FEM1C_HUMAN
ID FEM1C_HUMAN Reviewed; 617 AA.
AC Q96JP0; B2RE47; Q8N3V8; Q9H704; Q9NPL6; Q9NPL9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Protein fem-1 homolog C {ECO:0000305};
DE Short=FEM1c {ECO:0000303|PubMed:14527725};
DE AltName: Full=FEM1-gamma;
GN Name=FEM1C {ECO:0000303|PubMed:14527725, ECO:0000312|HGNC:HGNC:16933};
GN Synonyms=KIAA1785 {ECO:0000303|PubMed:11347906};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Cartilage;
RX PubMed=11733146; DOI=10.1016/s0378-1119(01)00756-9;
RA Krakow D., Sebald E., King L.M., Cohn D.H.;
RT "Identification of human FEM1A, the ortholog of a C. elegans sex-
RT differentiation gene.";
RL Gene 279:213-219(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=14527725; DOI=10.1016/s0378-1119(03)00712-1;
RA Ventura-Holman T., Lu D., Si X., Izevbigie E.B., Maher J.F.;
RT "The Fem1c genes: conserved members of the Fem1 gene family in
RT vertebrates.";
RL Gene 314:133-139(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-271 AND 301-617.
RG The European IMAGE consortium;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 279-617.
RC TISSUE=Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP VARIANTS [LARGE SCALE ANALYSIS] ASN-434 AND ASN-462.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [11]
RP FUNCTION.
RX PubMed=26138980; DOI=10.1126/science.aab0515;
RA Lin H.C., Ho S.C., Chen Y.Y., Khoo K.H., Hsu P.H., Yen H.C.;
RT "SELENOPROTEINS. CRL2 aids elimination of truncated selenoproteins produced
RT by failed UGA/Sec decoding.";
RL Science 349:91-95(2015).
RN [12]
RP FUNCTION, AND PATHWAY.
RX PubMed=28118078; DOI=10.1080/15384101.2017.1284715;
RA Dankert J.F., Pagan J.K., Starostina N.G., Kipreos E.T., Pagano M.;
RT "FEM1 proteins are ancient regulators of SLBP degradation.";
RL Cell Cycle 16:556-564(2017).
RN [13]
RP FUNCTION, PATHWAY, AND IDENTIFICATION IN A CRL2 E3 UBIQUITIN-PROTEIN LIGASE
RP COMPLEX.
RX PubMed=29779948; DOI=10.1016/j.cell.2018.04.028;
RA Koren I., Timms R.T., Kula T., Xu Q., Li M.Z., Elledge S.J.;
RT "The eukaryotic proteome is shaped by E3 ubiquitin ligases targeting C-
RT terminal degrons.";
RL Cell 173:1622-1635(2018).
RN [14]
RP FUNCTION, PATHWAY, AND IDENTIFICATION IN A CRL2 E3 UBIQUITIN-PROTEIN LIGASE
RP COMPLEX.
RX PubMed=29775578; DOI=10.1016/j.molcel.2018.04.006;
RA Lin H.C., Yeh C.W., Chen Y.F., Lee T.T., Hsieh P.Y., Rusnac D.V., Lin S.Y.,
RA Elledge S.J., Zheng N., Yen H.S.;
RT "C-terminal end-directed protein elimination by CRL2 ubiquitin ligases.";
RL Mol. Cell 70:602-613(2018).
RN [15] {ECO:0007744|PDB:6LBG, ECO:0007744|PDB:6LBN, ECO:0007744|PDB:6LDP, ECO:0007744|PDB:6LE6, ECO:0007744|PDB:6LEN, ECO:0007744|PDB:6LEY, ECO:0007744|PDB:6LF0}
RP X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 1-403 IN COMPLEX WITH C-DEGRONS,
RP FUNCTION, PATHWAY, AND MUTAGENESIS OF ASP-77; ARG-121; PHE-125; ASP-126;
RP HIS-148; HIS-150; TYR-158; 183-ASN--ASP-188 AND 183-ASN--GLU-191.
RX PubMed=33398168; DOI=10.1038/s41589-020-00704-3;
RA Chen X., Liao S., Makaros Y., Guo Q., Zhu Z., Krizelman R., Dahan K.,
RA Tu X., Yao X., Koren I., Xu C.;
RT "Molecular basis for arginine C-terminal degron recognition by Cul2FEM1 E3
RT ligase.";
RL Nat. Chem. Biol. 17:254-262(2021).
