O95405 (ZFYV9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	ZFYVE9
Synonyms:	MADHIP, SARA, SMADIP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1425 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.1 Ref.8
Subunit structure	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. Ref.1 Ref.8
Subcellular location	Cytoplasm. Early endosome membrane Ref.1 Ref.6 Ref.8.
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. The FYVE-type zinc finger is necessary and sufficient for its localization into early endosomes and mediates the association with PI3P.
Sequence similarities	Contains 1 FYVE-type zinc finger.
Sequence caution	The sequence AAC99462.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAD31694.1 differs from that shown. Reason: Frameshift at position 1243.

Ontologies

Keywords
Cellular component	Cytoplasm Endosome Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Receptor
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	SMAD protein complex assembly Inferred from direct assay Ref.1. Source: UniProtKB SMAD protein import into nucleus Inferred from mutant phenotype Ref.1. Source: UniProtKB endocytosis Non-traceable author statement PubMed 12809483. Source: UniProtKB negative regulation of transforming growth factor beta receptor signaling pathway Traceable author statement. Source: Reactome transforming growth factor beta receptor signaling pathway Inferred from mutant phenotype Ref.1. Source: UniProtKB
Cellular_component	early endosome membrane Inferred from direct assay Ref.6. Source: UniProtKB
Molecular_function	1-phosphatidylinositol binding Inferred from direct assay Ref.6. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type peptidase activity Non-traceable author statement Ref.2. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
LRP12	Q9Y561	2	EBI-296817,EBI-296693
RHO	P08100	2	EBI-296817,EBI-1394177
STX3	Q13277	3	EBI-296817,EBI-1394295

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O95405-1)

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.

Isoform 2 (identifier: O95405-2)

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.

Isoform 3 (identifier: O95405-3)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1425

1425

Zinc finger FYVE domain-containing protein 9

PRO_0000098715

Regions

Zinc finger

699 – 758

60

FYVE-type

Region

767 – 823

57

SBD

Natural variations

Alternative sequence

760 – 818

59

Missing in isoform 2.

VSP_004315

Alternative sequence

760 – 762

3

AQA → GKY in isoform 3.

VSP_004316

Alternative sequence

763 – 1425

663

Missing in isoform 3.

VSP_004317

Natural variant

287

1

Y → C.
Corresponds to variant rs9803965 [ dbSNP | Ensembl ].

VAR_052985

Natural variant

414

1

Q → P.
Corresponds to variant rs3790525 [ dbSNP | Ensembl ].

VAR_052986

Natural variant

639

1

I → V.
Corresponds to variant rs11809887 [ dbSNP | Ensembl ].

VAR_052987

Experimental info

Mutagenesis

782

1

Y → A: Diminishes complex formation with SMAD2.

Mutagenesis

782

1

Y → E: Diminishes complex formation with SMAD2.

Mutagenesis

783

1

C → A: Diminishes complex formation with SMAD2.

Mutagenesis

783

1

C → E: Diminishes complex formation with SMAD2.

Mutagenesis

788

1

P → A: Diminishes complex formation with SMAD2.

Mutagenesis

788

1

P → E: Diminishes complex formation with SMAD2.

Mutagenesis

790

1

Q → A: No effect on complex formation with SMAD2.

Mutagenesis

793

1

Q → A: No effect on complex formation with SMAD2.

Mutagenesis

805

1

V → A: Diminishes complex formation with SMAD2.

Mutagenesis

805

1

V → E: Diminishes complex formation with SMAD2.

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

1425

Helix Strand Turn

Details...

