FBF1_HUMAN - dbPTM
FBF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FBF1_HUMAN
UniProt AC Q8TES7
Protein Name Fas-binding factor 1
Gene Name FBF1
Organism Homo sapiens (Human).
Sequence Length 1133
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasm, cytoskeleton, spindle pole. Cell junction. Localizes specifically to the distal appendage region of the centriole, which anchors the mother centriole to the pla
Protein Description Keratin-binding protein required for epithelial cell polarization. Involved in apical junction complex (AJC) assembly via its interaction with PARD3. Required for ciliogenesis..
Protein Sequence MAPKTKKGCKVTLPEKPVKLASHTRDTTGVSQMFPSSKARTKSLLGDDVFSTMAGLEEADAEVSGISEADPQALLQAMKDLDGMDADILGLKKSNSAPSKKAAKDPGKGELPNHPKPAGGAIPTKKSLPSPSSSGHQNRRFSSEDLEDPLRGLLSYDEGGITKQPPVTQSKTASDKSPSTVRDQGPSIPLTPGDTPIRKKEELLFDDGDDIMATLGFGDSPKAEKRQIGDQEGPRPARSTLDELLGRGMATKLLARPGTGEHREFKLDKKYQRPQDSEDMWGDEDFTFGAYQPTVVSSEGRQSRRQSVSRFFADSGADPKGEPGSKQSPPMASSPIQPRKGGADWLGLKDEDLDLFPASPTREAHRESSVPVTPSVPPPASQHSTPAGLPPSRAKPPTEGAGSPAKASQASKLRASKEEKEDWLSHALSRKKSQGLAREQHAGTSEGLHLAGTAGHPPSGSQPLTSTQGLEHAAAGGSSGTTARERPCVRPGVSGSPVTQNHAASALPTGSPKRGTAPGDLSATEPATCFPSTQKPTEPSVPVQPLLPESLARSLLPSTEYQKQLLAAQVQLQCSPAELQAELLHSQARLAELEAQVRKLELERAQHELLLGSLQQQHQADLELIESAHRSRIKVLETSYQQREERLRRENEELSARYLSQCQEAEQARAELTAQHQRRLAAIAQEKDQEMERLRELQRASILDMRRDHEEQLQRLKLLKDREVDAATSATSHTRSLNSIIHQMEKFSSSLHELSSRVEASHLTTSQERELGIRQRDEQLRALQERLGQQQRDMEEERSRQQEVIGKMEARLNEQSRLLEQERWRVTAEQSKAESMQRALEEQRKVTAQQMAMERAELERAKSALLEEQKSVMLKCGEERRRLAAEWAEFSAQQKLSKERAEREAERALQVDTQREGTLISLAKQAELKIRASELRAEEKQLAAERAALEQERQELRLEKERINATALRVKLRAEEVESMSKVASEKYEEGERALREAQQVQAEQQARLQAVQQQQERLRKQEQHMHQEHLSLAQQRLQLDRARQDLPSSLVGLFPRAQGPAASSQSALMPPAPTTRWCSQPPTGLDPSPLHLHARLALLRHMAEQDRDFLENEQFFLETLKKGSYNLTSHSA
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
22PhosphorylationEKPVKLASHTRDTTG
CCCCEECCCCCCCCC		35.5122210691
27PhosphorylationLASHTRDTTGVSQMF
ECCCCCCCCCCHHHC		23.35-
36PhosphorylationGVSQMFPSSKARTKS
CCHHHCCCCHHHHHH		32.9522210691
96PhosphorylationLGLKKSNSAPSKKAA
HCCCCCCCCCCHHHC		48.9629743597
99PhosphorylationKKSNSAPSKKAAKDP
CCCCCCCCHHHCCCC		46.6425072903
127PhosphorylationGAIPTKKSLPSPSSS
CCCCCCCCCCCCCCC		47.2528555341
130PhosphorylationPTKKSLPSPSSSGHQ
CCCCCCCCCCCCCCC		42.5825159151
132PhosphorylationKKSLPSPSSSGHQNR
CCCCCCCCCCCCCCC		41.2825159151
134PhosphorylationSLPSPSSSGHQNRRF
CCCCCCCCCCCCCCC		44.63-
142PhosphorylationGHQNRRFSSEDLEDP
CCCCCCCCHHHCCCH		30.8930266825
143PhosphorylationHQNRRFSSEDLEDPL
CCCCCCCHHHCCCHH		32.2030266825
168PhosphorylationITKQPPVTQSKTASD
CCCCCCCCCCCCCCC		32.6623684312
170PhosphorylationKQPPVTQSKTASDKS
CCCCCCCCCCCCCCC		23.7023684312
177PhosphorylationSKTASDKSPSTVRDQ
CCCCCCCCCCCCCCC		29.1328348404
180PhosphorylationASDKSPSTVRDQGPS
CCCCCCCCCCCCCCC		23.97-
191PhosphorylationQGPSIPLTPGDTPIR
CCCCCCCCCCCCCCC		21.6325159151
195PhosphorylationIPLTPGDTPIRKKEE
CCCCCCCCCCCCHHH		26.9125159151
247MethylationTLDELLGRGMATKLL
HHHHHHCCCHHHHHH		31.51-
315PhosphorylationVSRFFADSGADPKGE
HHHHHHCCCCCCCCC		32.2422985185
325PhosphorylationDPKGEPGSKQSPPMA
CCCCCCCCCCCCCCC		37.9328985074
