dbPTM

FNIP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FNIP1_HUMAN
UniProt AC	Q8TF40
Protein Name	Folliculin-interacting protein 1
Gene Name	FNIP1
Organism	Homo sapiens (Human).
Sequence Length	1166
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. Competes with the activating co-chaperone AHSA1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins. [PubMed: 27353360 May be involved in energy and/or nutrient sensing through the AMPK and mTOR signaling pathways]
Protein Sequence	MAPTLFQKLFSKRTGLGAPGRDARDPDCGFSWPLPEFDPSQIRLIVYQDCERRGRNVLFDSSVKRRNEDISVSKLGSDAQVKVFGKCCQLKPGGDSSSSLDSSVTSSSDIKDQCLKYQGSRCSSDANMLGEMMFGSVAMSYKGSTLKIHQIRSPPQLMLSKVFTARTGSSICGSLNTLQDSLEFINQDNNTLKADNNTVINGLLGNIGLSQFCSPRRAFSEQGPLRLIRSASFFAVHSNPMDMPGRELNEDRDSGIARSASLSSLLITPFPSPNSSLTRSCASSYQRRWRRSQTTSLENGVFPRWSIEESFNLSDESCGPNPGIVRKKKIAIGVIFSLSKDEDENNKFNEFFFSHFPLFESHMNKLKSAIEQAMKMSRRSADASQRSLAYNRIVDALNEFRTTICNLYTMPRIGEPVWLTMMSGTPEKNHLCYRFMKEFTFLMENASKNQFLPALITAVLTNHLAWVPTVMPNGQPPIKIFLEKHSSQSVDMLAKTHPYNPLWAQLGDLYGAIGSPVRLARTVVVGKRQDMVQRLLYFLTYFIRCSELQETHLLENGEDEAIVMPGTVITTTLEKGEIEESEYVLVTMHRNKSSLLFKESEEIRTPNCNCKYCSHPLLGQNVENISQQEREDIQNSSKELLGISDECQMISPSDCQEENAVDVKQYRDKLRTCFDAKLETVVCTGSVPVDKCALSESGLESTEETWQSEKLLDSDSHTGKAMRSTGMVVEKKPPDKIVPASFSCEAAQTKVTFLIGDSMSPDSDTELRSQAVVDQITRHHTKPLKEERGAIDQHQETKQTTKDQSGESDTQNMVSEEPCELPCWNHSDPESMSLFDEYFNDDSIETRTIDDVPFKTSTDSKDHCCMLEFSKILCTKNNKQNNEFCKCIETVPQDSCKTCFPQQDQRDTLSILVPHGDKESSDKKIAVGTEWDIPRNESSDSALGDSESEDTGHDMTRQVSSYYGGEQEDWAEEDEIPFPGSKLIEVSAVQPNIANFGRSLLGGYCSSYVPDFVLQGIGSDERFRQCLMSDLSHAVQHPVLDEPIAEAVCIIADMDKWTVQVASSQRRVTDNKLGKEVLVSSLVSNLLHSTLQLYKHNLSPNFCVMHLEDRLQELYFKSKMLSEYLRGQMRVHVKELGVVLGIESSDLPLLAAVASTHSPYVAQILL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Ubiquitination	MAPTLFQKLFSKRTG CCCHHHHHHHHCCCC	44.13	-
11	Phosphorylation	TLFQKLFSKRTGLGA HHHHHHHHCCCCCCC	31.50	24719451
64	Ubiquitination	VLFDSSVKRRNEDIS EECCCCCCCCCCCCC	47.81	-
71	Phosphorylation	KRRNEDISVSKLGSD CCCCCCCCCHHCCCC	32.43	24719451
77	Phosphorylation	ISVSKLGSDAQVKVF CCCHHCCCCCEEEEE	39.96	20068231
96	Phosphorylation	QLKPGGDSSSSLDSS CCCCCCCCCHHCCCC	35.08	25849741
97	Phosphorylation	LKPGGDSSSSLDSSV CCCCCCCCHHCCCCC	28.78	28450419
