FNIP2_HUMAN - dbPTM
FNIP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FNIP2_HUMAN
UniProt AC Q9P278
Protein Name Folliculin-interacting protein 2
Gene Name FNIP2
Organism Homo sapiens (Human).
Sequence Length 1114
Subcellular Localization Cytoplasm . Colocalizes with FLCN in the cytoplasm.
Protein Description Acts as a co-chaperone of HSP90AA1. Inhibits the ATPase activity of HSP90AA1 leading to reduction in its chaperone activity. Facilitates the binding of client protein FLCN to HSP90AA1. [PubMed: 27353360 May play a role in the signal transduction pathway of apoptosis induced by O6-methylguanine-mispaired lesions (By similarity May be involved in energy and/or nutrient sensing through the AMPK and mTOR signaling pathways]
Protein Sequence MAPTLLQKLFNKRGSSGSSAAASAQGRAPKEGPAFSWSCSEFDLNEIRLIVYQDCDRRGRQVLFDSKAVQKIEEVTAQKTEDVPIKISAKCCQGSSSVSSSSSSSISSHSSSGGSSHHAKEQLPKYQYTRPASDVNMLGEMMFGSVAMSYKGSTLKIHYIRSPPQLMISKVFSARMGSFCGSTNNLQDSFEYINQDPNLGKLNTNQNSLGPCRTGSNLAHSTPVDMPSRGQNEDRDSGIARSASLSSLLITPFPSPSSSTSSSSSYQRRWLRSQTTSLENGIIPRRSTDETFSLAEETCSSNPAMVRRKKIAISIIFSLCEKEEAQRNFQDFFFSHFPLFESHMNRLKSAIEKAMISCRKIAESSLRVQFYVSRLMEALGEFRGTIWNLYSVPRIAEPVWLTMMSGTLEKNQLCQRFLKEFTLLIEQINKNQFFAALLTAVLTYHLAWVPTVMPVDHPPIKAFSEKRTSQSVNMLAKTHPYNPLWAQLGDLYGAIGSPVRLTRTVVVGKQKDLVQRILYVLTYFLRCSELQENQLTWSGNHGEGDQVLNGSKIITALEKGEVEESEYVVITVRNEPALVPPILPPTAAERHNPWPTGFPECPEGTDSRDLGLKPDKEANRRPEQGSEACSAGCLGPASDASWKPQNAFCGDEKNKEAPQDGSSRLPSCEVLGAGMKMDQQAVCELLKVEMPTRLPDRSVAWPCPDRHLREKPSLEKVTFQIGSFASPESDFESRMKKMEERVKACGPSLEASEAADVAQDPQVSRSPFKPGFQENVCCPQNRLSEGDEGESDKGFAEDRGSRNDMAADIAGQLSHAADLGTASHGAGGTGGRRLEATRGLYVKAAEGPVLEPVAPRCVQRGPGLVAGANIPCGDDNKKANFRTEGDIPRNESSDSALGDSDDEACASAMLDLGHGGDRTGGSLEVELPLPRSQSISTQNVRNFGRSLLAGYCPTYMPDLVLHGTGSDEKLKQCLVADLVHTVHHPVLDEPIAEAVCIIADTDKWSVQVATSQRKVTDNMKLGQDVLVSSQVSSLLQSILQLYKLHLPADFCIMHLEDRLQEMYLKSKMLSEYLRGHTRVHVKELGVVLGIESNDLPLLTAIASTHSPYVAQILL
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
15PhosphorylationKLFNKRGSSGSSAAA
HHHHHCCCCCHHHHH		35.2427251275
16PhosphorylationLFNKRGSSGSSAAAS
HHHHCCCCCHHHHHH		45.5827251275
18PhosphorylationNKRGSSGSSAAASAQ
HHCCCCCHHHHHHHC		20.8230257219
19PhosphorylationKRGSSGSSAAASAQG
HCCCCCHHHHHHHCC		26.0030257219
67AcetylationRQVLFDSKAVQKIEE
CEEEECHHHHHHHHH		55.1920167786
86UbiquitinationKTEDVPIKISAKCCQ
CCCCCCEEEEEEECC		25.2529967540
95PhosphorylationSAKCCQGSSSVSSSS