327PhosphorylationKGEPGSKQSPPMASS
CCCCCCCCCCCCCCC		63.9719413330
328PhosphorylationGEPGSKQSPPMASSP
CCCCCCCCCCCCCCC		34.4123090842
333PhosphorylationKQSPPMASSPIQPRK
CCCCCCCCCCCCCCC		30.3225159151
334PhosphorylationQSPPMASSPIQPRKG
CCCCCCCCCCCCCCC		19.2427050516
340AcetylationSSPIQPRKGGADWLG
CCCCCCCCCCCCCCC		69.277675471
359PhosphorylationDLDLFPASPTREAHR
CCCCCCCCCCHHHHH		27.3528985074
361PhosphorylationDLFPASPTREAHRES
CCCCCCCCHHHHHHC		38.3527732954
368PhosphorylationTREAHRESSVPVTPS
CHHHHHHCCCCCCCC		36.27-
373PhosphorylationRESSVPVTPSVPPPA
HHCCCCCCCCCCCCC		12.0828985074
375PhosphorylationSSVPVTPSVPPPASQ
CCCCCCCCCCCCCCC		37.58-
381PhosphorylationPSVPPPASQHSTPAG
CCCCCCCCCCCCCCC		33.91-
384PhosphorylationPPPASQHSTPAGLPP
CCCCCCCCCCCCCCH		28.5728985074
385PhosphorylationPPASQHSTPAGLPPS
CCCCCCCCCCCCCHH		18.29-
398PhosphorylationPSRAKPPTEGAGSPA
HHHCCCCCCCCCCHH		56.4228102081
403PhosphorylationPPTEGAGSPAKASQA
CCCCCCCCHHHHHHH		22.5828985074
408PhosphorylationAGSPAKASQASKLRA
CCCHHHHHHHHHHHC		26.10-
433PhosphorylationHALSRKKSQGLAREQ
HHHHHHHHHCCHHHH		32.30-
494PhosphorylationPCVRPGVSGSPVTQN
CCCCCCCCCCCCCCC		39.2029449344
496PhosphorylationVRPGVSGSPVTQNHA
CCCCCCCCCCCCCCC		14.5322210691
499PhosphorylationGVSGSPVTQNHAASA
CCCCCCCCCCCCHHC		27.3423312004
505PhosphorylationVTQNHAASALPTGSP
CCCCCCHHCCCCCCC		30.9927732954
509PhosphorylationHAASALPTGSPKRGT
CCHHCCCCCCCCCCC		51.6627732954
511PhosphorylationASALPTGSPKRGTAP
HHCCCCCCCCCCCCC		29.7127732954
575PhosphorylationAQVQLQCSPAELQAE
HHHHHCCCHHHHHHH		17.74-
701PhosphorylationLRELQRASILDMRRD
HHHHHHHHHHHHCCC		26.3529970186
731PhosphorylationVDAATSATSHTRSLN
CCHHHHCCHHHHHHH		22.3229116813
732PhosphorylationDAATSATSHTRSLNS
CHHHHCCHHHHHHHH		23.6828985074
736PhosphorylationSATSHTRSLNSIIHQ
HCCHHHHHHHHHHHH		32.8129978859
739PhosphorylationSHTRSLNSIIHQMEK
HHHHHHHHHHHHHHH		28.3629978859
756PhosphorylationSSLHELSSRVEASHL
HHHHHHHHHHHHHHC		53.63-
835PhosphorylationAEQSKAESMQRALEE
HHHHHHHHHHHHHHH		25.6929116813
863PhosphorylationAELERAKSALLEEQK
HHHHHHHHHHHHHHH		24.14-
933PhosphorylationAELKIRASELRAEEK
HHHHHHHHHHHHHHH		27.58-
960SumoylationRQELRLEKERINATA
HHHHHHHHHHHCHHH		57.8128112733
1064PhosphorylationRAQGPAASSQSALMP
CCCCCCCCCCCCCCC		30.8929083192
1065PhosphorylationAQGPAASSQSALMPP
CCCCCCCCCCCCCCC		24.3529083192
1067PhosphorylationGPAASSQSALMPPAP
CCCCCCCCCCCCCCC		25.8929083192
1075PhosphorylationALMPPAPTTRWCSQP
CCCCCCCCCCCCCCC		30.9729083192
1076PhosphorylationLMPPAPTTRWCSQPP
CCCCCCCCCCCCCCC		22.5529083192
1120PhosphorylationNEQFFLETLKKGSYN
HCHHHHHHHHHCCCC		46.1325954137
1132PhosphorylationSYNLTSHSA------
CCCCCCCCC------		35.1327251275
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 FBF1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FBF1_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 FBF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IFT20_HUMANIFT20physical
16189514
A4_HUMANAPPphysical
21832049
ADIP_HUMANSSX2IPphysical
25416956
K1C40_HUMANKRT40physical
25416956
TTC32_HUMANTTC32physical
25416956
MIPO1_HUMANMIPOL1physical
25416956
DEUP1_HUMANCCDC67physical
25416956
ABLM1_HUMANABLIM1physical
26638075
