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O95405

- ZFYV9_HUMAN

UniProt

O95405 - ZFYV9_HUMAN

Protein

Zinc finger FYVE domain-containing protein 9

Gene

ZFYVE9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (14 Aug 2001)
      Previous versions | rss
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    Functioni

    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.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri699 – 75860FYVE-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. 1-phosphatidylinositol binding Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. serine-type peptidase activity Source: UniProtKB

    GO - Biological processi

    1. endocytosis Source: UniProtKB
    2. negative regulation of transforming growth factor beta receptor signaling pathway Source: Reactome
    3. proteolysis Source: GOC
    4. SMAD protein complex assembly Source: UniProtKB
    5. SMAD protein import into nucleus Source: UniProtKB
    6. transforming growth factor beta receptor signaling pathway Source: UniProtKB

    Keywords - Molecular functioni

    Receptor

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_120727. Downregulation of TGF-beta receptor signaling.
    REACT_120850. TGF-beta receptor signaling activates SMADs.
    REACT_169103. SMAD2/3 Phosphorylation Motif Mutants in Cancer.
    REACT_169165. SMAD2/3 MH2 Domain Mutants in Cancer.
    REACT_169263. TGFBR1 KD Mutants in Cancer.
    SignaLinkiO95405.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Zinc finger FYVE domain-containing protein 9
    Alternative name(s):
    Mothers against decapentaplegic homolog-interacting protein
    Short name:
    Madh-interacting protein
    Novel serine protease
    Short name:
    NSP
    Receptor activation anchor
    Short name:
    hSARA
    Smad anchor for receptor activation
    Gene namesi
    Name:ZFYVE9
    Synonyms:MADHIP, SARA, SMADIP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:6775. ZFYVE9.

    Subcellular locationi

    GO - Cellular componenti

    1. early endosome Source: UniProtKB
    2. early endosome membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi782 – 7821Y → A: Diminishes complex formation with SMAD2. 1 Publication
    Mutagenesisi782 – 7821Y → E: Diminishes complex formation with SMAD2. 1 Publication
    Mutagenesisi783 – 7831C → A: Diminishes complex formation with SMAD2. 1 Publication
    Mutagenesisi783 – 7831C → E: Diminishes complex formation with SMAD2. 1 Publication
    Mutagenesisi788 – 7881P → A: Diminishes complex formation with SMAD2. 1 Publication
    Mutagenesisi788 – 7881P → E: Diminishes complex formation with SMAD2. 1 Publication
    Mutagenesisi790 – 7901Q → A: No effect on complex formation with SMAD2. 1 Publication
    Mutagenesisi793 – 7931Q → A: No effect on complex formation with SMAD2. 1 Publication
    Mutagenesisi805 – 8051V → A: Diminishes complex formation with SMAD2. 1 Publication
    Mutagenesisi805 – 8051V → E: Diminishes complex formation with SMAD2. 1 Publication

    Organism-specific databases

    PharmGKBiPA30532.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14251425Zinc finger FYVE domain-containing protein 9PRO_0000098715Add
    BLAST

    Proteomic databases

    MaxQBiO95405.
    PaxDbiO95405.
    PRIDEiO95405.

    PTM databases

    PhosphoSiteiO95405.

    Expressioni

    Tissue specificityi

    Ubiquitous. In the brain found primarily in the cerebrovascular smooth muscle cells and reactive astrocytes.

    Gene expression databases

    BgeeiO95405.
    CleanExiHS_ZFYVE9.
    GenevestigatoriO95405.

    Organism-specific databases

    HPAiCAB017702.

    Interactioni

    Subunit structurei

    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.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LRP12Q9Y5612EBI-296817,EBI-296693
    PPP1CAP621363EBI-296817,EBI-357253
    RHOP081002EBI-296817,EBI-1394177
    SMAD2Q157962EBI-296817,EBI-1040141
    SMAD3P840222EBI-296817,EBI-347161
    STX3Q132773EBI-296817,EBI-1394295

    Protein-protein interaction databases

    BioGridi114773. 39 interactions.
    IntActiO95405. 37 interactions.
    MINTiMINT-243774.
    STRINGi9606.ENSP00000287727.

