FLCN_HUMAN - dbPTM
FLCN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FLCN_HUMAN
UniProt AC Q8NFG4
Protein Name Folliculin
Gene Name FLCN
Organism Homo sapiens (Human).
Sequence Length 579
Subcellular Localization Cytoplasm . Nucleus . Mainly localized in the nucleus. Colocalizes with FNIP1 and FNIP2 in the cytoplasm.
Protein Description May be a tumor suppressor. May be involved in energy and/or nutrient sensing through the AMPK and mTOR signaling pathways. May regulate phosphorylation of RPS6KB1..
Protein Sequence MNAIVALCHFCELHGPRTLFCTEVLHAPLPQGDGNEDSPGQGEQAEEEEGGIQMNSRMRAHSPAEGASVESSSPGPKKSDMCEGCRSLAAGHPGYISHDKETSIKYVSHQHPSHPQLFSIVRQACVRSLSCEVCPGREGPIFFGDEQHGFVFSHTFFIKDSLARGFQRWYSIITIMMDRIYLINSWPFLLGKVRGIIDELQGKALKVFEAEQFGCPQRAQRMNTAFTPFLHQRNGNAARSLTSLTSDDNLWACLHTSFAWLLKACGSRLTEKLLEGAPTEDTLVQMEKLADLEEESESWDNSEAEEEEKAPVLPESTEGRELTQGPAESSSLSGCGSWQPRKLPVFKSLRHMRQVLGAPSFRMLAWHVLMGNQVIWKSRDVDLVQSAFEVLRTMLPVGCVRIIPYSSQYEEAYRCNFLGLSPHVQIPPHVLSSEFAVIVEVHAAARSTLHPVGCEDDQSLSKYEFVVTSGSPVAADRVGPTILNKIEAALTNQNLSVDVVDQCLVCLKEEWMNKVKVLFKFTKVDSRPKEDTQKLLSILGASEEDNVKLLKFWMTGLSKTYKSHLMSTVRSPTASESRN
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
62PhosphorylationNSRMRAHSPAEGASV
CHHHHCCCCCCCCCC		25.4819664994
62 (in isoform 2)Phosphorylation-25.48-
68PhosphorylationHSPAEGASVESSSPG
CCCCCCCCCCCCCCC		36.9629255136
71PhosphorylationAEGASVESSSPGPKK
CCCCCCCCCCCCCCH		33.6830266825
71 (in isoform 2)Phosphorylation-33.68-
72PhosphorylationEGASVESSSPGPKKS
CCCCCCCCCCCCCHH		27.3530266825
72 (in isoform 2)Phosphorylation-27.35-
73PhosphorylationGASVESSSPGPKKSD
CCCCCCCCCCCCHHH		43.0619664994
73 (in isoform 2)Phosphorylation-43.06-
100UbiquitinationPGYISHDKETSIKYV
CCEECCCCCCCCEEE		58.42-
130PhosphorylationQACVRSLSCEVCPGR
HHHHHHCCCEECCCC		14.9628857561
203UbiquitinationIIDELQGKALKVFEA
HHHHHCCCCHHHHHH		37.27-
206 (in isoform 2)Ubiquitination-50.1421890473
206 (in isoform 1)Ubiquitination-50.1421890473
206UbiquitinationELQGKALKVFEAEQF
HHCCCCHHHHHHHHH		50.1421890473
224PhosphorylationQRAQRMNTAFTPFLH
HHHHHHHHCCHHHHH		17.50-
227PhosphorylationQRMNTAFTPFLHQRN
HHHHHCCHHHHHHCC		15.6328555341
272UbiquitinationCGSRLTEKLLEGAPT
HCCHHHHHHHCCCCC		53.81-
286SulfoxidationTEDTLVQMEKLADLE
CHHCHHHHHHHHCHH		3.7021406390
296PhosphorylationLADLEEESESWDNSE
HHCHHHHHHCCCCHH		39.9630266825
298PhosphorylationDLEEESESWDNSEAE
CHHHHHHCCCCHHHH		49.3530266825
302PhosphorylationESESWDNSEAEEEEK
HHHCCCCHHHHHHHH		35.3930266825
323PhosphorylationSTEGRELTQGPAESS
CCCCCCCCCCCCCCC		27.0826699800
329PhosphorylationLTQGPAESSSLSGCG
CCCCCCCCCCCCCCC		27.6026699800
330PhosphorylationTQGPAESSSLSGCGS
CCCCCCCCCCCCCCC		27.1426699800
331PhosphorylationQGPAESSSLSGCGSW
CCCCCCCCCCCCCCC		35.5126699800
333PhosphorylationPAESSSLSGCGSWQP
