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   27-MAR-2024, entry version 173.
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; 82.
DR   DIP; DIP-5933N; -.
DR   IntAct; P82094; 27.
DR   MINT; P82094; -.
DR   STRING; 9606.ENSP00000494067; -.
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; 9606-ENSP00000381567; -.
DR   PeptideAtlas; P82094; -.
DR   ProteomicsDB; 57702; -. [P82094-1]
DR   ProteomicsDB; 57703; -. [P82094-2]
DR   Pumba; P82094; -.
DR   Antibodypedia; 1796; 122 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   AGR; HGNC:11870; -.
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; EEMHGYI; -.
DR   OrthoDB; 3717503at2759; -.
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 1159 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 196 other cell types or tissues.
DR   ExpressionAtlas; P82094; baseline and differential.
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   PANTHER; PTHR46515:SF1; TATA ELEMENT MODULATORY FACTOR; 1.
DR   PANTHER; PTHR46515; TATA ELEMENT MODULATORY FACTOR TMF1; 1.
DR   Pfam; PF12329; TMF_DNA_bd; 1.
DR   Pfam; PF12325; TMF_TATA_bd; 1.
DR   Genevisible; P82094; HS.
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
//