Helix

779 – 781

3

Helix

788 – 792

5

Turn

793 – 795

3

Beta strand

797 – 800

4

Beta strand

804 – 807

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 14, 2001. Version 2. Checksum: ADE5CB530C1272C6	FASTA	1,425	156,403
	10 20 30 40 50 60 MENYFQAEAY NLDKVLDEFE QNEDETVSST LLDTKWNKIL DPPSHRLSFN PTLASVNESA 70 80 90 100 110 120 VSNESQPQLK VFSLAHSAPL TTEEEDHCAN GQDCNLNPEI ATMWIDENAV AEDQLIKRNY 130 140 150 160 170 180 SWDDQCSAVE VGEKKCGNLA CLPDEKNVLV VAVMHNCDKR TLQNDLQDCN NYNSQSLMDA 190 200 210 220 230 240 FSCSLDNENR QTDQFSFSIN ESTEKDMNSE KQMDPLNRPK TEGRSVNHLC PTSSDSLASV 250 260 270 280 290 300 CSPSQLKDDG SIGRDPSMSA ITSLTVDSVI SSQGTDGCPA VKKQENYIPD EDLTGKISSP 310 320 330 340 350 360 RTDLGSPNSF SHMSEGILMK KEPAEESTTE ESLRSGLPLL LKPDMPNGSG RNNDCERCSD 370 380 390 400 410 420 CLVPNEVRAD ENEGYEHEET LGTTEFLNMT EHFSESQDMT NWKLTKLNEM NDSQVNEEKE 430 440 450 460 470 480 KFLQISQPED TNGDSGGQCV GLADAGLDLK GTCISESEEC DFSTVIDTPA ANYLSNGCDS 490 500 510 520 530 540 YGMQDPGVSF VPKTLPSKED SVTEEKEIEE SKSECYSNIY EQRGNEATEG SGLLLNSTGD 550 560 570 580 590 600 LMKKNYLHNF CSQVPSVLGQ SSPKVVASLP SISVPFGGAR PKQPSNLKLQ IPKPLSDHLQ 610 620 630 640 650 660 NDFPANSGNN TKNKNDILGK AKLGENSATN VCSPSLGNIS NVDTNGEHLE SYEAEISTRP 670 680 690 700 710 720 CLALAPDSPD NDLRAGQFGI SARKPFTTLG EVAPVWVPDS QAPNCMKCEA RFTFTKRRHH 730 740 750 760 770 780 CRACGKVFCA SCCSLKCKLL YMDRKEARVC VICHSVLMNA QAWENMMSAS SQSPNPNNPA 790 800 810 820 830 840 EYCSTIPPLQ QAQASGALSS PPPTVMVPVG VLKHPGAEVA QPREQRRVWF ADGILPNGEV 850 860 870 880 890 900 ADAAKLTMNG TSSAGTLAVS HDPVKPVTTS PLPAETDICL FSGSITQVGS PVGSAMNLIP 910 920 930 940 950 960 EDGLPPILIS TGVKGDYAVE EKPSQISVMQ QLEDGGPDPL VFVLNANLLS MVKIVNYVNR 970 980 990 1000 1010 1020 KCWCFTTKGM HAVGQSEIVI LLQCLPDEKC LPKDIFNHFV QLYRDALAGN VVSNLGHSFF 1030 1040 1050 1060 1070 1080 SQSFLGSKEH GGFLYVTSTY QSLQDLVLPT PPYLFGILIQ KWETPWAKVF PIRLMLRLGA 1090 1100 1110 1120 1130 1140 EYRLYPCPLF SVRFRKPLFG ETGHTIMNLL ADFRNYQYTL PVVQGLVVDM EVRKTSIKIP 1150 1160 1170 1180 1190 1200 SNRYNEMMKA MNKSNEHVLA GGACFNEKAD SHLVCVQNDD GNYQTQAISI HNQPRKVTGA 1210 1220 1230 1240 1250 1260 SFFVFSGALK SSSGYLAKSS IVEDGVMVQI TAENMDSLRQ ALREMKDFTI TCGKADAEEP 1270 1280 1290 1300 1310 1320 QEHIHIQWVD DDKNVSKGVV SPIDGKSMET ITNVKIFHGS EYKANGKVIR WTEVFFLEND 1330 1340 1350 1360 1370 1380 DQHNCLSDPA DHSRLTEHVA KAFCLALCPH LKLLKEDGMT KLGLRVTLDS DQVGYQAGSN 1390 1400 1410 1420 GQPLPSQYMN DLDSALVPVI HGGACQLSEG PVVMELIFYI LENIV
	Isoform 2 [UniParc]. Checksum: C7779D54E2435CC9	FASTA	1,366	150,348
	10 20 30 40 50 60 MENYFQAEAY NLDKVLDEFE QNEDETVSST LLDTKWNKIL DPPSHRLSFN PTLASVNESA 70 80 90 100 110 120 VSNESQPQLK VFSLAHSAPL TTEEEDHCAN GQDCNLNPEI ATMWIDENAV AEDQLIKRNY 130 140 150 160 170 180 SWDDQCSAVE VGEKKCGNLA CLPDEKNVLV VAVMHNCDKR TLQNDLQDCN NYNSQSLMDA 190 200 210 220 230 240 FSCSLDNENR QTDQFSFSIN ESTEKDMNSE KQMDPLNRPK TEGRSVNHLC PTSSDSLASV 250 260 270 280 290 300 CSPSQLKDDG SIGRDPSMSA ITSLTVDSVI SSQGTDGCPA VKKQENYIPD EDLTGKISSP 310 320 330 340 350 360 RTDLGSPNSF SHMSEGILMK KEPAEESTTE ESLRSGLPLL LKPDMPNGSG RNNDCERCSD 370 380 390 400 410 420 CLVPNEVRAD ENEGYEHEET LGTTEFLNMT EHFSESQDMT NWKLTKLNEM NDSQVNEEKE 430 440 450 460 470 480 KFLQISQPED TNGDSGGQCV GLADAGLDLK GTCISESEEC DFSTVIDTPA ANYLSNGCDS 490 500 510 520 530 540 YGMQDPGVSF VPKTLPSKED SVTEEKEIEE