EEEECCCCCCCCCCC		8.12-
100PhosphorylationQGSSSVSSSSSSSIS
CCCCCCCCCCCCCCC		31.89-
101PhosphorylationGSSSVSSSSSSSISS
CCCCCCCCCCCCCCC		27.08-
102PhosphorylationSSSVSSSSSSSISSH
CCCCCCCCCCCCCCC		35.87-
105PhosphorylationVSSSSSSSISSHSSS
CCCCCCCCCCCCCCC		28.56-
108PhosphorylationSSSSSISSHSSSGGS
CCCCCCCCCCCCCCC		26.22-
110PhosphorylationSSSISSHSSSGGSSH
CCCCCCCCCCCCCCC		28.31-
112PhosphorylationSISSHSSSGGSSHHA
CCCCCCCCCCCCCCH		50.63-
115PhosphorylationSHSSSGGSSHHAKEQ
CCCCCCCCCCCHHHH		29.98-
116PhosphorylationHSSSGGSSHHAKEQL
CCCCCCCCCCHHHHC		23.67-
145PhosphorylationLGEMMFGSVAMSYKG
HHHHHHHCCCEEECC		8.7429449344
149PhosphorylationMFGSVAMSYKGSTLK
HHHCCCEEECCCEEE		17.6029449344
150PhosphorylationFGSVAMSYKGSTLKI
HHCCCEEECCCEEEE		13.2929449344
178PhosphorylationVFSARMGSFCGSTNN
HHHHCCCCCCCCCCC		14.1833259812
182PhosphorylationRMGSFCGSTNNLQDS
CCCCCCCCCCCCHHH		29.1928348404
183PhosphorylationMGSFCGSTNNLQDSF
CCCCCCCCCCCHHHH		17.2628348404
189PhosphorylationSTNNLQDSFEYINQD
CCCCCHHHHHHHHCC		13.6628348404
204PhosphorylationPNLGKLNTNQNSLGP
CCCCCCCCCCCCCCC		48.9327732954
208PhosphorylationKLNTNQNSLGPCRTG
CCCCCCCCCCCCCCC		25.5729255136
214PhosphorylationNSLGPCRTGSNLAHS
CCCCCCCCCCCCCCC		52.2428450419
216PhosphorylationLGPCRTGSNLAHSTP
CCCCCCCCCCCCCCC		28.2328450419
221PhosphorylationTGSNLAHSTPVDMPS
CCCCCCCCCCCCCCC		28.8828450419
222PhosphorylationGSNLAHSTPVDMPSR
CCCCCCCCCCCCCCC		19.9128450419
228PhosphorylationSTPVDMPSRGQNEDR
CCCCCCCCCCCCCCC		42.2623186163
242PhosphorylationRDSGIARSASLSSLL
CCCHHHCHHHHHHHE		17.1225849741
244PhosphorylationSGIARSASLSSLLIT
CHHHCHHHHHHHEEE		29.9918669648
246PhosphorylationIARSASLSSLLITPF
HHCHHHHHHHEEECC		19.2218669648
247PhosphorylationARSASLSSLLITPFP
HCHHHHHHHEEECCC		32.2718669648
260PhosphorylationFPSPSSSTSSSSSYQ
CCCCCCCCCCCHHHH		34.2824275569
273PhosphorylationYQRRWLRSQTTSLEN
HHHHHHHHHCCCCCC		29.7027732954
275PhosphorylationRRWLRSQTTSLENGI
HHHHHHHCCCCCCCC		21.4327732954
276PhosphorylationRWLRSQTTSLENGII
HHHHHHCCCCCCCCC		24.5527732954
277PhosphorylationWLRSQTTSLENGIIP
HHHHHCCCCCCCCCC		36.7527732954
288PhosphorylationGIIPRRSTDETFSLA
CCCCCCCCCCCCHHH		35.72-
291PhosphorylationPRRSTDETFSLAEET
CCCCCCCCCHHHHHH		22.72-
293PhosphorylationRSTDETFSLAEETCS
CCCCCCCHHHHHHHC		33.80-
405PhosphorylationPVWLTMMSGTLEKNQ
CHHHHHHCCCCCHHH		20.1529514088
407PhosphorylationWLTMMSGTLEKNQLC
