ID GLMN_HUMAN Reviewed; 594 AA. AC Q92990; Q5VVC3; Q9BVE8; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2003, sequence version 2. DT 10-JUN-2026, entry version 194. DE RecName: Full=Glomulin; DE AltName: Full=FK506-binding protein-associated protein; DE Short=FAP; DE AltName: Full=FKBP-associated protein; GN Name=GLMN; GN Synonyms=FAP48 {ECO:0000303|PubMed:8955134}, FAP68 GN {ECO:0000303|PubMed:11571281}, VMGLOM; 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] (ISOFORM 2), AND INTERACTION WITH FKBP4 AND RP FKBP1A. RC TISSUE=Leukemia; RX PubMed=8955134; DOI=10.1074/jbc.271.51.32923; RA Chambraud B., Radanyi C., Camonis J.H., Shazand K., Rajkowski K., RA Baulieu E.-E.; RT "FAP48, a new protein that forms specific complexes with both immunophilins RT FKBP59 and FKBP12. Prevention by the immunosuppressant drugs FK506 and RT rapamycin."; RL J. Biol. Chem. 271:32923-32929(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, PHOSPHORYLATION, AND RP INTERACTION WITH MET. RX PubMed=11571281; DOI=10.1074/jbc.m104323200; RA Grisendi S., Chambraud B., Gout I., Comoglio P.M., Crepaldi T.; RT "Ligand-regulated binding of FAP68 to the hepatocyte growth factor RT receptor."; RL J. Biol. Chem. 276:46632-46638(2001). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION, TISSUE RP SPECIFICITY, AND VARIANT GVMS ASN-393 DEL. RX PubMed=11845407; DOI=10.1086/339492; RA Brouillard P., Boon L.M., Mulliken J.B., Enjolras O., Ghassibe M., RA Warman M.L., Tan O.T., Olsen B.R., Vikkula M.; RT "Mutations in a novel factor, glomulin, are responsible for glomuvenous RT malformations ('glomangiomas')."; RL Am. J. Hum. Genet. 70:866-874(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). 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=Placenta; 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 INTERACTION WITH FKBP4. RX PubMed=12604780; DOI=10.1073/pnas.0438007100; RA Krummrei U., Baulieu E.-E., Chambraud B.; RT "The FKBP-associated protein FAP48 is an antiproliferative molecule and a RT player in T cell activation that increases IL2 synthesis."; RL Proc. Natl. Acad. Sci. U.S.A. 100:2444-2449(2003). RN [8] RP INTERACTION WITH FKBP4 AND FKBP1A, AND MUTAGENESIS OF PRO-219. RX PubMed=11164950; DOI=10.1016/s0167-0115(00)00206-8; RA Neye H.; RT "Mutation of FKBP associated protein 48 (FAP48) at proline 219 disrupts the RT interaction with FKBP12 and FKBP52."; RL Regul. Pept. 97:147-152(2001). RN [9] RP IDENTIFICATION IN A COMPLEX WITH CUL7; SKP1; FBXW8 AND RBX1, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=12904573; DOI=10.1073/pnas.1733908100; RA Arai T., Kasper J.S., Skaar J.R., Ali S.H., Takahashi C., DeCaprio J.A.; RT "Targeted disruption of p185/Cul7 gene results in abnormal vascular RT morphogenesis."; RL Proc. Natl. Acad. Sci. U.S.A. 100:9855-9860(2003). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP FUNCTION (ISOFORM 1), INTERACTION WITH RBX1, IDENTIFICATION IN A COMPLEX RP WITH RBX1 AND A CULLIN, AND CHARACTERIZATION OF VARIANT GVMS ASN-393 DEL. RX PubMed=22405651; DOI=10.1016/j.molcel.2012.02.005; RA Tron A.E., Arai T., Duda D.M., Kuwabara H., Olszewski J.L., Fujiwara Y., RA Bahamon B.N., Signoretti S., Schulman B.A., DeCaprio J.A.; RT "The glomuvenous malformation protein Glomulin binds Rbx1 and regulates RT cullin RING ligase-mediated turnover of Fbw7."; RL Mol. Cell 46:67-78(2012). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [15] {ECO:0007744|PDB:4F52} RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH RBX1 AND CUL1, RP FUNCTION (ISOFORM 1), REGION, DOMAIN, INTERACTION WITH RBX1, AND RP MUTAGENESIS OF LYS-425; ASN-476; LEU-567 AND ARG-574. RX PubMed=22748924; DOI=10.1016/j.molcel.2012.05.044; RA Duda D.M., Olszewski J.L., Tron A.E., Hammel M., Lambert L.J., RA Waddell M.B., Mittag T., DeCaprio J.A., Schulman B.A.; RT "Structure of a glomulin-RBX1-CUL1 complex: inhibition of a RING E3 ligase RT through masking of its E2-binding surface."; RL Mol. Cell 47:371-382(2012). CC -!- FUNCTION: [Isoform 1]: Regulatory component of cullin-RING-based SCF CC (SKP1-Cullin-F-box protein) E3 ubiquitin-protein ligase complexes CC (PubMed:22405651, PubMed:22748924). Inhibits E3 ubiquitin ligase CC activity by binding to RBX1 (via RING domain) and inhibiting its CC interaction with the E2 ubiquitin-conjugating enzyme CDC34 CC (PubMed:22405651, PubMed:22748924). Inhibits RBX1-mediated neddylation CC of CUL1 (PubMed:22405651). Required for normal stability and normal CC cellular levels of key components of SCF ubiquitin ligase complexes, CC including FBXW7, RBX1, CUL1, CUL2, CUL3, CUL4A, and thereby contributes CC to the regulation of CCNE1 and MYC levels (By similarity). Essential CC for normal development of the vasculature (PubMed:11845407). CC Contributes to the regulation of RPS6KB1 phosphorylation CC (PubMed:11571281). {ECO:0000250|UniProtKB:Q8BZM1, CC ECO:0000269|PubMed:11571281, ECO:0000269|PubMed:11845407, CC ECO:0000269|PubMed:22405651, ECO:0000269|PubMed:22748924}. CC -!- SUBUNIT: Interacts with FKBP4 and FKBP1A (PubMed:11164950, CC PubMed:12604780, PubMed:8955134). Isoform 1: Interacts with RBX1 (via CC RING domain) (PubMed:22405651, PubMed:22748924). Identified in CC complexes that contain RBX1 plus one of the cullins CUL1, CUL2, CUL3, CC and CUL4A (PubMed:22405651, PubMed:22748924). Identified in a SCF CC complex composed of CUL1, RBX1, SKP1, FBXW7 and GLMN (PubMed:22405651). CC Component of a SCF-like complex consisting of CUL7, RBX1, SKP1, FBXW8 CC and GLMN (PubMed:12904573). Interacts with unphosphorylated MET and is CC released upon MET phosphorylation (PubMed:11571281). CC {ECO:0000269|PubMed:11164950, ECO:0000269|PubMed:11571281, CC ECO:0000269|PubMed:12604780, ECO:0000269|PubMed:12904573, CC ECO:0000269|PubMed:22405651, ECO:0000269|PubMed:22748924, CC ECO:0000269|PubMed:8955134}. CC -!- INTERACTION: CC Q92990; O43281-2: EFS; NbExp=3; IntAct=EBI-726150, EBI-11525448; CC Q92990; Q02790: FKBP4; NbExp=5; IntAct=EBI-726150, EBI-1047444; CC Q92990; P50542-3: PEX5; NbExp=3; IntAct=EBI-726150, EBI-12181987; CC Q92990; P62877: RBX1; NbExp=7; IntAct=EBI-726150, EBI-398523; CC Q92990; O95863: SNAI1; NbExp=3; IntAct=EBI-726150, EBI-1045459; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=FAP68, FKBP-associated protein 68 kDa; CC IsoId=Q92990-1; Sequence=Displayed; CC Name=2; Synonyms=FAP48, FKBP-associated protein 48 kDa; CC IsoId=Q92990-2; Sequence=VSP_008882, VSP_008883; CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11845407}. CC -!- DOMAIN: The C-terminal half of the protein is important for interaction CC with RBX1. {ECO:0000269|PubMed:22748924}. CC -!- PTM: Phosphorylated on tyrosine residues. CC {ECO:0000269|PubMed:11571281}. CC -!