FIG4_HUMAN - dbPTM
FIG4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FIG4_HUMAN
UniProt AC Q92562
Protein Name Polyphosphoinositide phosphatase
Gene Name FIG4
Organism Homo sapiens (Human).
Sequence Length 907
Subcellular Localization Endosome membrane . Localization requires VAC14 and PIKFYVE.
Protein Description The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). In vitro, hydrolyzes all three D5-phosphorylated polyphosphoinositide substrates in the order PtdIns(4,5)P2 > PtdIns(3,5)P2 > PtdIns(3,4,5)P3. Plays a role in the biogenesis of endosome carrier vesicles (ECV) / multivesicular bodies (MVB) transport intermediates from early endosomes..
Protein Sequence MPTAAAPIISSVQKLVLYETRARYFLVGSNNAETKYRVLKIDRTEPKDLVIIDDRHVYTQQEVRELLGRLDLGNRTKMGQKGSSGLFRAVSAFGVVGFVRFLEGYYIVLITKRRKMADIGGHAIYKVEDTNMIYIPNDSVRVTHPDEARYLRIFQNVDLSSNFYFSYSYDLSHSLQYNLTVLRMPLEMLKSEMTQNRQESFDIFEDEGLITQGGSGVFGICSEPYMKYVWNGELLDIIKSTVHRDWLLYIIHGFCGQSKLLIYGRPVYVTLIARRSSKFAGTRFLKRGANCEGDVANEVETEQILCDASVMSFTAGSYSSYVQVRGSVPLYWSQDISTMMPKPPITLDQADPFAHVAALHFDQMFQRFGSPIIILNLVKEREKRKHERILSEELVAAVTYLNQFLPPEHTIVYIPWDMAKYTKSKLCNVLDRLNVIAESVVKKTGFFVNRPDSYCSILRPDEKWNELGGCVIPTGRLQTGILRTNCVDCLDRTNTAQFMVGKCALAYQLYSLGLIDKPNLQFDTDAVRLFEELYEDHGDTLSLQYGGSQLVHRVKTYRKIAPWTQHSKDIMQTLSRYYSNAFSDADRQDSINLFLGVFHPTEGKPHLWELPTDFYLHHKNTMRLLPTRRSYTYWWTPEVIKHLPLPYDEVICAVNLKKLIVKKFHKYEEEIDIHNEFFRPYELSSFDDTFCLAMTSSARDFMPKTVGIDPSPFTVRKPDETGKSVLGNKSNREEAVLQRKTAASAPPPPSEEAVSSSSEDDSGTDREEEGSVSQRSTPVKMTDAGDSAKVTENVVQPMKELYGINLSDGLSEEDFSIYSRFVQLGQSQHKQDKNSQQPCSRCSDGVIKLTPISAFSQDNIYEVQPPRVDRKSTEIFQAHIQASQGIMQPLGKEDSSMYREYIRNRYL
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
10PhosphorylationTAAAPIISSVQKLVL
CCHHHCHHHHHHHHH		25.7728188228
11PhosphorylationAAAPIISSVQKLVLY
CHHHCHHHHHHHHHH		20.4028188228
20PhosphorylationQKLVLYETRARYFLV
HHHHHHHCCCCEEEE		18.9726699800
24PhosphorylationLYETRARYFLVGSNN
HHHCCCCEEEECCCC		10.5726074081
29PhosphorylationARYFLVGSNNAETKY
CCEEEECCCCCCCEE		21.3027050516
34PhosphorylationVGSNNAETKYRVLKI
ECCCCCCCEEEEEEE		30.8526074081
35UbiquitinationGSNNAETKYRVLKID
CCCCCCCEEEEEEEC		23.67-
36PhosphorylationSNNAETKYRVLKIDR
CCCCCCEEEEEEECC		17.2426074081
47UbiquitinationKIDRTEPKDLVIIDD
EECCCCCCCEEEECC		58.42-
55MethylationDLVIIDDRHVYTQQE
CEEEECCCCCCCHHH		19.88115493089
76PhosphorylationRLDLGNRTKMGQKGS
CCCCCCCCCCCCCCH		29.4030622161
81UbiquitinationNRTKMGQKGSSGLFR
CCCCCCCCCHHHHHH		55.84-
125PhosphorylationDIGGHAIYKVEDTNM
CCCCEEEEEEECCCE		15.12-
190UbiquitinationRMPLEMLKSEMTQNR
HHHHHHHHHHHHCCC		42.9621906983
263PhosphorylationGQSKLLIYGRPVYVT
CCCEEEEECCEEEEE		13.67-
268PhosphorylationLIYGRPVYVTLIARR
EEECCEEEEEEEECC		7.15-
379UbiquitinationIIILNLVKEREKRKH