HHHHHCCCCCHHHHH		25.1620068231
464PhosphorylationHPPIKAFSEKRTSQS
CCCCHHHCCCCCHHH		47.2524719451
468PhosphorylationKAFSEKRTSQSVNML
HHHCCCCCHHHHHHH		42.0327251275
469PhosphorylationAFSEKRTSQSVNMLA
HHCCCCCHHHHHHHH		25.2127251275
471PhosphorylationSEKRTSQSVNMLAKT
CCCCCHHHHHHHHHH		18.4127251275
481PhosphorylationMLAKTHPYNPLWAQL
HHHHHCCCCHHHHHH		23.08-
492PhosphorylationWAQLGDLYGAIGSPV
HHHHHHHHHHCCCCE		14.84-
497PhosphorylationDLYGAIGSPVRLTRT
HHHHHCCCCEEEEEE		17.7026329039
641PhosphorylationLGPASDASWKPQNAF
CCCCCCCCCCCCCCC		40.3924719451
662PhosphorylationKEAPQDGSSRLPSCE
CCCCCCCCCCCCCCE		22.15-
667PhosphorylationDGSSRLPSCEVLGAG
CCCCCCCCCEECCCC		27.7430108239
718PhosphorylationKPSLEKVTFQIGSFA
CCCCCEEEEECCCCC		22.3827732954
723PhosphorylationKVTFQIGSFASPESD
EEEEECCCCCCCCHH		21.1922199227
726PhosphorylationFQIGSFASPESDFES
EECCCCCCCCHHHHH		27.4722617229
729PhosphorylationGSFASPESDFESRMK
CCCCCCCHHHHHHHH		51.4928450419
733PhosphorylationSPESDFESRMKKMEE
CCCHHHHHHHHHHHH		37.3527732954
801PhosphorylationGFAEDRGSRNDMAAD
CCCCCCCCCHHHHHH		28.8927251275
814PhosphorylationADIAGQLSHAADLGT
HHHHHHHHHHHHHCC		11.8224719451
829PhosphorylationASHGAGGTGGRRLEA
CCCCCCCCCHHCCEE		35.2324719451
934PhosphorylationLPLPRSQSISTQNVR
ECCCCCCCCCCHHHH		21.54-
1005PhosphorylationIADTDKWSVQVATSQ
EEECCCEEEEEECCC		14.3830631047
1011PhosphorylationWSVQVATSQRKVTDN
EEEEEECCCCCCCCC		20.4630631047
1032PhosphorylationVLVSSQVSSLLQSIL
HHHHHHHHHHHHHHH		13.97-
1063PhosphorylationEDRLQEMYLKSKMLS
HHHHHHHHHHHHHHH		15.38-
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 FNIP2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FNIP2_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 FNIP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FLCN_RATFlcnphysical
19914239
FLCN_HUMANFLCNphysical
25126726
GBRAP_HUMANGABARAPphysical
25126726
HS90A_HUMANHSP90AA1physical
27353360
STIP1_HUMANSTIP1physical
27353360
CDC37_HUMANCDC37physical
27353360
TEBP_HUMANPTGES3physical
27353360
FLCN_HUMANFLCNphysical
27353360
GCR_HUMANNR3C1physical
27353360
CDK4_HUMANCDK4physical
27353360
BRAF_HUMANBRAFphysical
27353360
FNIP2_HUMANFNIP2physical
27353360
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 FNIP2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-723 AND SER-726, ANDMASS SPECTROMETRY.

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