FMN1_HUMAN - dbPTM
FMN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FMN1_HUMAN
UniProt AC Q68DA7
Protein Name Formin-1
Gene Name FMN1
Organism Homo sapiens (Human).
Sequence Length 1419
Subcellular Localization Nucleus. Cytoplasm. Cell junction, adherens junction. Cell membrane
Peripheral membrane protein
Cytoplasmic side. Localization to the adherens junctions is alpha-catenin-dependent. Also localizes to F-actin bundles originating from adherens junctio
Protein Description Plays a role in the formation of adherens junction and the polymerization of linear actin cables..
Protein Sequence MEGTHCTLQLHKPITELCYISFCLPKGEVRGFSYKGTVTLDRSNKGFHNCYQVREESDIISLSQEPDEHPGDIFFKQTPTKDILTELYKLTTERERLLTNLLSSDHILGITMGNQEGKLQELSVSLAPEDDCFQSAGDWQGELPVGPLNKRSTHGNKKPRRSSGRRESFGALPQKRTKRKGRGGRESAPLMGKDKICSSHSLPLSRTRPNLWVLEEKGNLLPNGALACSLQRRESCPPDIPKTPDTDLGFGSFETAFKDTGLGREVLPPDCSSTEAGGDGIRRPPSGLEHQQTGLSESHQDPEKHPEAEKDEMEKPAKRTCKQKPVSKVVAKVQDLSSQVQRVVKTHSKGKETIAIRPAAHAEFVPKADLLTLPGAEAGAHGSRRQGKERQGDRSSQSPAGETASISSVSASAEGAVNKVPLKVIESEKLDEAPEGKRLGFPVHTSVPHTRPETRNKRRAGLPLGGHKSLFLDLPHKVGPDSSQPRGDKKKPSPPAPAALGKVFNNSASQSSTHKQTSPVPSPLSPRLPSPQQHHRILRLPALPGEREAALNDSPCRKSRVFSGCVSADTLEPPSSAKVTETKGASPAFLRAGQPRLVPGETLEKSLGPGKTTAEPQHQSPPGISSEGFPWDGFNEQTPKDLPNRDGGAWVLGYRAGPACPFLLHEEREKSNRSELYLDLHPDHSLTEQDDRTPGRLQAVWPPPKTKDTEEKVGLKYTEAEYQAAILHLKREHKEEIENLQAQFELRAFHIRGEHAMITARLEETIENLKHELEHRWRGGCEERKDVCISTDDDCPPKTFRNVCVQTDRETFLKPCESESKTTRSNQLVPKKLNISSLSQLSPPNDHKDIHAALQPMEGMASNQQKALPPPPASIPPPPPLPSGLGSLSPAPPMPPVSAGPPLPPPPPPPPPLPPPSSAGPPPPPPPPPLPNSPAPPNPGGPPPAPPPPGLAPPPPPGLFFGLGSSSSQCPRKPAIEPSCPMKPLYWTRIQISDRSQNATPTLWDSLEEPDIRDPSEFEYLFSKDTTQQKKKPLSETYEKKNKVKKIIKLLDGKRSQTVGILISSLHLEMKDIQQAIFNVDDSVVDLETLAALYENRAQEDELVKIRKYYETSKEEELKLLDKPEQFLHELAQIPNFAERAQCIIFRSVFSEGITSLHRKVEIITRASKDLLHVKSVKDILALILAFGNYMNGGNRTRGQADGYSLEILPKLKDVKSRDNGINLVDYVVKYYLRYYDQEAGTEKSVFPLPEPQDFFLASQVKFEDLIKDLRKLKRQLEASEKQMVVVCKESPKEYLQPFKDKLEEFFQKAKKEHKMEESHLENAQKSFETTVRYFGMKPKSGEKEITPSYVFMVWYEFCSDFKTIWKRESKNISKERLKMAQESVSKLTSEKKVETKKINPTASLKERLRQKEASVTTN
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
7 (in isoform 3)Phosphorylation-15.2224719451
7 (in isoform 5)Phosphorylation-15.2224719451
11 (in isoform 3)Phosphorylation-22.3828348404
11 (in isoform 5)Phosphorylation-22.3828348404
34PhosphorylationGEVRGFSYKGTVTLD
CEECEEEEEEEEEEE		15.92-
80PhosphorylationIFFKQTPTKDILTEL
CCCCCCCCHHHHHHH		44.74-
85PhosphorylationTPTKDILTELYKLTT
CCCHHHHHHHHHHHH		25.03-
85 (in isoform 3)Phosphorylation-25.0322617229
85 (in isoform 5)Phosphorylation-25.0322617229
