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O95405

- ZFYV9_HUMAN

UniProt

O95405 - ZFYV9_HUMAN

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Protein

Zinc finger FYVE domain-containing protein 9

Gene
ZFYVE9, MADHIP, SARA, SMADIP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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-typeAdd
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
Complete GO annotation...

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

Cytoplasm. Early endosome membrane 3 Publications

GO - Cellular componenti

  1. early endosome Source: UniProtKB
  2. early endosome membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

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

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.2 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.

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

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. VSP_004315Add
BLAST
Alternative sequencei760 – 7623AQA → GKY in isoform 3. VSP_004316
Alternative sequencei763 – 1425663Missing in isoform 3. VSP_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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 135 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

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