UniProtKB/Swiss-Prot Q9NVW2: Variant p.Arg387Cys

E3 ubiquitin-protein ligase RLIM
Gene: RLIM
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Variant information Variant position:

387 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 Arginine (R) to Cysteine (C) at position 387 (R387C, p.Arg387Cys). 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 (R) to medium size and polar (C) 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 TOKAS; likely pathogenic; does not rescue microcephaly in zebrafish morphants suggesting impaired function; no effect on RLIM proteasomal degradation; no effect on nuclear localization; no effect on dimerization; no effect on ZFP42/REX1 protein ubiquitination in transfected cells; decreased ubiquitin-protein transferase activity in vitro and decreased ability to promote E2 ubiquitin discharge. Any additional useful information about the variant.

Sequence information Variant position:

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

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

FSRSERAGVRTYVSTIRIPI R RILNTGLSETTSVAIQTMLR 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                         FSRSERAGVRTYVSTIRIPIRRILNTGLSETTSVAIQTMLR

Mouse                         FSRSERAGVRTYVSTIRIPIRRILNTGLSETTSVAIQTMLR

Xenopus tropicalis            FSRSERAGVRTYVSTIRIPIRRILNTGLSETTSVAIQTMLR

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 – 624	E3 ubiquitin-protein ligase RLIM

Literature citations
RNF12 X-Linked Intellectual Disability Mutations Disrupt E3 Ligase Activity and Neural Differentiation.
Bustos F.; Segarra-Fas A.; Chaugule V.K.; Brandenburg L.; Branigan E.; Toth R.; Macartney T.; Knebel A.; Hay R.T.; Walden H.; Findlay G.M.;
Cell Rep. 23:1599-1611(2018)
Cited for: FUNCTION; CATALYTIC ACTIVITY; SUBCELLULAR LOCATION; SUBUNIT; CHARACTERIZATION OF VARIANTS CYS-356; CYS-387; ARG-587 AND CYS-599;
X-exome sequencing of 405 unresolved families identifies seven novel intellectual disability genes.
Hu H.; Haas S.A.; Chelly J.; Van Esch H.; Raynaud M.; de Brouwer A.P.; Weinert S.; Froyen G.; Frints S.G.; Laumonnier F.; Zemojtel T.; Love M.I.; Richard H.; Emde A.K.; Bienek M.; Jensen C.; Hambrock M.; Fischer U.; Langnick C.; Feldkamp M.; Wissink-Lindhout W.; Lebrun N.; Castelnau L.; Rucci J.; Montjean R.; Dorseuil O.; Billuart P.; Stuhlmann T.; Shaw M.; Corbett M.A.; Gardner A.; Willis-Owen S.; Tan C.; Friend K.L.; Belet S.; van Roozendaal K.E.; Jimenez-Pocquet M.; Moizard M.P.; Ronce N.; Sun R.; O'Keeffe S.; Chenna R.; van Boemmel A.; Goeke J.; Hackett A.; Field M.; Christie L.; Boyle J.; Haan E.; Nelson J.; Turner G.; Baynam G.; Gillessen-Kaesbach G.; Mueller U.; Steinberger D.; Budny B.; Badura-Stronka M.; Latos-Bielenska A.; Ousager L.B.; Wieacker P.; Rodriguez Criado G.; Bondeson M.L.; Anneren G.; Dufke A.; Cohen M.; Van Maldergem L.; Vincent-Delorme C.; Echenne B.; Simon-Bouy B.; Kleefstra T.; Willemsen M.; Fryns J.P.; Devriendt K.; Ullmann R.; Vingron M.; Wrogemann K.; Wienker T.F.; Tzschach A.; van Bokhoven H.; Gecz J.; Jentsch T.J.; Chen W.; Ropers H.H.; Kalscheuer V.M.;
Mol. Psychiatry 21:133-148(2016)
Cited for: VARIANTS TOKAS CYS-387; ARG-587 AND CYS-599; INVOLVEMENT IN TOKAS;
Pathogenic variants in E3 ubiquitin ligase RLIM/RNF12 lead to a syndromic X-linked intellectual disability and behavior disorder.
Frints S.G.M.; Ozanturk A.; Rodriguez Criado G.; Grasshoff U.; de Hoon B.; Field M.; Manouvrier-Hanu S.; E Hickey S.; Kammoun M.; Gripp K.W.; Bauer C.; Schroeder C.; Toutain A.; Mihalic Mosher T.; Kelly B.J.; White P.; Dufke A.; Rentmeester E.; Moon S.; Koboldt D.C.; van Roozendaal K.E.P.; Hu H.; Haas S.A.; Ropers H.H.; Murray L.; Haan E.; Shaw M.; Carroll R.; Friend K.; Liebelt J.; Hobson L.; De Rademaeker M.; Geraedts J.; Fryns J.P.; Vermeesch J.; Raynaud M.; Riess O.; Gribnau J.; Katsanis N.; Devriendt K.; Bauer P.; Gecz J.; Golzio C.; Gontan C.; Kalscheuer V.M.;
Mol. Psychiatry 24:1748-1768(2019)
Cited for: VARIANTS TOKAS LEU-77; CYS-356; CYS-365; CYS-387; HIS-577; ARG-587; ASN-598; CYS-599 AND CYS-611; CHARACTERIZATION OF VARIANTS TOKAS LEU-77; CYS-356; CYS-365; CYS-387; HIS-577; ARG-587; ASN-598; CYS-599 AND CYS-611; INVOLVEMENT IN TOKAS; FUNCTION;

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.