FEM1C
entrez
56929
canonical
uniprot
Q96JP0
canonical
ensembl
ENSG00000145780
resolver
ensp
ENSP00000274457
resolver
ensp
ENSP00000526030
resolver
ensp
ENSP00000526031
resolver
ensp
ENSP00000526032
resolver
ensp
ENSP00000526033
resolver
enst
ENST00000274457
resolver
enst
ENST00000855971
resolver
enst
ENST00000855972
resolver
enst
ENST00000855973
resolver
enst
ENST00000855974
resolver
genesymbol
FEM1C
resolver
genesymbol_syn
KIAA1785
resolver
hgnc
HGNC:16933
resolver
uniprot
B2RE47
resolver
uniprot
Q8N3V8
resolver
uniprot
Q9H704
resolver
uniprot
Q9NPL6
resolver
uniprot
Q9NPL9
resolver
uniprot_entry
FEM1C_HUMAN
resolver
uniprot_sec
B2RE47
resolver
uniprot_sec
Q8N3V8
resolver
uniprot_sec
Q9H704
resolver
uniprot_sec
Q9NPL6
resolver
uniprot_sec
Q9NPL9
resolver
amino_acid_sequence
MDLKTAVFNAARDGKLRLLTKLLASKSKEEVSSLISEKTNGATPLLMAARYGHLDMVEFLLEQCSASIEVGGSVNFDGETIEGAPPLWAASAAGHLKVVQSLLNHGASVNNTTLTNSTPLRAACFDGHLEIVKYLVEHKADLEVSNRHGHTCLMISCYKGHKEIAQYLLEKGADVNRKSVKGNTALHDCAESGSLDIMKMLLMYCAKMEKDGYGMTPLLSASVTGHTNIVDFLTHHAQTSKTERINALELLGATFVDKKRDLLGALKYWKKAMNMRYSDRTNIISKPVPQTLIMAYDYAKEVNSAEELEGLIADPDEMRMQALLIRERILGPSHPDTSYYIRYRGAVYADSGNFKRCINLWKYALDMQQSNLDPLSPMTASSLLSFAELFSFMLQDRAKGLLGTTVTFDDLMGILCKSVLEIERAIKQTQCPADPLQLNKALSIILHLICLLEKVPCTLEQDHFKKQTIYRFLKLHPRGKNNFSPLHLAVDKNTTCVGRYPVCKFPSLQVTAILIECGADVNVRDSDDNSPLHIAALNNHPDIMNLLIKSGAHFDATNLHKQTASDLLDEKEIAKNLIQPINHTTLQCLAARVIVNHRIYYKGHIPEKLETFVSLHR
uniprot
proteins
disease_involvement
DISEASE: Note=A dominant de novo FEM1C variant was identified in a patient with neurodevelopmental disorder with absent speech, pyramidal signs, and limb ataxia. {ECO:0000269|PubMed:36336956}.
uniprot
proteins
function
FUNCTION: Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (PubMed:29775578, PubMed:29779948, PubMed:33398168, PubMed:33398170, PubMed:38326650). The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms (PubMed:29775578, PubMed:29779948, PubMed:33398168, PubMed:33398170). The CRL2(FEM1C) complex specifically recognizes proteins with an arginine at the C-terminus: recognizes and binds proteins ending with -Lys/Arg-Xaa-Arg and -Lys/Arg-Xaa-Xaa-Arg C-degrons, such as SIL1 or OR51B2, leading to their ubiquitination and degradation (PubMed:33398168, PubMed:33398170, PubMed:38326650). The CRL2(FEM1C) complex mediates ubiquitination and degradation of truncated MSRB1/SEPX1 selenoproteins produced by failed UGA/Sec decoding (PubMed:26138980). Promotes ubiquitination and degradation of SLBP (PubMed:28118078). {ECO:0000269|PubMed:26138980, ECO:0000269|PubMed:28118078, ECO:0000269|PubMed:29775578, ECO:0000269|PubMed:29779948, ECO:0000269|PubMed:33398168, ECO:0000269|PubMed:33398170}.
