TMF1_HUMAN
ID TMF1_HUMAN Reviewed; 1093 AA.
AC P82094; B7ZLJ2; Q17R87; Q59GK0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=TATA element modulatory factor;
DE Short=TMF;
DE AltName: Full=Androgen receptor coactivator 160 kDa protein;
DE AltName: Full=Androgen receptor-associated protein of 160 kDa;
GN Name=TMF1; Synonyms=ARA160;
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 1), AND FUNCTION.
RC TISSUE=Cervix carcinoma;
RX PubMed=1409643; DOI=10.1073/pnas.89.20.9372;
RA Garcia J.A., Ou S.-H.I., Wu F., Lusis A.J., Sparkes R.S., Gaynor R.B.;
RT "Cloning and chromosomal mapping of a human immunodeficiency virus 1 'TATA'
RT element modulatory factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:9372-9376(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RX PubMed=10428808; DOI=10.1074/jbc.274.32.22373;
RA Hsiao P.W., Chang C.;
RT "Isolation and characterization of ARA160 as the first androgen receptor N-
RT terminal-associated coactivator in human prostate cells.";
RL J. Biol. Chem. 274:22373-22379(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno F.R.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
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 SUBCELLULAR LOCATION, AND IDENTIFICATION IN SWI/SNF COMPLEXES.
RX PubMed=12044884; DOI=10.1016/s0014-5793(02)02803-x;
RA Mori K., Kato H.;
RT "A putative nuclear receptor coactivator (TMF/ARA160) associates with
RT hbrm/hSNF2 alpha and BRG-1/hSNF2 beta and localizes in the Golgi
RT apparatus.";
RL FEBS Lett. 520:127-132(2002).
RN [8]
RP FUNCTION, MUTAGENESIS OF 333-LEU--ASP-335, INTERACTION WITH TCEB1 AND
RP STAT3, AND INDUCTION.
RX PubMed=15467733; DOI=10.1038/sj.onc.1208149;
RA Perry E., Tsruya R., Levitsky P., Pomp O., Taller M., Weisberg S.,
RA Parris W., Kulkarni S., Malovani H., Pawson T., Shpungin S., Nir U.;
RT "TMF/ARA160 is a BC-box-containing protein that mediates the degradation of
RT Stat3.";
RL Oncogene 23:8908-8919(2004).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RAB6A.
RX PubMed=17698061; DOI=10.1016/j.yexcr.2007.07.010;
RA Yamane J., Kubo A., Nakayama K., Yuba-Kubo A., Katsuno T., Tsukita S.,
RA Tsukita S.;
RT "Functional involvement of TMF/ARA160 in Rab6-dependent retrograde membrane
RT traffic.";
RL Exp. Cell Res. 313:3472-3485(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-77; SER-112; SER-328;
RP SER-338; SER-344 AND SER-925, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-328 AND SER-344, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217 AND SER-344, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-77; SER-136; SER-199;
RP SER-328; SER-333; SER-344; SER-542 AND SER-933, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-328 AND SER-344, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Potential coactivator of the androgen receptor. Mediates
CC STAT3 degradation. May play critical roles in two RAB6-dependent
CC retrograde transport processes: one from endosomes to the Golgi and the
CC other from the Golgi to the ER. This protein binds the HIV-1 TATA
CC element and inhibits transcriptional activation by the TATA-binding
CC protein (TBP). {ECO:0000269|PubMed:10428808,
CC ECO:0000269|PubMed:1409643, ECO:0000269|PubMed:15467733,
CC ECO:0000269|PubMed:17698061}.
CC -!- SUBUNIT: Interacts with TRNP1; may regulate TRNP1 proteasomal
CC degradation (By similarity). Component of the SNF/SWI transcription
CC factor complexes. Interacts with RAB6A. Interacts with STAT3 and FER.
CC Interacts with TCEB1. {ECO:0000250, ECO:0000269|PubMed:12044884,
CC ECO:0000269|PubMed:15467733, ECO:0000269|PubMed:17698061}.
CC -!- INTERACTION:
CC P82094; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-949763, EBI-11522780;
CC P82094; P04150: NR3C1; NbExp=3; IntAct=EBI-949763, EBI-493507;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Golgi apparatus membrane.
CC Note=Concentrated at the budding structures localized at the tips of
CC cisternae.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P82094-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P82094-2; Sequence=VSP_037411;
CC -!- INDUCTION: Down-regulated in malignant brain tumors.
CC {ECO:0000269|PubMed:15467733}.
CC -!- DOMAIN: The Elongin BC complex binding domain is also known as BC-box
CC with the consensus [APST]-L-x(3)-C-x(3)-[AILV].
