CAVN1_MOUSE
ID CAVN1_MOUSE Reviewed; 392 AA.
AC O54724; Q2TAW6;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Caveolae-associated protein 1;
DE AltName: Full=Cav-p60;
DE AltName: Full=Cavin-1;
DE AltName: Full=Polymerase I and transcript release factor;
GN Name=Cavin1; Synonyms=Ptrf {ECO:0000312|MGI:MGI:1277968};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC53588.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH TTF1 AND RNA
RP POLYMERASE I.
RX PubMed=9582279; DOI=10.1093/emboj/17.10.2855;
RA Jansa P., Mason S.W., Hoffmann-Rohrer U., Grummt I.;
RT "Cloning and functional characterization of PTRF, a novel protein which
RT induces dissociation of paused ternary transcription complexes.";
RL EMBO J. 17:2855-2864(1998).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAL60240.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ {ECO:0000312|EMBL:AAL60240.1};
RX PubMed=11161808; DOI=10.1006/geno.2000.6433;
RA Miyoshi K., Cui Y., Riedlinger G., Robinson P., Lehoczky J., Zon L.,
RA Oka T., Dewar K., Hennighausen L.;
RT "Structure of the mouse Stat 3/5 locus: evolution from Drosophila to
RT zebrafish to mouse.";
RL Genomics 71:150-155(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000269|PubMed:15489334};
RC TISSUE=Eye {ECO:0000269|PubMed:15489334};
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 [5] {ECO:0000305}
RP INTERACTION WITH ZNF148.
RX PubMed=10727401; DOI=10.1042/bj3470055;
RA Hasegawa T., Takeuchi A., Miyaishi O., Xiao H., Mao J., Isobe K.;
RT "PTRF (polymerase I and transcript-release factor) is tissue-specific and
RT interacts with the BFCOL1 (binding factor of a type-I collagen promoter)
RT zinc-finger transcription factor which binds to the two mouse type-I
RT collagen gene promoters.";
RL Biochem. J. 347:55-59(2000).
RN [6] {ECO:0000305}
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=11139612; DOI=10.1093/nar/29.2.423;
RA Jansa P., Burek C., Sander E.E., Grummt I.;
RT "The transcript release factor PTRF augments ribosomal gene transcription
RT by facilitating reinitiation of RNA polymerase I.";
RL Nucleic Acids Res. 29:423-429(2001).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-310, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=18191225; DOI=10.1016/j.cell.2007.11.042;
RA Hill M.M., Bastiani M., Luetterforst R., Kirkham M., Kirkham A.,
RA Nixon S.J., Walser P., Abankwa D., Oorschot V.M., Martin S., Hancock J.F.,
RA Parton R.G.;
RT "PTRF-Cavin, a conserved cytoplasmic protein required for caveola formation
RT and function.";
RL Cell 132:113-124(2008).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18840361; DOI=10.1016/j.cmet.2008.07.008;
RA Liu L., Brown D., McKee M., Lebrasseur N.K., Yang D., Albrecht K.H.,
RA Ravid K., Pilch P.F.;
RT "Deletion of Cavin/PTRF causes global loss of caveolae, dyslipidemia, and
RT glucose intolerance.";
RL Cell Metab. 8:310-317(2008).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18056712; DOI=10.1074/jbc.m707890200;
RA Liu L., Pilch P.F.;
RT "A critical role of cavin (polymerase I and transcript release factor) in
RT caveolae formation and organization.";
RL J. Biol. Chem. 283:4314-4322(2008).
RN [12]
RP FUNCTION, IDENTIFICATION IN THE CAVIN COMPLEX, INTERACTION WITH CAV1;
RP CAVIN2; CAVIN3 AND CAVIN4, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=19546242; DOI=10.1083/jcb.200903053;
RA Bastiani M., Liu L., Hill M.M., Jedrychowski M.P., Nixon S.J., Lo H.P.,
RA Abankwa D., Luetterforst R., Fernandez-Rojo M., Breen M.R., Gygi S.P.,
RA Vinten J., Walser P.J., North K.N., Hancock J.F., Pilch P.F., Parton R.G.;
RT "MURC/Cavin-4 and cavin family members form tissue-specific caveolar
RT complexes.";
RL J. Cell Biol. 185:1259-1273(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169 AND SER-302, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; THR-40; SER-42; SER-169;
RP SER-171; SER-173; THR-198; SER-204; SER-205; TYR-310 AND SER-391, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [15]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23652019; DOI=10.1038/ncomms2808;
RA Hansen C.G., Shvets E., Howard G., Riento K., Nichols B.J.;
RT "Deletion of cavin genes reveals tissue-specific mechanisms for
RT morphogenesis of endothelial caveolae.";
RL Nat. Commun. 4:1831-1831(2013).
