| UniProt ID | ZFYV9_HUMAN | |
|---|---|---|
| UniProt AC | O95405 | |
| Protein Name | Zinc finger FYVE domain-containing protein 9 | |
| Gene Name | ZFYVE9 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 1425 | |
| Subcellular Localization | Cytoplasm. Early endosome membrane. | |
| Protein Description | 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.. | |
| Protein Sequence | MENYFQAEAYNLDKVLDEFEQNEDETVSSTLLDTKWNKILDPPSHRLSFNPTLASVNESAVSNESQPQLKVFSLAHSAPLTTEEEDHCANGQDCNLNPEIATMWIDENAVAEDQLIKRNYSWDDQCSAVEVGEKKCGNLACLPDEKNVLVVAVMHNCDKRTLQNDLQDCNNYNSQSLMDAFSCSLDNENRQTDQFSFSINESTEKDMNSEKQMDPLNRPKTEGRSVNHLCPTSSDSLASVCSPSQLKDDGSIGRDPSMSAITSLTVDSVISSQGTDGCPAVKKQENYIPDEDLTGKISSPRTDLGSPNSFSHMSEGILMKKEPAEESTTEESLRSGLPLLLKPDMPNGSGRNNDCERCSDCLVPNEVRADENEGYEHEETLGTTEFLNMTEHFSESQDMTNWKLTKLNEMNDSQVNEEKEKFLQISQPEDTNGDSGGQCVGLADAGLDLKGTCISESEECDFSTVIDTPAANYLSNGCDSYGMQDPGVSFVPKTLPSKEDSVTEEKEIEESKSECYSNIYEQRGNEATEGSGLLLNSTGDLMKKNYLHNFCSQVPSVLGQSSPKVVASLPSISVPFGGARPKQPSNLKLQIPKPLSDHLQNDFPANSGNNTKNKNDILGKAKLGENSATNVCSPSLGNISNVDTNGEHLESYEAEISTRPCLALAPDSPDNDLRAGQFGISARKPFTTLGEVAPVWVPDSQAPNCMKCEARFTFTKRRHHCRACGKVFCASCCSLKCKLLYMDRKEARVCVICHSVLMNAQAWENMMSASSQSPNPNNPAEYCSTIPPLQQAQASGALSSPPPTVMVPVGVLKHPGAEVAQPREQRRVWFADGILPNGEVADAAKLTMNGTSSAGTLAVSHDPVKPVTTSPLPAETDICLFSGSITQVGSPVGSAMNLIPEDGLPPILISTGVKGDYAVEEKPSQISVMQQLEDGGPDPLVFVLNANLLSMVKIVNYVNRKCWCFTTKGMHAVGQSEIVILLQCLPDEKCLPKDIFNHFVQLYRDALAGNVVSNLGHSFFSQSFLGSKEHGGFLYVTSTYQSLQDLVLPTPPYLFGILIQKWETPWAKVFPIRLMLRLGAEYRLYPCPLFSVRFRKPLFGETGHTIMNLLADFRNYQYTLPVVQGLVVDMEVRKTSIKIPSNRYNEMMKAMNKSNEHVLAGGACFNEKADSHLVCVQNDDGNYQTQAISIHNQPRKVTGASFFVFSGALKSSSGYLAKSSIVEDGVMVQITAENMDSLRQALREMKDFTITCGKADAEEPQEHIHIQWVDDDKNVSKGVVSPIDGKSMETITNVKIFHGSEYKANGKVIRWTEVFFLENDDQHNCLSDPADHSRLTEHVAKAFCLALCPHLKLLKEDGMTKLGLRVTLDSDQVGYQAGSNGQPLPSQYMNDLDSALVPVIHGGACQLSEGPVVMELIFYILENIV | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 26 | Phosphorylation | FEQNEDETVSSTLLD HHHCCCCCHHHHHHH | 37.70 | - | |
| 28 | Phosphorylation | QNEDETVSSTLLDTK HCCCCCHHHHHHHCC | 25.65 | - | |
| 30 | Phosphorylation | EDETVSSTLLDTKWN CCCCHHHHHHHCCHH | 24.67 | - | |
| 44 | Phosphorylation | NKILDPPSHRLSFNP HHCCCCCCCCCCCCC | 26.99 | 25627689 | |
| 48 | Phosphorylation | DPPSHRLSFNPTLAS CCCCCCCCCCCCCCC | 23.96 | 25627689 | |
| 52 | Phosphorylation | HRLSFNPTLASVNES CCCCCCCCCCCCCHH | 35.74 | 25627689 | |