CC -!- PTM: Phosphorylated by FER. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD54608.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD92346.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L01042; AAD54608.1; ALT_FRAME; mRNA.
DR EMBL; AB209109; BAD92346.1; ALT_INIT; mRNA.
DR EMBL; AC109587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW65468.1; -; Genomic_DNA.
DR EMBL; BC117418; AAI17419.1; -; mRNA.
DR EMBL; BC126123; AAI26124.1; -; mRNA.
DR EMBL; BC143840; AAI43841.1; -; mRNA.
DR CCDS; CCDS43105.1; -. [P82094-1]
DR CCDS; CCDS87105.1; -. [P82094-2]
DR PIR; A47212; A47212.
DR RefSeq; NP_009045.2; NM_007114.2. [P82094-1]
DR RefSeq; XP_011532358.1; XM_011534056.2.
DR AlphaFoldDB; P82094; -.
DR SMR; P82094; -.
DR BioGRID; 112965; 62.
DR DIP; DIP-5933N; -.
DR IntAct; P82094; 25.
DR MINT; P82094; -.
DR STRING; 9606.ENSP00000381567; -.
DR GlyGen; P82094; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P82094; -.
DR MetOSite; P82094; -.
DR PhosphoSitePlus; P82094; -.
DR BioMuta; TMF1; -.
DR DMDM; 218511858; -.
DR EPD; P82094; -.
DR jPOST; P82094; -.
DR MassIVE; P82094; -.
DR MaxQB; P82094; -.
DR PaxDb; P82094; -.
DR PeptideAtlas; P82094; -.
DR PRIDE; P82094; -.
DR ProteomicsDB; 57702; -. [P82094-1]
DR ProteomicsDB; 57703; -. [P82094-2]
DR Antibodypedia; 1796; 106 antibodies from 23 providers.
DR DNASU; 7110; -.
DR Ensembl; ENST00000398559.7; ENSP00000381567.2; ENSG00000144747.17. [P82094-1]
DR Ensembl; ENST00000646708.1; ENSP00000494067.1; ENSG00000144747.17. [P82094-2]
DR GeneID; 7110; -.
DR KEGG; hsa:7110; -.
DR MANE-Select; ENST00000398559.7; ENSP00000381567.2; NM_007114.3; NP_009045.2.
DR UCSC; uc003dnn.4; human. [P82094-1]
DR CTD; 7110; -.
DR DisGeNET; 7110; -.
DR GeneCards; TMF1; -.
DR HGNC; HGNC:11870; TMF1.
DR HPA; ENSG00000144747; Low tissue specificity.
DR MIM; 601126; gene.
DR neXtProt; NX_P82094; -.
DR OpenTargets; ENSG00000144747; -.
DR PharmGKB; PA36571; -.
DR VEuPathDB; HostDB:ENSG00000144747; -.
DR eggNOG; KOG4673; Eukaryota.
DR GeneTree; ENSGT00390000010697; -.
DR HOGENOM; CLU_009915_0_0_1; -.
DR InParanoid; P82094; -.
DR OMA; LQVDMNE; -.
DR OrthoDB; 145696at2759; -.
DR PhylomeDB; P82094; -.
DR TreeFam; TF329420; -.
DR PathwayCommons; P82094; -.
DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR SignaLink; P82094; -.
DR BioGRID-ORCS; 7110; 9 hits in 1081 CRISPR screens.
DR ChiTaRS; TMF1; human.
DR GeneWiki; TMF1; -.
DR GenomeRNAi; 7110; -.
DR Pharos; P82094; Tbio.
DR PRO; PR:P82094; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P82094; protein.
DR Bgee; ENSG00000144747; Expressed in calcaneal tendon and 194 other tissues.
DR ExpressionAtlas; P82094; baseline and differential.
DR Genevisible; P82094; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0050681; F:nuclear androgen receptor binding; IPI:ARUK-UCL.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IDA:ARUK-UCL.
DR GO; GO:0001675; P:acrosome assembly; IEA:Ensembl.
DR GO; GO:0030521; P:androgen receptor signaling pathway; IDA:ARUK-UCL.
DR GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
DR GO; GO:1904019; P:epithelial cell apoptotic process; IEA:Ensembl.
DR GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
DR GO; GO:0033327; P:Leydig cell differentiation; IEA:Ensembl.
DR GO; GO:0032275; P:luteinizing hormone secretion; IEA:Ensembl.
DR GO; GO:1904036; P:negative regulation of epithelial cell apoptotic process; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0001819; P:positive regulation of cytokine production; IEA:Ensembl.