88PhosphorylationKDILTELYKLTTERE
HHHHHHHHHHHHHHH		9.56-
88 (in isoform 3)Phosphorylation-9.5625849741
88 (in isoform 5)Phosphorylation-9.5625849741
114 (in isoform 3)Phosphorylation-26.3828348404
114 (in isoform 5)Phosphorylation-26.3828348404
115 (in isoform 3)Phosphorylation-55.9024719451
115 (in isoform 5)Phosphorylation-55.9024719451
140 (in isoform 3)Phosphorylation-39.9827251275
140 (in isoform 5)Phosphorylation-39.9827251275
144 (in isoform 3)Phosphorylation-25.3927251275
144 (in isoform 5)Phosphorylation-25.3927251275
145 (in isoform 3)Phosphorylation-22.5327251275
145 (in isoform 5)Phosphorylation-22.5327251275
146 (in isoform 3)Phosphorylation-21.0223090842
146 (in isoform 5)Phosphorylation-21.0223090842
148 (in isoform 3)Phosphorylation-10.9723090842
148 (in isoform 5)Phosphorylation-10.9723090842
150 (in isoform 3)Phosphorylation-56.2423090842
150 (in isoform 5)Phosphorylation-56.2423090842
161 (in isoform 3)Phosphorylation-43.6423090842
161 (in isoform 5)Phosphorylation-43.6423090842
162 (in isoform 3)Phosphorylation-38.1223090842
162 (in isoform 5)Phosphorylation-38.1223090842
163 (in isoform 3)Phosphorylation-34.2123090842
163 (in isoform 5)Phosphorylation-34.2123090842
168PhosphorylationRSSGRRESFGALPQK
CCCCCHHCCCCCCCH		27.4629255136
168 (in isoform 3)Phosphorylation-27.4625849741
168 (in isoform 5)Phosphorylation-27.4625849741
170 (in isoform 3)Phosphorylation-35.1721815630
170 (in isoform 5)Phosphorylation-35.1721815630
180 (in isoform 3)Phosphorylation-55.29-
180 (in isoform 5)Phosphorylation-55.29-
187PhosphorylationKGRGGRESAPLMGKD
CCCCCCCCCCCCCCC		33.5529255136
198PhosphorylationMGKDKICSSHSLPLS
CCCCCCCCCCCCCCC		34.2629255136
199PhosphorylationGKDKICSSHSLPLSR
CCCCCCCCCCCCCCC		16.8129255136
201PhosphorylationDKICSSHSLPLSRTR
CCCCCCCCCCCCCCC		33.3629255136
205PhosphorylationSSHSLPLSRTRPNLW
CCCCCCCCCCCCCEE		29.6625850435
207PhosphorylationHSLPLSRTRPNLWVL
CCCCCCCCCCCEEEE		47.2923312004
231 (in isoform 3)Phosphorylation-26.5425849741
231 (in isoform 5)Phosphorylation-26.5425849741
235PhosphorylationCSLQRRESCPPDIPK
HHCCCHHCCCCCCCC		30.0629255136
240 (in isoform 3)Phosphorylation-4.6822210691
240 (in isoform 5)Phosphorylation-4.6822210691
243PhosphorylationCPPDIPKTPDTDLGF
CCCCCCCCCCCCCCC		22.5029255136
246PhosphorylationDIPKTPDTDLGFGSF
CCCCCCCCCCCCCCH		34.0429255136
247 (in isoform 3)Phosphorylation-52.7722210691
247 (in isoform 5)Phosphorylation-52.7722210691
251 (in isoform 3)Phosphorylation-29.6230177828
251 (in isoform 5)Phosphorylation-29.6230177828