98	Phosphorylation	KPGGDSSSSLDSSVT CCCCCCCHHCCCCCC	38.58	28450419
99	Phosphorylation	PGGDSSSSLDSSVTS CCCCCCHHCCCCCCC	37.84	28450419
102	Phosphorylation	DSSSSLDSSVTSSSD CCCHHCCCCCCCCHH	31.81	28450419
103	Phosphorylation	SSSSLDSSVTSSSDI CCHHCCCCCCCCHHH	29.13	28450419
105	Phosphorylation	SSLDSSVTSSSDIKD HHCCCCCCCCHHHHH	25.49	30576142
106	Phosphorylation	SLDSSVTSSSDIKDQ HCCCCCCCCHHHHHH	26.20	23186163
107	Phosphorylation	LDSSVTSSSDIKDQC CCCCCCCCHHHHHHH	23.75	23186163
108	Phosphorylation	DSSVTSSSDIKDQCL CCCCCCCHHHHHHHH	43.02	30576142
124	Phosphorylation	YQGSRCSSDANMLGE HCCCCCCCCHHHHHH	44.35	23532336
140	Phosphorylation	MFGSVAMSYKGSTLK HHHHEEEEECCCEEE	17.60	-
142	Acetylation	GSVAMSYKGSTLKIH HHEEEEECCCEEEEE	38.79	25953088
147	Ubiquitination	SYKGSTLKIHQIRSP EECCCEEEEEEECCC	37.93	-
161	Ubiquitination	PPQLMLSKVFTARTG CCCEEEEECEECCCC	37.09	21890473
161 (in isoform 1)	Ubiquitination	-	37.09	21890473
161 (in isoform 2)	Ubiquitination	-	37.09	21890473
161 (in isoform 3)	Ubiquitination	-	37.09	21890473
167	Phosphorylation	SKVFTARTGSSICGS EECEECCCCCCCCCC	38.66	27732954
169	Phosphorylation	VFTARTGSSICGSLN CEECCCCCCCCCCCC	18.86	27732954
170	Phosphorylation	FTARTGSSICGSLNT EECCCCCCCCCCCCH	24.20	26657352
174	Phosphorylation	TGSSICGSLNTLQDS CCCCCCCCCCHHHHH	17.65	26657352
177	Phosphorylation	SICGSLNTLQDSLEF CCCCCCCHHHHHHHH	30.96	27732954
181	Phosphorylation	SLNTLQDSLEFINQD CCCHHHHHHHHHHCC	19.48	29507054
191	Phosphorylation	FINQDNNTLKADNNT HHHCCCCCEECCCCC	35.57	28634120
210	Phosphorylation	LLGNIGLSQFCSPRR HHCHHCHHHHCCCCC	18.92	24719451
214	Phosphorylation	IGLSQFCSPRRAFSE HCHHHHCCCCCCCCC	23.80	21712546
220	Phosphorylation	CSPRRAFSEQGPLRL CCCCCCCCCCCCHHH	28.20	19664994
230	Phosphorylation	GPLRLIRSASFFAVH CCHHHHHCCCEEEEE	22.67	30266825
232	Phosphorylation	LRLIRSASFFAVHSN HHHHHCCCEEEEECC	23.34	30266825
238	Phosphorylation	ASFFAVHSNPMDMPG CCEEEEECCCCCCCC	35.71	30266825
254	Phosphorylation	ELNEDRDSGIARSAS CCCCCCCCHHHCCCC	32.75	29255136
259	Phosphorylation	RDSGIARSASLSSLL CCCHHHCCCCHHHEE	17.12	28176443
261	Phosphorylation	SGIARSASLSSLLIT CHHHCCCCHHHEEEE	29.99	28176443
263	Phosphorylation	IARSASLSSLLITPF HHCCCCHHHEEEECC	19.22	28176443