RN [16] {ECO:0007744|PDB:6XKC, ECO:0007744|PDB:7JYA}
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 1-244 IN COMPLEX WITH C-DEGRON,
RP FUNCTION, PATHWAY, DOMAIN, AND MUTAGENESIS OF PHE-76; ASP-77; SER-117;
RP ARG-121; PHE-125; ASP-126; ASP-188 AND GLU-191.
RX PubMed=33398170; DOI=10.1038/s41589-020-00703-4;
RA Yan X., Wang X., Li Y., Zhou M., Li Y., Song L., Mi W., Min J., Dong C.;
RT "Molecular basis for ubiquitin ligase CRL2FEM1C-mediated recognition of C-
RT degron.";
RL Nat. Chem. Biol. 17:263-271(2021).
CC -!- FUNCTION: Substrate-recognition component of a Cul2-RING (CRL2) E3
CC ubiquitin-protein ligase complex of the DesCEND (destruction via C-end
CC degrons) pathway, which recognizes a C-degron located at the extreme C
CC terminus of target proteins, leading to their ubiquitination and
CC degradation (PubMed:29779948, PubMed:29775578, PubMed:33398170,
CC PubMed:33398168). The C-degron recognized by the DesCEND pathway is
CC usually a motif of less than ten residues and can be present in full-
CC length proteins, truncated proteins or proteolytically cleaved forms
CC (PubMed:29779948, PubMed:29775578, PubMed:33398170, PubMed:33398168).
CC The CRL2(FEM1C) complex specifically recognizes proteins with an
CC arginine at the C-terminus: recognizes and binds proteins ending with
CC -Lys/Arg-Xaa-Arg and -Lys/Arg-Xaa-Xaa-Arg C-degrons, such as SIL1 or
CC OR51B2, leading to their ubiquitination and degradation
CC (PubMed:33398170, PubMed:33398168). The CRL2(FEM1C) complex mediates
CC ubiquitination and degradation of truncated MSRB1/SEPX1 selenoproteins
CC produced by failed UGA/Sec decoding (PubMed:26138980). Promotes
CC ubiquitination and degradation of SLBP (PubMed:28118078).
CC {ECO:0000269|PubMed:26138980, ECO:0000269|PubMed:28118078,
CC ECO:0000269|PubMed:29775578, ECO:0000269|PubMed:29779948,
CC ECO:0000269|PubMed:33398168, ECO:0000269|PubMed:33398170}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:28118078, ECO:0000269|PubMed:29775578,
CC ECO:0000269|PubMed:29779948, ECO:0000269|PubMed:33398168,
CC ECO:0000269|PubMed:33398170}.
CC -!- SUBUNIT: Component of a CRL2 E3 ubiquitin-protein ligase complex, also
CC named ECS (Elongin BC-CUL2/5-SOCS-box protein) complex, composed of
CC CUL2, Elongin BC (ELOB and ELOC), RBX1 and substrate-specific adapter
CC FEM1C. {ECO:0000269|PubMed:29775578, ECO:0000269|PubMed:29779948}.
CC -!- INTERACTION:
CC Q96JP0; Q96MT8-3: CEP63; NbExp=3; IntAct=EBI-2515330, EBI-11522539;
CC Q96JP0; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-2515330, EBI-741037;
CC Q96JP0; Q9UDY8-2: MALT1; NbExp=3; IntAct=EBI-2515330, EBI-12056869;
CC Q96JP0; Q9UJA3-4: MCM8; NbExp=3; IntAct=EBI-2515330, EBI-13052514;
CC Q96JP0; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-2515330, EBI-302345;
CC Q96JP0; Q96KN7: RPGRIP1; NbExp=3; IntAct=EBI-2515330, EBI-1050213;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in kidney,
CC cardiac tissue, skeletal muscle and testis. Expressed at lower levels
CC in other tissues, including cartilage. {ECO:0000269|PubMed:11733146,
CC ECO:0000269|PubMed:14527725}.
CC -!- DOMAIN: The first seven ANK repeats at the N-terminus (1-242) are
CC essnetial for recognition of Lys/Arg-Xaa-Arg and -Lys/Arg-Xaa-Xaa-Arg
CC C-degrons. {ECO:0000269|PubMed:33398170}.
CC -!- SIMILARITY: Belongs to the fem-1 family. {ECO:0000305}.