RN [16]
RP DOMAIN LEUCINE ZIPPER, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL,
RP PHOSPHORYLATION AT SER-389 AND SER-391, AND MUTAGENESIS OF SER-389 AND
RP SER-391.
RX PubMed=25514038; DOI=10.1016/j.bbrc.2014.12.035;
RA Wei Z., Zou X., Wang H., Lei J., Wu Y., Liao K.;
RT "The N-terminal leucine-zipper motif in PTRF/cavin-1 is essential and
RT sufficient for its caveolae-association.";
RL Biochem. Biophys. Res. Commun. 456:750-756(2015).
RN [17]
RP INTERACTION WITH CAV1; CAVIN2 AND CAVIN3, AND SUBUNIT.
RX PubMed=25588833; DOI=10.1242/jcs.161463;
RA Mohan J., Moren B., Larsson E., Holst M.R., Lundmark R.;
RT "Cavin3 interacts with cavin1 and caveolin1 to increase surface dynamics of
RT caveolae.";
RL J. Cell Sci. 128:979-991(2015).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TTF1, PHOSPHORYLATION AT
RP TYR-158, MUTAGENESIS OF TYR-158, NUCLEAR EXPORT SIGNAL, AND UBIQUITINATION.
RX PubMed=27528195; DOI=10.7554/elife.17508;
RA Liu L., Pilch P.F.;
RT "PTRF/Cavin-1 promotes efficient ribosomal RNA transcription in response to
RT metabolic challenges.";
RL Elife 5:0-0(2016).
RN [19]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=30188967; DOI=10.1093/abbs/gmy105;
RA Wei Z., Liu T., Lei J., Wu Y., Wang S., Liao K.;
RT "Fam198a, a member of secreted kinase, secrets through caveolae biogenesis
RT pathway.";
RL Acta Biochim. Biophys. Sin. 50:968-975(2018).
CC -!- FUNCTION: Plays an important role in caveolae formation and
CC organization. Essential for the formation of caveolae in all tissues
CC (PubMed:18191225, PubMed:18840361, PubMed:18056712, PubMed:30188967).
CC Core component of the CAVIN complex which is essential for recruitment
CC of the complex to the caveolae in presence of calveolin-1 (CAV1)
CC (PubMed:19546242). Essential for normal oligomerization of CAV1
CC (PubMed:23652019). Promotes ribosomal transcriptional activity in
CC response to metabolic challenges in the adipocytes and plays an
CC important role in the formation of the ribosomal transcriptional loop
CC (PubMed:27528195). Dissociates transcription complexes paused by DNA-
CC bound TTF1, thereby releasing both RNA polymerase I and pre-RNA from
CC the template (PubMed:9582279, PubMed:11139612). The caveolae biogenesis
CC pathway is required for the secretion of proteins such as GASK1A
CC (PubMed:30188967). {ECO:0000269|PubMed:11139612,
CC ECO:0000269|PubMed:18056712, ECO:0000269|PubMed:18191225,
CC ECO:0000269|PubMed:18840361, ECO:0000269|PubMed:19546242,
CC ECO:0000269|PubMed:23652019, ECO:0000269|PubMed:27528195,
CC ECO:0000269|PubMed:30188967, ECO:0000269|PubMed:9582279}.
CC -!- SUBUNIT: Component of the CAVIN complex composed of CAVIN1, CAVIN2,
CC CAVIN3 and CAVIN4 (PubMed:19546242). Homotrimer (PubMed:25588833).
CC Interacts with LIPE in the adipocyte cytoplasm (By similarity).
CC Interacts with RNA polymerase I (PubMed:9582279). Interacts with TTF1
CC (PubMed:9582279, PubMed:27528195). Binds the 3' end of pre-rRNA
CC (PubMed:9582279). Interacts with transcription factor ZNF148
CC (PubMed:10727401). Interacts with CAV1, CAVIN2 and CAVIN3
CC (PubMed:25588833, PubMed:19546242). Interacts with CAVIN4
CC (PubMed:19546242). {ECO:0000250|UniProtKB:Q6NZI2,
CC ECO:0000269|PubMed:10727401, ECO:0000269|PubMed:19546242,
CC ECO:0000269|PubMed:25588833, ECO:0000269|PubMed:27528195,
CC ECO:0000269|PubMed:9582279}.
