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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O15392: Variant p.Lys129Glu

Baculoviral IAP repeat-containing protein 5
Gene: BIRC5
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Variant information Variant position: help 129 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 Lysine (K) to Glutamate (E) at position 129 (K129E, p.Lys129Glu). 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 Change from large size and basic (K) to medium size and acidic (E) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 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

Variant description: help Loss of acetylation; localization primarily within the cytoplasm; increased likelihood of existing as monomer; stronger binding to XPO1/CRM1. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 129 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 142 The length of the canonical sequence.
Location on the sequence: help AKNKIAKETNNKKKEFEETA K KVRRAIEQLAAMD 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                         AKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD

                              AKNKIAKETNNKQKEFEETAKKVRCAIEQLAAAE

Mouse                         AKNKIAKETNNKQKEFEETAKTTRQSIEQLAA--

Rat                           AKNKIAKETNNKQKEFEETRRTVRQSIEQLAALR

Pig                           AKNKIAKETNNKQKEFEETAKKVRCAIEQLAASE

Bovine                        TKNKIAKETNNKQKEFEETAKKVRCAIEQLAALE

Cat                           AKNKIAKETNHKQKEFEETAKRVRCAIEQLAALE

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 1 – 142 Baculoviral IAP repeat-containing protein 5
Site 126 – 126 Interaction with FBXL7
Modified residue 110 – 110 N6-acetyllysine
Modified residue 112 – 112 N6-acetyllysine
Modified residue 115 – 115 N6-acetyllysine
Modified residue 117 – 117 Phosphothreonine; by AURKB
Modified residue 121 – 121 N6-acetyllysine
Modified residue 129 – 129 N6-acetyllysine
Alternative sequence 74 – 142 IEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD -> MQRKPTIRRKNLRKLRRKCAVPSSSWLPWIEASGRSCLVPEWLHHFQGLFPGATSLPVGPLAMS. In isoform 3.
Alternative sequence 74 – 142 IEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD -> MRELC. In isoform 6.
Alternative sequence 74 – 142 IEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD -> M. In isoform 7.
Alternative sequence 105 – 142 DRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD -> VRETLPPPRSFIR. In isoform 5.
Alternative sequence 114 – 142 AKETNNKKKEFEETAKKVRRAIEQLAAMD -> ERALLAE. In isoform 4.
Mutagenesis 117 – 117 T -> A. Prevents phosphorylation by AURKB. Still able to localize correctly but prevents interaction with INCENP.
Mutagenesis 117 – 117 T -> E. Mimics phosphorylation. Disrupts subcellular localization during mitosis and prevents interaction with INCENP.
Mutagenesis 126 – 126 E -> A. Loss of FBXL7 binding.
Mutagenesis 129 – 129 K -> AQ. Mimics acetylation. Localization primarily within the nucleus.
Mutagenesis 129 – 129 K -> R. Loss of acetylation. Localization primarily within the cytoplasm.
Helix 98 – 139



Literature citations
DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage.
Zody M.C.; Garber M.; Adams D.J.; Sharpe T.; Harrow J.; Lupski J.R.; Nicholson C.; Searle S.M.; Wilming L.; Young S.K.; Abouelleil A.; Allen N.R.; Bi W.; Bloom T.; Borowsky M.L.; Bugalter B.E.; Butler J.; Chang J.L.; Chen C.-K.; Cook A.; Corum B.; Cuomo C.A.; de Jong P.J.; DeCaprio D.; Dewar K.; FitzGerald M.; Gilbert J.; Gibson R.; Gnerre S.; Goldstein S.; Grafham D.V.; Grocock R.; Hafez N.; Hagopian D.S.; Hart E.; Norman C.H.; Humphray S.; Jaffe D.B.; Jones M.; Kamal M.; Khodiyar V.K.; LaButti K.; Laird G.; Lehoczky J.; Liu X.; Lokyitsang T.; Loveland J.; Lui A.; Macdonald P.; Major J.E.; Matthews L.; Mauceli E.; McCarroll S.A.; Mihalev A.H.; Mudge J.; Nguyen C.; Nicol R.; O'Leary S.B.; Osoegawa K.; Schwartz D.C.; Shaw-Smith C.; Stankiewicz P.; Steward C.; Swarbreck D.; Venkataraman V.; Whittaker C.A.; Yang X.; Zimmer A.R.; Bradley A.; Hubbard T.; Birren B.W.; Rogers J.; Lander E.S.; Nusbaum C.;
Nature 440:1045-1049(2006)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]; VARIANT GLU-129; Acetylation directs survivin nuclear localization to repress STAT3 oncogenic activity.
Wang H.; Holloway M.P.; Ma L.; Cooper Z.A.; Riolo M.; Samkari A.; Elenitoba-Johnson K.S.; Chin Y.E.; Altura R.A.;
J. Biol. Chem. 285:36129-36137(2010)
Cited for: FUNCTION; SUBCELLULAR LOCATION; INTERACTION WITH STAT3 AND XPO1/CRM1; ACETYLATION AT LYS-23; LYS-90; LYS-110; LYS-112; LYS-115; LYS-121 AND LYS-129; MUTAGENESIS OF LYS-129; CHARACTERIZATION OF VARIANT GLU-129;
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.