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UniProtKB/Swiss-Prot P28069: Variant p.Pro76Leu

Pituitary-specific positive transcription factor 1
Gene: POU1F1
Variant information

Variant position:  76
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  LP/P [Disclaimer]
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 Leucine (L) at position 76 (P76L, p.Pro76Leu).
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:  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:  -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

Variant description:  In CPHD1; reduces transactivation capacity on the GH1 gene; increases the functional binding on the GH1 promoter; increases the interaction with ELK1, LHX3 and PITX1.
Any additional useful information about the variant.



Sequence information

Variant position:  76
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  291
The length of the canonical sequence.

Location on the sequence:   PSCHYGNQPSTYGVMAGSLT  P CLYKFPDHTLSHGFPPIHQP
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                         PSCHYGNQPSTYGVMAG--------------------------------------SLTPCLYKFPDHTLS-------HGFP-------------PIHQP

                              PSCHYGNQPSTYGVMAG------------------------

Rhesus macaque                PSCHYGNQPSTYGVMAG------------------------

Mouse                         PSCHYGNQPSTYGVMAG------------------------

Rat                           PSCHYGNQPSTYGVMAG------------------------

Pig                           PSCHYGNQPSTYGVMAG------------------------

Bovine                        PFCHYGNQSSTYGVMAG------------------------

Sheep                         PSCHYGNQSSTYGVMAG------------------------

Chicken                       PSCHYGNQASTYGVMAGIKPATPEMLSASLSQSRILQTCSM

Fission yeast                 TNGFFHRDMKPENILIS---------SNSDSSSFNVKIADF

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.

TypePositionsDescription
Chain 1 – 291 Pituitary-specific positive transcription factor 1
Mutagenesis 74 – 74 L -> A. No effect on the interaction with ELK1, LHX3 and PITX1.
Mutagenesis 75 – 75 T -> A. Increases the interaction with LHX3. No effect on the interaction with ELK1.
Mutagenesis 76 – 76 P -> A. Increases the interaction with LHX3 and PITX1. No effect on the interaction with ELK1.
Mutagenesis 77 – 77 C -> A. Increases the interaction with LHX3 and PITX1. No effect on the interaction with ELK1.
Mutagenesis 78 – 78 L -> A. Increases the interaction with LHX3 and PITX1. No effect on the interaction with ELK1.


Literature citations

Functional characterization of a human POU1F1 mutation associated with isolated growth hormone deficiency: a novel etiology for IGHD.
Sobrier M.L.; Tsai Y.C.; Perez C.; Leheup B.; Bouceba T.; Duquesnoy P.; Copin B.; Sizova D.; Penzo A.; Stanger B.Z.; Cooke N.E.; Liebhaber S.A.; Amselem S.;
Hum. Mol. Genet. 25:472-483(2016)
Cited for: VARIANT CPHD1 LEU-76; CHARACTERIZATION OF VARIANT CPHD1 LEU-76; FUNCTION; INTERACTION WITH ELK1; LHX3 AND PITX1; DNA-BINDING; SUBCELLULAR LOCATION; MUTAGENESIS OF LEU-74; THR-75; PRO-76; CYS-77 AND LEU-78;

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.