FYCO1_HUMAN - dbPTM
FYCO1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FYCO1_HUMAN
UniProt AC Q9BQS8
Protein Name FYVE and coiled-coil domain-containing protein 1
Gene Name FYCO1
Organism Homo sapiens (Human).
Sequence Length 1478
Subcellular Localization Cytoplasmic vesicle, autophagosome. Endosome. Lysosome. Localizes to the external but not to the internal membrane of autophagosomes, and upon autophagosome/late endosome/lysosome fusion, it stays on the external surface of autolysosomes.
Protein Description May mediate microtubule plus end-directed vesicle transport..
Protein Sequence MASTNAESQLQRIIRDLQDAVTELSKEFQEAGEPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGNKKDYWDYFCACLAKVKGANDGIRFVKSISELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVTSDWYYARSPFLQPKLSSDIVGQLYELTEVQFDLASRGFDLDAAWPTFARRTLTTGSSAYLWKPPSRSSSMSSLVSSYLQTQEMVSNFDLNSPLNNEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQATQNTVKELQTCLQGLELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDTKGRQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLAGPPGPELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEERWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRACFQKLSEGPGSPDSSGSGTSQGEPSPALSPASPGPQATGGQGANTDYRPPDDAVFDIITDEELCQIQESGSSLPETPTETDSLDPNAAEQDTTSTSLTPEDTEDMPVGQDSEICLLKSGELMIKVPLTVDEIASFGEGSRELFVRSSTYSLIPITVAEAGLTISWVFSSDPKSISFSVVFQEAEDTPLDQCKVLIPTTRCNSHKENIQGQLKVRTPGIYMLIFDNTFSRFVSKKVFYHLTVDRPVIYDGSDFL
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
2Acetylation------MASTNAESQ
------CCCCCHHHH		36.0522223895
3Phosphorylation-----MASTNAESQL
-----CCCCCHHHHH		33.7728857561
4Phosphorylation----MASTNAESQLQ
----CCCCCHHHHHH		45.5728857561
8PhosphorylationMASTNAESQLQRIIR
CCCCCHHHHHHHHHH		33.5129255136
22PhosphorylationRDLQDAVTELSKEFQ
HHHHHHHHHHHHHHH		32.6920860994
25PhosphorylationQDAVTELSKEFQEAG
HHHHHHHHHHHHHCC		24.7320860994
44UbiquitinationDDSTSLHKFSYKLEY
CCCCCHHHHHHHHHH		41.1029967540
46PhosphorylationSTSLHKFSYKLEYLL
CCCHHHHHHHHHHHH		26.5929496963
67UbiquitinationKATLLGNKKDYWDYF
HHHHCCCCHHHHHHH		45.2729967540
92UbiquitinationNDGIRFVKSISELRT
CCHHHHHHHHHHHHH		39.08-
92UbiquitinationNDGIRFVKSISELRT
CCHHHHHHHHHHHHH		39.0829967540
95PhosphorylationIRFVKSISELRTSLG
HHHHHHHHHHHHHCC		37.3624719451
129UbiquitinationQQCFMNTKVTSDWYY
HHHHHCCCCCCCCEE		38.21-
129UbiquitinationQQCFMNTKVTSDWYY
HHHHHCCCCCCCCEE		38.21-
148PhosphorylationFLQPKLSSDIVGQLY
CCCCCCCCCHHHHHH		41.6232142685
156PhosphorylationDIVGQLYELTEVQFD
CHHHHHHHHHHCCHH		58.7832142685
182PhosphorylationWPTFARRTLTTGSSA
CCCCCCCCCCCCCCC		23.9323403867
184PhosphorylationTFARRTLTTGSSAYL
CCCCCCCCCCCCCEE		28.6223403867
185PhosphorylationFARRTLTTGSSAYLW
CCCCCCCCCCCCEEC		37.8723403867
187PhosphorylationRRTLTTGSSAYLWKP