    Structurei

    Secondary structure

    1
    1425
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi779 – 7813
    Helixi788 – 7925
    Turni793 – 7953
    Beta strandi797 – 8004
    Beta strandi804 – 8074
    Beta strandi901 – 9033
    Beta strandi907 – 9093
    Beta strandi918 – 9225
    Helixi925 – 9328
    Beta strandi940 – 9456
    Beta strandi948 – 95710
    Beta strandi960 – 97011
    Helixi971 – 9733
    Beta strandi977 – 9837
    Helixi994 – 100714
    Beta strandi1017 – 10193
    Beta strandi1030 – 10367
    Beta strandi1039 – 10413
    Beta strandi1050 – 106011
    Turni1061 – 10633
    Helixi1064 – 10696
    Helixi1071 – 108212
    Beta strandi1089 – 10913
    Helixi1106 – 11094
    Beta strandi1113 – 11153
    Beta strandi1127 – 11315
    Beta strandi1134 – 11407
    Helixi1141 – 11433
    Helixi1144 – 11529
    Beta strandi1156 – 11627
    Beta strandi1170 – 11778
    Beta strandi1183 – 119210
    Beta strandi1196 – 11994
    Beta strandi1201 – 12077
    Beta strandi1218 – 12225
    Beta strandi1225 – 12295
    Helixi1232 – 124312
    Beta strandi1248 – 12503
    Beta strandi1263 – 12708
    Turni1282 – 12843
    Beta strandi1291 – 12955
    Beta strandi1302 – 13043
    Beta strandi1307 – 131610
    Helixi1334 – 134714
    Helixi1348 – 13503
    Helixi1351 – 13566
    Beta strandi1361 – 13688
    Beta strandi1373 – 13797
    Helixi1386 – 13883
    Helixi1389 – 140012
    Beta strandi1413 – 142210

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DEVX-ray2.20B/D771-811[»]
    1MK2X-ray2.74B773-810[»]
    4BKWX-ray2.53A895-1425[»]
    DisProtiDP00141.
    ProteinModelPortaliO95405.
    SMRiO95405. Positions 689-761, 771-811, 895-1424.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO95405.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni767 – 82357SBDAdd
    BLAST

    Domaini

    The SMAD binding domain (SBD) interacts with the MH2 domains of SMAD2 or SMAD3.
    The FYVE-type zinc finger is necessary and sufficient for its localization into early endosomes and mediates the association with PI3P.