252PhosphorylationDTDLGFGSFETAFKD
CCCCCCCCHHHHCCC		20.0429255136
252 (in isoform 3)Phosphorylation-20.0430177828
252 (in isoform 5)Phosphorylation-20.0430177828
266 (in isoform 3)Phosphorylation-10.5522210691
266 (in isoform 5)Phosphorylation-10.5522210691
278 (in isoform 3)Phosphorylation-36.70-
278 (in isoform 5)Phosphorylation-36.70-
294 (in isoform 3)Phosphorylation-23.9122210691
294 (in isoform 5)Phosphorylation-23.9122210691
296 (in isoform 3)Phosphorylation-38.1022210691
296 (in isoform 5)Phosphorylation-38.1022210691
365 (in isoform 3)Phosphorylation-3.4126657352
365 (in isoform 5)Phosphorylation-3.4126657352
379 (in isoform 3)Phosphorylation-15.0426657352
379 (in isoform 5)Phosphorylation-15.0426657352
395PhosphorylationKERQGDRSSQSPAGE
CCCCCCCCCCCCCCC		37.1527732954
396PhosphorylationERQGDRSSQSPAGET
CCCCCCCCCCCCCCC		35.2527732954
397 (in isoform 3)Phosphorylation-55.4725849741
397 (in isoform 5)Phosphorylation-55.4725849741
398PhosphorylationQGDRSSQSPAGETAS
CCCCCCCCCCCCCCC		20.7527732954
403PhosphorylationSQSPAGETASISSVS
CCCCCCCCCCCCCCC		25.4527732954
405PhosphorylationSPAGETASISSVSAS
CCCCCCCCCCCCCCC		30.3527732954
407PhosphorylationAGETASISSVSASAE
CCCCCCCCCCCCCCC		23.3830576142
408PhosphorylationGETASISSVSASAEG
CCCCCCCCCCCCCCC		20.5830576142
427PhosphorylationVPLKVIESEKLDEAP
CCEEEEECCCCCCCC		28.9828555341
445PhosphorylationRLGFPVHTSVPHTRP
CCCCCCCCCCCCCCC		31.4926074081
445 (in isoform 3)Phosphorylation-31.4924719451
445 (in isoform 5)Phosphorylation-31.4924719451
446PhosphorylationLGFPVHTSVPHTRPE
CCCCCCCCCCCCCCC		20.8326074081
447 (in isoform 3)Phosphorylation-4.1825849741
447 (in isoform 5)Phosphorylation-4.1825849741
450PhosphorylationVHTSVPHTRPETRNK
CCCCCCCCCCCCCCC		41.6826074081
454PhosphorylationVPHTRPETRNKRRAG
CCCCCCCCCCCCCCC		42.0726074081
458 (in isoform 3)Phosphorylation-36.9125849741
458 (in isoform 5)Phosphorylation-36.9125849741
482PhosphorylationPHKVGPDSSQPRGDK
CCCCCCCCCCCCCCC		33.7229632367
483PhosphorylationHKVGPDSSQPRGDKK
CCCCCCCCCCCCCCC		52.1424275569
493PhosphorylationRGDKKKPSPPAPAAL
CCCCCCCCCCCCHHH		53.0129255136
494 (in isoform 3)Phosphorylation-37.2823663014
512PhosphorylationNNSASQSSTHKQTSP
CCCCCCCCCCCCCCC		27.2227251789
517PhosphorylationQSSTHKQTSPVPSPL
CCCCCCCCCCCCCCC		39.5429255136
518PhosphorylationSSTHKQTSPVPSPLS
CCCCCCCCCCCCCCC		22.7729255136
522PhosphorylationKQTSPVPSPLSPRLP
CCCCCCCCCCCCCCC		38.4129255136
525PhosphorylationSPVPSPLSPRLPSPQ
CCCCCCCCCCCCCHH		16.0329255136
530PhosphorylationPLSPRLPSPQQHHRI
CCCCCCCCHHHCCCC		39.6829255136