CCCCCCCCCCEECCC		15.0923403867
188PhosphorylationRTLTTGSSAYLWKPP
CCCCCCCCCEECCCC		23.4423403867
190PhosphorylationLTTGSSAYLWKPPSR
CCCCCCCEECCCCCC		18.2923403867
193UbiquitinationGSSAYLWKPPSRSSS
CCCCEECCCCCCCCC		44.44-
193UbiquitinationGSSAYLWKPPSRSSS
CCCCEECCCCCCCCC		44.44-
196PhosphorylationAYLWKPPSRSSSMSS
CEECCCCCCCCCHHH		54.0122167270
198PhosphorylationLWKPPSRSSSMSSLV
ECCCCCCCCCHHHHH		30.9727251275
199PhosphorylationWKPPSRSSSMSSLVS
CCCCCCCCCHHHHHH		29.0227251275
200PhosphorylationKPPSRSSSMSSLVSS
CCCCCCCCHHHHHHH		24.7527251275
202PhosphorylationPSRSSSMSSLVSSYL
CCCCCCHHHHHHHHH		23.5927251275
203PhosphorylationSRSSSMSSLVSSYLQ
CCCCCHHHHHHHHHH		24.9327251275
206PhosphorylationSSMSSLVSSYLQTQE
CCHHHHHHHHHHHHH		20.6822210691
216PhosphorylationLQTQEMVSNFDLNSP
HHHHHHHHCCCCCCC		30.3922210691
216UbiquitinationLQTQEMVSNFDLNSP
HHHHHHHHCCCCCCC		30.3933845483
268PhosphorylationQELRAAVSQQGEQLQ
HHHHHHHHHHHHHHH		16.4424719451
276PhosphorylationQQGEQLQTERERGRT
HHHHHHHHHHHHCCC		45.6724719451
305PhosphorylationLQKQWEVTQATQNTV
HHHHHHHHHHHHHHH		10.8529116813
308PhosphorylationQWEVTQATQNTVKEL
HHHHHHHHHHHHHHH		16.7229116813
317PhosphorylationNTVKELQTCLQGLEL
HHHHHHHHHHHHHHH		28.0123403867
342PhosphorylationTALRRLESMLQPLAQ
HHHHHHHHHHHHHHH		29.4126657352
357PhosphorylationELEATRDSLDKKNQH
HHHHHHHHHHHHHHH		34.8727535140
367PhosphorylationKKNQHLASFPGWLAM
HHHHHHHCCHHHHHH		38.03-
368UbiquitinationKNQHLASFPGWLAMA
HHHHHHCCHHHHHHH		5.5833845483
376UbiquitinationPGWLAMAQQKADTAS
HHHHHHHHHHCCCCC		32.0233845483
381PhosphorylationMAQQKADTASDTKGR
HHHHHCCCCCCCCCC		32.68-
416UbiquitinationALERERTKVEEVNRQ
HHHHHHHHHHHHHHH		54.6033845483
501UbiquitinationKKQQQEEKELLEQEV
HHHHHHHHHHHHHHH		53.5624816145
547PhosphorylationIQDKDHLSQQVGMLE
HCCHHHHHHHHHHHH		18.36-
579PhosphorylationEALVPVNSSLQEAWG
CCEEECCCHHHHHHC		32.4325850435
580PhosphorylationALVPVNSSLQEAWGK
CEEECCCHHHHHHCC		28.9425850435
598UbiquitinationEQRGLQEAQLDDTKV
HHHCCHHHCCCCCCC		11.4132015554
603PhosphorylationQEAQLDDTKVQEGSQ
HHHCCCCCCCCCCCH		32.5523312004
609PhosphorylationDTKVQEGSQEEELRQ
CCCCCCCCHHHHHHH		33.4025159151
623UbiquitinationQANRELEKELQNVVG
HHHHHHHHHHHHHHC		76.0929967540
646PhosphorylationLQALQADYQALQQRE
HHHHHHHHHHHHHHH		9.9427461979
662PhosphorylationAIQGSLASLEAEQAS
HHHHHHHHHHHHHHH		31.8427251275
735PhosphorylationRELRALESQCQQQTQ
HHHHHHHHHHHHHHH		36.7927251275
750UbiquitinationLIEVLTAEKGQQGVG
HHHHHHHCCCCCCCC		53.1132015554
758UbiquitinationKGQQGVGPPTDNEAR
CCCCCCCCCCCHHHH		26.6432015554
798UbiquitinationQVVDLQAKMRAALDD
HHHHHHHHHHHHCCC		18.8932015554
811PhosphorylationDDQDKVQSQLSMAEA
CCHHHHHHHHHHHHH		35.7629978859
814PhosphorylationDKVQSQLSMAEAVLR
HHHHHHHHHHHHHHH		14.3329978859
849PhosphorylationVQELLQCSEREGALQ
HHHHHHHHHHHCHHH		27.0823312004
