UniProtKB/Swiss-Prot O15392: Variant p.Lys129Glu

Baculoviral IAP repeat-containing protein 5
Gene: BIRC5
Feedback?

Variant information Variant position:

129 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 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:

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:

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:

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:

Links to websites of interest for the variant.

Variant rs2071214 [ dbSNP | Ensembl ]

Sequence information Variant position:

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

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

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:

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:

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	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.