DR GO; GO:2000845; P:positive regulation of testosterone secretion; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; ISS:UniProtKB.
DR GO; GO:0007289; P:spermatid nucleus differentiation; IEA:Ensembl.
DR InterPro; IPR022092; TMF_DNA-bd.
DR InterPro; IPR022091; TMF_TATA-bd.
DR Pfam; PF12329; TMF_DNA_bd; 1.
DR Pfam; PF12325; TMF_TATA_bd; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; DNA-binding; Golgi apparatus;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..1093
FT /note="TATA element modulatory factor"
FT /id="PRO_0000072589"
FT REGION 38..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..342
FT /note="Interaction with Elongin BC complex"
FT REGION 919..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 439..922
FT /evidence="ECO:0000255"
FT COILED 984..1092
FT /evidence="ECO:0000255"
FT COMPBIAS 53..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..939
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B9EKI3"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B9EKI3"
FT MOD_RES 542
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 925
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 928
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B9EKI3"
FT MOD_RES 929
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:B9EKI3"
FT MOD_RES 933
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 449
FT /note="K -> KVTL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037411"
FT VARIANT 430
FT /note="Q -> E (in dbSNP:rs35447207)"
FT /id="VAR_051439"
FT VARIANT 448
FT /note="C -> Y (in dbSNP:rs34428015)"
FT /id="VAR_051440"
FT VARIANT 682
FT /note="Q -> R (in dbSNP:rs3736422)"
FT /id="VAR_051441"
FT VARIANT 798
FT /note="D -> H (in dbSNP:rs1532918)"
FT /id="VAR_024284"
FT MUTAGEN 333..335
FT /note="SLD->AAA: Strongly reduced the ubiquitination
FT directing activity of the protein."
FT /evidence="ECO:0000269|PubMed:15467733"
SQ SEQUENCE 1093 AA; 122842 MW; 566BBE3EC36EF11C CRC64;
MSWFNASQLS SFAKQALSQA QKSIDRVLDI QEEEPSIWAE TIPYGEPGIS SPVSGGWDTS
TWGLKSNTEP QSPPIASPKA ITKPVRRTVV DESENFFSAF LSPTDVQTIQ KSPVVSKPPA
KSQRPEEEVK SSLHESLHIG QSRTPETTES QVKDSSLCVS GETLAAGTSS PKTEGKHEET
VNKESDMKVP TVSLKVSESV IDVKTTMESI SNTSTQSLTA ETKDIALEPK EQKHEDRQSN
TPSPPVSTFS SGTSTTSDIE VLDHESVISE SSASSRQETT DSKSSLHLMQ TSFQLLSASA
CPEYNRLDDF QKLTESCCSS DAFERIDSFS VQSLDSRSVS EINSDDELSG KGYALVPIIV
NSSTPKSKTV ESAEGKSEEV NETLVIPTEE AEMEESGRSA TPVNCEQPDI LVSSTPINEG
QTVLDKVAEQ CEPAESQPEA LSEKEDVCKT VEFLNEKLEK REAQLLSLSK EKALLEEAFD
NLKDEMFRVK EESSSISSLK DEFTQRIAEA EKKVQLACKE RDAAKKEIKN IKEELATRLN
SSETADLLKE KDEQIRGLME EGEKLSKQQL HNSNIIKKLR AKDKENENMV AKLNKKVKEL
EEELQHLKQV LDGKEEVEKQ HRENIKKLNS MVERQEKDLG RLQVDMDELE EKNRSIQAAL
DSAYKELTDL HKANAAKDSE AQEAALSREM KAKEELSAAL EKAQEEARQQ QETLAIQVGD
LRLALQRTEQ AAARKEDYLR HEIGELQQRL QEAENRNQEL SQSVSSTTRP LLRQIENLQA
TLGSQTSSWE KLEKNLSDRL GESQTLLAAA VERERAATEE LLANKIQMSS MESQNSLLRQ
ENSRFQAQLE SEKNRLCKLE DENNRYQVEL ENLKDEYVRT LEETRKEKTL LNSQLEMERM
KVEQERKKAI FTQETIKEKE RKPFSVSSTP TMSRSSSISG VDMAGLQTSF LSQDESHDHS
FGPMPISANG SNLYDAVRMG AGSSIIENLQ SQLKLREGEI THLQLEIGNL EKTRSIMAEE
LVKLTNQNDE LEEKVKEIPK LRTQLRDLDQ RYNTILQMYG EKAEEAEELR LDLEDVKNMY
KTQIDELLRQ SLS
