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Zinc finger FYVE domain-containing protein 9 (Mothers against decapentaplegic homolog-interacting protein) (Madh-interacting protein) (Novel serine protease) (NSP) (Receptor activation anchor) (hSARA) (Smad anchor for receptor activation)

 ZFYV9_HUMAN             Reviewed;        1425 AA.
O95405; Q5T0F6; Q5T0F7; Q9UNE1; Q9Y5R7;
14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
14-AUG-2001, sequence version 2.
02-DEC-2020, entry version 186.
RecName: Full=Zinc finger FYVE domain-containing protein 9;
AltName: Full=Mothers against decapentaplegic homolog-interacting protein;
Short=Madh-interacting protein;
AltName: Full=Novel serine protease;
Short=NSP;
AltName: Full=Receptor activation anchor;
Short=hSARA;
AltName: Full=Smad anchor for receptor activation;
Name=ZFYVE9; Synonyms=MADHIP, SARA, SMADIP;
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 1), INTERACTION WITH SMAD2; SMAD3;
TGFBR1 AND TGFBR2, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=9865696; DOI=10.1016/s0092-8674(00)81701-8;
Tsukazaki T., Chiang T.A., Davison A.F., Attisano L., Wrana J.L.;
"SARA, a FYVE domain protein that recruits Smad2 to the TGFbeta receptor.";
Cell 95:779-791(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
TISSUE=Fetal brain;
PubMed=9582421; DOI=10.1016/s0169-328x(97)00366-5;
Meckelein B., Marshall D.C.L., Conn K.J., Pietropaolo M., Van Nostrand W.,
Abraham C.R.;
"Identification of a novel serine protease-like molecule in human brain.";
Brain Res. Mol. Brain Res. 55:181-197(1998).
[3]
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).
[4]
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
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).
[6]
SUBCELLULAR LOCATION.
PubMed=11877415; DOI=10.1074/jbc.m107983200;
Panopoulou E., Gillooly D.J., Wrana J.L., Zerial M., Stenmark H.,
Murphy C., Fotsis T.;
"Early endosomal regulation of Smad-dependent signaling in endothelial
cells.";
J. Biol. Chem. 277:18046-18052(2002).
[7]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PML; SMAD2 AND SMAD3.
PubMed=15356634; DOI=10.1038/nature02783;
Lin H.K., Bergmann S., Pandolfi P.P.;
"Cytoplasmic PML function in TGF-beta signalling.";
Nature 431:205-211(2004).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[12]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 771-811 IN COMPLEX WITH SMAD2, AND
MUTAGENESIS.
PubMed=10615055; DOI=10.1126/science.287.5450.92;
Wu G., Chen Y.-G., Ozdamar B., Gyuricza C.A., Chong P.A., Wrana J.L.,
Massague J., Shi Y.;
"Structural basis of Smad2 recognition by the Smad anchor for receptor
activation.";
Science 287:92-97(2000).
[13]
X-RAY CRYSTALLOGRAPHY (2.74 ANGSTROMS) OF 773-810 IN COMPLEX WITH SMAD3.
PubMed=12154125; DOI=10.1101/gad.1002002;
Qin B.Y., Lam S.S., Correia J.J., Lin K.;
"Smad3 allostery links TGF-beta receptor kinase activation to
transcriptional control.";
Genes Dev. 16:1950-1963(2002).
-!- FUNCTION: Early endosomal protein that functions to recruit SMAD2/SMAD3
to intracellular membranes and to the TGF-beta receptor. Plays a
significant role in TGF-mediated signaling by regulating the
subcellular location of SMAD2 and SMAD3 and modulating the
transcriptional activity of the SMAD3/SMAD4 complex. Possibly
associated with TGF-beta receptor internalization.
{ECO:0000269|PubMed:15356634, ECO:0000269|PubMed:9865696}.
-!- SUBUNIT: Interacts (via the SBD region) with SMAD2; the interaction
recruits SMAD2 to the TGF-beta receptor and is disrupted by
phosphorylation of SMAD2 upon TGF-beta receptor activation. Interacts
with SMAD3. Interacts with TGFBR1 and TGFBR2; the interaction recruits
SMAD2 to the TGF-beta receptor. Interacts with PML.
