ZFYV9_HUMAN - dbPTM
ZFYV9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
26PhosphorylationFEQNEDETVSSTLLD
HHHCCCCCHHHHHHH
37.70-
28PhosphorylationQNEDETVSSTLLDTK
HCCCCCHHHHHHHCC
25.65-
30PhosphorylationEDETVSSTLLDTKWN
CCCCHHHHHHHCCHH
24.67-
44PhosphorylationNKILDPPSHRLSFNP
HHCCCCCCCCCCCCC
26.9925627689
48PhosphorylationDPPSHRLSFNPTLAS
CCCCCCCCCCCCCCC
23.9625627689
52PhosphorylationHRLSFNPTLASVNES
CCCCCCCCCCCCCHH
35.7425627689
120PhosphorylationDQLIKRNYSWDDQCS
HHHHHCCCCCCCCCC
18.3829978859
121PhosphorylationQLIKRNYSWDDQCSA
HHHHCCCCCCCCCCE
27.8126657352
225PhosphorylationRPKTEGRSVNHLCPT
CCCCCCCCCCCCCCC
37.8229978859
232PhosphorylationSVNHLCPTSSDSLAS
CCCCCCCCCCCCHHH
39.6129978859
233PhosphorylationVNHLCPTSSDSLASV
CCCCCCCCCCCHHHH
19.7929978859
234PhosphorylationNHLCPTSSDSLASVC
CCCCCCCCCCHHHHC
33.4329978859
236PhosphorylationLCPTSSDSLASVCSP
CCCCCCCCHHHHCCH
27.9929978859
239PhosphorylationTSSDSLASVCSPSQL
CCCCCHHHHCCHHHC
29.0229978859
242PhosphorylationDSLASVCSPSQLKDD
CCHHHHCCHHHCCCC
25.9825159151
257PhosphorylationGSIGRDPSMSAITSL
CCCCCCCCCHHHEEE
29.65-
271PhosphorylationLTVDSVISSQGTDGC
EEHHHHHHCCCCCCC
17.91-
272PhosphorylationTVDSVISSQGTDGCP
EHHHHHHCCCCCCCC
22.85-
275PhosphorylationSVISSQGTDGCPAVK
HHHHCCCCCCCCCCC
22.91-
287PhosphorylationAVKKQENYIPDEDLT
CCCCCCCCCCCHHCC
17.0627642862
298PhosphorylationEDLTGKISSPRTDLG
HHCCCCCCCCCCCCC
37.4624719451
299PhosphorylationDLTGKISSPRTDLGS
HCCCCCCCCCCCCCC
23.1324719451
302 (in isoform 2)Phosphorylation-38.6718669648
302PhosphorylationGKISSPRTDLGSPNS
CCCCCCCCCCCCCCC
38.6722199227
306PhosphorylationSPRTDLGSPNSFSHM
CCCCCCCCCCCCCCC
28.3625159151
309PhosphorylationTDLGSPNSFSHMSEG
CCCCCCCCCCCCCCC
31.3522199227
311PhosphorylationLGSPNSFSHMSEGIL
CCCCCCCCCCCCCEE
20.3522199227
314PhosphorylationPNSFSHMSEGILMKK
CCCCCCCCCCEEECC
27.5222199227
413PhosphorylationKLNEMNDSQVNEEKE
EHHHCCHHHCHHHHH
30.9021815630
497PhosphorylationFVPKTLPSKEDSVTE
CCCCCCCCCCCCCCC
52.3624719451
501PhosphorylationTLPSKEDSVTEEKEI
CCCCCCCCCCCHHHH
31.8428985074
503PhosphorylationPSKEDSVTEEKEIEE
CCCCCCCCCHHHHHH
42.2423312004
513PhosphorylationKEIEESKSECYSNIY
HHHHHHHHHHHHHHH
42.0221945579
516PhosphorylationEESKSECYSNIYEQR
HHHHHHHHHHHHHHH
10.7421945579
517PhosphorylationESKSECYSNIYEQRG
HHHHHHHHHHHHHHC
28.5421945579
520PhosphorylationSECYSNIYEQRGNEA
HHHHHHHHHHHCCCC
15.4021945579
528PhosphorylationEQRGNEATEGSGLLL
HHHCCCCCCCCCEEE
34.4021945579
531PhosphorylationGNEATEGSGLLLNST
CCCCCCCCCEEECCH
21.7521945579
537PhosphorylationGSGLLLNSTGDLMKK
CCCEEECCHHHHHHH
33.4621945579
538PhosphorylationSGLLLNSTGDLMKKN
CCEEECCHHHHHHHH
33.3721945579
556PhosphorylationNFCSQVPSVLGQSSP
HHHHHCCHHHCCCCC
30.9922199227
561PhosphorylationVPSVLGQSSPKVVAS
CCHHHCCCCCCEEEC
46.9725627689
562PhosphorylationPSVLGQSSPKVVASL
CHHHCCCCCCEEECC
22.3522199227
568O-linked_GlycosylationSSPKVVASLPSISVP
CCCCEEECCCCEECC
29.2423301498
568PhosphorylationSSPKVVASLPSISVP
CCCCEEECCCCEECC
29.2427251275
571PhosphorylationKVVASLPSISVPFGG
CEEECCCCEECCCCC
32.5627251275
573PhosphorylationVASLPSISVPFGGAR
EECCCCEECCCCCCC
28.2427251275
635PhosphorylationATNVCSPSLGNISNV
CCCCCCCCCCCCCCC
32.3921659604
668PhosphorylationCLALAPDSPDNDLRA
EEEECCCCCCCCCCC
32.8526657352
681PhosphorylationRAGQFGISARKPFTT
CCCCCCEECCCCCCC
23.5428857561
687PhosphorylationISARKPFTTLGEVAP
EECCCCCCCCCCCCC
29.6422210691
688PhosphorylationSARKPFTTLGEVAPV
ECCCCCCCCCCCCCE
32.9022210691
1082PhosphorylationMLRLGAEYRLYPCPL
HHHHCCEEEEEECCC
12.8424719451
1091PhosphorylationLYPCPLFSVRFRKPL
EEECCCEEEEECCCC
21.7724719451
1198PhosphorylationHNQPRKVTGASFFVF
CCCCCCCCCCEEEEE
30.0228787133
1219PhosphorylationSSGYLAKSSIVEDGV
CCCEECCCCCCCCCE
21.4928270605
1220PhosphorylationSGYLAKSSIVEDGVM
CCEECCCCCCCCCEE
29.9128270605
1231PhosphorylationDGVMVQITAENMDSL
CCEEEEEEECCHHHH
15.7228270605
1237PhosphorylationITAENMDSLRQALRE
EEECCHHHHHHHHHH
18.0628270605

