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Q13523

- PRP4B_HUMAN

UniProt

Q13523 - PRP4B_HUMAN

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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

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 kinase activity Source: ProtInc
  4. 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
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 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
Complete GO annotation...

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

BgeeiQ13523.
CleanExiHS_PRPF4B.
ExpressionAtlasiQ13523. baseline and differential.
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. 45 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.
GeneTreeiENSGT00760000119032.
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.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAAETQSLR EQPEMEDANS EKSINEENGE VSEDQSQNKH SRHKKKKHKH
60 70 80 90 100
RSKHKKHKHS SEEDKDKKHK HKHKHKKHKR KEIIDASDKE GMSPAKRTKL
110 120 130 140 150
DDLALLEDLE KQRALIKAEL DNELMEGKVQ SGMGLILQGY ESGSEEEGEI
160 170 180 190 200
HEKARNGNRS STRSSSTKGK LELVDNKITT KKRSKSRSKE RTRHRSDKKK
210 220 230 240 250
SKGGIEIVKE KTTRSKSKER KKSKSPSKRS KSQDQARKSK SPTLRRRSQE
260 270 280 290 300
KIGKARSPTD DKVKIEDKSK SKDRKKSPII NESRSRDRGK KSRSPVDLRG
310 320 330 340 350
KSKDRRSRSK ERKSKRSETD KEKKPIKSPS KDASSGKENR SPSRRPGRSP
360 370 380 390 400
KRRSLSPKPR DKSRRSRSPL LNDRRSKQSK SPSRTLSPGR RAKSRSLERK
410 420 430 440 450
RREPERRRLS SPRTRPRDDI LSRRERSKDA SPINRWSPTR RRSRSPIRRR
460 470 480 490 500
SRSPLRRSRS PRRRSRSPRR RDRGRRSRSR LRRRSRSRGG RRRRSRSKVK
510 520 530 540 550
EDKFKGSLSE GMKVEQESSS DDNLEDFDVE EEDEEALIEQ RRIQRQAIVQ
560 570 580 590 600
KYKYLAEDSN MSVPSEPSSP QSSTRTRSPS PDDILERVAA DVKEYERENV
610 620 630 640 650
DTFEASVKAK HNLMTVEQNN GSSQKKLLAP DMFTESDDMF AAYFDSARLR
660 670 680 690 700
AAGIGKDFKE NPNLRDNWTD AEGYYRVNIG EVLDKRYNVY GYTGQGVFSN
710 720 730 740 750
VVRARDNARA NQEVAVKIIR NNELMQKTGL KELEFLKKLN DADPDDKFHC
760 770 780 790 800
LRLFRHFYHK QHLCLVFEPL SMNLREVLKK YGKDVGLHIK AVRSYSQQLF
810 820 830 840 850
LALKLLKRCN ILHADIKPDN ILVNESKTIL KLCDFGSASH VADNDITPYL
860 870 880 890 900
VSRFYRAPEI IIGKSYDYGI DMWSVGCTLY ELYTGKILFP GKTNNHMLKL
910 920 930 940 950
AMDLKGKMPN KMIRKGVFKD QHFDQNLNFM YIEVDKVTER EKVTVMSTIN
960 970 980 990 1000
PTKDLLADLI GCQRLPEDQR KKVHQLKDLL DQILMLDPAK RISINQALQH

AFIQEKI
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. 45 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.
GeneTreei ENSGT00760000119032.
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

Bgeei Q13523.
CleanExi HS_PRPF4B.
ExpressionAtlasi Q13523. baseline and differential.
Genevestigatori Q13523.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "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 29, 2014
This is version 163 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