ZFYV9_HUMAN
ID ZFYV9_HUMAN Reviewed; 1425 AA.
AC O95405; Q5T0F6; Q5T0F7; Q9UNE1; Q9Y5R7;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Zinc finger FYVE domain-containing protein 9;
DE AltName: Full=Mothers against decapentaplegic homolog-interacting protein;
DE Short=Madh-interacting protein;
DE AltName: Full=Novel serine protease;
DE Short=NSP;
DE AltName: Full=Receptor activation anchor;
DE Short=hSARA;
DE AltName: Full=Smad anchor for receptor activation;
GN Name=ZFYVE9; Synonyms=MADHIP, SARA, SMADIP;
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), INTERACTION WITH SMAD2; SMAD3;
RP TGFBR1 AND TGFBR2, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9865696; DOI=10.1016/s0092-8674(00)81701-8;
RA Tsukazaki T., Chiang T.A., Davison A.F., Attisano L., Wrana J.L.;
RT "SARA, a FYVE domain protein that recruits Smad2 to the TGFbeta receptor.";
RL Cell 95:779-791(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Fetal brain;
RX PubMed=9582421; DOI=10.1016/s0169-328x(97)00366-5;
RA Meckelein B., Marshall D.C.L., Conn K.J., Pietropaolo M., Van Nostrand W.,
RA Abraham C.R.;
RT "Identification of a novel serine protease-like molecule in human brain.";
RL Brain Res. Mol. Brain Res. 55:181-197(1998).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=11877415; DOI=10.1074/jbc.m107983200;
RA Panopoulou E., Gillooly D.J., Wrana J.L., Zerial M., Stenmark H.,
RA Murphy C., Fotsis T.;
RT "Early endosomal regulation of Smad-dependent signaling in endothelial
RT cells.";
RL J. Biol. Chem. 277:18046-18052(2002).
RN [7]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PML; SMAD2 AND SMAD3.
RX PubMed=15356634; DOI=10.1038/nature02783;
RA Lin H.K., Bergmann S., Pandolfi P.P.;
RT "Cytoplasmic PML function in TGF-beta signalling.";
RL Nature 431:205-211(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668, AND IDENTIFICATION BY
RP 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).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 771-811 IN COMPLEX WITH SMAD2, AND
RP MUTAGENESIS.
RX PubMed=10615055; DOI=10.1126/science.287.5450.92;
RA Wu G., Chen Y.-G., Ozdamar B., Gyuricza C.A., Chong P.A., Wrana J.L.,
RA Massague J., Shi Y.;
RT "Structural basis of Smad2 recognition by the Smad anchor for receptor
RT activation.";
RL Science 287:92-97(2000).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.74 ANGSTROMS) OF 773-810 IN COMPLEX WITH SMAD3.
RX PubMed=12154125; DOI=10.1101/gad.1002002;
RA Qin B.Y., Lam S.S., Correia J.J., Lin K.;
RT "Smad3 allostery links TGF-beta receptor kinase activation to
RT transcriptional control.";
RL Genes Dev. 16:1950-1963(2002).
CC -!- FUNCTION: Early endosomal protein that functions to recruit SMAD2/SMAD3
CC to intracellular membranes and to the TGF-beta receptor. Plays a
CC significant role in TGF-mediated signaling by regulating the
CC subcellular location of SMAD2 and SMAD3 and modulating the
CC transcriptional activity of the SMAD3/SMAD4 complex. Possibly
CC associated with TGF-beta receptor internalization.
CC {ECO:0000269|PubMed:15356634, ECO:0000269|PubMed:9865696}.
CC -!- SUBUNIT: Interacts (via the SBD region) with SMAD2; the interaction
CC recruits SMAD2 to the TGF-beta receptor and is disrupted by
CC phosphorylation of SMAD2 upon TGF-beta receptor activation. Interacts
CC with SMAD3. Interacts with TGFBR1 and TGFBR2; the interaction recruits
CC SMAD2 to the TGF-beta receptor. Interacts with PML.
