UniProtKB/Swiss-Prot Q9NVX2: Variant p.Pro6Ala

Notchless protein homolog 1
Gene: NLE1
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Variant information Variant position:

6 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 Proline (P) to Alanine (A) at position 6 (P6A, p.Pro6Ala). 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 (P) to small size and hydrophobic (A) 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 rs1471615 [ dbSNP | Ensembl ]

Sequence information Variant position:

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

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

MAAAV P DEAVARDVQRLLVQFQDEGG 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                         MAAAVPDEA---------------VARDVQRLLVQFQD-EGG

Mouse                         MAAAVVEEA---------------AA

Bovine                        AAAAAADEA---------------AT

Xenopus laevis                ------------------------MK

Baker's yeast                 MSTLIPPPSKKQKKEAQLPREVAIIP

Fission yeast                 MATLLPPKSKRQKKESLNPTTIE-IP

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
Initiator methionine	1 – 1	Removed
Chain	2 – 485	Notchless protein homolog 1
Modified residue	2 – 2	N-acetylalanine
Alternative sequence	1 – 292	Missing. In isoform 2.

Literature citations
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] (ISOFORM 1); VARIANTS ALA-6 AND LYS-169; 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] (ISOFORM 1); VARIANTS ALA-6 AND LYS-169; Submission
Bienvenut W.V.;
Cited for: PROTEIN SEQUENCE OF 2-12 AND 87-99; CLEAVAGE OF INITIATOR METHIONINE; ACETYLATION AT ALA-2; SUBCELLULAR LOCATION; IDENTIFICATION BY MASS SPECTROMETRY; VARIANT ALA-6; 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] ALA-6; CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]; 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)
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; VARIANT [LARGE SCALE ANALYSIS] ALA-6; CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]; N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
Van Damme P.; Lasa M.; Polevoda B.; Gazquez C.; Elosegui-Artola A.; Kim D.S.; De Juan-Pardo E.; Demeyer K.; Hole K.; Larrea E.; Timmerman E.; Prieto J.; Arnesen T.; Sherman F.; Gevaert K.; Aldabe R.;
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012)
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; VARIANT [LARGE SCALE ANALYSIS] ALA-6; CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS];

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