uniprot
proteins
mass_dalton
68673
uniprot
proteins
mutagenesis
MUTAGEN 76; /note="F->A: Strongly reduced binding to C-degron with an arginine at the C-terminus."; /evidence="ECO:0000269|PubMed:33398170"; MUTAGEN 77; /note="D->A: Reduced binding to C-degron with an arginine at the C-terminus. Abolished binding to C-degron with an arginine at the C-terminus; when associated with A-126."; /evidence="ECO:0000269|PubMed:33398168, ECO:0000269|PubMed:33398170"; MUTAGEN 117; /note="S->A: Abolished binding to C-degron with an arginine at the C-terminus."; /evidence="ECO:0000269|PubMed:33398170"; MUTAGEN 121; /note="R->A: Reduced binding to C-degron with an arginine at the C-terminus."; /evidence="ECO:0000269|PubMed:33398168, ECO:0000269|PubMed:33398170"; MUTAGEN 125; /note="F->A: Strongly reduced binding to C-degron with an arginine at the C-terminus."; /evidence="ECO:0000269|PubMed:33398168, ECO:0000269|PubMed:33398170"; MUTAGEN 126; /note="D->A: Reduced binding to C-degron with an arginine at the C-terminus. Abolished binding to C-degron with an arginine at the C-terminus; when associated with A-77."; /evidence="ECO:0000269|PubMed:33398168, ECO:0000269|PubMed:33398170"; MUTAGEN 148; /note="H->A: Strongly reduced binding to C-degron with an arginine at the C-terminus."; /evidence="ECO:0000269|PubMed:33398168"; MUTAGEN 150; /note="H->N: Modifies specificity for C-degron at the C-terminus and promotes increased affinity for C-degrons usually recognized by FEM1B; when associated with A-183--F-188."; /evidence="ECO:0000269|PubMed:33398168"; MUTAGEN 158; /note="Y->A: Strongly reduced binding to C-degron with an arginine at the C-terminus."; /evidence="ECO:0000269|PubMed:33398168"; MUTAGEN 183..191; /note="NTALHDCAE->ATALHACAA: Abolished binding to C-degron with an arginine at the C-terminus."; /evidence="ECO:0000269|PubMed:33398168"; MUTAGEN 183..188; /note="NTALHD->ATALHF: Modifies specificity for C-degron at the C-terminus and promotes increased affinity for C-degrons usually recognized by FEM1B; when associated with N-150."; /evidence="ECO:0000269|PubMed:33398168"; MUTAGEN 188; /note="D->A: Reduced binding to C-degron with an arginine at the C-terminus."; /evidence="ECO:0000269|PubMed:33398170"; MUTAGEN 188; /note="D->K: Nearly abolished binding to C-degron with an arginine at the C-terminus."; /evidence="ECO:0000269|PubMed:33398170"; MUTAGEN 191; /note="E->A: Reduced binding to C-degron with an arginine at the C-terminus."; /evidence="ECO:0000269|PubMed:33398170"; MUTAGEN 191; /note="E->K: Strongly reduced binding to C-degron with an arginine at the C-terminus."; /evidence="ECO:0000269|PubMed:33398170
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:28118078, ECO:0000269|PubMed:29775578, ECO:0000269|PubMed:29779948, ECO:0000269|PubMed:33398168, ECO:0000269|PubMed:33398170, ECO:0000269|PubMed:38326650}.
uniprot
proteins
protein_family
Fem-1 family
uniprot
proteins
pubmed
11347906
uniprot
proteins
pubmed
11733146
uniprot
proteins
pubmed
14527725
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
26138980
uniprot
proteins
pubmed
28118078
uniprot
proteins
pubmed
29775578
uniprot
proteins
pubmed
29779948
uniprot
proteins
pubmed
33398168
uniprot
proteins
pubmed
33398170
uniprot
proteins
pubmed
36336956
uniprot
proteins
pubmed
38326650
uniprot
proteins
sequence_length
617
uniprot
proteins