F120B_HUMAN - dbPTM
F120B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F120B_HUMAN
UniProt AC Q96EK7
Protein Name Constitutive coactivator of peroxisome proliferator-activated receptor gamma
Gene Name FAM120B
Organism Homo sapiens (Human).
Sequence Length 910
Subcellular Localization Nucleus.
Protein Description Functions as a transactivator of PPARG and ESR1. Functions in adipogenesis through PPARG activation (By similarity)..
Protein Sequence MGVRGLQGFVGSTCPHICTVVNFKELAEHHRSKYPGCTPTIVVDAMCCLRYWYTPESWICGGQWREYFSALRDFVKTFTAAGIKLIFFFDGMVEQDKRDEWVKRRLKNNREISRIFHYIKSHKEQPGRNMFFIPSGLAVFTRFALKTLGQETLCSLQEADYEVASYGLQHNCLGILGEDTDYLIYDTCPYFSISELCLESLDTVMLCREKLCESLGLCVADLPLLACLLGNDIIPEGMFESFRYKCLSSYTSVKENFDKKGNIILAVSDHISKVLYLYQGEKKLEEILPLGPNKALFYKGMASYLLPGQKSPWFFQKPKGVITLDKQVISTSSDAESREEVPMCSDAESRQEVPMCTGPESRREVPVYTDSEPRQEVPMCSDPEPRQEVPTCTGPESRREVPMCSDPEPRQEVPMCTGPEARQEVPMYTDSEPRQEVPMYTDSEPRQEVPMYTGSEPRQEVPMYTGPESRQEVPMYTGPESRQEVLIRTDPESRQEIMCTGHESKQEVPICTDPISKQEDSMCTHAEINQKLPVATDFEFKLEALMCTNPEIKQEDPTNVGPEVKQQVTMVSDTEILKVARTHHVQAESYLVYNIMSSGEIECSNTLEDELDQALPSQAFIYRPIRQRVYSLLLEDCQDVTSTCLAVKEWFVYPGNPLRHPDLVRPLQMTIPGGTPSLKILWLNQEPEIQVRRLDTLLACFNLSSSREELQAVESPFQALCCLLIYLFVQVDTLCLEDLHAFIAQALCLQGKSTSQLVNLQPDYINPRAVQLGSLLVRGLTTLVLVNSACGFPWKTSDFMPWNVFDGKLFHQKYLQSEKGYAVEVLLEQNRSRLTKFHNLKAVVCKACMKENRRITGRAHWGSHHAGRWGRQGSSYHRTGSGYSRSSQGQPWRDQGPGSRQYEHDQWRRY
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
24UbiquitinationICTVVNFKELAEHHR
EEEEECHHHHHHHHH		46.76-
33UbiquitinationLAEHHRSKYPGCTPT
HHHHHHHCCCCCCCH		56.26-
103UbiquitinationDKRDEWVKRRLKNNR
HHHHHHHHHHHHCCH		32.64-
120UbiquitinationSRIFHYIKSHKEQPG
HHHHHHHHHCCCCCC		39.06-
145UbiquitinationAVFTRFALKTLGQET
HHHHHHHHHHHCCHH		3.91-
178UbiquitinationNCLGILGEDTDYLIY
CCEEECCCCCCEEEE		55.05-
272PhosphorylationLAVSDHISKVLYLYQ
EEEEHHHHHHHHHHH		17.1928387310
294UbiquitinationILPLGPNKALFYKGM
HCCCCCCHHHHCCCC		49.99-
299 (in isoform 2)Ubiquitination-34.5721890473
299UbiquitinationPNKALFYKGMASYLL
CCHHHHCCCCHHHCC		34.5721890473
317 (in isoform 2)Ubiquitination-43.4721890473
317UbiquitinationKSPWFFQKPKGVITL
CCCCHHCCCCCEEEE		43.4721890473
319UbiquitinationPWFFQKPKGVITLDK
CCHHCCCCCEEEECC		73.22-
322UbiquitinationFQKPKGVITLDKQVI
HCCCCCEEEECCEEE		4.2821890473
322 (in isoform 1)Ubiquitination-4.2821890473
326UbiquitinationKGVITLDKQVISTSS
CCEEEECCEEEECCC		49.96-
330PhosphorylationTLDKQVISTSSDAES
EECCEEEECCCCCHH		24.3127732954
331PhosphorylationLDKQVISTSSDAESR
ECCEEEECCCCCHHH		22.5624719451
332PhosphorylationDKQVISTSSDAESRE
CCEEEECCCCCHHHC		21.3027732954
333PhosphorylationKQVISTSSDAESREE
CEEEECCCCCHHHCC		40.7127732954
340UbiquitinationSDAESREEVPMCSDA
CCCHHHCCCCCCCCH		51.3021890473
340 (in isoform 1)Ubiquitination-51.3021890473
345PhosphorylationREEVPMCSDAESRQE
HCCCCCCCCHHHHCC		33.3428985074
368PhosphorylationSRREVPVYTDSEPRQ
HHCCCCCCCCCCCCC		9.9628796482
369PhosphorylationRREVPVYTDSEPRQE
HCCCCCCCCCCCCCC		33.0328796482
371PhosphorylationEVPVYTDSEPRQEVP
CCCCCCCCCCCCCCC		41.5228796482
381PhosphorylationRQEVPMCSDPEPRQE
CCCCCCCCCCCCCCC		50.3721712546
391PhosphorylationEPRQEVPTCTGPESR
CCCCCCCCCCCCHHH		28.0724043423