CC {ECO:0000269|PubMed:10615055, ECO:0000269|PubMed:12154125,
CC ECO:0000269|PubMed:15356634, ECO:0000269|PubMed:9865696}.
CC -!- INTERACTION:
CC O95405; Q9Y561: LRP12; NbExp=2; IntAct=EBI-296817, EBI-296693;
CC O95405; P62136: PPP1CA; NbExp=3; IntAct=EBI-296817, EBI-357253;
CC O95405; P36873: PPP1CC; NbExp=5; IntAct=EBI-296817, EBI-356283;
CC O95405; P08100: RHO; NbExp=2; IntAct=EBI-296817, EBI-1394177;
CC O95405; Q15796: SMAD2; NbExp=6; IntAct=EBI-296817, EBI-1040141;
CC O95405; P84022: SMAD3; NbExp=5; IntAct=EBI-296817, EBI-347161;
CC O95405; Q13277: STX3; NbExp=3; IntAct=EBI-296817, EBI-1394295;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Early endosome membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O95405-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95405-2; Sequence=VSP_004315;
CC Name=3;
CC IsoId=O95405-3; Sequence=VSP_004316, VSP_004317;
CC -!- TISSUE SPECIFICITY: Ubiquitous. In the brain found primarily in the
CC cerebrovascular smooth muscle cells and reactive astrocytes.
CC -!- DOMAIN: The SMAD binding domain (SBD) interacts with the MH2 domains of
CC SMAD2 or SMAD3.
CC -!- DOMAIN: The FYVE-type zinc finger is necessary and sufficient for its
CC localization into early endosomes and mediates the association with
CC PI3P.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC99462.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAD31694.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF104304; AAC99462.1; ALT_INIT; mRNA.
DR EMBL; AF130419; AAD31694.1; ALT_FRAME; mRNA.
DR EMBL; AF130420; AAD31695.1; -; mRNA.
DR EMBL; AC105754; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL513218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06790.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06791.1; -; Genomic_DNA.
DR EMBL; BC032680; AAH32680.1; -; mRNA.
DR CCDS; CCDS563.1; -. [O95405-1]
DR CCDS; CCDS564.1; -. [O95405-2]
DR RefSeq; NP_004790.2; NM_004799.3. [O95405-1]
DR RefSeq; NP_015563.2; NM_007324.3. [O95405-2]
DR RefSeq; XP_011540739.1; XM_011542437.2. [O95405-1]
DR PDB; 1DEV; X-ray; 2.20 A; B/D=771-811.
DR PDB; 1MK2; X-ray; 2.74 A; B=773-810.
DR PDB; 4BKW; X-ray; 2.53 A; A=895-1425.
DR PDB; 5MJY; X-ray; 2.25 A; E/F=1-22.
DR PDBsum; 1DEV; -.
DR PDBsum; 1MK2; -.
DR PDBsum; 4BKW; -.
DR PDBsum; 5MJY; -.
DR AlphaFoldDB; O95405; -.
DR SMR; O95405; -.
DR BioGRID; 114773; 88.
DR CORUM; O95405; -.
DR IntAct; O95405; 43.
DR MINT; O95405; -.
DR STRING; 9606.ENSP00000287727; -.
DR GlyGen; O95405; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95405; -.
DR PhosphoSitePlus; O95405; -.
DR BioMuta; ZFYVE9; -.
DR EPD; O95405; -.
DR jPOST; O95405; -.
DR MassIVE; O95405; -.
DR MaxQB; O95405; -.
DR PaxDb; O95405; -.
DR PeptideAtlas; O95405; -.
DR PRIDE; O95405; -.
DR ProteomicsDB; 50856; -. [O95405-1]
DR ProteomicsDB; 50857; -. [O95405-2]
DR ProteomicsDB; 50858; -. [O95405-3]
DR Antibodypedia; 32995; 121 antibodies from 25 providers.
DR DNASU; 9372; -.