264	Phosphorylation	ARSASLSSLLITPFP HCCCCHHHEEEECCC	32.27	28176443
268	Phosphorylation	SLSSLLITPFPSPNS CHHHEEEECCCCCCC	20.88	28450419
272	Phosphorylation	LLITPFPSPNSSLTR EEEECCCCCCCHHHH	36.77	28176443
275	Phosphorylation	TPFPSPNSSLTRSCA ECCCCCCCHHHHHHH	30.06	30108239
276	Phosphorylation	PFPSPNSSLTRSCAS CCCCCCCHHHHHHHH	40.16	30108239
278	Phosphorylation	PSPNSSLTRSCASSY CCCCCHHHHHHHHHH	23.60	28176443
283	Phosphorylation	SLTRSCASSYQRRWR HHHHHHHHHHHHHHH	33.63	28102081
284	Phosphorylation	LTRSCASSYQRRWRR HHHHHHHHHHHHHHH	13.53	28102081
285	Phosphorylation	TRSCASSYQRRWRRS HHHHHHHHHHHHHHH	11.98	28102081
292	Phosphorylation	YQRRWRRSQTTSLEN HHHHHHHHCCCCCCC	24.25	30266825
294	Phosphorylation	RRWRRSQTTSLENGV HHHHHHCCCCCCCCC	21.43	30266825
295	Phosphorylation	RWRRSQTTSLENGVF HHHHHCCCCCCCCCC	24.55	25849741
296	Phosphorylation	WRRSQTTSLENGVFP HHHHCCCCCCCCCCC	36.75	30266825
306	Phosphorylation	NGVFPRWSIEESFNL CCCCCCCCHHHHCCC	22.77	28348404
380	Phosphorylation	AMKMSRRSADASQRS HHHHHHHCCCHHHHH	29.41	27282143
384	Phosphorylation	SRRSADASQRSLAYN HHHCCCHHHHHHHHH	27.03	27282143
387	Phosphorylation	SADASQRSLAYNRIV CCCHHHHHHHHHHHH	15.09	28555341
390	Phosphorylation	ASQRSLAYNRIVDAL HHHHHHHHHHHHHHH	15.40	28555341
484	Ubiquitination	PIKIFLEKHSSQSVD CEEEEEECCCCCCHH	51.43	-
496	Phosphorylation	SVDMLAKTHPYNPLW CHHHHHHCCCCCHHH	23.60	21712546
499	Phosphorylation	MLAKTHPYNPLWAQL HHHHCCCCCHHHHHH	23.08	21712546
510	Phosphorylation	WAQLGDLYGAIGSPV HHHHHHHHHHCCCCC	14.84	21712546
515	Phosphorylation	DLYGAIGSPVRLART HHHHHCCCCCEEEEE	17.70	26329039
527	Ubiquitination	ARTVVVGKRQDMVQR EEEEEECCCHHHHHH	34.96	-
592	Ubiquitination	LVTMHRNKSSLLFKE EEEEECCCCCCCEEC	41.18	-
593	Phosphorylation	VTMHRNKSSLLFKES EEEECCCCCCCEECC	29.75	25159151
594	Phosphorylation	TMHRNKSSLLFKESE EEECCCCCCCEECCC	30.60	25159151
612	Phosphorylation	TPNCNCKYCSHPLLG CCCCCCCCCCCCCCC	11.03	23312004
614	Phosphorylation	NCNCKYCSHPLLGQN CCCCCCCCCCCCCCC	25.67	25159151
626	Phosphorylation	GQNVENISQQEREDI CCCHHHCCHHHHHHH	37.08	27251275
636	Phosphorylation	EREDIQNSSKELLGI HHHHHHHHHHHHHCC	26.81	27251275
651	Phosphorylation	SDECQMISPSDCQEE CCCCCCCCHHHCCCC	17.01	28102081
