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Glomulin (FK506-binding protein-associated protein) (FAP) (FKBP-associated protein)

 GLMN_HUMAN              Reviewed;         594 AA.
Q92990; Q5VVC3; Q9BVE8;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
14-NOV-2003, sequence version 2.
12-SEP-2018, entry version 151.
RecName: Full=Glomulin;
AltName: Full=FK506-binding protein-associated protein;
Short=FAP;
AltName: Full=FKBP-associated protein;
Name=GLMN; Synonyms=FAP48, FAP68, VMGLOM;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Leukemia;
PubMed=8955134; DOI=10.1074/jbc.271.51.32923;
Chambraud B., Radanyi C., Camonis J.H., Shazand K., Rajkowski K.,
Baulieu E.-E.;
"FAP48, a new protein that forms specific complexes with both
immunophilins FKBP59 and FKBP12. Prevention by the immunosuppressant
drugs FK506 and rapamycin.";
J. Biol. Chem. 271:32923-32929(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, PHOSPHORYLATION, AND
INTERACTION WITH MET.
PubMed=11571281; DOI=10.1074/jbc.M104323200;
Grisendi S., Chambraud B., Gout I., Comoglio P.M., Crepaldi T.;
"Ligand-regulated binding of FAP68 to the hepatocyte growth factor
receptor.";
J. Biol. Chem. 276:46632-46638(2001).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANT GVMS
ASN-393 DEL.
PubMed=11845407; DOI=10.1086/339492;
Brouillard P., Boon L.M., Mulliken J.B., Enjolras O., Ghassibe M.,
Warman M.L., Tan O.T., Olsen B.R., Vikkula M.;
"Mutations in a novel factor, glomulin, are responsible for
glomuvenous malformations ('glomangiomas').";
Am. J. Hum. Genet. 70:866-874(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION.
PubMed=12604780; DOI=10.1073/pnas.0438007100;
Krummrei U., Baulieu E.-E., Chambraud B.;
"The FKBP-associated protein FAP48 is an antiproliferative molecule
and a player in T cell activation that increases IL2 synthesis.";
Proc. Natl. Acad. Sci. U.S.A. 100:2444-2449(2003).
[8]
MUTAGENESIS OF PRO-219.
PubMed=11164950; DOI=10.1016/S0167-0115(00)00206-8;
Neye H.;
"Mutation of FKBP associated protein 48 (FAP48) at proline 219
disrupts the interaction with FKBP12 and FKBP52.";
Regul. Pept. 97:147-152(2001).
[9]
IDENTIFICATION IN A COMPLEX WITH CUL7; SKP1; FBXW8 AND RBX1.
PubMed=12904573; DOI=10.1073/pnas.1733908100;
Arai T., Kasper J.S., Skaar J.R., Ali S.H., Takahashi C.,
DeCaprio J.A.;
"Targeted disruption of p185/Cul7 gene results in abnormal vascular
morphogenesis.";
Proc. Natl. Acad. Sci. U.S.A. 100:9855-9860(2003).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: Essential for normal development of the vasculature. May
represent a naturally occurring ligand of the immunophilins FKBP59
and FKBP12. May function as an membrane anchoring protein. Isoform
1 may stimulate the p70S6K pathway. Isoform 2 may inhibit cell
proliferation and increase IL2 production.
{ECO:0000269|PubMed:11571281, ECO:0000269|PubMed:12604780}.
-!- SUBUNIT: Monomer. Isoform 1 interacts with notphosphorylated MET
and is released upon receptor phosphorylation. Isoform 2 interacts
with FKBP59 and FKBP12. Isoform 1 is part of a SCF-like complex
consisting of CUL7, RBX1, SKP1, FBXW8 and GLMN isoform 1.
{ECO:0000269|PubMed:11571281, ECO:0000269|PubMed:12904573}.
-!- INTERACTION:
Q02790:FKBP4; NbExp=3; IntAct=EBI-726150, EBI-1047444;
P62877:RBX1; NbExp=4; IntAct=EBI-726150, EBI-398523;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=FAP68, FKBP-associated protein 68 kDa;
IsoId=Q92990-1; Sequence=Displayed;
Name=2; Synonyms=FAP48, FKBP-associated protein 48 kDa;
IsoId=Q92990-2; Sequence=VSP_008882, VSP_008883;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- PTM: Phosphorylated on tyrosine residues.
{ECO:0000269|PubMed:11571281}.
-!- DISEASE: Glomuvenous malformations (GVMs) [MIM:138000]:
Characterized by the presence of smooth-muscle-like glomus cells
in the media surrounding distended vascular lumens.