{ECO:0000269|PubMed:10615055, ECO:0000269|PubMed:12154125,
ECO:0000269|PubMed:15356634, ECO:0000269|PubMed:9865696}.
-!- INTERACTION:
O95405; Q9Y561: LRP12; NbExp=2; IntAct=EBI-296817, EBI-296693;
O95405; P62136: PPP1CA; NbExp=3; IntAct=EBI-296817, EBI-357253;
O95405; P36873: PPP1CC; NbExp=5; IntAct=EBI-296817, EBI-356283;
O95405; P08100: RHO; NbExp=2; IntAct=EBI-296817, EBI-1394177;
O95405; Q15796: SMAD2; NbExp=2; IntAct=EBI-296817, EBI-1040141;
O95405; P84022: SMAD3; NbExp=5; IntAct=EBI-296817, EBI-347161;
O95405; Q13277: STX3; NbExp=3; IntAct=EBI-296817, EBI-1394295;
-!- SUBCELLULAR LOCATION: Cytoplasm. Early endosome membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O95405-1; Sequence=Displayed;
Name=2;
IsoId=O95405-2; Sequence=VSP_004315;
Name=3;
IsoId=O95405-3; Sequence=VSP_004316, VSP_004317;
-!- TISSUE SPECIFICITY: Ubiquitous. In the brain found primarily in the
cerebrovascular smooth muscle cells and reactive astrocytes.
-!- DOMAIN: The SMAD binding domain (SBD) interacts with the MH2 domains of
SMAD2 or SMAD3.
-!- DOMAIN: The FYVE-type zinc finger is necessary and sufficient for its
localization into early endosomes and mediates the association with
PI3P.
-!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
premature stop codon in the mRNA, leading to nonsense-mediated mRNA
decay. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC99462.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
Sequence=AAD31694.1; Type=Frameshift; Evidence={ECO:0000305};
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EMBL; AF104304; AAC99462.1; ALT_INIT; mRNA.
EMBL; AF130419; AAD31694.1; ALT_FRAME; mRNA.
EMBL; AF130420; AAD31695.1; -; mRNA.
EMBL; AC105754; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL513218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX06790.1; -; Genomic_DNA.
EMBL; CH471059; EAX06791.1; -; Genomic_DNA.
EMBL; BC032680; AAH32680.1; -; mRNA.
CCDS; CCDS563.1; -. [O95405-1]
CCDS; CCDS564.1; -. [O95405-2]
RefSeq; NP_004790.2; NM_004799.3. [O95405-1]
RefSeq; NP_015563.2; NM_007324.3. [O95405-2]
RefSeq; XP_011540739.1; XM_011542437.2. [O95405-1]
PDB; 1DEV; X-ray; 2.20 A; B/D=771-811.
PDB; 1MK2; X-ray; 2.74 A; B=773-810.
PDB; 4BKW; X-ray; 2.53 A; A=895-1425.
PDB; 5MJY; X-ray; 2.25 A; E/F=1-22.
PDBsum; 1DEV; -.
PDBsum; 1MK2; -.
PDBsum; 4BKW; -.
PDBsum; 5MJY; -.
SMR; O95405; -.
BioGRID; 114773; 48.
CORUM; O95405; -.
IntAct; O95405; 42.
MINT; O95405; -.
STRING; 9606.ENSP00000287727; -.
iPTMnet; O95405; -.
PhosphoSitePlus; O95405; -.
BioMuta; ZFYVE9; -.
EPD; O95405; -.
jPOST; O95405; -.
MassIVE; O95405; -.
MaxQB; O95405; -.
PaxDb; O95405; -.
PeptideAtlas; O95405; -.
PRIDE; O95405; -.
ProteomicsDB; 50856; -. [O95405-1]
ProteomicsDB; 50857; -. [O95405-2]
ProteomicsDB; 50858; -. [O95405-3]
Antibodypedia; 32995; 104 antibodies.