ACDSB_HUMANACADSBphysical
26638075
PUR8_HUMANADSLphysical
26638075
AGK_HUMANAGKphysical
26638075
CP131_HUMANCEP131physical
26638075
BCAS3_HUMANBCAS3physical
26638075
TM256_HUMANTMEM256physical
26638075
CBL_HUMANCBLphysical
26638075
C2D1A_HUMANCC2D1Aphysical
26638075
CC85C_HUMANCCDC85Cphysical
26638075
CCNB1_HUMANCCNB1physical
26638075
CE170_HUMANCEP170physical
26638075
CEP85_HUMANCEP85physical
26638075
CLH1_HUMANCLTCphysical
26638075
CPVL_HUMANCPVLphysical
26638075
CSPP1_HUMANCSPP1physical
26638075
CTBP1_HUMANCTBP1physical
26638075
CATB_HUMANCTSBphysical
26638075
DYN2_HUMANDNM2physical
26638075
DNMBP_HUMANDNMBPphysical
26638075
4ET_HUMANEIF4ENIF1physical
26638075
RB6I2_HUMANERC1physical
26638075
WAC2A_HUMANFAM21Aphysical
26638075
FLOT1_HUMANFLOT1physical
26638075
GARS_HUMANGARSphysical
26638075
GCC1_HUMANGCC1physical
26638075
GPTC1_HUMANGPATCH1physical
26638075
GRB2_HUMANGRB2physical
26638075
HAUS3_HUMANHAUS3physical
26638075
HAUS6_HUMANHAUS6physical
26638075
HAUS8_HUMANHAUS8physical
26638075
HXK1_HUMANHK1physical
26638075
HYOU1_HUMANHYOU1physical
26638075
IFT74_HUMANIFT74physical
26638075
IFT81_HUMANIFT81physical
26638075
IF2B2_HUMANIGF2BP2physical
26638075
ITSN2_HUMANITSN2physical
26638075
LASP1_HUMANLASP1physical
26638075
MGST3_HUMANMGST3physical
26638075
MYBPP_HUMANMYCBPAPphysical
26638075
NEDD1_HUMANNEDD1physical
26638075
NMT1_HUMANNMT1physical
26638075
NNTM_HUMANNNTphysical
26638075
NRBF2_HUMANNRBF2physical
26638075
5NTC_HUMANNT5C2physical
26638075
PCM1_HUMANPCM1physical
26638075
PEA15_HUMANPEA15physical
26638075
PLK1_HUMANPLK1physical
26638075
PRKRA_HUMANPRKRAphysical
26638075
SCFD1_HUMANSCFD1physical
26638075
SCLT1_HUMANSCLT1physical
26638075
SDCG3_HUMANSDCCAG3physical
26638075
C560_HUMANSDHCphysical
26638075
SC24B_HUMANSEC24Bphysical
26638075
SIR2_HUMANSIRT2physical
26638075
SNX9_HUMANSNX9physical
26638075
SRBS1_HUMANSORBS1physical
26638075
SRSF2_HUMANSRSF2physical
26638075
ADIP_HUMANSSX2IPphysical
26638075
STAM1_HUMANSTAMphysical
26638075
STAM2_HUMANSTAM2physical
26638075
STT3B_HUMANSTT3Bphysical
26638075
ZO1_HUMANTJP1physical
26638075
ZO2_HUMANTJP2physical
26638075
TNIP1_HUMANTNIP1physical
26638075
TNR6B_HUMANTNRC6Bphysical
26638075
ASPP2_HUMANTP53BP2physical
26638075
TRI26_HUMANTRIM26physical
26638075
EFTS_HUMANTSFMphysical
26638075
TTL12_HUMANTTLL12physical
26638075
TXLNA_HUMANTXLNAphysical
26638075
TXLNG_HUMANTXLNGphysical
26638075
UN45A_HUMANUNC45Aphysical
26638075
VINC_HUMANVCLphysical
26638075
WDR83_HUMANWDR83physical
26638075
SYYM_HUMANYARS2physical
26638075
CHSP1_HUMANCARHSP1physical
26638075
FKB15_HUMANFKBP15physical
26638075
LZTS2_HUMANLZTS2physical
26638075
OFD1_HUMANOFD1physical
26638075
PDIA3_HUMANPDIA3physical
26638075
KAPCA_HUMANPRKACAphysical
26638075
PSMD7_HUMANPSMD7physical
26638075
RAB2A_HUMANRAB2Aphysical
26638075
RAB7A_HUMANRAB7Aphysical
26638075
SCRIB_HUMANSCRIBphysical
26638075
SPTN5_HUMANSPTBN5physical
26638075
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 FBF1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328 AND SER-334, ANDMASS SPECTROMETRY.

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