CC -!- SUBCELLULAR LOCATION: Membrane, caveola {ECO:0000269|PubMed:18056712,
CC ECO:0000269|PubMed:18191225, ECO:0000269|PubMed:19546242,
CC ECO:0000269|PubMed:25514038}. Cell membrane
CC {ECO:0000269|PubMed:18056712, ECO:0000269|PubMed:18191225}. Microsome
CC {ECO:0000250|UniProtKB:Q6NZI2}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:30188967}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:18191225, ECO:0000269|PubMed:19546242}.
CC Mitochondrion {ECO:0000250|UniProtKB:Q6NZI2}. Nucleus
CC {ECO:0000269|PubMed:25514038, ECO:0000269|PubMed:27528195}.
CC Note=Translocates to the cytoplasm from caveolae upon insulin
CC stimulation (By similarity). Colocalizes with CAV1 in lipid rafts in
CC adipocytes (PubMed:18056712). Localizes in the caveolae in a caveolin-
CC dependent manner (PubMed:19546242). {ECO:0000250|UniProtKB:Q6NZI2,
CC ECO:0000269|PubMed:18056712, ECO:0000269|PubMed:19546242}.
CC -!- TISSUE SPECIFICITY: Expressed in the heart, stomach, adipose tissue and
CC lung (at protein level). Expressed in testis, kidney, muscle, liver,
CC spleen and brain. {ECO:0000269|PubMed:11161808,
CC ECO:0000269|PubMed:18191225, ECO:0000269|PubMed:19546242}.
CC -!- DOMAIN: The leucine-zipper domain 1 is essential for its localization
CC in the caveolae. {ECO:0000269|PubMed:25514038}.
CC -!- PTM: Phosphorylated. Present in active and inactive forms. Changes in
CC phosphorylation pattern may alter activity. Phosphorylation at Tyr-158
CC is essential for its function in the regulation of the ribosomal
CC transcriptional activity. {ECO:0000269|PubMed:11139612,
CC ECO:0000269|PubMed:27528195}.
CC -!- PTM: Monoubiquitinated. {ECO:0000269|PubMed:27528195}.
CC -!- DISRUPTION PHENOTYPE: Mice show a metabolic phenotype of significantly
CC reduced adipose tissue mass, higher circulating triglyceride levels,
CC glucose intolerance, and hyperinsulinemia, consistent with a
CC lipodystrophy. Cells from various tissues, including lung epithelium,
CC intestinal smooth muscle, skeletal muscle, and endothelial cells showed
CC no detectable caveolae cells. {ECO:0000269|PubMed:18840361}.
CC -!- SIMILARITY: Belongs to the CAVIN family. {ECO:0000305}.
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; AF036249; AAC53588.1; -; mRNA.
DR EMBL; AF458959; AAL60240.1; -; Genomic_DNA.
DR EMBL; AL591466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC110698; AAI10699.1; -; mRNA.
DR EMBL; BC117527; AAI17528.1; -; mRNA.
DR EMBL; BC116701; AAI16702.1; -; mRNA.
DR CCDS; CCDS25442.1; -.
DR RefSeq; NP_033012.1; NM_008986.2.
DR PDB; 4QKV; X-ray; 3.00 A; A/B/C=45-155.
DR PDBsum; 4QKV; -.
DR AlphaFoldDB; O54724; -.
DR SMR; O54724; -.
DR BioGRID; 202511; 13.
DR DIP; DIP-40506N; -.
DR IntAct; O54724; 12.
DR MINT; O54724; -.
DR STRING; 10090.ENSMUSP00000058321; -.
DR iPTMnet; O54724; -.
DR PhosphoSitePlus; O54724; -.
DR jPOST; O54724; -.
DR MaxQB; O54724; -.
DR PaxDb; O54724; -.
DR PeptideAtlas; O54724; -.
DR PRIDE; O54724; -.
DR ProteomicsDB; 265670; -.
DR Antibodypedia; 29228; 237 antibodies from 34 providers.
DR DNASU; 19285; -.
DR Ensembl; ENSMUST00000060792; ENSMUSP00000058321; ENSMUSG00000004044.
DR GeneID; 19285; -.
DR KEGG; mmu:19285; -.
DR UCSC; uc007lmr.2; mouse.
DR CTD; 284119; -.
DR MGI; MGI:1277968; Cavin1.
DR VEuPathDB; HostDB:ENSMUSG00000004044; -.
DR eggNOG; ENOG502QV3D; Eukaryota.
DR GeneTree; ENSGT00950000182910; -.
DR HOGENOM; CLU_039470_0_0_1; -.
DR InParanoid; O54724; -.
DR OMA; GRCPGAH; -.
DR OrthoDB; 1060453at2759; -.
DR PhylomeDB; O54724; -.
DR TreeFam; TF331031; -.
