GLMN_HUMAN
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 03-AUG-2022, entry version 176.
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},
GN FAP68 {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:8955134,
CC PubMed:12604780, PubMed:11164950). 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=4; IntAct=EBI-726150, EBI-1047444;
CC Q92990; P50542-3: PEX5; NbExp=3; IntAct=EBI-726150, EBI-12181987;
CC Q92990; P62877: RBX1; NbExp=6; 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="http://atlasgeneticsoncology.org/Genes/GLMNID43022ch1p22.html";
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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_053274.2. [Q92990-1]
DR RefSeq; XP_011538848.1; XM_011540546.2. [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; 137.
DR CORUM; Q92990; -.
DR IntAct; Q92990; 72.
DR MINT; Q92990; -.
DR STRING; 9606.ENSP00000359385; -.
DR GlyGen; Q92990; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q92990; -.
DR PhosphoSitePlus; Q92990; -.
DR SwissPalm; Q92990; -.
DR BioMuta; GLMN; -.
DR DMDM; 38372884; -.
DR EPD; Q92990; -.
DR jPOST; Q92990; -.
DR MassIVE; Q92990; -.
DR MaxQB; Q92990; -.
DR PaxDb; Q92990; -.
DR PeptideAtlas; Q92990; -.
DR PRIDE; Q92990; -.
DR ProteomicsDB; 75652; -. [Q92990-1]
DR ProteomicsDB; 75653; -. [Q92990-2]
DR TopDownProteomics; Q92990-1; -. [Q92990-1]
DR Antibodypedia; 33642; 253 antibodies from 27 providers.
DR DNASU; 11146; -.
DR Ensembl; ENST00000370360.8; ENSP00000359385.3; ENSG00000174842.17. [Q92990-1]
DR Ensembl; ENST00000495106.5; ENSP00000436829.1; ENSG00000174842.17. [Q92990-2]
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 CTD; 11146; -.
DR DisGeNET; 11146; -.
DR GeneCards; GLMN; -.
DR HGNC; HGNC:14373; GLMN.
DR HPA; ENSG00000174842; Tissue enriched (retina).
DR MalaCards; GLMN; -.
DR MIM; 138000; phenotype.
DR MIM; 601749; gene.
DR neXtProt; NX_Q92990; -.
DR OpenTargets; ENSG00000174842; -.
DR Orphanet; 83454; Glomuvenous malformation.
DR PharmGKB; PA134870088; -.
DR VEuPathDB; HostDB:ENSG00000174842; -.
DR eggNOG; ENOG502QQAV; Eukaryota.
DR GeneTree; ENSGT00390000018446; -.
DR HOGENOM; CLU_029654_3_0_1; -.
DR InParanoid; Q92990; -.
DR OMA; CIFMYKQ; -.
DR OrthoDB; 1088011at2759; -.
DR PhylomeDB; Q92990; -.
DR TreeFam; TF105319; -.
DR PathwayCommons; Q92990; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q92990; -.
DR SIGNOR; Q92990; -.
DR BioGRID-ORCS; 11146; 242 hits in 1078 CRISPR screens.
DR ChiTaRS; GLMN; human.
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 cerebellar hemisphere and 170 other tissues.
DR ExpressionAtlas; Q92990; baseline and differential.
DR Genevisible; Q92990; HS.
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: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:0001843; P:neural tube closure; IEA:Ensembl.
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:0040029; P:regulation of gene expression, epigenetic; IMP: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; PTHR15430; 1.
DR Pfam; PF08568; Kinetochor_Ybp2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Disease variant;
KW Phosphoprotein; 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 ubiquitin-
FT 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 ubiquitin-
FT 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 ubiquitin-
FT 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 ubiquitin-
FT 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 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..294
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..504
FT /evidence="ECO:0007829|PDB:4F52"
FT HELIX 506..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