878PhosphorylationRALQEELSQAKCSSE
HHHHHHHHHHHCCCH		31.2217525332
883PhosphorylationELSQAKCSSEEAQLE
HHHHHHCCCHHHHHH		39.8328348404
884PhosphorylationLSQAKCSSEEAQLEH
HHHHHCCCHHHHHHH		49.2628348404
969MalonylationQEKLKAAKAAAGSLP
HHHHHHHHHHHCCCH		43.3426320211
1136PhosphorylationDLNRTKKYLEERLIE
HHHHHHHHHHHHHHH		22.39-
1155PhosphorylationKDALWQKSDALEFQQ
CCHHHCCCHHHHHHH		17.0226437602
1165PhosphorylationLEFQQKLSAEERWLG
HHHHHHHCHHHHHCC		40.4421815630
1343PhosphorylationSEICLLKSGELMIKV
CEEEEEECCCEEEEE		37.1529255136
1427PhosphorylationIPTTRCNSHKENIQG
EECCCCCCCCHHCCC		39.29-
1451PhosphorylationYMLIFDNTFSRFVSK
EEEEECCCCHHHCCC		25.4924972180
1453PhosphorylationLIFDNTFSRFVSKKV
EEECCCCHHHCCCHH		23.8324972180
1472PhosphorylationTVDRPVIYDGSDFL-
ECCCCEEECCCCCC-		17.93-
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 FYCO1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FYCO1_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 FYCO1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MIC1_HUMANC18orf8physical
20562859
CCZ1B_HUMANCCZ1physical
20562859
CCZ1_HUMANCCZ1physical
20562859
MAP4_HUMANMAP4physical
20562859
MON1B_HUMANMON1Bphysical
20562859
LMNA_HUMANLMNAphysical
20562859
RFA2_HUMANRPA2physical
20562859
LAP2A_HUMANTMPOphysical
20562859
LAP2B_HUMANTMPOphysical
20562859
RFA1_HUMANRPA1physical
20562859
SC23B_HUMANSEC23Bphysical
20562859
SC24B_HUMANSEC24Bphysical
20562859
CCAR1_HUMANCCAR1physical
20562859
FOXK1_HUMANFOXK1physical
20562859
RFA3_HUMANRPA3physical
20562859
EMD_HUMANEMDphysical
20562859
KINH_HUMANKIF5Bphysical
20562859
KIF23_HUMANKIF23physical
20562859
A4_HUMANAPPphysical
21832049
KDM1A_HUMANKDM1Aphysical
23455924
ANM6_HUMANPRMT6physical
23455924
TCPH_HUMANCCT7physical
26186194
TCPW_HUMANCCT6Bphysical
26186194
TCPZ_HUMANCCT6Aphysical
26186194
TCPB_HUMANCCT2physical
26186194
TCPG_HUMANCCT3physical
26186194
DTNA_HUMANDTNAphysical
26186194
TCPA_HUMANTCP1physical
26186194
DCMC_HUMANMLYCDphysical
26186194
SAS6_HUMANSASS6physical
26186194
PEPL_HUMANPPLphysical
26496610
DDX60_HUMANDDX60physical
26496610
GOPC_HUMANGOPCphysical
26496610
NOL9_HUMANNOL9physical
26496610
PDIP3_HUMANPOLDIP3physical
26496610
AEDO_HUMANADOphysical
26496610
RFT1_HUMANRFT1physical
26496610
DCMC_HUMANMLYCDphysical
28514442
SAS6_HUMANSASS6physical
28514442
DTNA_HUMANDTNAphysical
28514442
TCPZ_HUMANCCT6Aphysical
28514442
TCPG_HUMANCCT3physical
28514442
TCPB_HUMANCCT2physical
28514442
TCPA_HUMANTCP1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610019Cataract 18 (CTRCT18)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FYCO1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-878, AND MASSSPECTROMETRY.

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