CC -!- CAUTION: Was initially thought to be the ortholog of mouse FEM1A.
CC {ECO:0000305|PubMed:11733146}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15096.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF391093; AAL37627.1; -; mRNA.
DR EMBL; AY249188; AAO64429.1; -; mRNA.
DR EMBL; AB058688; BAB47414.1; -; mRNA.
DR EMBL; AK025265; BAB15096.1; ALT_INIT; mRNA.
DR EMBL; AK315803; BAG38144.1; -; mRNA.
DR EMBL; CH471086; EAW48963.1; -; Genomic_DNA.
DR EMBL; BC028369; AAH28369.1; -; mRNA.
DR EMBL; AL365409; CAB96953.1; -; mRNA.
DR EMBL; AL365415; CAB96957.1; -; mRNA.
DR EMBL; AL831817; CAD38531.1; -; mRNA.
DR CCDS; CCDS4118.1; -.
DR RefSeq; NP_064562.1; NM_020177.2.
DR RefSeq; XP_005272092.1; XM_005272035.4.
DR PDB; 6LBG; X-ray; 2.51 A; A/B=1-390.
DR PDB; 6LBN; X-ray; 2.90 A; A/B=1-390.
DR PDB; 6LDP; X-ray; 2.35 A; A/B=1-390.
DR PDB; 6LE6; X-ray; 2.33 A; A/B=1-390.
DR PDB; 6LEN; X-ray; 2.38 A; A/B=1-390.
DR PDB; 6LEY; X-ray; 2.39 A; A/B=1-390.
DR PDB; 6LF0; X-ray; 2.11 A; A/B=1-403.
DR PDB; 6XKC; X-ray; 2.03 A; A/B/C/D/E/F=1-244.
DR PDB; 7JYA; X-ray; 2.46 A; A/B/C=2-371.
DR PDBsum; 6LBG; -.
DR PDBsum; 6LBN; -.
DR PDBsum; 6LDP; -.
DR PDBsum; 6LE6; -.
DR PDBsum; 6LEN; -.
DR PDBsum; 6LEY; -.
DR PDBsum; 6LF0; -.
DR PDBsum; 6XKC; -.
DR PDBsum; 7JYA; -.
DR AlphaFoldDB; Q96JP0; -.
DR SMR; Q96JP0; -.
DR BioGRID; 121256; 25.
DR IntAct; Q96JP0; 14.
DR STRING; 9606.ENSP00000274457; -.
DR GlyGen; Q96JP0; 1 site.
DR iPTMnet; Q96JP0; -.
DR PhosphoSitePlus; Q96JP0; -.
DR BioMuta; FEM1C; -.
DR DMDM; 74751963; -.
DR EPD; Q96JP0; -.
DR jPOST; Q96JP0; -.
DR MassIVE; Q96JP0; -.
DR MaxQB; Q96JP0; -.
DR PaxDb; Q96JP0; -.
DR PeptideAtlas; Q96JP0; -.
DR PRIDE; Q96JP0; -.
DR ProteomicsDB; 76997; -.
DR Antibodypedia; 25422; 126 antibodies from 26 providers.
DR DNASU; 56929; -.
DR Ensembl; ENST00000274457.5; ENSP00000274457.3; ENSG00000145780.8.
DR GeneID; 56929; -.
DR KEGG; hsa:56929; -.
DR MANE-Select; ENST00000274457.5; ENSP00000274457.3; NM_020177.3; NP_064562.1.
DR UCSC; uc003krb.2; human.
DR CTD; 56929; -.
DR DisGeNET; 56929; -.
DR GeneCards; FEM1C; -.
DR HGNC; HGNC:16933; FEM1C.
DR HPA; ENSG00000145780; Tissue enhanced (bone).
DR MIM; 608767; gene.
DR neXtProt; NX_Q96JP0; -.
DR OpenTargets; ENSG00000145780; -.
DR PharmGKB; PA134891999; -.
DR VEuPathDB; HostDB:ENSG00000145780; -.
DR eggNOG; KOG0508; Eukaryota.
DR GeneTree; ENSGT00940000158626; -.
DR HOGENOM; CLU_020042_2_0_1; -.
DR InParanoid; Q96JP0; -.
DR OMA; KQTQCPP; -.
DR OrthoDB; 252380at2759; -.
DR PhylomeDB; Q96JP0; -.
DR TreeFam; TF351376; -.
