Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q8IWV7: Variant p.His136Arg

E3 ubiquitin-protein ligase UBR1
Gene: UBR1
Feedback?
Variant information Variant position: help 136 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Histidine (H) to Arginine (R) at position 136 (H136R, p.His136Arg). 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 medium size and polar (H) to large size and basic (R) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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 In JBS; prevents proper folding of the UBR-type zinc finger; may decrease protein stability; loss of activity in a yeast-based assay. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 136 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1749 The length of the canonical sequence.
Location on the sequence: help AIDPTCVLCMDCFQDSVHKN H RYKMHTSTGGGFCDCGDTEA 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                         AIDPTCVLCMDCFQDSVHKNHRYKMHTSTG--GGFCDCGDTEA

Mouse                         AIDPTCVLCMDCFQSSVHKNHRYKMHTSTG--GGFCDCGDT

Caenorhabditis elegans        ATDGTCVMCLQCFEVSIHKSHKYKMHSSSG--SGYCDCGDA

Drosophila                    GVDPTCVLCVNCFKRSAHRFHKYKMSTSGG--GGCCDCGDD

Baker's yeast                 GCDDTCVLCIHCFNPKDHVNHHVCTDICTEFTSGICDCGDE

Fission yeast                 SVDSNSALCVKCFRATSHKDHETSFTVSAG-SGGCCDCGNA
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 2 – 1749 E3 ubiquitin-protein ligase UBR1
Zinc finger 97 – 168 UBR-type
Binding site 124 – 124
Binding site 124 – 124
Binding site 127 – 127
Binding site 127 – 127
Binding site 127 – 127
Binding site 133 – 133
Binding site 133 – 133
Binding site 136 – 136
Binding site 136 – 136
Binding site 148 – 148
Binding site 149 – 149
Binding site 149 – 149
Binding site 150 – 150
Binding site 151 – 151
Binding site 151 – 151
Binding site 153 – 153



Literature citations
Structural basis of substrate recognition and specificity in the N-end rule pathway.
Matta-Camacho E.; Kozlov G.; Li F.F.; Gehring K.;
Nat. Struct. Mol. Biol. 17:1182-1187(2010)
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 98-167 IN COMPLEX WITH ZINC; UBR-TYPE ZINC-FINGER; FUNCTION; VARIANT JB5 ARG-136; Deficiency of UBR1, a ubiquitin ligase of the N-end rule pathway, causes pancreatic dysfunction, malformations and mental retardation (Johanson-Blizzard syndrome).
Zenker M.; Mayerle J.; Lerch M.M.; Tagariello A.; Zerres K.; Durie P.R.; Beier M.; Hulskamp G.; Guzman C.; Rehder H.; Beemer F.A.; Hamel B.C.J.; Vanlieferinghen P.; Gershoni-Baruch R.; Vieira M.W.; Dumic M.; Auslender R.; Gil-da-Silva-Lopes V.L.; Steinlicht S.; Rauh M.; Shalev S.A.; Thiel C.; Winterpacht A.; Kwon Y.T.; Varshavsky A.; Reis A.;
Nat. Genet. 37:1345-1350(2005)
Cited for: VARIANTS JBS ARG-136 AND SER-1279; FUNCTION; DISEASE; TISSUE SPECIFICITY; SUBCELLULAR LOCATION; DEVELOPMENTAL STAGE; Ubiquitin ligases of the N-end rule pathway: assessment of mutations in UBR1 that cause the Johanson-Blizzard syndrome.
Hwang C.S.; Sukalo M.; Batygin O.; Addor M.C.; Brunner H.; Aytes A.P.; Mayerle J.; Song H.K.; Varshavsky A.; Zenker M.;
PLoS ONE 6:E24925-E24925(2011)
Cited for: VARIANTS JBS LEU-122; ARG-136 AND GLU-1102; CHARACTERIZATION OF VARIANTS JBS LEU-122; ARG-136 AND GLU-1102; Mutations in the human UBR1 gene and the associated phenotypic spectrum.
Sukalo M.; Fiedler A.; Guzman C.; Spranger S.; Addor M.C.; McHeik J.N.; Oltra Benavent M.; Cobben J.M.; Gillis L.A.; Shealy A.G.; Deshpande C.; Bozorgmehr B.; Everman D.B.; Stattin E.L.; Liebelt J.; Keller K.M.; Bertola D.R.; van Karnebeek C.D.; Bergmann C.; Liu Z.; Dueker G.; Rezaei N.; Alkuraya F.S.; Ogur G.; Alrajoudi A.; Venegas-Vega C.A.; Verbeek N.E.; Richmond E.J.; Kirbiyik O.; Ranganath P.; Singh A.; Godbole K.; Ali F.A.; Alves C.; Mayerle J.; Lerch M.M.; Witt H.; Zenker M.;
Hum. Mutat. 35:521-531(2014)
Cited for: VARIANTS JBS LEU-122; PHE-127; ARG-136; ARG-166; ARG-217; ARG-286; PRO-317; 389-ALA--PHE-392 DEL; ASP-563; VAL-660 DEL; PRO-700; CYS-754; HIS-754; GLU-1102; GLY-1242; SER-1279; LEU-1426; PHE-1427; PRO-1431 AND ARG-1661;
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.