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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

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-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. 1-phosphatidylinositol binding Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW
  3. 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

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00750000117280.
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

        10         20         30         40         50
MENYFQAEAY NLDKVLDEFE QNEDETVSST LLDTKWNKIL DPPSHRLSFN
60 70 80 90 100
PTLASVNESA VSNESQPQLK VFSLAHSAPL TTEEEDHCAN GQDCNLNPEI
110 120 130 140 150
ATMWIDENAV AEDQLIKRNY SWDDQCSAVE VGEKKCGNLA CLPDEKNVLV
160 170 180 190 200
VAVMHNCDKR TLQNDLQDCN NYNSQSLMDA FSCSLDNENR QTDQFSFSIN
210 220 230 240 250
ESTEKDMNSE KQMDPLNRPK TEGRSVNHLC PTSSDSLASV CSPSQLKDDG
260 270 280 290 300
SIGRDPSMSA ITSLTVDSVI SSQGTDGCPA VKKQENYIPD EDLTGKISSP
310 320 330 340 350
RTDLGSPNSF SHMSEGILMK KEPAEESTTE ESLRSGLPLL LKPDMPNGSG
360 370 380 390 400
RNNDCERCSD CLVPNEVRAD ENEGYEHEET LGTTEFLNMT EHFSESQDMT
410 420 430 440 450
NWKLTKLNEM NDSQVNEEKE KFLQISQPED TNGDSGGQCV GLADAGLDLK
460 470 480 490 500
GTCISESEEC DFSTVIDTPA ANYLSNGCDS YGMQDPGVSF VPKTLPSKED
510 520 530 540 550
SVTEEKEIEE SKSECYSNIY EQRGNEATEG SGLLLNSTGD LMKKNYLHNF
560 570 580 590 600
CSQVPSVLGQ SSPKVVASLP SISVPFGGAR PKQPSNLKLQ IPKPLSDHLQ
610 620 630 640 650
NDFPANSGNN TKNKNDILGK AKLGENSATN VCSPSLGNIS NVDTNGEHLE
660 670 680 690 700
SYEAEISTRP CLALAPDSPD NDLRAGQFGI SARKPFTTLG EVAPVWVPDS
710 720 730 740 750
QAPNCMKCEA RFTFTKRRHH CRACGKVFCA SCCSLKCKLL YMDRKEARVC
760 770 780 790 800
VICHSVLMNA QAWENMMSAS SQSPNPNNPA EYCSTIPPLQ QAQASGALSS
810 820 830 840 850
PPPTVMVPVG VLKHPGAEVA QPREQRRVWF ADGILPNGEV ADAAKLTMNG
860 870 880 890 900
TSSAGTLAVS HDPVKPVTTS PLPAETDICL FSGSITQVGS PVGSAMNLIP
910 920 930 940 950
EDGLPPILIS TGVKGDYAVE EKPSQISVMQ QLEDGGPDPL VFVLNANLLS
960 970 980 990 1000
MVKIVNYVNR KCWCFTTKGM HAVGQSEIVI LLQCLPDEKC LPKDIFNHFV
1010 1020 1030 1040 1050
QLYRDALAGN VVSNLGHSFF SQSFLGSKEH GGFLYVTSTY QSLQDLVLPT
1060 1070 1080 1090 1100
PPYLFGILIQ KWETPWAKVF PIRLMLRLGA EYRLYPCPLF SVRFRKPLFG
1110 1120 1130 1140 1150
ETGHTIMNLL ADFRNYQYTL PVVQGLVVDM EVRKTSIKIP SNRYNEMMKA
1160 1170 1180 1190 1200
MNKSNEHVLA GGACFNEKAD SHLVCVQNDD GNYQTQAISI HNQPRKVTGA
1210 1220 1230 1240 1250
SFFVFSGALK SSSGYLAKSS IVEDGVMVQI TAENMDSLRQ ALREMKDFTI
1260 1270 1280 1290 1300
TCGKADAEEP QEHIHIQWVD DDKNVSKGVV SPIDGKSMET ITNVKIFHGS
1310 1320 1330 1340 1350
EYKANGKVIR WTEVFFLEND DQHNCLSDPA DHSRLTEHVA KAFCLALCPH
1360 1370 1380 1390 1400
LKLLKEDGMT KLGLRVTLDS DQVGYQAGSN GQPLPSQYMN DLDSALVPVI
1410 1420
HGGACQLSEG PVVMELIFYI LENIV
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 AAC99462.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAD31694.1 differs from that shown. Reason: Frameshift at position 1243. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
GeneTreei ENSGT00750000117280.
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

ChiTaRSi ZFYVE9. human.
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: November 26, 2014
This is version 138 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