi

    Entry nameiPRP4B_HUMAN
    AccessioniPrimary (citable) accession number: Q13523
    Secondary accession number(s): A8K5C9
    , Q5D0F6, Q5TAY8, Q8IVC3, Q8TDP2, Q96QT7, Q9UEE6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 162 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3