FMNL3_HUMAN - dbPTM
FMNL3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FMNL3_HUMAN
UniProt AC Q8IVF7
Protein Name Formin-like protein 3
Gene Name FMNL3
Organism Homo sapiens (Human).
Sequence Length 1028
Subcellular Localization Cytoplasm . Cell membrane
Lipid-anchor . Enriched in lamellipodia.
Protein Description Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. Required for developmental angiogenesis (By similarity). In this process, required for microtubule reorganization and for efficient endothelial cell elongation. In quiescent endothelial cells, triggers rearrangement of the actin cytoskeleton, but does not alter microtubule alignement..
Protein Sequence MGNLESAEGVPGEPPSVPLLLPPGKMPMPEPCELEERFALVLSSMNLPPDKARLLRQYDNEKKWDLICDQERFQVKNPPHTYIQKLQSFLDPSVTRKKFRRRVQESTKVLRELEISLRTNHIGWVREFLNDENKGLDVLVDYLSFAQCSVMFDFEGLESGDDGAFDKLRSWSRSIEDLQPPSALSAPFTNSLARSARQSVLRYSTLPGRRALKNSRLVSQKDDVHVCILCLRAIMNYQYGFNLVMSHPHAVNEIALSLNNKNPRTKALVLELLAAVCLVRGGHEIILAAFDNFKEVCKELHRFEKLMEYFRNEDSNIDFMVACMQFINIVVHSVEDMNFRVHLQYEFTKLGLEEFLQKSRHTESEKLQVQIQAYLDNVFDVGGLLEDAETKNVALEKVEELEEHVSHLTEKLLDLENENMMRVAELEKQLLQREKELESIKETYENTSHQVHTLRRLIKEKEEAFQRRCHLEPNVRGLESVDSEALARVGPAELSEGMPPSDLDLLAPAPPPEEVLPLPPPPAPPLPPPPPPLPDKCPPAPPLPGAAPSVVLTVGLSAIRIKKPIKTKFRLPVFNWTALKPNQISGTVFSELDDEKILEDLDLDKFEELFKTKAQGPALDLICSKNKTAQKAASKVTLLEANRAKNLAITLRKAGRSAEEICRAIHTFDLQTLPVDFVECLMRFLPTEAEVKLLRQYERERQPLEELAAEDRFMLLFSKVERLTQRMAGMAFLGNFQDNLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNSSKRGAVYGFKLQSLDLLLDTKSTDRKMTLLHFIALTVKEKYPDLANFWHELHFVEKAAAVSLENVLLDVKELGRGMELIRRECSIHDNSVLRNFLSTNEGKLDKLQRDAKTAEEAYNAVVRYFGESPKTTPPSVFFPVFVRFIRSYKEAEQENEARKKQEEVMREKQLAQEAKKLDAKTPSQRNKWQQQELIAELRRRQAKEHRPVYEGKDGTIEDIITVLKSVPFTARTAKRGSRFFCDAAHHDESNC
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
2N-myristoyl glycine------MGNLESAEG
------CCCCCCCCC		59.75-
2Myristoylation------MGNLESAEG
------CCCCCCCCC		59.7520213681
6Phosphorylation--MGNLESAEGVPGE
--CCCCCCCCCCCCC		34.4824850871
16PhosphorylationGVPGEPPSVPLLLPP
CCCCCCCCCCEECCC		47.2724850871
58PhosphorylationKARLLRQYDNEKKWD
HHHHHHHHCCCCCCE		17.8220068231
88PhosphorylationTYIQKLQSFLDPSVT
HHHHHHHHHCCHHHC		37.9121406692
93PhosphorylationLQSFLDPSVTRKKFR
HHHHCCHHHCHHHHH		35.4730266825
93 (in isoform 3)Phosphorylation-35.4727251275
95PhosphorylationSFLDPSVTRKKFRRR
HHCCHHHCHHHHHHH		40.9030266825
170PhosphorylationGAFDKLRSWSRSIED
CHHHHHHHHHHCHHH		39.5829514088
172PhosphorylationFDKLRSWSRSIEDLQ
HHHHHHHHHCHHHCC		19.8629514088
174PhosphorylationKLRSWSRSIEDLQPP
HHHHHHHCHHHCCCC		25.4730266825
174 (in isoform 3)Phosphorylation-25.4724719451
182PhosphorylationIEDLQPPSALSAPFT
HHHCCCCCHHCCCCC		48.8330266825
185PhosphorylationLQPPSALSAPFTNSL
CCCCCHHCCCCCHHH		33.3429255136
189 (in isoform 3)Phosphorylation-23.8827251275
189PhosphorylationSALSAPFTNSLARSA
CHHCCCCCHHHHHHH		23.8829255136
191PhosphorylationLSAPFTNSLARSARQ
HCCCCCHHHHHHHHH		21.9829255136
199PhosphorylationLARSARQSVLRYSTL
HHHHHHHHHHHHCCC		19.9828348404
199 (in isoform 3)Phosphorylation-19.9827251275
203PhosphorylationARQSVLRYSTLPGRR
HHHHHHHHCCCCCHH		11.2226657352
204PhosphorylationRQSVLRYSTLPGRRA
HHHHHHHCCCCCHHH		19.6226657352
