UniProtKB/Swiss-Prot O95391: Variant p.Met229Thr

Pre-mRNA-splicing factor SLU7
Gene: SLU7
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Variant information Variant position:

229 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

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:

From Methionine (M) to Threonine (T) at position 229 (M229T, p.Met229Thr). 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:

Change from medium size and hydrophobic (M) to medium size and polar (T) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-1 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:

Links to websites of interest for the variant.

Variant rs2961944 [ dbSNP | Ensembl ]

Sequence information Variant position:

229 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

586 The length of the canonical sequence.
Location on the sequence:

LVEQANSPKHQWGEEEPNSQ M EKDHNSEDEDEDKYADDIDM 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:

The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         LVEQANSPKHQWGEEEPNSQMEKDHNSEDEDEDKYADDIDM

Mouse                         LVEQANSPKHQWGEEEPNSQMEKDHNSEDEDEDKYADDIDM

Rat                           LVEQANSPKHQWGEEEPNSQMEKDHNSEDEDEDKYADDIDM

Bovine                        LVEQANSPKHQWGEEEPNSQTEKDHNSEDEDEDKYADDIDM

Chicken                       L-----------------EQVERDHNSEDEDEDKYADDIDM

Xenopus laevis                LSEQVSSPRHQWGEDEQNSQTEKDRNSEDEDEDKYADDIDM

Zebrafish                     LMDQANSRKHE--------EAVQDHSSEDEDEDKYVDDFDM

Caenorhabditis elegans        ------------GEVEP----ATTEDGAPKDEDMYAEDADM

Drosophila                    ---------------------DAEISDEEGNEDKYVDEVDM

Slime mold                    ---------GDKKTPDVDETLSKELMDNEEKEGSYDSETVA

Baker's yeast                 ---------TLW---------DTDEEIELMKLELYKDSVGS

Fission yeast                 ---------------------EENRDASENSAVKASRNSTV

Sequence annotation in neighborhood:

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.

Type	Positions	Description
Chain	2 – 586	Pre-mRNA-splicing factor SLU7
Region	206 – 254	Disordered
Compositional bias	223 – 238	Basic and acidic residues
Modified residue	215 – 215	Phosphoserine
Modified residue	227 – 227	Phosphoserine
Modified residue	235 – 235	Phosphoserine

Literature citations
Human step II splicing factor hSlu7 functions in restructuring the spliceosome between the catalytic steps of splicing.
Chua K.; Reed R.;
Genes Dev. 13:841-850(1999)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; FUNCTION; SUBCELLULAR LOCATION; INTERACTION WITH LATE SPLICEOSOMAL COMPLEX; VARIANT THR-229; Submission
Mural R.J.; Istrail S.; Sutton G.G.; Florea L.; Halpern A.L.; Mobarry C.M.; Lippert R.; Walenz B.; Shatkay H.; Dew I.; Miller J.R.; Flanigan M.J.; Edwards N.J.; Bolanos R.; Fasulo D.; Halldorsson B.V.; Hannenhalli S.; Turner R.; Yooseph S.; Lu F.; Nusskern D.R.; Shue B.C.; Zheng X.H.; Zhong F.; Delcher A.L.; Huson D.H.; Kravitz S.A.; Mouchard L.; Reinert K.; Remington K.A.; Clark A.G.; Waterman M.S.; Eichler E.E.; Adams M.D.; Hunkapiller M.W.; Myers E.W.; Venter J.C.;
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]; VARIANT THR-229; 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)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]; VARIANTS VAL-111 AND THR-229; 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-215; VARIANT [LARGE SCALE ANALYSIS] THR-229; 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-215; SER-227 AND SER-235; VARIANT [LARGE SCALE ANALYSIS] THR-229; 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-215; SER-227 AND SER-235; VARIANT [LARGE SCALE ANALYSIS] THR-229; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS];

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