    Sequence similaritiesi

    Contains 1 FYVE-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri699 – 75860FYVE-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG283908.
    HOGENOMiHOG000231131.
    HOVERGENiHBG079085.
    InParanoidiO95405.
    KOiK04679.
    OMAiTMWIDEN.
    OrthoDBiEOG7JDQWQ.
    PhylomeDBiO95405.
    TreeFamiTF324904.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    4.10.720.10. 1 hit.
    InterProiIPR022557. DUF3480.
    IPR024608. SARA_Smad-bd.
    IPR000306. Znf_FYVE.
    IPR017455. Znf_FYVE-rel.
    IPR011011. Znf_FYVE_PHD.
    IPR017165. Znf_FYVE_SARA/endofin.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF11979. DUF3480. 1 hit.
    PF01363. FYVE. 1 hit.
    PF11409. SARA. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037289. SARA/endofin. 1 hit.
    SMARTiSM00064. FYVE. 1 hit.
    [Graphical view]
    SUPFAMiSSF57903. SSF57903. 1 hit.
    PROSITEiPS50178. ZF_FYVE. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95405-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MENYFQAEAY NLDKVLDEFE QNEDETVSST LLDTKWNKIL DPPSHRLSFN     50
    PTLASVNESA VSNESQPQLK VFSLAHSAPL TTEEEDHCAN GQDCNLNPEI 100
    ATMWIDENAV AEDQLIKRNY SWDDQCSAVE VGEKKCGNLA CLPDEKNVLV 150
    VAVMHNCDKR TLQNDLQDCN NYNSQSLMDA FSCSLDNENR QTDQFSFSIN 200
    ESTEKDMNSE KQMDPLNRPK TEGRSVNHLC PTSSDSLASV CSPSQLKDDG 250
    SIGRDPSMSA ITSLTVDSVI SSQGTDGCPA VKKQENYIPD EDLTGKISSP 300
    RTDLGSPNSF SHMSEGILMK KEPAEESTTE ESLRSGLPLL LKPDMPNGSG 350
    RNNDCERCSD CLVPNEVRAD ENEGYEHEET LGTTEFLNMT EHFSESQDMT 400
    NWKLTKLNEM NDSQVNEEKE KFLQISQPED TNGDSGGQCV GLADAGLDLK 450
    GTCISESEEC DFSTVIDTPA ANYLSNGCDS YGMQDPGVSF VPKTLPSKED 500
    SVTEEKEIEE SKSECYSNIY EQRGNEATEG SGLLLNSTGD LMKKNYLHNF 550
    CSQVPSVLGQ SSPKVVASLP SISVPFGGAR PKQPSNLKLQ IPKPLSDHLQ 600
    NDFPANSGNN TKNKNDILGK AKLGENSATN VCSPSLGNIS NVDTNGEHLE 650
    SYEAEISTRP CLALAPDSPD NDLRAGQFGI SARKPFTTLG EVAPVWVPDS 700
    QAPNCMKCEA RFTFTKRRHH CRACGKVFCA SCCSLKCKLL YMDRKEARVC 750
    VICHSVLMNA QAWENMMSAS SQSPNPNNPA EYCSTIPPLQ QAQASGALSS 800
    PPPTVMVPVG VLKHPGAEVA QPREQRRVWF ADGILPNGEV ADAAKLTMNG 850
    TSSAGTLAVS HDPVKPVTTS PLPAETDICL FSGSITQVGS PVGSAMNLIP 900
    EDGLPPILIS TGVKGDYAVE EKPSQISVMQ QLEDGGPDPL VFVLNANLLS 950
    MVKIVNYVNR KCWCFTTKGM HAVGQSEIVI LLQCLPDEKC LPKDIFNHFV 1000
    QLYRDALAGN VVSNLGHSFF SQSFLGSKEH GGFLYVTSTY QSLQDLVLPT 1050
    PPYLFGILIQ KWETPWAKVF PIRLMLRLGA EYRLYPCPLF SVRFRKPLFG 1100
    ETGHTIMNLL ADFRNYQYTL PVVQGLVVDM EVRKTSIKIP SNRYNEMMKA 1150
    MNKSNEHVLA GGACFNEKAD SHLVCVQNDD GNYQTQAISI HNQPRKVTGA 1200
    SFFVFSGALK SSSGYLAKSS IVEDGVMVQI TAENMDSLRQ ALREMKDFTI 1250
    TCGKADAEEP QEHIHIQWVD DDKNVSKGVV SPIDGKSMET ITNVKIFHGS 1300
    EYKANGKVIR WTEVFFLEND DQHNCLSDPA DHSRLTEHVA KAFCLALCPH 1350
    LKLLKEDGMT KLGLRVTLDS DQVGYQAGSN GQPLPSQYMN DLDSALVPVI 1400
    HGGACQLSEG PVVMELIFYI LENIV 1425
    Length:1,425
    Mass (Da):156,403
    Last modified:August 14, 2001 - v2
    Checksum:iADE5CB530C1272C6
    GO
    Isoform 2 (identifier: O95405-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         760-818: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:1,366
    Mass (Da):150,348
    Checksum:iC7779D54E2435CC9
    GO
    Isoform 3 (identifier: O95405-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         760-762: AQA → GKY
         763-1425: Missing.