393PhosphorylationRQEVPTCTGPESRRE
CCCCCCCCCCHHHCC		59.2424043423
397PhosphorylationPTCTGPESRREVPMC
CCCCCCHHHCCCCCC		39.5124043423
415SulfoxidationEPRQEVPMCTGPEAR
CCCCCCCCCCCHHHH		3.7421406390
417PhosphorylationRQEVPMCTGPEARQE
CCCCCCCCCHHHHHC		49.9024719451
428PhosphorylationARQEVPMYTDSEPRQ
HHHCCCCCCCCCCCC		11.0028796482
429PhosphorylationRQEVPMYTDSEPRQE
HHCCCCCCCCCCCCC		27.1428796482
431PhosphorylationEVPMYTDSEPRQEVP
CCCCCCCCCCCCCCC		41.5228796482
440PhosphorylationPRQEVPMYTDSEPRQ
CCCCCCCCCCCCCCC		11.0028796482
441PhosphorylationRQEVPMYTDSEPRQE
CCCCCCCCCCCCCCC		27.1428796482
443PhosphorylationEVPMYTDSEPRQEVP
CCCCCCCCCCCCCCC		41.5228796482
452PhosphorylationPRQEVPMYTGSEPRQ
CCCCCCCCCCCCCCC		11.2421945579
453PhosphorylationRQEVPMYTGSEPRQE
CCCCCCCCCCCCCCC		28.1621945579
455PhosphorylationEVPMYTGSEPRQEVP
CCCCCCCCCCCCCCC		36.3121945579
464PhosphorylationPRQEVPMYTGPESRQ
CCCCCCCCCCCCHHC		11.5021945579
465PhosphorylationRQEVPMYTGPESRQE
CCCCCCCCCCCHHCC		39.7521945579
476PhosphorylationSRQEVPMYTGPESRQ
HHCCCCCCCCCCHHC		11.5021945579
477PhosphorylationRQEVPMYTGPESRQE
HCCCCCCCCCCHHCE		39.7521945579
500PhosphorylationSRQEIMCTGHESKQE
HCCEEEECCCCCCCC		24.9629083192
504PhosphorylationIMCTGHESKQEVPIC
EEECCCCCCCCCCCC		33.6829083192
553SumoylationMCTNPEIKQEDPTNV
HHCCCCCCCCCCCCC		46.07-
565SumoylationTNVGPEVKQQVTMVS
CCCCHHHHHEEEEEC		33.09-
578UbiquitinationVSDTEILKVARTHHV
ECCHHHHHHHHHCCC		39.24-
670PhosphorylationLVRPLQMTIPGGTPS
HCCEEEEECCCCCCC		15.85-
675PhosphorylationQMTIPGGTPSLKILW
EEECCCCCCCEEEEE		18.67-
677PhosphorylationTIPGGTPSLKILWLN
ECCCCCCCEEEEEEC		41.98-
764PhosphorylationLVNLQPDYINPRAVQ
HHCCCCCCCCHHHHH		14.8528152594
781PhosphorylationSLLVRGLTTLVLVNS
HHHHHHHHHEEEECC		22.40-
788PhosphorylationTTLVLVNSACGFPWK
HHEEEECCCCCCCCC		19.91-
813UbiquitinationDGKLFHQKYLQSEKG
CCCEEHHHHHHCCCC		39.0821890473
836UbiquitinationQNRSRLTKFHNLKAV
CCHHHHHHHHCHHHH		49.5821890473
836UbiquitinationQNRSRLTKFHNLKAV
CCHHHHHHHHCHHHH		49.58-
836 (in isoform 1)Ubiquitination-49.5821890473
841AcetylationLTKFHNLKAVVCKAC
HHHHHCHHHHHHHHH		44.4425953088
841UbiquitinationLTKFHNLKAVVCKAC
HHHHHCHHHHHHHHH		44.44-
846UbiquitinationNLKAVVCKACMKENR
CHHHHHHHHHHHHCC		32.77-
863PhosphorylationTGRAHWGSHHAGRWG
CCCCCCCCCCCCCCC		13.6024719451
868MethylationWGSHHAGRWGRQGSS
CCCCCCCCCCCCCCC		33.20-
871MethylationHHAGRWGRQGSSYHR
CCCCCCCCCCCCCCC		30.63-
874PhosphorylationGRWGRQGSSYHRTGS
CCCCCCCCCCCCCCC		21.2726437602
878MethylationRQGSSYHRTGSGYSR
CCCCCCCCCCCCCCC		32.33-
881PhosphorylationSSYHRTGSGYSRSSQ
CCCCCCCCCCCCCCC		33.66-
885MethylationRTGSGYSRSSQGQPW
CCCCCCCCCCCCCCC		31.6624129315
893MethylationSSQGQPWRDQGPGSR
CCCCCCCCCCCCCCC		32.81-
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 F120B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of F120B_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 F120B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RL30_HUMANRPL30physical
21988832
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of F120B_HUMAN

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Related Literatures of Post-Translational Modification

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