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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q13523: Variant p.Ile83Val

Serine/threonine-protein kinase PRP4 homolog
Gene: PRP4K
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Variant information Variant position: help 83 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LB/B The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance

Residue change: help From Isoleucine (I) to Valine (V) at position 83 (I83V, p.Ile83Val). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Similar physico-chemical property. Both residues are medium size and hydrophobic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 3 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page

Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 83 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1007 The length of the canonical sequence.
Location on the sequence: help EDKDKKHKHKHKHKKHKRKE I IDASDKEGMSPAKRTKLDDL The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: help The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human                         EDKDKKHKHKHKHKKHKRKEIIDASDKEGMSPAKRTKLDDL

Mouse                         EDRDKKHKHKHKHKKHKRKEVIEASDKEGLSPAKRTKLDDL

Rat                           EDRDKKHKHKHKHKKHKRKEVLDASDKEGLSPAKRTKLDDL

Bovine                        EDKDRKHKHKHKHKKHKRKEVADASDKEGMSPAKRTKLDDL

Slime mold                    --------------------------KRGLESSSPT-----

Sequence annotation in neighborhood: help The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
  • Type: the type of sequence feature.
  • Positions: endpoints of the sequence feature.
  • Description: contains additional information about the feature.
TypePositionsDescription
Chain 2 – 1007 Serine/threonine-protein kinase PRP4 homolog
Region 1 – 99 Disordered
Compositional bias 81 – 99 Basic and acidic residues
Modified residue 87 – 87 Phosphoserine
Modified residue 93 – 93 Phosphoserine
Modified residue 99 – 99 N6-acetyllysine; alternate
Cross 99 – 99 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate



Literature citations
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)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; CHARACTERIZATION; VARIANT VAL-83; PHOSPHORYLATION BY CLK1; 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)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; VARIANT VAL-83; FUNCTION; SUBCELLULAR LOCATION; SUBUNIT; PHOSPHORYLATION; 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)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]; VARIANT VAL-83; 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)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]; VARIANT VAL-83; 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)
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]; 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)
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]; 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)
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; VARIANT [LARGE SCALE ANALYSIS] VAL-83; CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]; 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)
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]; 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)
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]; Toward a comprehensive characterization of a human cancer cell phosphoproteome.
Zhou H.; Di Palma S.; Preisinger C.; Peng M.; Polat A.N.; Heck A.J.; Mohammed S.;
J. Proteome Res. 12:260-271(2013)
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; SER-87; SER-93; SER-166; SER-277; SER-292; SER-294; SER-366; SER-368; SER-427; SER-431 AND SER-437; VARIANT [LARGE SCALE ANALYSIS] VAL-83; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS];
Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.