    Show »
    Length:762
    Mass (Da):83,721
    Checksum:iB96C60B807CFF367
    GO

    Sequence cautioni

    The sequence AAD31694.1 differs from that shown. Reason: Frameshift at position 1243.
    The sequence AAC99462.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti287 – 2871Y → C.
    Corresponds to variant rs9803965 [ dbSNP | Ensembl ].
    VAR_052985
    Natural varianti414 – 4141Q → P.
    Corresponds to variant rs3790525 [ dbSNP | Ensembl ].
    VAR_052986
    Natural varianti639 – 6391I → V.
    Corresponds to variant rs11809887 [ dbSNP | Ensembl ].
    VAR_052987

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei760 – 81859Missing in isoform 2. 1 PublicationVSP_004315Add
    BLAST
    Alternative sequencei760 – 7623AQA → GKY in isoform 3. 1 PublicationVSP_004316
    Alternative sequencei763 – 1425663Missing in isoform 3. 1 PublicationVSP_004317Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF104304 mRNA. Translation: AAC99462.1. Different initiation.
    AF130419 mRNA. Translation: AAD31694.1. Frameshift.
    AF130420 mRNA. Translation: AAD31695.1.
    AL513218, AC105754 Genomic DNA. Translation: CAI12285.1.
    AL513218, AC105754 Genomic DNA. Translation: CAI12286.1.
    CH471059 Genomic DNA. Translation: EAX06790.1.
    CH471059 Genomic DNA. Translation: EAX06791.1.
    BC032680 mRNA. Translation: AAH32680.1.
    CCDSiCCDS563.1. [O95405-1]
    CCDS564.1. [O95405-2]
    RefSeqiNP_004790.2. NM_004799.3. [O95405-1]
    NP_015563.2. NM_007324.3. [O95405-2]
    UniGeneiHs.532345.

    Genome annotation databases

    EnsembliENST00000287727; ENSP00000287727; ENSG00000157077. [O95405-1]
    ENST00000357206; ENSP00000349737; ENSG00000157077. [O95405-2]
    ENST00000371591; ENSP00000360647; ENSG00000157077. [O95405-1]
    GeneIDi9372.
    KEGGihsa:9372.
    UCSCiuc001ctn.4. human. [O95405-3]
    uc001cto.4. human. [O95405-1]
    uc001ctp.4. human. [O95405-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF104304 mRNA. Translation: AAC99462.1 . Different initiation.
    AF130419 mRNA. Translation: AAD31694.1 . Frameshift.
    AF130420 mRNA. Translation: AAD31695.1 .
    AL513218 , AC105754 Genomic DNA. Translation: CAI12285.1 .
    AL513218 , AC105754 Genomic DNA. Translation: CAI12286.1 .
    CH471059 Genomic DNA. Translation: EAX06790.1 .
    CH471059 Genomic DNA. Translation: EAX06791.1 .
    BC032680 mRNA. Translation: AAH32680.1 .
    CCDSi CCDS563.1. [O95405-1 ]
    CCDS564.1. [O95405-2 ]
    RefSeqi NP_004790.2. NM_004799.3. [O95405-1 ]
    NP_015563.2. NM_007324.3. [O95405-2 ]
    UniGenei Hs.532345.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DEV X-ray 2.20 B/D 771-811 [» ]
    1MK2 X-ray 2.74 B 773-810 [» ]
    4BKW X-ray 2.53 A 895-1425 [» ]
    DisProti DP00141.
    ProteinModelPortali O95405.
    SMRi O95405. Positions 689-761, 771-811, 895-1424.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114773. 39 interactions.
    IntActi O95405. 37 interactions.
    MINTi MINT-243774.
    STRINGi 9606.ENSP00000287727.

    PTM databases

    PhosphoSitei O95405.

    Proteomic databases

    MaxQBi O95405.
    PaxDbi O95405.
    PRIDEi O95405.