DR Ensembl; ENST00000287727.8; ENSP00000287727.3; ENSG00000157077.16. [O95405-1]
DR Ensembl; ENST00000357206.6; ENSP00000349737.2; ENSG00000157077.16. [O95405-2]
DR Ensembl; ENST00000371591.2; ENSP00000360647.1; ENSG00000157077.16. [O95405-1]
DR GeneID; 9372; -.
DR KEGG; hsa:9372; -.
DR MANE-Select; ENST00000287727.8; ENSP00000287727.3; NM_004799.4; NP_004790.2.
DR UCSC; uc001cto.5; human. [O95405-1]
DR CTD; 9372; -.
DR DisGeNET; 9372; -.
DR GeneCards; ZFYVE9; -.
DR HGNC; HGNC:6775; ZFYVE9.
DR HPA; ENSG00000157077; Low tissue specificity.
DR MIM; 603755; gene.
DR neXtProt; NX_O95405; -.
DR OpenTargets; ENSG00000157077; -.
DR PharmGKB; PA30532; -.
DR VEuPathDB; HostDB:ENSG00000157077; -.
DR eggNOG; KOG1841; Eukaryota.
DR GeneTree; ENSGT00940000154290; -.
DR HOGENOM; CLU_004326_1_0_1; -.
DR InParanoid; O95405; -.
DR OMA; GLTETCQ; -.
DR OrthoDB; 278124at2759; -.
DR PhylomeDB; O95405; -.
DR TreeFam; TF324904; -.
DR PathwayCommons; O95405; -.
DR Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling. [O95405-1]
DR Reactome; R-HSA-2173789; TGF-beta receptor signaling activates SMADs. [O95405-1]
DR Reactome; R-HSA-3304356; SMAD2/3 Phosphorylation Motif Mutants in Cancer. [O95405-1]
DR Reactome; R-HSA-3656532; TGFBR1 KD Mutants in Cancer. [O95405-1]
DR SignaLink; O95405; -.
DR SIGNOR; O95405; -.
DR BioGRID-ORCS; 9372; 15 hits in 1085 CRISPR screens.
DR ChiTaRS; ZFYVE9; human.
DR EvolutionaryTrace; O95405; -.
DR GeneWiki; Zinc_finger_FYVE_domain-containing_protein_9; -.
DR GenomeRNAi; 9372; -.
DR Pharos; O95405; Tbio.
DR PRO; PR:O95405; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O95405; protein.
DR Bgee; ENSG00000157077; Expressed in calcaneal tendon and 161 other tissues.
DR Genevisible; O95405; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005769; C:early endosome; NAS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0006897; P:endocytosis; NAS:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 4.10.720.10; -; 1.
DR IDEAL; IID00112; -.
DR InterPro; IPR022557; DUF3480.
DR InterPro; IPR035438; SARA/endofin.
DR InterPro; IPR024608; SARA_Smad-bd.
DR InterPro; IPR037145; SARA_Smad-bd_sf.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF11979; DUF3480; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF11409; SARA; 1.
DR PIRSF; PIRSF037289; SARA/endofin; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Endosome; Membrane;
KW Metal-binding; Phosphoprotein; Receptor; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..1425
FT /note="Zinc finger FYVE domain-containing protein 9"
FT /id="PRO_0000098715"
FT ZN_FING 699..758
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 201..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..823
FT /note="SBD"
FT COMPBIAS 204..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 705
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 708
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 721
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 724
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 729
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 732
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 750
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 753
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 760..818
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9582421"
FT /id="VSP_004315"
FT VAR_SEQ 760..762
FT /note="AQA -> GKY (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9582421"
FT /id="VSP_004316"
FT VAR_SEQ 763..1425
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9582421"
FT /id="VSP_004317"
FT VARIANT 287
FT /note="Y -> C (in dbSNP:rs9803965)"
FT /id="VAR_052985"
FT VARIANT 414
FT /note="Q -> P (in dbSNP:rs3790525)"
FT /id="VAR_052986"
FT VARIANT 639
FT /note="I -> V (in dbSNP:rs11809887)"
FT /id="VAR_052987"
FT MUTAGEN 782
FT /note="Y->A: Diminishes complex formation with SMAD2."