DNASU; 9372; -.
Ensembl; ENST00000287727; ENSP00000287727; ENSG00000157077. [O95405-1]
Ensembl; ENST00000357206; ENSP00000349737; ENSG00000157077. [O95405-2]
Ensembl; ENST00000371591; ENSP00000360647; ENSG00000157077. [O95405-1]
GeneID; 9372; -.
KEGG; hsa:9372; -.
UCSC; uc001cto.5; human. [O95405-1]
CTD; 9372; -.
DisGeNET; 9372; -.
EuPathDB; HostDB:ENSG00000157077.14; -.
GeneCards; ZFYVE9; -.
HGNC; HGNC:6775; ZFYVE9.
HPA; ENSG00000157077; Low tissue specificity.
MIM; 603755; gene.
neXtProt; NX_O95405; -.
OpenTargets; ENSG00000157077; -.
PharmGKB; PA30532; -.
eggNOG; KOG1841; Eukaryota.
GeneTree; ENSGT00940000154290; -.
HOGENOM; CLU_004326_1_0_1; -.
InParanoid; O95405; -.
OMA; HIQWVED; -.
OrthoDB; 278124at2759; -.
PhylomeDB; O95405; -.
TreeFam; TF324904; -.
PathwayCommons; O95405; -.
Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling. [O95405-1]
Reactome; R-HSA-2173789; TGF-beta receptor signaling activates SMADs. [O95405-1]
Reactome; R-HSA-3304356; SMAD2/3 Phosphorylation Motif Mutants in Cancer. [O95405-1]
Reactome; R-HSA-3656532; TGFBR1 KD Mutants in Cancer. [O95405-1]
SignaLink; O95405; -.
SIGNOR; O95405; -.
BioGRID-ORCS; 9372; 6 hits in 850 CRISPR screens.
ChiTaRS; ZFYVE9; human.
EvolutionaryTrace; O95405; -.
GeneWiki; Zinc_finger_FYVE_domain-containing_protein_9; -.
GenomeRNAi; 9372; -.
Pharos; O95405; Tbio.
PRO; PR:O95405; -.
Proteomes; UP000005640; Chromosome 1.
RNAct; O95405; protein.
Bgee; ENSG00000157077; Expressed in frontal cortex and 204 other tissues.
Genevisible; O95405; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005769; C:early endosome; IBA:GO_Central.
GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
GO; GO:0005545; F:1-phosphatidylinositol binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
GO; GO:0006897; P:endocytosis; NAS:UniProtKB.
GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
DisProt; DP00141; -.
Gene3D; 3.30.40.10; -; 1.
Gene3D; 4.10.720.10; -; 1.
IDEAL; IID00112; -.
InterPro; IPR022557; DUF3480.
InterPro; IPR035438; SARA/endofin.
InterPro; IPR024608; SARA_Smad-bd.
InterPro; IPR037145; SARA_Smad-bd_sf.
InterPro; IPR000306; Znf_FYVE.
InterPro; IPR017455; Znf_FYVE-rel.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF11979; DUF3480; 1.
Pfam; PF01363; FYVE; 1.
Pfam; PF11409; SARA; 1.
PIRSF; PIRSF037289; SARA/endofin; 1.
SMART; SM00064; FYVE; 1.
SUPFAM; SSF57903; SSF57903; 1.
PROSITE; PS50178; ZF_FYVE; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cytoplasm; Endosome; Membrane;
Metal-binding; Phosphoprotein; Polymorphism; Receptor; Reference proteome;
Zinc; Zinc-finger.