554PhosphorylationREAALNDSPCRKSRV
HHHHHCCCCCCCCCC		25.4829255136
586PhosphorylationVTETKGASPAFLRAG
CEECCCCCHHHHHCC		25.9829255136
602PhosphorylationPRLVPGETLEKSLGP
CCCCCCCHHHHHCCC		46.2429396449
612PhosphorylationKSLGPGKTTAEPQHQ
HHCCCCCCCCCCCCC		36.8327732954
613PhosphorylationSLGPGKTTAEPQHQS
HCCCCCCCCCCCCCC		32.2927732954
620PhosphorylationTAEPQHQSPPGISSE
CCCCCCCCCCCCCCC		30.8227251789
625PhosphorylationHQSPPGISSEGFPWD
CCCCCCCCCCCCCCC		28.4027732954
626PhosphorylationQSPPGISSEGFPWDG
CCCCCCCCCCCCCCC		39.5627732954
785UbiquitinationRGGCEERKDVCISTD
CCCCCCCCCEEEECC		58.77-
822PhosphorylationPCESESKTTRSNQLV
CCCCCCCCCCCCCCC		36.40-
823PhosphorylationCESESKTTRSNQLVP
CCCCCCCCCCCCCCC		35.52-
836PhosphorylationVPKKLNISSLSQLSP
CCCCCCHHHHHHCCC		24.9325850435
837PhosphorylationPKKLNISSLSQLSPP
CCCCCHHHHHHCCCC		28.3926657352
839PhosphorylationKLNISSLSQLSPPND
CCCHHHHHHCCCCCC		30.9026657352
842PhosphorylationISSLSQLSPPNDHKD
HHHHHHCCCCCCHHH		30.5829255136
1023PhosphorylationSEFEYLFSKDTTQQK
HHHHHHHCCCCCCCC		27.3324719451
1049AcetylationNKVKKIIKLLDGKRS
HHHHHHHHHHCCCHH		46.6127452117
1056PhosphorylationKLLDGKRSQTVGILI
HHHCCCHHHHHHHHH		33.42-
1058PhosphorylationLDGKRSQTVGILISS
HCCCHHHHHHHHHHH		23.19-
1064PhosphorylationQTVGILISSLHLEMK
HHHHHHHHHHHHHHH		24.33-
1065PhosphorylationTVGILISSLHLEMKD
HHHHHHHHHHHHHHH		16.89-
1109PhosphorylationELVKIRKYYETSKEE
HHHHHHHHHHCCHHH		9.1825072903
1110PhosphorylationLVKIRKYYETSKEEE
HHHHHHHHHCCHHHH		18.7625072903
1112PhosphorylationKIRKYYETSKEEELK
HHHHHHHCCHHHHHH		29.0425072903
1113PhosphorylationIRKYYETSKEEELKL
HHHHHHCCHHHHHHH		26.5725072903
1227PhosphorylationNGINLVDYVVKYYLR
CCCCHHHHHHHHHHH		10.3224719451
1259PhosphorylationPQDFFLASQVKFEDL
CCCEEHHHHCCHHHH		37.3426074081
1327PhosphorylationHLENAQKSFETTVRY
HHHHHHHHHHHHHHH		19.0826503514
1334PhosphorylationSFETTVRYFGMKPKS
HHHHHHHHCCCCCCC		10.5129978859
1341PhosphorylationYFGMKPKSGEKEITP
HCCCCCCCCCCCCCH		61.7929978859
1402PhosphorylationETKKINPTASLKERL
CCCCCCCCHHHHHHH		25.1325002506
1404PhosphorylationKKINPTASLKERLRQ
CCCCCCHHHHHHHHH		42.3123312004
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 FMN1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FMN1_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 FMN1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CP2S1_HUMANCYP2S1physical
28514442
SNAG_HUMANNAPGphysical
28514442
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 FMN1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518 AND SER-522, ANDMASS SPECTROMETRY.

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