FAF_DROME - dbPTM
FAF_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FAF_DROME
UniProt AC P55824
Protein Name Probable ubiquitin carboxyl-terminal hydrolase FAF
Gene Name faf
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 2778
Subcellular Localization
Protein Description Required for eye and embryo development, and plays a role in compound eye assembly and oogenesis respectively. In the larval eye disks, cells outside the assembling facets require this protein for short-range cell interactions that prevent the mystery cells from becoming photoreceptors. It is also required for nuclear migration and cellularization in early embryogenesis and could play a role in pole cell determination, development or function..
Protein Sequence MTFDTRRHTTGQPGSTAPSSSSSTTSTTTTTTSPAQSAGSGSGIGTGTGTVANSSLPGGGSGSLDGNQDQQPATDSQSSDDVAASLSANSVDSTITIVPPEKLISSFPTTKLRSLTQKISNPRWVVPVLPEQELEVLLNAAIELTQAGVDHDCEPCVEFYRNGLSTSFAKILTDEAVNSWKNNIHHCILVSCGKLLHLIAIHMQRDNPYLLDLLAIVFDPENKFNTFNAGRQPECFAAPDYIWGQLDSNKMYARPPPEPKNARGWLVDLINRFGQLGGFDNLLERFNIGLELLKRNQNKCTGKNISVEGRVENGAQDNRLTLALIHSLLRPFGQCYELLMPATIAKYFMPTWNVVLDLLDSFTDEELKREVKPEGRNDYINGIVKSARLLASRLTGQEELIRDLEMFRLKMILRLLQVSSFNGKMNALNEINKVLSSVAYFSHRSQPLPHCMPEDEMDWLTADRMAQWIKSSDVLGVVLKDSLHQPQYVEKLEKIIRFLIKEQALTLDDLDAVWRAQAGKHEAIVKNVHDLLAKLAWDFTPEQLDHLFEAFQASMTTANKRQRERLLELIRRLAEDDKNGVMAQKVLKLFWTLAHSQEVPPEVLDQALGAHVKILDYSCSQERDAQKTIWLDKCVDELKSGDGWVLPALRLIRDICCLYDTTTNHAQRTQTSTNRQQVIERLQNDYSLVILVTNSLTAYMEKVRQMVTDSPGLDATRILIDGRFPHHVQIAERLEFLKFLLKDGQLWLCADQAKQIWHCLAVNAVFPADREECFRWFGKLMGEEPDLDPGINKDFFENNILQLDPHLLTESGIKCFERFFKAVNSKEDKLKAIHRGYMLDNEDLIGKDYLWRVITTGGEEIASKAIDLLKEVSTALGPRLQENIAEFHEMFIGECCSRLRTHYGNIVILGKTQLQEELDAPDQSDNTNDESKDSKMRFIEAEKMCRILKVLQEYVKECDRSFSGDRVHLPLSRVTRGKNTILYIRFQNPGRSIDDMEIVTHSNETMAAFKRNLLKRIKGTSTANIKVDLFYANDEMIGVSDEINPLYQYTIRDKMNLTAKLTPVGTGLASSPDSSSDSSTGSPPRPCPDMQRVESESTLPGVIISQNYQYTEFFLKLYQLGSDLEHGRLRDSAKVLLHLLPCDRQTIRQLKIMCKVPKAAVTVAVTGDKIAKDEEEKLYPTEQAGIEDEEEHCTPEQMFLHPTPAQVLYNLSVLHGLLIPALDPLGESALLVQSAWMHSGCAHFVLELLTKNNFLPSADMHTKRASFQCVLRLAKLFLYIVGSVLSRVGDEPMICDLDNGSRSQVDILKQNFSTMPSSSQGTLRAISAKLAVILAREMLSASPEGDRCRTLFSSTLQWSCPDISTIKAVVQLAWASSCGNLQALGNSSGDFEDEVIVPDGQDFSMCKEALEVLTISFILNPSANEALTSDPNWPKFITSIVLKNPLRHVRQVASEQLFLASTYCAGDRRPFVYMVNLLVGALKTLVPQYESTCAEFFSVLCRTLSYGCIYNWPLQISEGLLGDEIKWLQRIRENVHATGDTQVHEELLEGHLCLAKELMFFLGADSKAQLNELIHELIDDFLFTASREFLHLRRHGSLRQDTVPPPVCRSPHTIAAACDLLIALCQLCVPNMKLLTNTLIDFVCTDTDPLREWDYLPPVGARPTKGFCGLKNAGATCYMNSVLQQLYMVPAVRVGILRAHGAATTDGEDFSGDSDLTGGGLGSALFSGPASALVSLPSSSSTIEDGLHDVRKNYHVVILKHVQAIFAHLGHSALQYYVPRGLWTHFKLLGEPVNLREQQDAVEFFMSLLESLDEGLKALGQPQLMNATLGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHSSLTESLEQYVKGELLEGADAYHCDKCDKKVVTVKRVCVKKLPPVLAIQLKRFEYDYERVCAIKFNDYFEFPRILDMEPYTVSGLAKLEGEVVEVGDNCQTNVETTKYELTGIVVHSGQASGGHYFSYILSKNPANGKCQWYKFDDGEVTECKMHEDEEMKAECFGGEYMGETYDNNLKRMQYRRQKRWWNAYMLFYTRCDQTPVQYEPSVEQLSLAESRNMVLPLPKPIERSVRHQNIRFLHSRSIFSVEFFNFIKKLVSCNLLSARSNKITPAAEELSLLGVQLASQFLFHTGFRTKKSLRGPVMEWYDALSHHIRSSALVRKWFANHALLSPPSRLGEYILMAPSPDVRTVFVKLVVFFCHFAINDEPLTGYDGANLCEQVLISVLRLLKSEAADYGKHLPHYFSLFSMYVGLGTREKQQLLRLNVPLQFIQVALDDGPGPAIKYQYPEFSKLHQVVSHLIRCSDVSEKCQSSNQNARPLSNPFKDPNVAHEELTPLSTECMDLLFNRTGYIKKVIEDTNVGDEGLKLLQYCSWENPHFSRAVLTELLWQCGFAYCHDMRHHTDLLLNILLIDDSWQHHRIHNALNGVAEEREGLLETIQRAKTHYQKRAYQIIKCLTQLFHKSPIALQMLHTNSNITRHWSIAVEWLQGELDRQRGIGCQYNSYSWSPPAQSNDNTNGYMLERSQSAKNTWSMAFELCPDEVSEKTDENNEPNLETNMDENKSEPVAQPGGVLEGSTGGTEQLPENKTPTTSSPSTAAWPARGDSNAIPRLSRQLFGAYTSTGSGSTSGGSAPTSALTTTAGSGANSETESSAQETTGETTINGLTNSLDQMEITAKKKCRRVIIKKLVESKDEEDATTATTAATTEVTTSPATAIATAATLEPAGMSELTTMVEKNLIISQENPQAKSSLQ
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
301PhosphorylationKRNQNKCTGKNISVE
HHHCCCCCCCCCEEE
53.4519429919
306PhosphorylationKCTGKNISVEGRVEN
CCCCCCCEEEEEECC
24.4122817900
924PhosphorylationELDAPDQSDNTNDES
HHCCCCCCCCCCCCC
39.9622817900
1342PhosphorylationAREMLSASPEGDRCR
HHHHHHCCCCCCHHH
21.8019429919
2614PhosphorylationEQLPENKTPTTSSPS
CCCCCCCCCCCCCCC
37.1319429919
2616PhosphorylationLPENKTPTTSSPSTA
CCCCCCCCCCCCCCC
44.5419429919
2617O-linked_GlycosylationPENKTPTTSSPSTAA
CCCCCCCCCCCCCCC
28.5420146544
2617PhosphorylationPENKTPTTSSPSTAA
CCCCCCCCCCCCCCC
28.5419429919
2618PhosphorylationENKTPTTSSPSTAAW
CCCCCCCCCCCCCCC
42.6129892262
2619PhosphorylationNKTPTTSSPSTAAWP
CCCCCCCCCCCCCCC
22.3021082442
2638PhosphorylationSNAIPRLSRQLFGAY
CCHHHHHHHHHHCEE
21.1822817900

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 FAF_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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 FAF_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CLH_DROMEChcgenetic
10725248
POK_DROMEaopgenetic
9431804
JRA_DROMEJragenetic
9431804
1433Z_DROME14-3-3zetagenetic
9431804
PSB1_DROMEProsbeta6genetic
8525378
RAS1_DROMERas85Dgenetic
9332974
UBCD1_DROMEeffgenetic
10570463
UBCD1_DROMEeffgenetic
11102374
PNT1_DROMEpntgenetic
9431804
PNT2_DROMEpntgenetic
9431804
PRI2_DROMEDNApol-alpha60genetic
11102374
DYN_DROMEshigenetic
10725248

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FAF_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-924, AND MASSSPECTROMETRY.

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