| 120 | Phosphorylation | DQLIKRNYSWDDQCS HHHHHCCCCCCCCCC | 18.38 | 29978859 | |
| 121 | Phosphorylation | QLIKRNYSWDDQCSA HHHHCCCCCCCCCCE | 27.81 | 26657352 | |
| 225 | Phosphorylation | RPKTEGRSVNHLCPT CCCCCCCCCCCCCCC | 37.82 | 29978859 | |
| 232 | Phosphorylation | SVNHLCPTSSDSLAS CCCCCCCCCCCCHHH | 39.61 | 29978859 | |
| 233 | Phosphorylation | VNHLCPTSSDSLASV CCCCCCCCCCCHHHH | 19.79 | 29978859 | |
| 234 | Phosphorylation | NHLCPTSSDSLASVC CCCCCCCCCCHHHHC | 33.43 | 29978859 | |
| 236 | Phosphorylation | LCPTSSDSLASVCSP CCCCCCCCHHHHCCH | 27.99 | 29978859 | |
| 239 | Phosphorylation | TSSDSLASVCSPSQL CCCCCHHHHCCHHHC | 29.02 | 29978859 | |
| 242 | Phosphorylation | DSLASVCSPSQLKDD CCHHHHCCHHHCCCC | 25.98 | 25159151 | |
| 257 | Phosphorylation | GSIGRDPSMSAITSL CCCCCCCCCHHHEEE | 29.65 | - | |
| 271 | Phosphorylation | LTVDSVISSQGTDGC EEHHHHHHCCCCCCC | 17.91 | - | |
| 272 | Phosphorylation | TVDSVISSQGTDGCP EHHHHHHCCCCCCCC | 22.85 | - | |
| 275 | Phosphorylation | SVISSQGTDGCPAVK HHHHCCCCCCCCCCC | 22.91 | - | |
| 287 | Phosphorylation | AVKKQENYIPDEDLT CCCCCCCCCCCHHCC | 17.06 | 27642862 | |
| 298 | Phosphorylation | EDLTGKISSPRTDLG HHCCCCCCCCCCCCC | 37.46 | 24719451 | |
| 299 | Phosphorylation | DLTGKISSPRTDLGS HCCCCCCCCCCCCCC | 23.13 | 24719451 | |
| 302 (in isoform 2) | Phosphorylation | - | 38.67 | 18669648 | |
| 302 | Phosphorylation | GKISSPRTDLGSPNS CCCCCCCCCCCCCCC | 38.67 | 22199227 | |
| 306 | Phosphorylation | SPRTDLGSPNSFSHM CCCCCCCCCCCCCCC | 28.36 | 25159151 | |
| 309 | Phosphorylation | TDLGSPNSFSHMSEG CCCCCCCCCCCCCCC | 31.35 | 22199227 | |
| 311 | Phosphorylation | LGSPNSFSHMSEGIL CCCCCCCCCCCCCEE | 20.35 | 22199227 | |
| 314 | Phosphorylation | PNSFSHMSEGILMKK CCCCCCCCCCEEECC | 27.52 | 22199227 | |
| 413 | Phosphorylation | KLNEMNDSQVNEEKE EHHHCCHHHCHHHHH | 30.90 | 21815630 | |
| 497 | Phosphorylation | FVPKTLPSKEDSVTE CCCCCCCCCCCCCCC | 52.36 | 24719451 | |
| 501 | Phosphorylation | TLPSKEDSVTEEKEI CCCCCCCCCCCHHHH | 31.84 | 28985074 | |
| 503 | Phosphorylation | PSKEDSVTEEKEIEE CCCCCCCCCHHHHHH | 42.24 | 23312004 | |
| 513 | Phosphorylation | KEIEESKSECYSNIY HHHHHHHHHHHHHHH | 42.02 | 21945579 | |
| 516 | Phosphorylation | EESKSECYSNIYEQR HHHHHHHHHHHHHHH | 10.74 | 21945579 | |