    Protocols and materials databases

    DNASUi 9372.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000287727 ; ENSP00000287727 ; ENSG00000157077 . [O95405-1 ]
    ENST00000357206 ; ENSP00000349737 ; ENSG00000157077 . [O95405-2 ]
    ENST00000371591 ; ENSP00000360647 ; ENSG00000157077 . [O95405-1 ]
    GeneIDi 9372.
    KEGGi hsa:9372.
    UCSCi uc001ctn.4. human. [O95405-3 ]
    uc001cto.4. human. [O95405-1 ]
    uc001ctp.4. human. [O95405-2 ]

    Organism-specific databases

    CTDi 9372.
    GeneCardsi GC01P052608.
    H-InvDB HIX0000582.
    HGNCi HGNC:6775. ZFYVE9.
    HPAi CAB017702.
    MIMi 603755. gene.
    neXtProti NX_O95405.
    PharmGKBi PA30532.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG283908.
    HOGENOMi HOG000231131.
    HOVERGENi HBG079085.
    InParanoidi O95405.
    KOi K04679.
    OMAi TMWIDEN.
    OrthoDBi EOG7JDQWQ.
    PhylomeDBi O95405.
    TreeFami TF324904.

    Enzyme and pathway databases

    Reactomei REACT_120727. Downregulation of TGF-beta receptor signaling.
    REACT_120850. TGF-beta receptor signaling activates SMADs.
    REACT_169103. SMAD2/3 Phosphorylation Motif Mutants in Cancer.
    REACT_169165. SMAD2/3 MH2 Domain Mutants in Cancer.
    REACT_169263. TGFBR1 KD Mutants in Cancer.
    SignaLinki O95405.

    Miscellaneous databases

    EvolutionaryTracei O95405.
    GeneWikii Zinc_finger_FYVE_domain-containing_protein_9.
    GenomeRNAii 9372.
    NextBioi 35102.
    PROi O95405.
    SOURCEi Search...

    Gene expression databases

    Bgeei O95405.
    CleanExi HS_ZFYVE9.
    Genevestigatori O95405.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    4.10.720.10. 1 hit.
    InterProi IPR022557. DUF3480.
    IPR024608. SARA_Smad-bd.
    IPR000306. Znf_FYVE.
    IPR017455. Znf_FYVE-rel.
    IPR011011. Znf_FYVE_PHD.
    IPR017165. Znf_FYVE_SARA/endofin.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF11979. DUF3480. 1 hit.
    PF01363. FYVE. 1 hit.
    PF11409. SARA. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037289. SARA/endofin. 1 hit.
    SMARTi SM00064. FYVE. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57903. SSF57903. 1 hit.
    PROSITEi PS50178. ZF_FYVE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "SARA, a FYVE domain protein that recruits Smad2 to the TGFbeta receptor."
      Tsukazaki T., Chiang T.A., Davison A.F., Attisano L., Wrana J.L.
      Cell 95:779-791(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH SMAD2; SMAD3; TGFBR1 AND TGFBR2, FUNCTION, SUBCELLULAR LOCATION.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
      Tissue: Fetal brain.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      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.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Testis.
    6. "Early endosomal regulation of Smad-dependent signaling in endothelial cells."
      Panopoulou E., Gillooly D.J., Wrana J.L., Zerial M., Stenmark H., Murphy C., Fotsis T.
      J. Biol. Chem. 277:18046-18052(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
    8. "Cytoplasmic PML function in TGF-beta signalling."
      Lin H.K., Bergmann S., Pandolfi P.P.
      Nature 431:205-211(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PML; SMAD2 AND SMAD3.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Structural basis of Smad2 recognition by the Smad anchor for receptor activation."
      Wu G., Chen Y.-G., Ozdamar B., Gyuricza C.A., Chong P.A., Wrana J.L., Massague J., Shi Y.
      Science 287:92-97(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 771-811 IN COMPLEX WITH SMAD2, MUTAGENESIS.
    11. "Smad3 allostery links TGF-beta receptor kinase activation to transcriptional control."
      Qin B.Y., Lam S.S., Correia J.J., Lin K.
      Genes Dev. 16:1950-1963(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.74 ANGSTROMS) OF 773-810 IN COMPLEX WITH SMAD3.

    Entry informationi

    Entry nameiZFYV9_HUMAN
    AccessioniPrimary (citable) accession number: O95405
    Secondary accession number(s): Q5T0F6
    , Q5T0F7, Q9UNE1, Q9Y5R7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 14, 2001
    Last sequence update: August 14, 2001
    Last modified: October 1, 2014
    This is version 136 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3