CHAIN 1..1425
/note="Zinc finger FYVE domain-containing protein 9"
/id="PRO_0000098715"
ZN_FING 699..758
/note="FYVE-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
REGION 767..823
/note="SBD"
MOD_RES 306
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 668
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:24275569"
VAR_SEQ 760..818
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:9582421"
/id="VSP_004315"
VAR_SEQ 760..762
/note="AQA -> GKY (in isoform 3)"
/evidence="ECO:0000303|PubMed:9582421"
/id="VSP_004316"
VAR_SEQ 763..1425
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:9582421"
/id="VSP_004317"
VARIANT 287
/note="Y -> C (in dbSNP:rs9803965)"
/id="VAR_052985"
VARIANT 414
/note="Q -> P (in dbSNP:rs3790525)"
/id="VAR_052986"
VARIANT 639
/note="I -> V (in dbSNP:rs11809887)"
/id="VAR_052987"
MUTAGEN 782
/note="Y->A: Diminishes complex formation with SMAD2."
/evidence="ECO:0000269|PubMed:10615055"
MUTAGEN 782
/note="Y->E: Diminishes complex formation with SMAD2."
/evidence="ECO:0000269|PubMed:10615055"
MUTAGEN 783
/note="C->A: Diminishes complex formation with SMAD2."
/evidence="ECO:0000269|PubMed:10615055"
MUTAGEN 783
/note="C->E: Diminishes complex formation with SMAD2."
/evidence="ECO:0000269|PubMed:10615055"
MUTAGEN 788
/note="P->A: Diminishes complex formation with SMAD2."
/evidence="ECO:0000269|PubMed:10615055"
MUTAGEN 788
/note="P->E: Diminishes complex formation with SMAD2."
/evidence="ECO:0000269|PubMed:10615055"
MUTAGEN 790
/note="Q->A: No effect on complex formation with SMAD2."
/evidence="ECO:0000269|PubMed:10615055"
MUTAGEN 793
/note="Q->A: No effect on complex formation with SMAD2."
/evidence="ECO:0000269|PubMed:10615055"
MUTAGEN 805
/note="V->A: Diminishes complex formation with SMAD2."
/evidence="ECO:0000269|PubMed:10615055"
MUTAGEN 805
/note="V->E: Diminishes complex formation with SMAD2."
/evidence="ECO:0000269|PubMed:10615055"
HELIX 4..20
/evidence="ECO:0000244|PDB:5MJY"
HELIX 779..781
/evidence="ECO:0000244|PDB:1DEV"
HELIX 788..792
/evidence="ECO:0000244|PDB:1DEV"
TURN 793..795
/evidence="ECO:0000244|PDB:1DEV"
STRAND 797..800
/evidence="ECO:0000244|PDB:1MK2"
STRAND 804..807
/evidence="ECO:0000244|PDB:1DEV"
STRAND 901..903
/evidence="ECO:0000244|PDB:4BKW"
STRAND 907..909
/evidence="ECO:0000244|PDB:4BKW"
STRAND 918..922
/evidence="ECO:0000244|PDB:4BKW"
HELIX 925..932
/evidence="ECO:0000244|PDB:4BKW"
STRAND 940..945
/evidence="ECO:0000244|PDB:4BKW"
STRAND 948..957
/evidence="ECO:0000244|PDB:4BKW"
STRAND 960..970
/evidence="ECO:0000244|PDB:4BKW"
HELIX 971..973
/evidence="ECO:0000244|PDB:4BKW"
STRAND 977..983
/evidence="ECO:0000244|PDB:4BKW"
HELIX 994..1007
/evidence="ECO:0000244|PDB:4BKW"
STRAND 1017..1019
/evidence="ECO:0000244|PDB:4BKW"
STRAND 1030..1036
/evidence="ECO:0000244|PDB:4BKW"
STRAND 1039..1041
/evidence="ECO:0000244|PDB:4BKW"
STRAND 1050..1060
/evidence="ECO:0000244|PDB:4BKW"
TURN 1061..1063
/evidence="ECO:0000244|PDB:4BKW"
HELIX 1064..1069
/evidence="ECO:0000244|PDB:4BKW"
HELIX 1071..1082
/evidence="ECO:0000244|PDB:4BKW"
STRAND 1089..1091
/evidence="ECO:0000244|PDB:4BKW"
HELIX 1106..1109
/evidence="ECO:0000244|PDB:4BKW"
STRAND 1113..1115
/evidence="ECO:0000244|PDB:4BKW"
STRAND 1127..1131
/evidence="ECO:0000244|PDB:4BKW"
STRAND 1134..1140
/evidence="ECO:0000244|PDB:4BKW"
HELIX 1141..1143
/evidence="ECO:0000244|PDB:4BKW"
HELIX 1144..1152
/evidence="ECO:0000244|PDB:4BKW"
STRAND 1156..1162
/evidence="ECO:0000244|PDB:4BKW"
STRAND 1170..1177
/evidence="ECO:0000244|PDB:4BKW"
STRAND 1183..1192
/evidence="ECO:0000244|PDB:4BKW"
STRAND 1196..1199
/evidence="ECO:0000244|PDB:4BKW"
STRAND 1201..1207
/evidence="ECO:0000244|PDB:4BKW"
STRAND 1218..1222
/evidence="ECO:0000244|PDB:4BKW"
STRAND 1225..1229
/evidence="ECO:0000244|PDB:4BKW"
HELIX 1232..1243
/evidence="ECO:0000244|PDB:4BKW"
STRAND 1248..1250
/evidence="ECO:0000244|PDB:4BKW"
STRAND 1263..1270
/evidence="ECO:0000244|PDB:4BKW"
TURN 1282..1284
/evidence="ECO:0000244|PDB:4BKW"
STRAND 1291..1295
/evidence="ECO:0000244|PDB:4BKW"
STRAND 1302..1304
/evidence="ECO:0000244|PDB:4BKW"
STRAND 1307..1316
/evidence="ECO:0000244|PDB:4BKW"
HELIX 1334..1347
/evidence="ECO:0000244|PDB:4BKW"
HELIX 1348..1350
/evidence="ECO:0000244|PDB:4BKW"
HELIX 1351..1356
/evidence="ECO:0000244|PDB:4BKW"
STRAND 1361..1368
/evidence="ECO:0000244|PDB:4BKW"
STRAND 1373..1379
/evidence="ECO:0000244|PDB:4BKW"
HELIX 1386..1388
/evidence="ECO:0000244|PDB:4BKW"
HELIX 1389..1400
/evidence="ECO:0000244|PDB:4BKW"
STRAND 1413..1422
/evidence="ECO:0000244|PDB:4BKW"
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


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EIAAB47151 Homo sapiens,hSARA,Human,Madh-interacting protein,MADHIP,Mothers against decapentaplegic homolog-interacting protein,Novel serine protease,NSP,Receptor activation anchor,SARA,Smad anchor for receptor
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EIAAB47224 Homo sapiens,Human,MCH-R1-interacting zinc finger protein,Melanin-concentrating hormone receptor 1-interacting zinc finger protein,MIZIP,Zinc finger MYND domain-containing protein 19,ZMYND19
EIAAB47225 MCH-R1-interacting zinc finger protein,Melanin-concentrating hormone receptor 1-interacting zinc finger protein,Mizip,Mouse,Mus musculus,Zinc finger MYND domain-containing protein 19,Zmynd19
EIAAB47226 MCH-R1-interacting zinc finger protein,Melanin-concentrating hormone receptor 1-interacting zinc finger protein,Mizip,Rat,Rattus norvegicus,Zinc finger MYND domain-containing protein 19,Zmynd19
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EIAAB47949 HNF-4a coactivator,Homo sapiens,Human,Thyroid hormone receptor interactor 3,Thyroid receptor-interacting protein 3,TR-interacting protein 3,TRIP3,TRIP-3,Zinc finger HIT domain-containing protein 3,ZNH
EIAAB47947 Mouse,Mus musculus,Thyroid hormone receptor interactor 3,Thyroid receptor-interacting protein 3,TR-interacting protein 3,Trip3,TRIP-3,Zinc finger HIT domain-containing protein 3,Znhit3
EIAAB31034 Androgen receptor-interacting protein 3,ARIP3,DAB2-interacting protein,DIP,E3 SUMO-protein ligase PIAS2,Homo sapiens,Human,Miz1,Msx-interacting zinc finger protein,PIAS2,PIAS-NY protein,PIASX,Protein
EIAAB31033 Androgen receptor-interacting protein 3,ARIP3,DAB2-interacting protein,DIP,E3 SUMO-protein ligase PIAS2,Miz1,Mouse,Msx-interacting zinc finger protein,Mus musculus,Pias2,Piasx,Protein inhibitor of act
EIAAB31032 Androgen receptor-interacting protein 3,ARIP3,DAB2-interacting protein,DIP,E3 SUMO-protein ligase PIAS2,Miz1,Msx-interacting-zinc finger protein,Pias2,Piasx,Protein inhibitor of activated STAT x,Prote