FT /evidence="ECO:0000269|PubMed:10615055"
FT MUTAGEN 782
FT /note="Y->E: Diminishes complex formation with SMAD2."
FT /evidence="ECO:0000269|PubMed:10615055"
FT MUTAGEN 783
FT /note="C->A: Diminishes complex formation with SMAD2."
FT /evidence="ECO:0000269|PubMed:10615055"
FT MUTAGEN 783
FT /note="C->E: Diminishes complex formation with SMAD2."
FT /evidence="ECO:0000269|PubMed:10615055"
FT MUTAGEN 788
FT /note="P->A: Diminishes complex formation with SMAD2."
FT /evidence="ECO:0000269|PubMed:10615055"
FT MUTAGEN 788
FT /note="P->E: Diminishes complex formation with SMAD2."
FT /evidence="ECO:0000269|PubMed:10615055"
FT MUTAGEN 790
FT /note="Q->A: No effect on complex formation with SMAD2."
FT /evidence="ECO:0000269|PubMed:10615055"
FT MUTAGEN 793
FT /note="Q->A: No effect on complex formation with SMAD2."
FT /evidence="ECO:0000269|PubMed:10615055"
FT MUTAGEN 805
FT /note="V->A: Diminishes complex formation with SMAD2."
FT /evidence="ECO:0000269|PubMed:10615055"
FT MUTAGEN 805
FT /note="V->E: Diminishes complex formation with SMAD2."
FT /evidence="ECO:0000269|PubMed:10615055"
FT HELIX 4..20
FT /evidence="ECO:0007829|PDB:5MJY"
FT HELIX 779..781
FT /evidence="ECO:0007829|PDB:1DEV"
FT HELIX 788..792
FT /evidence="ECO:0007829|PDB:1DEV"
FT TURN 793..795
FT /evidence="ECO:0007829|PDB:1DEV"
FT STRAND 797..800
FT /evidence="ECO:0007829|PDB:1MK2"
FT STRAND 804..807
FT /evidence="ECO:0007829|PDB:1DEV"
FT STRAND 901..903
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 907..909
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 918..922
FT /evidence="ECO:0007829|PDB:4BKW"
FT HELIX 925..932
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 940..945
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 948..957
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 960..970
FT /evidence="ECO:0007829|PDB:4BKW"
FT HELIX 971..973
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 977..983
FT /evidence="ECO:0007829|PDB:4BKW"
FT HELIX 994..1007
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 1017..1019
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 1030..1036
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 1039..1041
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 1050..1060
FT /evidence="ECO:0007829|PDB:4BKW"
FT TURN 1061..1063
FT /evidence="ECO:0007829|PDB:4BKW"
FT HELIX 1064..1069
FT /evidence="ECO:0007829|PDB:4BKW"
FT HELIX 1071..1082
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 1089..1091
FT /evidence="ECO:0007829|PDB:4BKW"
FT HELIX 1106..1109
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 1113..1115
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 1127..1131
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 1134..1140
FT /evidence="ECO:0007829|PDB:4BKW"
FT HELIX 1141..1143
FT /evidence="ECO:0007829|PDB:4BKW"
FT HELIX 1144..1152
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 1156..1162