- DISEASE: Glomuvenous malformations (GVMs) [MIM:138000]: Characterized CC by the presence of smooth-muscle-like glomus cells in the media CC surrounding distended vascular lumens. {ECO:0000269|PubMed:11845407, CC ECO:0000269|PubMed:22405651}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/43022/GLMN"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U73704; AAC50908.1; -; mRNA. DR EMBL; AJ347709; CAC69882.1; -; mRNA. DR EMBL; AJ302735; CAC82938.1; -; mRNA. DR EMBL; AJ302727; CAC88124.1; -; Genomic_DNA. DR EMBL; AJ302728; CAC88124.1; JOINED; Genomic_DNA. DR EMBL; AJ302729; CAC88124.1; JOINED; Genomic_DNA. DR EMBL; AJ302730; CAC88124.1; JOINED; Genomic_DNA. DR EMBL; AJ302731; CAC88124.1; JOINED; Genomic_DNA. DR EMBL; AJ302732; CAC88124.1; JOINED; Genomic_DNA. DR EMBL; AJ302733; CAC88124.1; JOINED; Genomic_DNA. DR EMBL; AJ302734; CAC88124.1; JOINED; Genomic_DNA. DR EMBL; AL451010; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471097; EAW73098.1; -; Genomic_DNA. DR EMBL; BC001257; AAH01257.1; -; mRNA. DR CCDS; CCDS738.1; -. [Q92990-1] DR RefSeq; NP_001306612.1; NM_001319683.1. DR RefSeq; NP_444504.1; NM_053274.3. [Q92990-1] DR RefSeq; XP_011538848.1; XM_011540546.3. [Q92990-1] DR RefSeq; XP_054189955.1; XM_054333980.1. [Q92990-1] DR PDB; 4F52; X-ray; 3.00 A; E/F=1-594. DR PDBsum; 4F52; -. DR AlphaFoldDB; Q92990; -. DR SMR; Q92990; -. DR BioGRID; 116318; 186. DR CORUM; Q92990; -. DR FunCoup; Q92990; 1358. DR IntAct; Q92990; 124. DR MINT; Q92990; -. DR NDEx; MUSIC2-C5199-GLMN; Osteosarcoma (U2OS) cell map - Ubiquitin-proteasome complex (41 proteins). DR STRING; 9606.ENSP00000359385; -. DR BindingDB; Q92990; -. DR ChEMBL; CHEMBL5465342; -. DR GlyGen; Q92990; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q92990; -. DR PhosphoSitePlus; Q92990; -. DR SwissPalm; Q92990; -. DR BioMuta; GLMN; -. DR DMDM; 38372884; -. DR jPOST; Q92990; -. DR MassIVE; Q92990; -. DR PaxDb; 9606-ENSP00000359385; -. DR PeptideAtlas; Q92990; -. DR ProteomicsDB; 75652; -. [Q92990-1] DR ProteomicsDB; 75653; -. [Q92990-2] DR Pumba; Q92990; -. DR TopDownProteomics; Q92990-1; -. [Q92990-1] DR Antibodypedia; 33642; 249 antibodies from 27 providers. DR DNASU; 11146; -. DR Ensembl; ENST00000370360.8; ENSP00000359385.3; ENSG00000174842.18. [Q92990-1] DR Ensembl; ENST00000495106.5; ENSP00000436829.1; ENSG00000174842.18. [Q92990-2] DR Ensembl; ENST00000896609.1; ENSP00000566668.1; ENSG00000174842.18. [Q92990-1] DR GeneID; 11146; -. DR KEGG; hsa:11146; -. DR MANE-Select; ENST00000370360.8; ENSP00000359385.3; NM_053274.3; NP_444504.1. DR UCSC; uc001dor.4; human. [Q92990-1] DR AGR; HGNC:14373; -. DR ClinPGx; PA134870088; -. DR CTD; 11146; -. DR DisGeNET; 11146; -. DR GeneCards; GLMN; -. DR HGNC; HGNC:14373; GLMN. DR HPA; ENSG00000174842; Tissue enhanced (retina). DR MalaCards; GLMN; -. DR MIM; 138000; phenotype. DR MIM; 601749; gene. DR OpenTargets; ENSG00000174842; -. DR Orphanet; 83454; Glomuvenous malformation. DR VEuPathDB; HostDB:ENSG00000174842; -. DR eggNOG; ENOG502QQAV; Eukaryota. DR GeneTree; ENSGT00390000018446; -. DR HOGENOM; CLU_029654_3_0_1; -. DR InParanoid; Q92990; -. DR OMA; TLCPMEH; -. DR OrthoDB; 619536at2759; -. DR PAN-GO; Q92990; 2 GO annotations based on evolutionary models. DR PhylomeDB; Q92990; -. DR PathwayCommons; Q92990; -. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; Q92990; -. DR SIGNOR; Q92990; -. DR Agora; ENSG00000174842; -. DR BioGRID-ORCS; 11146; 248 hits in 1157 CRISPR screens. DR ChiTaRS; GLMN; human. DR EvolutionaryTrace; Q92990; -. DR GeneWiki; GLMN; -. DR GenomeRNAi; 11146; -. DR Pharos; Q92990; Tbio. DR PRO; PR:Q92990; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q92990; protein. DR Bgee; ENSG00000174842; Expressed in primordial germ cell in gonad and 172 other cell types or tissues. DR ExpressionAtlas; Q92990; baseline and differential. DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; IPI:MGI. DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IPI:MGI. DR GO; GO:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; IPI:MGI. DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IPI:MGI. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005171; F:hepatocyte growth factor receptor binding; IDA:MGI. DR GO; GO:0005102; F:signaling receptor binding; IDA:MGI. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:MGI. DR GO; GO:0055105; F:ubiquitin-protein transferase inhibitor activity; IGI:MGI. DR GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:MGI. DR GO; GO:0040029; P:epigenetic regulation of gene expression; IMP:UniProtKB. DR GO; GO:0042692; P:muscle cell differentiation; IMP:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:MGI. DR GO; GO:0042130; P:negative regulation of T cell proliferation; IDA:UniProtKB. DR GO; GO:0001819; P:positive regulation of cytokine production; IMP:UniProtKB. DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IDA:MGI. DR GO; GO:0042327; P:positive regulation of phosphorylation; IDA:UniProtKB. DR GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:MGI. DR GO; GO:0001570; P:vasculogenesis; IMP:UniProtKB. DR IDEAL; IID00518; -. DR InterPro; IPR019516; Glomulin/ALF4. DR InterPro; IPR013877; YAP-bd/ALF4/Glomulin. DR PANTHER; PTHR15430; GLOMULIN; 1. DR PANTHER; PTHR15430:SF1; GLOMULIN; 1. DR Pfam; PF08568; Kinetochor_Ybp2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Disease variant; KW Phosphoprotein; Proteomics identification; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT CHAIN 2..594 FT /note="Glomulin" FT /id="PRO_0000087513" FT REGION 2..553 FT /note="Alpha-helical region with structural similarity to FT HEAT repeats" FT /evidence="ECO:0000269|PubMed:22748924" FT REGION 300..594 FT /note="Important for interaction with RBX1" FT /evidence="ECO:0000269|PubMed:22748924" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT VAR_SEQ 406..417 FT /note="CLLNTSNHSGVE -> EHVTTNGLQDHS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:8955134" FT /id="VSP_008882" FT VAR_SEQ 418..594 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:8955134" FT /id="VSP_008883" FT VARIANT 336 FT /note="L -> S (in dbSNP:rs35258161)" FT /id="VAR_061653" FT VARIANT 393 FT /note="Missing (in GVMs; loss of interaction with CUL1 and FT RBX1; dbSNP:rs773442562)" FT /evidence="ECO:0000269|PubMed:11845407, FT ECO:0000269|PubMed:22405651" FT /id="VAR_017241" FT MUTAGEN 219 FT /note="P->A: Loss of interaction with FKBP4 and FKBP1A." FT /evidence="ECO:0000269|PubMed:11164950" FT MUTAGEN 425 FT /note="K->A: Disrupts interaction with RBX1. Loss of FT inhibition of SCF (SKP1-Cullin-F-box protein) E3 FT ubiquitin-protein ligase activity." FT /evidence="ECO:0000269|PubMed:22748924" FT MUTAGEN 476 FT /note="N->A: Disrupts interaction with RBX1. Loss of FT inhibition of SCF (SKP1-Cullin-F-box protein) E3 FT ubiquitin-protein ligase activity." FT /evidence="ECO:0000269|PubMed:22748924" FT MUTAGEN 567 FT /note="L->A: Disrupts interaction with RBX1. Loss of FT inhibition of SCF (SKP1-Cullin-F-box protein) E3 FT ubiquitin-protein ligase activity." FT /evidence="ECO:0000269|PubMed:22748924" FT MUTAGEN 574 FT /note="R->A: Disrupts interaction with