DR PathwayCommons; Q96JP0; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR SignaLink; Q96JP0; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 56929; 13 hits in 1114 CRISPR screens.
DR ChiTaRS; FEM1C; human.
DR GenomeRNAi; 56929; -.
DR Pharos; Q96JP0; Tbio.
DR PRO; PR:Q96JP0; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q96JP0; protein.
DR Bgee; ENSG00000145780; Expressed in sperm and 177 other tissues.
DR Genevisible; Q96JP0; HS.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IDA:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0140627; P:ubiquitin-dependent protein catabolic process via the C-end degron rule pathway; IDA:UniProtKB.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 1.25.40.20; -; 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13606; Ank_3; 1.
DR Pfam; PF13857; Ank_5; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 9.
DR SUPFAM; SSF48403; SSF48403; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 7.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ANK repeat; Reference proteome; Repeat;
KW TPR repeat; Ubl conjugation pathway.
FT CHAIN 1..617
FT /note="Protein fem-1 homolog C"
FT /id="PRO_0000324536"
FT REPEAT 2..31
FT /note="ANK 1"
FT REPEAT 40..70
FT /note="ANK 2"
FT REPEAT 82..111
FT /note="ANK 3"
FT REPEAT 115..144
FT /note="ANK 4"
FT REPEAT 148..177
FT /note="ANK 5"
FT REPEAT 181..210
FT /note="ANK 6"
FT REPEAT 213..242
FT /note="ANK 7"
FT REPEAT 245..279
FT /note="TPR 1"
FT REPEAT 338..371
FT /note="TPR 2"
FT REPEAT 481..523
FT /note="ANK 8"
FT REPEAT 527..556
FT /note="ANK 9"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VARIANT 434
FT /note="D -> N (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_039810"
FT VARIANT 462
FT /note="D -> N (in a breast cancer sample; somatic mutation;
FT dbSNP:rs753336652)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_039811"
FT MUTAGEN 76
FT /note="F->A: Strongly reduced binding to C-degron with an
FT arginine at the C-terminus."
FT /evidence="ECO:0000269|PubMed:33398170"
FT MUTAGEN 77
FT /note="D->A: Reduced binding to C-degron with an arginine
FT at the C-terminus. Abolished binding to C-degron with an
FT arginine at the C-terminus; when associated with A-126."
FT /evidence="ECO:0000269|PubMed:33398168,
FT ECO:0000269|PubMed:33398170"
FT MUTAGEN 117
FT /note="S->A: Abolished binding to C-degron with an arginine
FT at the C-terminus."
FT /evidence="ECO:0000269|PubMed:33398170"
FT MUTAGEN 121
FT /note="R->A: Reduced binding to C-degron with an arginine
FT at the C-terminus."
FT /evidence="ECO:0000269|PubMed:33398168,
FT ECO:0000269|PubMed:33398170"
FT MUTAGEN 125
FT /note="F->A: Strongly reduced binding to C-degron with an
FT arginine at the C-terminus."
FT /evidence="ECO:0000269|PubMed:33398168,
FT ECO:0000269|PubMed:33398170"
FT MUTAGEN 126
FT /note="D->A: Reduced binding to C-degron with an arginine
FT at the C-terminus. Abolished binding to C-degron with an
FT arginine at the C-terminus; when associated with A-77."
FT /evidence="ECO:0000269|PubMed:33398168,
FT ECO:0000269|PubMed:33398170"
FT MUTAGEN 148
FT /note="H->A: Strongly reduced binding to C-degron with an
FT arginine at the C-terminus."
FT /evidence="ECO:0000269|PubMed:33398168"
FT MUTAGEN 150
FT /note="H->N: Modifies specificity for C-degron at the C-
FT terminus and promotes increased affinity for C-degrons
FT usually recognized by FEM1B; when associated with A-183--F-
FT 188."
FT /evidence="ECO:0000269|PubMed:33398168"
FT MUTAGEN 158
FT /note="Y->A: Strongly reduced binding to C-degron with an
FT arginine at the C-terminus."
FT /evidence="ECO:0000269|PubMed:33398168"
FT MUTAGEN 183..191
FT /note="NTALHDCAE->ATALHACAA: Abolished binding to C-degron
FT with an arginine at the C-terminus."
FT /evidence="ECO:0000269|PubMed:33398168"
FT MUTAGEN 183..188
FT /note="NTALHD->ATALHF: Modifies specificity for C-degron at
FT the C-terminus and promotes increased affinity for C-
FT degrons usually recognized by FEM1B; when associated with
FT N-150."