EIAAB47414 Androgen receptor N-terminal-interacting protein,Arnip,Chimp,CH-rich-interacting match with PLAG1,E3 ubiquitin-protein ligase Pirh2,Mouse,Mus musculus,Rchy1,RING finger and CHY zinc finger domain-cont
EIAAB47457 Early B-cell factor-associated zinc finger protein,Ebfaz,Kiaa0760,Mouse,Mus musculus,Nur12,Oaz,Olf1_EBF-associated zinc finger protein,Smad- and Olf-interacting zinc finger protein,Zfp423,Zinc finger
EIAAB46924 Homo sapiens,Human,SIZN1,Smad-interacting zinc finger protein 1,ZCCHC12,Zinc finger CCHC domain-containing protein 12
EIAAB46926 Mouse,Mus musculus,Sizn1,Smad-interacting zinc finger protein 1,Zcchc12,Zinc finger CCHC domain-containing protein 12
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EIAAB46826 FANCC-interacting protein,Fanconi anemia zinc finger protein,FAZF,Homo sapiens,Human,Testis zinc finger protein,TZFP,ZBTB32,Zinc finger and BTB domain-containing protein 32,Zinc finger protein 538,ZNF
EIAAB47456 Oaz,Olf1_EBF-associated zinc finger protein,Rat,Rattus norvegicus,rOAZ,Smad- and Olf-interacting zinc finger protein,Zfp423,Zinc finger protein 423,Znf423
EIAAB29989 Mouse,Mus musculus,PAX transactivation activation domain-interacting protein,PAX-interacting protein 1,Paxip1,Ptip
EIAAB29988 CAGF28,Homo sapiens,Human,PAX transactivation activation domain-interacting protein,PAX-interacting protein 1,PAXIP1,PAXIP1L,PTIP
Pathways :
WP2199: Seed Development
WP2272: Pathogenic Escherichia coli infection
WP2292: Chemokine signaling pathway
WP1689: Porphyrin and chlorophyll metabolism
WP1659: Glycine, serine and threonine metabolism
WP1657: Glycerolipid metabolism
WP1939: Unfolded Protein Response
WP1700: Selenoamino acid metabolism
WP1165: G Protein Signaling Pathways
WP232: G Protein Signaling Pathways
WP1663: Homologous recombination
WP35: G Protein Signaling Pathways
WP813: G Protein Signaling Pathways
WP1673: Naphthalene and anthracene degradation
WP210: Cytoplasmic Ribosomal Proteins
WP1049: G Protein Signaling Pathways
WP1531: Vitamin D synthesis
WP1888: Post-translational protein modification
WP2371: Parkinsons Disease Pathway
WP1678: Nucleotide excision repair
WP1613: 1,4-Dichlorobenzene degradation
WP1625: Base excision repair
WP1909: Signal regulatory protein (SIRP) family interactions
WP1690: Propanoate metabolism
WP1694: Pyrimidine metabolism

Related Genes :
[ZFYVE9 MADHIP SARA SMADIP] Zinc finger FYVE domain-containing protein 9 (Mothers against decapentaplegic homolog-interacting protein) (Madh-interacting protein) (Novel serine protease) (NSP) (Receptor activation anchor) (hSARA) (Smad anchor for receptor activation)
[SMAD2 MADH2 MADR2] Mothers against decapentaplegic homolog 2 (MAD homolog 2) (Mothers against DPP homolog 2) (JV18-1) (Mad-related protein 2) (hMAD-2) (SMAD family member 2) (SMAD 2) (Smad2) (hSMAD2)
[SMAD3 MADH3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (hMAD-3) (JV15-2) (SMAD family member 3) (SMAD 3) (Smad3) (hSMAD3)
[Smad4 Dpc4 Madh4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (Deletion target in pancreatic carcinoma 4 homolog) (SMAD family member 4) (SMAD 4) (Smad4)