| 517 | Phosphorylation | ESKSECYSNIYEQRG HHHHHHHHHHHHHHC | 28.54 | 21945579 | |
| 520 | Phosphorylation | SECYSNIYEQRGNEA HHHHHHHHHHHCCCC | 15.40 | 21945579 | |
| 528 | Phosphorylation | EQRGNEATEGSGLLL HHHCCCCCCCCCEEE | 34.40 | 21945579 | |
| 531 | Phosphorylation | GNEATEGSGLLLNST CCCCCCCCCEEECCH | 21.75 | 21945579 | |
| 537 | Phosphorylation | GSGLLLNSTGDLMKK CCCEEECCHHHHHHH | 33.46 | 21945579 | |
| 538 | Phosphorylation | SGLLLNSTGDLMKKN CCEEECCHHHHHHHH | 33.37 | 21945579 | |
| 556 | Phosphorylation | NFCSQVPSVLGQSSP HHHHHCCHHHCCCCC | 30.99 | 22199227 | |
| 561 | Phosphorylation | VPSVLGQSSPKVVAS CCHHHCCCCCCEEEC | 46.97 | 25627689 | |
| 562 | Phosphorylation | PSVLGQSSPKVVASL CHHHCCCCCCEEECC | 22.35 | 22199227 | |
| 568 | O-linked_Glycosylation | SSPKVVASLPSISVP CCCCEEECCCCEECC | 29.24 | 23301498 | |
| 568 | Phosphorylation | SSPKVVASLPSISVP CCCCEEECCCCEECC | 29.24 | 27251275 | |
| 571 | Phosphorylation | KVVASLPSISVPFGG CEEECCCCEECCCCC | 32.56 | 27251275 | |
| 573 | Phosphorylation | VASLPSISVPFGGAR EECCCCEECCCCCCC | 28.24 | 27251275 | |
| 635 | Phosphorylation | ATNVCSPSLGNISNV CCCCCCCCCCCCCCC | 32.39 | 21659604 | |
| 668 | Phosphorylation | CLALAPDSPDNDLRA EEEECCCCCCCCCCC | 32.85 | 26657352 | |
| 681 | Phosphorylation | RAGQFGISARKPFTT CCCCCCEECCCCCCC | 23.54 | 28857561 | |
| 687 | Phosphorylation | ISARKPFTTLGEVAP EECCCCCCCCCCCCC | 29.64 | 22210691 | |
| 688 | Phosphorylation | SARKPFTTLGEVAPV ECCCCCCCCCCCCCE | 32.90 | 22210691 | |
| 1082 | Phosphorylation | MLRLGAEYRLYPCPL HHHHCCEEEEEECCC | 12.84 | 24719451 | |
| 1091 | Phosphorylation | LYPCPLFSVRFRKPL EEECCCEEEEECCCC | 21.77 | 24719451 | |
| 1198 | Phosphorylation | HNQPRKVTGASFFVF CCCCCCCCCCEEEEE | 30.02 | 28787133 | |
| 1219 | Phosphorylation | SSGYLAKSSIVEDGV CCCEECCCCCCCCCE | 21.49 | 28270605 | |
| 1220 | Phosphorylation | SGYLAKSSIVEDGVM CCEECCCCCCCCCEE | 29.91 | 28270605 | |
| 1231 | Phosphorylation | DGVMVQITAENMDSL CCEEEEEEECCHHHH | 15.72 | 28270605 | |
| 1237 | Phosphorylation | ITAENMDSLRQALRE EEECCHHHHHHHHHH | 18.06 | 28270605 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of ZFYV9_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ZFYV9_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of ZFYV9_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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