FT /evidence="ECO:0000269|PubMed:33398168"
FT MUTAGEN 188
FT /note="D->A: Reduced binding to C-degron with an arginine
FT at the C-terminus."
FT /evidence="ECO:0000269|PubMed:33398170"
FT MUTAGEN 188
FT /note="D->K: Nearly abolished binding to C-degron with an
FT arginine at the C-terminus."
FT /evidence="ECO:0000269|PubMed:33398170"
FT MUTAGEN 191
FT /note="E->A: Reduced binding to C-degron with an arginine
FT at the C-terminus."
FT /evidence="ECO:0000269|PubMed:33398170"
FT MUTAGEN 191
FT /note="E->K: Strongly reduced binding to C-degron with an
FT arginine at the C-terminus."
FT /evidence="ECO:0000269|PubMed:33398170"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:6XKC"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:6XKC"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:6LBG"
FT HELIX 28..35
FT /evidence="ECO:0007829|PDB:6XKC"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:6LBN"
FT HELIX 44..50
FT /evidence="ECO:0007829|PDB:6XKC"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:6XKC"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:6XKC"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:6XKC"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:6XKC"
FT HELIX 86..92
FT /evidence="ECO:0007829|PDB:6XKC"
FT HELIX 96..104
FT /evidence="ECO:0007829|PDB:6XKC"
FT HELIX 119..126
FT /evidence="ECO:0007829|PDB:6XKC"
FT HELIX 129..137
FT /evidence="ECO:0007829|PDB:6XKC"
FT HELIX 152..159
FT /evidence="ECO:0007829|PDB:6XKC"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:6XKC"
FT HELIX 185..192
FT /evidence="ECO:0007829|PDB:6XKC"
FT HELIX 195..203
FT /evidence="ECO:0007829|PDB:6XKC"
FT HELIX 217..223
FT /evidence="ECO:0007829|PDB:6XKC"
FT HELIX 227..238
FT /evidence="ECO:0007829|PDB:6XKC"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:6XKC"
FT HELIX 262..276
FT /evidence="ECO:0007829|PDB:6LF0"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:6LDP"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:6LF0"
FT HELIX 305..309
FT /evidence="ECO:0007829|PDB:6LF0"
FT HELIX 310..313
FT /evidence="ECO:0007829|PDB:6LDP"
FT HELIX 315..330
FT /evidence="ECO:0007829|PDB:6LF0"
FT HELIX 335..350
FT /evidence="ECO:0007829|PDB:6LF0"
FT HELIX 354..370
FT /evidence="ECO:0007829|PDB:6LF0"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:6LE6"
FT HELIX 386..393
FT /evidence="ECO:0007829|PDB:6LF0"
SQ SEQUENCE 617 AA; 68673 MW; 6218B3963C486369 CRC64;
MDLKTAVFNA ARDGKLRLLT KLLASKSKEE VSSLISEKTN GATPLLMAAR YGHLDMVEFL
LEQCSASIEV GGSVNFDGET IEGAPPLWAA SAAGHLKVVQ SLLNHGASVN NTTLTNSTPL
RAACFDGHLE IVKYLVEHKA DLEVSNRHGH TCLMISCYKG HKEIAQYLLE KGADVNRKSV
KGNTALHDCA ESGSLDIMKM LLMYCAKMEK DGYGMTPLLS ASVTGHTNIV DFLTHHAQTS
KTERINALEL LGATFVDKKR DLLGALKYWK KAMNMRYSDR TNIISKPVPQ TLIMAYDYAK
EVNSAEELEG LIADPDEMRM QALLIRERIL GPSHPDTSYY IRYRGAVYAD SGNFKRCINL
WKYALDMQQS NLDPLSPMTA SSLLSFAELF SFMLQDRAKG LLGTTVTFDD LMGILCKSVL
EIERAIKQTQ CPADPLQLNK ALSIILHLIC LLEKVPCTLE QDHFKKQTIY RFLKLHPRGK
NNFSPLHLAV DKNTTCVGRY PVCKFPSLQV TAILIECGAD VNVRDSDDNS PLHIAALNNH
PDIMNLLIKS GAHFDATNLH KQTASDLLDE KEIAKNLIQP INHTTLQCLA ARVIVNHRIY
YKGHIPEKLE TFVSLHR