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 1170..1177
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 1183..1192
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 1196..1199
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 1201..1207
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 1218..1222
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 1225..1229
FT /evidence="ECO:0007829|PDB:4BKW"
FT HELIX 1232..1243
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 1248..1250
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 1263..1270
FT /evidence="ECO:0007829|PDB:4BKW"
FT TURN 1282..1284
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 1291..1295
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 1302..1304
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 1307..1316
FT /evidence="ECO:0007829|PDB:4BKW"
FT HELIX 1334..1347
FT /evidence="ECO:0007829|PDB:4BKW"
FT HELIX 1348..1350
FT /evidence="ECO:0007829|PDB:4BKW"
FT HELIX 1351..1356
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 1361..1368
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 1373..1379
FT /evidence="ECO:0007829|PDB:4BKW"
FT HELIX 1386..1388
FT /evidence="ECO:0007829|PDB:4BKW"
FT HELIX 1389..1400
FT /evidence="ECO:0007829|PDB:4BKW"
FT STRAND 1413..1422
FT /evidence="ECO:0007829|PDB:4BKW"
SQ SEQUENCE 1425 AA; 156403 MW; ADE5CB530C1272C6 CRC64;
MENYFQAEAY NLDKVLDEFE QNEDETVSST LLDTKWNKIL DPPSHRLSFN PTLASVNESA
VSNESQPQLK VFSLAHSAPL TTEEEDHCAN GQDCNLNPEI ATMWIDENAV AEDQLIKRNY
SWDDQCSAVE VGEKKCGNLA CLPDEKNVLV VAVMHNCDKR TLQNDLQDCN NYNSQSLMDA
FSCSLDNENR QTDQFSFSIN ESTEKDMNSE KQMDPLNRPK TEGRSVNHLC PTSSDSLASV
CSPSQLKDDG SIGRDPSMSA ITSLTVDSVI SSQGTDGCPA VKKQENYIPD EDLTGKISSP
RTDLGSPNSF SHMSEGILMK KEPAEESTTE ESLRSGLPLL LKPDMPNGSG RNNDCERCSD
CLVPNEVRAD ENEGYEHEET LGTTEFLNMT EHFSESQDMT NWKLTKLNEM NDSQVNEEKE
KFLQISQPED TNGDSGGQCV GLADAGLDLK GTCISESEEC DFSTVIDTPA ANYLSNGCDS
YGMQDPGVSF VPKTLPSKED SVTEEKEIEE SKSECYSNIY EQRGNEATEG SGLLLNSTGD
LMKKNYLHNF CSQVPSVLGQ SSPKVVASLP SISVPFGGAR PKQPSNLKLQ IPKPLSDHLQ
NDFPANSGNN TKNKNDILGK AKLGENSATN VCSPSLGNIS NVDTNGEHLE SYEAEISTRP
CLALAPDSPD NDLRAGQFGI SARKPFTTLG EVAPVWVPDS QAPNCMKCEA RFTFTKRRHH
CRACGKVFCA SCCSLKCKLL YMDRKEARVC VICHSVLMNA QAWENMMSAS SQSPNPNNPA
EYCSTIPPLQ QAQASGALSS PPPTVMVPVG VLKHPGAEVA QPREQRRVWF ADGILPNGEV
ADAAKLTMNG TSSAGTLAVS HDPVKPVTTS PLPAETDICL FSGSITQVGS PVGSAMNLIP
EDGLPPILIS TGVKGDYAVE EKPSQISVMQ QLEDGGPDPL VFVLNANLLS MVKIVNYVNR
KCWCFTTKGM HAVGQSEIVI LLQCLPDEKC LPKDIFNHFV QLYRDALAGN VVSNLGHSFF
SQSFLGSKEH GGFLYVTSTY QSLQDLVLPT PPYLFGILIQ KWETPWAKVF PIRLMLRLGA
EYRLYPCPLF SVRFRKPLFG ETGHTIMNLL ADFRNYQYTL PVVQGLVVDM EVRKTSIKIP
SNRYNEMMKA MNKSNEHVLA GGACFNEKAD SHLVCVQNDD GNYQTQAISI HNQPRKVTGA
SFFVFSGALK SSSGYLAKSS IVEDGVMVQI TAENMDSLRQ ALREMKDFTI TCGKADAEEP
QEHIHIQWVD DDKNVSKGVV SPIDGKSMET ITNVKIFHGS EYKANGKVIR WTEVFFLEND
DQHNCLSDPA DHSRLTEHVA KAFCLALCPH LKLLKEDGMT KLGLRVTLDS DQVGYQAGSN
GQPLPSQYMN DLDSALVPVI HGGACQLSEG PVVMELIFYI LENIV