CCCCCCCCCCCCCCC		33.7026699800
337PhosphorylationSSLSGCGSWQPRKLP
CCCCCCCCCCCCCCH		26.9826699800
348PhosphorylationRKLPVFKSLRHMRQV
CCCHHHHHHHHHHHH		21.1224719451
406PhosphorylationCVRIIPYSSQYEEAY
CEEEEECCHHHHHHH		12.9525126726
463PhosphorylationDDQSLSKYEFVVTSG
CCCCCCEEEEEEECC		15.9527642862
477MethylationGSPVAADRVGPTILN
CCCCCHHCCCHHHHH		30.48-
534UbiquitinationRPKEDTQKLLSILGA
CCHHHHHHHHHHHCC		54.19-
537PhosphorylationEDTQKLLSILGASEE
HHHHHHHHHHCCCCH		26.6325126726
542PhosphorylationLLSILGASEEDNVKL
HHHHHCCCCHHHHHH		39.4625126726
558PhosphorylationKFWMTGLSKTYKSHL
HHHHHCCCHHHHHHH		25.05-
559UbiquitinationFWMTGLSKTYKSHLM
HHHHCCCHHHHHHHH		62.0021890473
559 (in isoform 1)Ubiquitination-62.0021890473
562UbiquitinationTGLSKTYKSHLMSTV
HCCCHHHHHHHHHHC		36.31-
567PhosphorylationTYKSHLMSTVRSPTA
HHHHHHHHHCCCCCH		30.0625159151
568PhosphorylationYKSHLMSTVRSPTAS
HHHHHHHHCCCCCHH		13.1325627689
571PhosphorylationHLMSTVRSPTASESR
HHHHHCCCCCHHHCC		23.4325159151
573PhosphorylationMSTVRSPTASESRN-
HHHCCCCCHHHCCC-		44.0226074081
575PhosphorylationTVRSPTASESRN---
HCCCCCHHHCCC---		38.2928985074
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
406SPhosphorylationKinaseULK1O75385
Uniprot
537SPhosphorylationKinaseULK1O75385
Uniprot
542SPhosphorylationKinaseULK1O75385
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FLCN_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 FLCN_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FNIP1_HUMANFNIP1physical
17028174
A4_HUMANAPPphysical
21832049
ULK1_HUMANULK1physical
25126726
SF3B1_HUMANSF3B1physical
27353360
SF3B3_HUMANSF3B3physical
27353360
HS90A_HUMANHSP90AA1physical
27353360
TCPQ_HUMANCCT8physical
27353360
TCPB_HUMANCCT2physical
27353360
TCPH_HUMANCCT7physical
27353360
TCPD_HUMANCCT4physical
27353360
AHSA1_HUMANAHSA1physical
27353360
CHIP_HUMANSTUB1physical
27353360
RL10_HUMANRPL10physical
27353360
FNIP1_HUMANFNIP1physical
27353360
FNIP2_HUMANFNIP2physical
27353360
PPP5_HUMANPPP5Cphysical
27353360
STIP1_HUMANSTIP1physical
27353360
CDC37_HUMANCDC37physical
27353360
TEBP_HUMANPTGES3physical
27353360
F120B_HUMANFAM120Bphysical
28514442
AGAP3_HUMANAGAP3physical
28514442
AGAP1_HUMANAGAP1physical
28514442
BANP_HUMANBANPphysical
28514442
ZN609_HUMANZNF609physical
28514442
PGK2_HUMANPGK2physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
135150Birt-Hogg-Dube syndrome (BHD)
173600Primary spontaneous pneumothorax (PSP)
144700Renal cell carcinoma (RCC)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FLCN_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-73 AND SER-302,AND MASS SPECTROMETRY.
"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-62 AND SER-73, AND MASSSPECTROMETRY.

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