[SMAD4 DPC4 MADH4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (Deletion target in pancreatic carcinoma 4) (SMAD family member 4) (SMAD 4) (Smad4) (hSMAD4)
[Smad3 Madh3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (mMad3) (SMAD family member 3) (SMAD 3) (Smad3)
[Smad1 Madh1 Madr1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (Dwarfin-A) (Dwf-A) (Mothers-against-DPP-related 1) (Mad-related protein 1) (mMad1) (SMAD family member 1) (SMAD 1) (Smad1)
[SMAD1 BSP1 MADH1 MADR1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (JV4-1) (Mad-related protein 1) (SMAD family member 1) (SMAD 1) (Smad1) (hSMAD1) (Transforming growth factor-beta-signaling protein 1) (BSP-1)
[Smad3 Madh3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (SMAD family member 3) (SMAD 3) (Smad3)
[Smad7 Madh7 Madh8] Mothers against decapentaplegic homolog 7 (MAD homolog 7) (Mothers against DPP homolog 7) (Mothers against decapentaplegic homolog 8) (MAD homolog 8) (Mothers against DPP homolog 8) (SMAD family member 7) (SMAD 7) (Smad7)
[SMAD7 MADH7 MADH8] Mothers against decapentaplegic homolog 7 (MAD homolog 7) (Mothers against DPP homolog 7) (Mothers against decapentaplegic homolog 8) (MAD homolog 8) (Mothers against DPP homolog 8) (SMAD family member 7) (SMAD 7) (Smad7) (hSMAD7)
[SMAD4 MADH4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (SMAD family member 4) (SMAD 4) (Smad4)
[Smad4 Madh4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (SMAD family member 4) (SMAD 4) (Smad4)
[SMAD6 MADH6] Mothers against decapentaplegic homolog 6 (MAD homolog 6) (Mothers against DPP homolog 6) (SMAD family member 6) (SMAD 6) (Smad6) (hSMAD6)
[SMAD3 MADH3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (SMAD family member 3) (SMAD 3) (Smad3)
[Smad1 Mad1 Madh1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (SMAD family member 1) (SMAD 1) (Smad1)
[Smad7 Madh7] Mothers against decapentaplegic homolog 7 (MAD homolog 7) (Mothers against DPP homolog 7) (SMAD family member 7) (SMAD 7) (Smad7)
[SMAD1] Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (SMAD family member 1) (SMAD 1) (Smad1)
[PIAS2 PIASX] E3 SUMO-protein ligase PIAS2 (EC 2.3.2.-) (Androgen receptor-interacting protein 3) (ARIP3) (DAB2-interacting protein) (DIP) (E3 SUMO-protein transferase PIAS2) (Msx-interacting zinc finger protein) (Miz1) (PIAS-NY protein) (Protein inhibitor of activated STAT x) (Protein inhibitor of activated STAT2)
[ZNF274 ZKSCAN19 SP2114] Neurotrophin receptor-interacting factor homolog (Zinc finger protein 274) (Zinc finger protein HFB101) (Zinc finger protein with KRAB and SCAN domains 19) (Zinc finger protein zfp2) (Zf2)
[Pias2 Miz1 Piasx] E3 SUMO-protein ligase PIAS2 (EC 2.3.2.-) (Androgen receptor-interacting protein 3) (ARIP3) (DAB2-interacting protein) (DIP) (E3 SUMO-protein transferase PIAS2) (Msx-interacting-zinc finger protein) (Protein inhibitor of activated STAT x) (Protein inhibitor of activated STAT2)
[RCHY1 ARNIP CHIMP PIRH2 RNF199 ZNF363] RING finger and CHY zinc finger domain-containing protein 1 (EC 2.3.2.27) (Androgen receptor N-terminal-interacting protein) (CH-rich-interacting match with PLAG1) (E3 ubiquitin-protein ligase Pirh2) (RING finger protein 199) (RING-type E3 ubiquitin transferase RCHY1) (Zinc finger protein 363) (p53-induced RING-H2 protein) (hPirh2)