SKSECYSNIY EQRGNEATEG SGLLLNSTGD 550 560 570 580 590 600 LMKKNYLHNF CSQVPSVLGQ SSPKVVASLP SISVPFGGAR PKQPSNLKLQ IPKPLSDHLQ 610 620 630 640 650 660 NDFPANSGNN TKNKNDILGK AKLGENSATN VCSPSLGNIS NVDTNGEHLE SYEAEISTRP 670 680 690 700 710 720 CLALAPDSPD NDLRAGQFGI SARKPFTTLG EVAPVWVPDS QAPNCMKCEA RFTFTKRRHH 730 740 750 760 770 780 CRACGKVFCA SCCSLKCKLL YMDRKEARVC VICHSVLMNV AQPREQRRVW FADGILPNGE 790 800 810 820 830 840 VADAAKLTMN GTSSAGTLAV SHDPVKPVTT SPLPAETDIC LFSGSITQVG SPVGSAMNLI 850 860 870 880 890 900 PEDGLPPILI STGVKGDYAV EEKPSQISVM QQLEDGGPDP LVFVLNANLL SMVKIVNYVN 910 920 930 940 950 960 RKCWCFTTKG MHAVGQSEIV ILLQCLPDEK CLPKDIFNHF VQLYRDALAG NVVSNLGHSF 970 980 990 1000 1010 1020 FSQSFLGSKE HGGFLYVTST YQSLQDLVLP TPPYLFGILI QKWETPWAKV FPIRLMLRLG 1030 1040 1050 1060 1070 1080 AEYRLYPCPL FSVRFRKPLF GETGHTIMNL LADFRNYQYT LPVVQGLVVD MEVRKTSIKI 1090 1100 1110 1120 1130 1140 PSNRYNEMMK AMNKSNEHVL AGGACFNEKA DSHLVCVQND DGNYQTQAIS IHNQPRKVTG 1150 1160 1170 1180 1190 1200 ASFFVFSGAL KSSSGYLAKS SIVEDGVMVQ ITAENMDSLR QALREMKDFT ITCGKADAEE 1210 1220 1230 1240 1250 1260 PQEHIHIQWV DDDKNVSKGV VSPIDGKSME TITNVKIFHG SEYKANGKVI RWTEVFFLEN 1270 1280 1290 1300 1310 1320 DDQHNCLSDP ADHSRLTEHV AKAFCLALCP HLKLLKEDGM TKLGLRVTLD SDQVGYQAGS 1330 1340 1350 1360 NGQPLPSQYM NDLDSALVPV IHGGACQLSE GPVVMELIFY ILENIV
	Isoform 3 [UniParc]. Checksum: B96C60B807CFF367	FASTA	762	83,721
	10 20 30 40 50 60 MENYFQAEAY NLDKVLDEFE QNEDETVSST LLDTKWNKIL DPPSHRLSFN PTLASVNESA 70 80 90 100 110 120 VSNESQPQLK VFSLAHSAPL TTEEEDHCAN GQDCNLNPEI ATMWIDENAV AEDQLIKRNY 130 140 150 160 170 180 SWDDQCSAVE VGEKKCGNLA CLPDEKNVLV VAVMHNCDKR TLQNDLQDCN NYNSQSLMDA 190 200 210 220 230 240 FSCSLDNENR QTDQFSFSIN ESTEKDMNSE KQMDPLNRPK TEGRSVNHLC PTSSDSLASV 250 260 270 280 290 300 CSPSQLKDDG SIGRDPSMSA ITSLTVDSVI SSQGTDGCPA VKKQENYIPD EDLTGKISSP 310 320 330 340 350 360 RTDLGSPNSF SHMSEGILMK KEPAEESTTE ESLRSGLPLL LKPDMPNGSG RNNDCERCSD 370 380 390 400 410 420 CLVPNEVRAD ENEGYEHEET LGTTEFLNMT EHFSESQDMT NWKLTKLNEM NDSQVNEEKE 430 440 450 460 470 480 KFLQISQPED TNGDSGGQCV GLADAGLDLK GTCISESEEC DFSTVIDTPA ANYLSNGCDS 490 500 510 520 530 540 YGMQDPGVSF VPKTLPSKED SVTEEKEIEE SKSECYSNIY EQRGNEATEG SGLLLNSTGD 550 560 570 580 590 600 LMKKNYLHNF CSQVPSVLGQ SSPKVVASLP SISVPFGGAR PKQPSNLKLQ IPKPLSDHLQ 610 620 630 640 650 660 NDFPANSGNN TKNKNDILGK AKLGENSATN VCSPSLGNIS NVDTNGEHLE SYEAEISTRP 670 680 690 700 710 720 CLALAPDSPD NDLRAGQFGI SARKPFTTLG EVAPVWVPDS QAPNCMKCEA RFTFTKRRHH 730 740 750 760 CRACGKVFCA SCCSLKCKLL YMDRKEARVC VICHSVLMNG KY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Identification of a novel serine protease-like molecule in human brain." Meckelein B., Marshall D.C.L., Conn K.J., Pietropaolo M., Van Nostrand W., Abraham C.R. Brain Res. Mol. Brain Res. 55:181-197(1998) [PubMed] [Europe PMC] [Abstract] 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]	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 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]	"An unappreciated role for RNA surveillance." Hillman R.T., Green R.E., Brenner S.E. Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract] 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]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00026338.
IPI00030648.
IPI00480079.