RBX1. Loss of FT inhibition of SCF (SKP1-Cullin-F-box protein) E3 FT ubiquitin-protein ligase activity." FT /evidence="ECO:0000269|PubMed:22748924" FT HELIX 2..13 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 28..37 FT /evidence="ECO:0007829|PDB:4F52" FT STRAND 38..40 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 43..49 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 55..60 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 62..65 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 66..74 FT /evidence="ECO:0007829|PDB:4F52" FT STRAND 80..82 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 84..96 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 99..101 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 102..106 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 107..110 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 115..117 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 118..135 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 140..156 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 158..160 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 173..192 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 199..222 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 236..250 FT /evidence="ECO:0007829|PDB:4F52" FT STRAND 251..253 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 255..257 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 283..290 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 291..295 FT /evidence="ECO:0007829|PDB:4F52" FT TURN 298..302 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 309..324 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 329..344 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 353..357 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 359..374 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 378..394 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 397..411 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 414..430 FT /evidence="ECO:0007829|PDB:4F52" FT TURN 440..442 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 444..453 FT /evidence="ECO:0007829|PDB:4F52" FT TURN 457..461 FT /evidence="ECO:0007829|PDB:4F52" FT TURN 464..466 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 468..484 FT /evidence="ECO:0007829|PDB:4F52" FT TURN 487..489 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 494..496 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 498..501 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 502..506 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 507..533 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 553..555 FT /evidence="ECO:0007829|PDB:4F52" FT HELIX 556..581 FT /evidence="ECO:0007829|PDB:4F52" SQ SEQUENCE 594 AA; 68208 MW; CE19050F1F692378 CRC64; MAVEELQSII KRCQILEEQD FKEEDFGLFQ LAGQRCIEEG HTDQLLEIIQ NEKNKVIIKN MGWNLVGPVV RCLLCKDKED SKRKVYFLIF DLLVKLCNPK ELLLGLLELI EEPSGKQISQ SILLLLQPLQ TVIQKLHNKA YSIGLALSTL WNQLSLLPVP YSKEQIQMDD YGLCQCCKAL IEFTKPFVEE VIDNKENSLE NEKLKDELLK FCFKSLKCPL LTAQFFEQSE EGGNDPFRYF ASEIIGFLSA IGHPFPKMIF NHGRKKRTWN YLEFEEEENK QLADSMASLA YLVFVQGIHI DQLPMVLSPL YLLQFNMGHI EVFLQRTEES VISKGLELLE NSLLRIEDNS LLYQYLEIKS FLTVPQGLVK VMTLCPIETL RKKSLAMLQL YINKLDSQGK YTLFRCLLNT SNHSGVEAFI IQNIKNQIDM SLKRTRNNKW FTGPQLISLL DLVLFLPEGA ETDLLQNSDR IMASLNLLRY LVIKDNENDN QTGLWTELGN IENNFLKPLH IGLNMSKAHY EAEIKNSQEA QKSKDLCSIT VSGEEIPNMP PEMQLKVLHS ALFTFDLIES VLARVEELIE IKTKSTSEEN IGIK //