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZFYV9_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PML_HUMANPMLphysical
15356634
SMAD2_HUMANSMAD2physical
9865696
SMAD3_HUMANSMAD3physical
9865696
SMAD2_HUMANSMAD2physical
18511908
PML_HUMANPMLphysical
16916642
SMAD2_HUMANSMAD2physical
16916642
RNF11_HUMANRNF11physical
23222715
STAM2_HUMANSTAM2physical
23222715
TS101_HUMANTSG101physical
23222715
SPT5H_HUMANSUPT5Hphysical
15231748
NU155_HUMANNUP155physical
15231748
BMP4_HUMANBMP4physical
15231748
PLAK_HUMANJUPphysical
15231748
ETS2_HUMANETS2physical
15231748
2AAA_HUMANPPP2R1Aphysical
15231748
CTNB1_HUMANCTNNB1physical
15231748
PP1G_HUMANPPP1CCphysical
15231748
BAG6_HUMANBAG6physical
15231748
PP1A_HUMANPPP1CAphysical
15231748
PP1B_HUMANPPP1CBphysical
15231748
IF4G1_HUMANEIF4G1physical
15231748
FHL2_HUMANFHL2physical
15231748
DAZP2_HUMANDAZAP2physical
15231748
SMAD2_HUMANSMAD2physical
15231748
FA46A_HUMANFAM46Aphysical
15231748
SCYL2_HUMANSCYL2physical
15231748
RBBP6_HUMANRBBP6physical
15231748
NIT1_HUMANNIT1physical
15231748
MIRO2_HUMANRHOT2physical
15231748
UBX11_HUMANUBXN11physical
15231748
SPART_HUMANSPG20physical
15231748
SUMF2_HUMANSUMF2physical
15231748
SVEP1_HUMANSVEP1physical
15231748
CHD6_HUMANCHD6physical
15231748
ANKL2_HUMANANKLE2physical
15231748
ERBIN_HUMANERBB2IPphysical
15231748
AMPB_HUMANRNPEPphysical
15231748
PKCB1_HUMANZMYND8physical
15231748
RNF11_HUMANRNF11physical
15231748
SMAD2_HUMANSMAD2physical
23687300
PPARG_HUMANPPARGphysical
23687300

Drug and Disease Associations
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.
Regulatory Network of ZFYV9_HUMAN

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Related Literatures of Post-Translational Modification

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