RefSeq

NP_004790.2. NM_004799.2.
NP_015562.1. NM_007323.1.
NP_015563.2. NM_007324.2.

UniGene

Hs.532345.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DEV	X-ray	2.20	B/D	771-811	[»]
1MK2	X-ray	2.74	B	773-810	[»]

DisProt

DP00141.

ProteinModelPortal

O95405.

ModBase

Search...

Protein-protein interaction databases

IntAct

O95405. 8 interactions.

MINT

MINT-243774.

STRING

9606.ENSP00000287727.

PTM databases

PhosphoSite

O95405.

Proteomic databases

PaxDb

O95405.

PRIDE

O95405.

Protocols and materials databases

DNASU

9372.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000287727; ENSP00000287727; ENSG00000157077.
ENST00000357206; ENSP00000349737; ENSG00000157077.
ENST00000361625; ENSP00000355358; ENSG00000157077.
ENST00000371591; ENSP00000360647; ENSG00000157077.

GeneID

9372.

KEGG

hsa:9372.

UCSC

uc001ctn.3. human.
uc001cto.3. human.
uc001ctp.3. human.

Organism-specific databases

CTD

9372.

GeneCards

GC01P052608.

H-InvDB

HIX0000582.

HGNC

HGNC:6775. ZFYVE9.

MIM

603755. gene.

neXtProt

NX_O95405.

PharmGKB

PA30532.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG283908.

HOGENOM

HOG000231131.

HOVERGEN

HBG079085.

InParanoid

O95405.

KO

K04679.

OMA

VFSLAHS.

PhylomeDB

O95405.

Enzyme and pathway databases

Pathway_Interaction_DB

tgfbrpathway. TGF-beta receptor signaling.

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

Bgee

O95405.

CleanEx

HS_ZFYVE9.

Genevestigator

O95405.

GermOnline

ENSG00000157077. Homo sapiens.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.
4.10.720.10. 1 hit.

InterPro

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]

Pfam

PF11979. DUF3480. 1 hit.
PF01363. FYVE. 1 hit.
PF11409. SARA. 1 hit.
[Graphical view]

PIRSF

PIRSF037289. SARA/endofin. 1 hit.

SMART

SM00064. FYVE. 1 hit.
[Graphical view]

SUPFAM

SSF57903. FYVE_PHD_ZnF. 1 hit.

PROSITE

PS50178. ZF_FYVE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O95405.

GenomeRNAi

9372.

NextBio

35102.

SOURCE

Search...

Entry information

Entry name

ZFYV9_HUMAN

Accession

Primary (citable) accession number: O95405
Secondary accession number(s): Q5T0F6 , Q5T0F7, Q9UNE1, Q9Y5R7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 14, 2001
Last sequence update:	August 14, 2001
Last modified:	May 1, 2013
This is version 121 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.