[MED14 ARC150 CRSP2 CXorf4 DRIP150 EXLM1 RGR1 TRAP170] Mediator of RNA polymerase II transcription subunit 14 (Activator-recruited cofactor 150 kDa component) (ARC150) (Cofactor required for Sp1 transcriptional activation subunit 2) (CRSP complex subunit 2) (Mediator complex subunit 14) (RGR1 homolog) (hRGR1) (Thyroid hormone receptor-associated protein complex 170 kDa component) (Trap170) (Transcriptional coactivator CRSP150) (Vitamin D3 receptor-interacting protein complex 150 kDa component) (DRIP150)
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Host translation inhibitor nsp1 (Leader protein) (Non-structural protein 1) (nsp1); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.-) (PL2-PRO) (Papain-like protease) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.69) (Main protease) (Mpro) (Non-structural protein 5) (nsp5) (SARS coronavirus main proteinase); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Non-structural protein 12) (nsp12); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Non-structural protein 13) (nsp13); Proofreading exoribonuclease (ExoN) (EC 3.1.13.-) (Guanine-N7 methyltransferase) (Non-structural protein 14) (nsp14); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (Non-structural protein 15) (nsp15); 2'-O-methyltransferase (EC 2.1.1.-) (Non-structural protein 16) (nsp16)]
[] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Host translation inhibitor nsp1 (Leader protein) (Non-structural protein 1) (nsp1); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.-) (PL2-PRO) (Papain-like protease) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.69) (Main protease) (Mpro) (Non-structural protein 5) (nsp5) (SARS coronavirus main proteinase); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[RIPK1 RIP RIP1] Receptor-interacting serine/threonine-protein kinase 1 (EC 2.7.11.1) (Cell death protein RIP) (Receptor-interacting protein 1) (RIP-1)
[TNIP2 ABIN2 FLIP1] TNFAIP3-interacting protein 2 (A20-binding inhibitor of NF-kappa-B activation 2) (ABIN-2) (Fetal liver LKB1-interacting protein)
[MED23 ARC130 CRSP3 DRIP130 KIAA1216 SUR2] Mediator of RNA polymerase II transcription subunit 23 (Activator-recruited cofactor 130 kDa component) (ARC130) (Cofactor required for Sp1 transcriptional activation subunit 3) (CRSP complex subunit 3) (Mediator complex subunit 23) (Protein sur-2 homolog) (hSur-2) (Transcriptional coactivator CRSP130) (Vitamin D3 receptor-interacting protein complex 130 kDa component) (DRIP130)
[TRIM28 KAP1 RNF96 TIF1B] Transcription intermediary factor 1-beta (TIF1-beta) (E3 SUMO-protein ligase TRIM28) (EC 2.3.2.27) (KRAB-associated protein 1) (KAP-1) (KRAB-interacting protein 1) (KRIP-1) (Nuclear corepressor KAP-1) (RING finger protein 96) (RING-type E3 ubiquitin transferase TIF1-beta) (Tripartite motif-containing protein 28)
[Rbck1 Pkcbpb15 Rbck Ubce7ip3] RanBP-type and C3HC4-type zinc finger-containing protein 1 (EC 2.3.2.31) (Heme-oxidized IRP2 ubiquitin ligase 1 homolog) (HOIL-1) (Protein kinase C-binding protein beta-15) (RBCC protein interacting with PKC) (RING-type E3 ubiquitin transferase HOIL-1) (Ubiquitin-conjugating enzyme 7-interacting protein 3)

Bibliography :