DR Reactome; R-MMU-73863; RNA Polymerase I Transcription Termination.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR BioGRID-ORCS; 19285; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Ptrf; mouse.
DR PRO; PR:O54724; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O54724; protein.
DR Bgee; ENSMUSG00000004044; Expressed in thoracic mammary gland and 224 other tissues.
DR Genevisible; O54724; MM.
DR GO; GO:0005901; C:caveola; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042134; F:rRNA primary transcript binding; IDA:UniProtKB.
DR GO; GO:2000147; P:positive regulation of cell motility; IMP:UniProtKB.
DR GO; GO:0009306; P:protein secretion; IMP:UniProtKB.
DR GO; GO:0009303; P:rRNA transcription; IMP:UniProtKB.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; IDA:UniProtKB.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; IDA:UniProtKB.
DR InterPro; IPR033297; Cavin-1.
DR InterPro; IPR026752; Cavin_fam.
DR PANTHER; PTHR15240; PTHR15240; 1.
DR PANTHER; PTHR15240:SF3; PTHR15240:SF3; 1.
DR Pfam; PF15237; PTRF_SDPR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell membrane; Coiled coil; Cytoplasm;
KW Endoplasmic reticulum; Isopeptide bond; Membrane; Microsome; Mitochondrion;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW rRNA-binding; Transcription; Transcription regulation;
KW Transcription termination; Ubl conjugation.
FT CHAIN 1..392
FT /note="Caveolae-associated protein 1"
FT /id="PRO_0000097095"
FT REGION 1..100
FT /note="Required for homotrimerization and for interaction
FT with CAVIN2 and CAVIN3"
FT /evidence="ECO:0000269|PubMed:25588833"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..64
FT /note="Nuclear export signal"
FT /evidence="ECO:0000269|PubMed:27528195"
FT REGION 55..77
FT /note="Leucine-zipper 1"
FT /evidence="ECO:0000269|PubMed:25514038"
FT REGION 138..154
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000305|PubMed:25514038"
FT REGION 168..188
FT /note="Leucine-zipper 2"
FT /evidence="ECO:0000305|PubMed:25514038"
FT REGION 173..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..251
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000305|PubMed:25514038"
FT REGION 259..299
FT /note="Leucine-zipper 3"
FT /evidence="ECO:0000305|PubMed:25514038"
FT REGION 347..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 201..284
FT /evidence="ECO:0000255"
FT COMPBIAS 176..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZI2"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P85125"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 40
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P85125"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZI2"
FT MOD_RES 158
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:27528195"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P85125"
FT MOD_RES 198
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 304
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZI2"
FT MOD_RES 310
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZI2"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZI2"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZI2"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25514038"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25514038,
FT ECO:0007744|PubMed:21183079"
FT CROSSLNK 118
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6NZI2"
FT CROSSLNK 124
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6NZI2"
FT CROSSLNK 163
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q6NZI2"
FT CROSSLNK 163
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q6NZI2"
FT CROSSLNK 167
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6NZI2"
FT CROSSLNK 172
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6NZI2"
FT CROSSLNK 328
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6NZI2"
FT MUTAGEN 158
FT /note="Y->F: Significant loss of phosphorylation and loss
FT of regulation of ribosomal transcriptional activity."
FT /evidence="ECO:0000269|PubMed:27528195"
FT MUTAGEN 389
FT /note="S->A: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:25514038"
FT MUTAGEN 391
FT /note="S->A: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:25514038"
FT HELIX 49..116
FT /evidence="ECO:0007829|PDB:4QKV"
FT HELIX 119..144
FT /evidence="ECO:0007829|PDB:4QKV"
SQ SEQUENCE 392 AA; 43954 MW; 6871CBC06DCF5C35 CRC64;
MEDVTLHIVE RPYSGFPDAS SEGPEPTQGE ARATEEPSGT GSDELIKSDQ VNGVLVLSLL
DKIIGAVDQI QLTQAQLEER QAEMEGAVQS IQGELSKLGK AHATTSNTVS KLLEKVRKVS
VNVKTVRGSL ERQAGQIKKL EVNEAELLRR RNFKVMIYQD EVKLPAKLSV SKSLKESEAL
PEKEGDELGE GERPEDDTAA IELSSDEAVE VEEVIEESRA ERIKRSGLRR VDDFKKAFSK
EKMEKTKVRT RENLEKTRLK TKENLEKTRH TLEKRMNKLG TRLVPVERRE KLKTSRDKLR
KSFTPDHVVY ARSKTAVYKV PPFTFHVKKI REGEVEVLKA TEMVEVGPED DEVGAERGEA
TDLLRGSSPD VHTLLEITEE SDAVLVDKSD SD