EEEHHHHHHHHHHHH		54.9722053931
425UbiquitinationMAKYTKSKLCNVLDR
HHHCCHHHHHHHHHH		59.63-
425MalonylationMAKYTKSKLCNVLDR
HHHCCHHHHHHHHHH		59.6332601280
443UbiquitinationIAESVVKKTGFFVNR
HHHHHHHHHCCCCCC		42.12-
559UbiquitinationHRVKTYRKIAPWTQH
HHHHHHHHHCCCCHH		32.57-
578PhosphorylationMQTLSRYYSNAFSDA
HHHHHHHHHHCCCCC		8.3727642862
630PhosphorylationRLLPTRRSYTYWWTP
CCCCCCCCCEEECCH		20.6628857561
631PhosphorylationLLPTRRSYTYWWTPE
CCCCCCCCEEECCHH		11.3120090780
632PhosphorylationLPTRRSYTYWWTPEV
CCCCCCCEEECCHHH		17.5728857561
658UbiquitinationICAVNLKKLIVKKFH
EEEHHHHHHHHHHHH		46.76-
704UbiquitinationSARDFMPKTVGIDPS
CCHHHCCCCCCCCCC		44.02-
721PhosphorylationTVRKPDETGKSVLGN
CEECCCCCCCCCCCC		58.2429083192
724O-linked_GlycosylationKPDETGKSVLGNKSN
CCCCCCCCCCCCCCC		24.7430620550
724PhosphorylationKPDETGKSVLGNKSN
CCCCCCCCCCCCCCC		24.7429083192
730PhosphorylationKSVLGNKSNREEAVL
CCCCCCCCCHHHHHH		45.1529083192
755PhosphorylationPPSEEAVSSSSEDDS
CCCHHHHCCCCCCCC		31.3927251275
756PhosphorylationPSEEAVSSSSEDDSG
CCHHHHCCCCCCCCC		31.1427251275
757PhosphorylationSEEAVSSSSEDDSGT
CHHHHCCCCCCCCCC		30.1827251275
758PhosphorylationEEAVSSSSEDDSGTD
HHHHCCCCCCCCCCC		47.1727251275
762PhosphorylationSSSSEDDSGTDREEE
CCCCCCCCCCCHHHC		56.7827251275
776PhosphorylationEGSVSQRSTPVKMTD
CCCCCCCCCCEEECC		29.4424719451
777PhosphorylationGSVSQRSTPVKMTDA
CCCCCCCCCEEECCC		34.0028450419
780AcetylationSQRSTPVKMTDAGDS
CCCCCCEEECCCCCC		36.9719811999
787PhosphorylationKMTDAGDSAKVTENV
EECCCCCCCCCCCCC		29.13-
819PhosphorylationEEDFSIYSRFVQLGQ
HHHHHHHHHHHHHHC		19.9924719451
830UbiquitinationQLGQSQHKQDKNSQQ
HHHCCHHHCCCCCCC		53.18-
833UbiquitinationQSQHKQDKNSQQPCS
CCHHHCCCCCCCCCC		56.88-
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 FIG4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FIG4_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 FIG4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VAC14_HUMANVAC14physical
19037259
VAC14_HUMANVAC14physical
26186194
MY18A_HUMANMYO18Aphysical
26186194
FYV1_HUMANPIKFYVEphysical
26186194
NEUA_HUMANCMASphysical
26186194
RPA43_HUMANTWISTNBphysical
26186194
FYV1_HUMANPIKFYVEphysical
28514442
SNX27_HUMANSNX27physical
28514442
Drug and Disease Associations
Kegg Disease
H00058 Amyotrophic lateral sclerosis (ALS); Lou Gehrig's disease
H00264 Charcot-Marie-Tooth disease (CMT); Hereditary motor and sensory neuropathy; Peroneal muscular atroph
OMIM Disease
611228Charcot-Marie-Tooth disease 4J (CMT4J)
612577Amyotrophic lateral sclerosis 11 (ALS11)
216340Yunis-Varon syndrome (YVS)
612691Polymicrogyria, bilateral temporooccipital (BTOP)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FIG4_HUMAN

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