{ECO:0000269|PubMed:11845407}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Rapamycin and FK506 abolish the interaction in a
dose dependent manner.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/GLMNID43022ch1p22.html";
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EMBL; U73704; AAC50908.1; -; mRNA.
EMBL; AJ347709; CAC69882.1; -; mRNA.
EMBL; AJ302735; CAC82938.1; -; mRNA.
EMBL; AJ302727; CAC88124.1; -; Genomic_DNA.
EMBL; AJ302728; CAC88124.1; JOINED; Genomic_DNA.
EMBL; AJ302729; CAC88124.1; JOINED; Genomic_DNA.
EMBL; AJ302730; CAC88124.1; JOINED; Genomic_DNA.
EMBL; AJ302731; CAC88124.1; JOINED; Genomic_DNA.
EMBL; AJ302732; CAC88124.1; JOINED; Genomic_DNA.
EMBL; AJ302733; CAC88124.1; JOINED; Genomic_DNA.
EMBL; AJ302734; CAC88124.1; JOINED; Genomic_DNA.
EMBL; AL451010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471097; EAW73098.1; -; Genomic_DNA.
EMBL; BC001257; AAH01257.1; -; mRNA.
CCDS; CCDS738.1; -. [Q92990-1]
RefSeq; NP_001306612.1; NM_001319683.1.
RefSeq; NP_444504.1; NM_053274.2. [Q92990-1]
RefSeq; XP_011538848.1; XM_011540546.2. [Q92990-1]
UniGene; Hs.49105; -.
PDB; 4F52; X-ray; 3.00 A; E/F=1-594.
PDBsum; 4F52; -.
ProteinModelPortal; Q92990; -.
SMR; Q92990; -.
BioGrid; 116318; 85.
CORUM; Q92990; -.
IntAct; Q92990; 14.
STRING; 9606.ENSP00000359385; -.
iPTMnet; Q92990; -.
PhosphoSitePlus; Q92990; -.
SwissPalm; Q92990; -.
BioMuta; GLMN; -.
DMDM; 38372884; -.
EPD; Q92990; -.
MaxQB; Q92990; -.
PaxDb; Q92990; -.
PeptideAtlas; Q92990; -.
PRIDE; Q92990; -.
ProteomicsDB; 75652; -.
ProteomicsDB; 75653; -. [Q92990-2]
TopDownProteomics; Q92990-1; -. [Q92990-1]
Ensembl; ENST00000370360; ENSP00000359385; ENSG00000174842. [Q92990-1]
Ensembl; ENST00000495106; ENSP00000436829; ENSG00000174842. [Q92990-2]
GeneID; 11146; -.
KEGG; hsa:11146; -.
UCSC; uc001dor.4; human. [Q92990-1]
CTD; 11146; -.
DisGeNET; 11146; -.
EuPathDB; HostDB:ENSG00000174842.16; -.
GeneCards; GLMN; -.
HGNC; HGNC:14373; GLMN.
HPA; HPA031446; -.
HPA; HPA031448; -.
MalaCards; GLMN; -.
MIM; 138000; phenotype.
MIM; 601749; gene.
neXtProt; NX_Q92990; -.
OpenTargets; ENSG00000174842; -.
Orphanet; 83454; Glomuvenous malformation.
PharmGKB; PA134870088; -.
eggNOG; ENOG410IG4H; Eukaryota.
eggNOG; ENOG410YJ4Z; LUCA.
GeneTree; ENSGT00390000018446; -.
HOGENOM; HOG000043079; -.
HOVERGEN; HBG044811; -.
InParanoid; Q92990; -.
OMA; KNQIDMS; -.
OrthoDB; EOG091G054M; -.
PhylomeDB; Q92990; -.
TreeFam; TF105319; -.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; Q92990; -.
SIGNOR; Q92990; -.
ChiTaRS; GLMN; human.
GeneWiki; GLMN; -.
GenomeRNAi; 11146; -.
PRO; PR:Q92990; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000174842; Expressed in 202 organ(s), highest expression level in caudate nucleus.
CleanEx; HS_GLMN; -.
ExpressionAtlas; Q92990; baseline and differential.
Genevisible; Q92990; HS.
GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; IPI:MGI.
GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IPI:MGI.
GO; GO:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; IPI:MGI.
GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IPI:MGI.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005622; C:intracellular; NAS:UniProtKB.
GO; GO:0005171; F:hepatocyte growth factor receptor binding; IPI:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:MGI.
GO; GO:0055105; F:ubiquitin-protein transferase inhibitor activity; IGI:MGI.
GO; GO:0042692; P:muscle cell differentiation; IMP:UniProtKB.
GO; GO:0042130; P:negative regulation of T cell proliferation; IDA:UniProtKB.
GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
GO; GO:0050715; P:positive regulation of cytokine secretion; IMP:UniProtKB.
GO; GO:0045086; P:positive regulation of interleukin-2 biosynthetic process; IMP:UniProtKB.
GO; GO:0042327; P:positive regulation of phosphorylation; IDA:UniProtKB.
GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:UniProtKB.
GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:MGI.
GO; GO:0001570; P:vasculogenesis; IMP:UniProtKB.
InterPro; IPR019516; Glomulin/ALF4.
InterPro; IPR013877; YAP-bd/ALF4/Glomulin.
PANTHER; PTHR15430; PTHR15430; 1.
Pfam; PF08568; Kinetochor_Ybp2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Coiled coil;
Complete proteome; Disease mutation; Phosphoprotein; Polymorphism;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
CHAIN 2 594 Glomulin.
/FTId=PRO_0000087513.
COILED 188 208 {ECO:0000255}.
COILED 272 289 {ECO:0000255}.
COMPBIAS 123 126 Poly-Leu.
COMPBIAS 273 278 Poly-Glu.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
VAR_SEQ 406 417 CLLNTSNHSGVE -> EHVTTNGLQDHS (in isoform
2). {ECO:0000303|PubMed:8955134}.
/FTId=VSP_008882.
VAR_SEQ 418 594 Missing (in isoform 2).
{ECO:0000303|PubMed:8955134}.
/FTId=VSP_008883.
VARIANT 336 336 L -> S (in dbSNP:rs35258161).
/FTId=VAR_061653.
VARIANT 393 393 Missing (in GVMs).
{ECO:0000269|PubMed:11845407}.
/FTId=VAR_017241.
MUTAGEN 219 219 P->A: Loss of interaction with FKBP12 and
FKBP59. {ECO:0000269|PubMed:11164950}.
HELIX 2 13 {ECO:0000244|PDB:4F52}.
HELIX 28 37 {ECO:0000244|PDB:4F52}.
STRAND 38 40 {ECO:0000244|PDB:4F52}.
HELIX 43 49 {ECO:0000244|PDB:4F52}.
HELIX 55 60 {ECO:0000244|PDB:4F52}.
HELIX 62 65 {ECO:0000244|PDB:4F52}.
HELIX 66 74 {ECO:0000244|PDB:4F52}.
STRAND 80 82 {ECO:0000244|PDB:4F52}.
HELIX 84 96 {ECO:0000244|PDB:4F52}.
HELIX 99 101 {ECO:0000244|PDB:4F52}.
HELIX 102 106 {ECO:0000244|PDB:4F52}.
HELIX 107 110 {ECO:0000244|PDB:4F52}.
HELIX 115 117 {ECO:0000244|PDB:4F52}.
HELIX 118 135 {ECO:0000244|PDB:4F52}.
HELIX 140 156 {ECO:0000244|PDB:4F52}.
HELIX 173 192 {ECO:0000244|PDB:4F52}.
HELIX 199 222 {ECO:0000244|PDB:4F52}.
HELIX 236 250 {ECO:0000244|PDB:4F52}.
STRAND 251 253 {ECO:0000244|PDB:4F52}.
HELIX 255 257 {ECO:0000244|PDB:4F52}.
HELIX 283 294 {ECO:0000244|PDB:4F52}.
TURN 298 302 {ECO:0000244|PDB:4F52}.
HELIX 309 324 {ECO:0000244|PDB:4F52}.
HELIX 329 344 {ECO:0000244|PDB:4F52}.
HELIX 353 357 {ECO:0000244|PDB:4F52}.
HELIX 359 374 {ECO:0000244|PDB:4F52}.
HELIX 378 394 {ECO:0000244|PDB:4F52}.
HELIX 397 411 {ECO:0000244|PDB:4F52}.
HELIX 414 430 {ECO:0000244|PDB:4F52}.
TURN 440 442 {ECO:0000244|PDB:4F52}.
HELIX 444 453 {ECO:0000244|PDB:4F52}.
TURN 457 461 {ECO:0000244|PDB:4F52}.
TURN 464 466 {ECO:0000244|PDB:4F52}.
HELIX 468 484 {ECO:0000244|PDB:4F52}.
TURN 487 489 {ECO:0000244|PDB:4F52}.
HELIX 494 496 {ECO:0000244|PDB:4F52}.
HELIX 498 504 {ECO:0000244|PDB:4F52}.
HELIX 506 533 {ECO:0000244|PDB:4F52}.
HELIX 553 555 {ECO:0000244|PDB:4F52}.
HELIX 556 581 {ECO:0000244|PDB:4F52}.
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


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