205PhosphorylationQSVLRYSTLPGRRAL
HHHHHHCCCCCHHHH		28.2123403867
255UbiquitinationPHAVNEIALSLNNKN
HHHHHHHHHHCCCCC		5.7323000965
307UbiquitinationLHRFEKLMEYFRNED
HHHHHHHHHHHHCCC		6.0923000965
326UbiquitinationFMVACMQFINIVVHS
HHHHHHHHHHHHEEC		1.5123000965
330UbiquitinationCMQFINIVVHSVEDM
HHHHHHHHEECHHHC		2.4723000965
333UbiquitinationFINIVVHSVEDMNFR
HHHHHEECHHHCCCE		18.6523000965
358UbiquitinationGLEEFLQKSRHTESE
CHHHHHHHCCCCCCH		52.1623000965
377UbiquitinationQIQAYLDNVFDVGGL
HHHHHHCCCCCCCCH		33.4923000965
443PhosphorylationELESIKETYENTSHQ
HHHHHHHHHHCCHHH		31.0023663014
444PhosphorylationLESIKETYENTSHQV
HHHHHHHHHCCHHHH		14.3123663014
447PhosphorylationIKETYENTSHQVHTL
HHHHHHCCHHHHHHH		18.6923663014
448PhosphorylationKETYENTSHQVHTLR
HHHHHCCHHHHHHHH		24.4123663014
453 (in isoform 3)Phosphorylation-24.0927251275
453PhosphorylationNTSHQVHTLRRLIKE
CCHHHHHHHHHHHHH		24.0923663014
480PhosphorylationPNVRGLESVDSEALA
CCCCCCCCCCHHHHH		35.9527470641
624PhosphorylationPALDLICSKNKTAQK
CHHHHHCCCCHHHHH		32.0627251275
624 (in isoform 3)Phosphorylation-32.0627251275
628O-linked_GlycosylationLICSKNKTAQKAASK
HHCCCCHHHHHHHHH		43.6530379171
645UbiquitinationLLEANRAKNLAITLR
HHHHHHHHHHHHHHH		49.62-
672PhosphorylationIHTFDLQTLPVDFVE
HHHCCCCCCCCCHHH		40.08-
687PhosphorylationCLMRFLPTEAEVKLL
HHHHHCCCHHHHHHH		50.39-
697PhosphorylationEVKLLRQYERERQPL
HHHHHHHHHHHCCCH		15.54-
718PhosphorylationDRFMLLFSKVERLTQ
HHHHHHHHHHHHHHH		35.4424719451
776PhosphorylationIILALGNYMNSSKRG
HHHHHHHHHCCCCCC		8.89-
779PhosphorylationALGNYMNSSKRGAVY
HHHHHHCCCCCCCCC		22.24-
780PhosphorylationLGNYMNSSKRGAVYG
HHHHHCCCCCCCCCE		22.74-
786PhosphorylationSSKRGAVYGFKLQSL
CCCCCCCCEEEHHHC		19.13-
799PhosphorylationSLDLLLDTKSTDRKM
HCCEEECCCCCCCHH		27.19-
807PhosphorylationKSTDRKMTLLHFIAL
CCCCCHHHHHHHHHH		29.2427499020
815PhosphorylationLLHFIALTVKEKYPD
HHHHHHHHHHHHCCC		22.1027499020
958PhosphorylationAKKLDAKTPSQRNKW
HHHCCCCCHHHCCHH		29.8723403867
960PhosphorylationKLDAKTPSQRNKWQQ
HCCCCCHHHCCHHHH		47.1824719451
992PhosphorylationVYEGKDGTIEDIITV
CCCCCCCCHHHHHHH		31.1829514088
1002O-linked_GlycosylationDIITVLKSVPFTART
HHHHHHHHCCCCHHC		30.7530379171
1009O-linked_GlycosylationSVPFTARTAKRGSRF
HCCCCHHCCCCCCCE		33.7830379171
1014PhosphorylationARTAKRGSRFFCDAA
HHCCCCCCCEECCCC		29.9227422710
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 FMNL3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FMNL3_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 FMNL3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
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 FMNL3_HUMAN

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Related Literatures of Post-Translational Modification
Myristoylation
ReferencePubMed
"Strategy for comprehensive identification of human N-myristoylatedproteins using an insect cell-free protein synthesis system.";
Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,Tsunasawa S., Utsumi T.;
Proteomics 10:1780-1793(2010).
Cited for: MYRISTOYLATION AT GLY-2.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174, AND MASSSPECTROMETRY.

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