653	Phosphorylation	ECQMISPSDCQEENA CCCCCCHHHCCCCCC	44.20	28102081
680	Phosphorylation	CFDAKLETVVCTGSV HHHCCCCEEEEECCC	28.77	30266825
684	Phosphorylation	KLETVVCTGSVPVDK CCCEEEEECCCCHHH	22.38	30266825
686	Phosphorylation	ETVVCTGSVPVDKCA CEEEEECCCCHHHHC	12.70	30266825
710	Ubiquitination	EETWQSEKLLDSDSH HHHHHHHHHCCCCCC	60.64	-
714	Phosphorylation	QSEKLLDSDSHTGKA HHHHHCCCCCCCCCC	40.77	25849741
716	Phosphorylation	EKLLDSDSHTGKAMR HHHCCCCCCCCCCHH	27.22	30266825
718	Phosphorylation	LLDSDSHTGKAMRST HCCCCCCCCCCHHHC	44.31	29255136
720	Acetylation	DSDSHTGKAMRSTGM CCCCCCCCCHHHCCC	39.92	25953088
724	Phosphorylation	HTGKAMRSTGMVVEK CCCCCHHHCCCEEEE	19.07	22210691
725	Phosphorylation	TGKAMRSTGMVVEKK CCCCHHHCCCEEEEC	20.94	22210691
741	Phosphorylation	PDKIVPASFSCEAAQ CCCEECCCCCCCCCC	16.18	29255136
743	Phosphorylation	KIVPASFSCEAAQTK CEECCCCCCCCCCCE	14.46	29255136
749	Phosphorylation	FSCEAAQTKVTFLIG CCCCCCCCEEEEEEC	23.82	29255136
752	Phosphorylation	EAAQTKVTFLIGDSM CCCCCEEEEEECCCC	17.80	28857561
758	Phosphorylation	VTFLIGDSMSPDSDT EEEEECCCCCCCCCH	18.88	29255136
760	Phosphorylation	FLIGDSMSPDSDTEL EEECCCCCCCCCHHH	29.52	29255136
763	Phosphorylation	GDSMSPDSDTELRSQ CCCCCCCCCHHHHHH	50.22	29255136
765	Phosphorylation	SMSPDSDTELRSQAV CCCCCCCHHHHHHHH	40.65	29255136
769	Phosphorylation	DSDTELRSQAVVDQI CCCHHHHHHHHHHHH	34.81	28857561
848	Phosphorylation	DDSIETRTIDDVPFK CCCCCEEECCCCCCC	35.86	23312004
855	Ubiquitination	TIDDVPFKTSTDSKD ECCCCCCCCCCCCCC	35.18	-
856	Phosphorylation	IDDVPFKTSTDSKDH CCCCCCCCCCCCCCC	36.92	23312004
857	Phosphorylation	DDVPFKTSTDSKDHC CCCCCCCCCCCCCCE	30.70	23312004
858	Phosphorylation	DVPFKTSTDSKDHCC CCCCCCCCCCCCCEE	49.91	23312004
860	Phosphorylation	PFKTSTDSKDHCCML CCCCCCCCCCCEEEE	39.82	23312004
876	Ubiquitination	FSKILCTKNNKQNNE EEEEEEECCCCCCCC	58.49	-
879	Ubiquitination	ILCTKNNKQNNEFCK EEEECCCCCCCCEEC	64.89	-
908	Phosphorylation	PQQDQRDTLSILVPH CCCCCCCCEEEEEEC	25.29	26546556
910	Phosphorylation	QDQRDTLSILVPHGD CCCCCCEEEEEECCC	18.90	28555341
918	Ubiquitination	ILVPHGDKESSDKKI EEEECCCCCCCCCEE	65.18	-
920	Phosphorylation	VPHGDKESSDKKIAV EECCCCCCCCCEEEE	49.96	21712546
921	Phosphorylation	PHGDKESSDKKIAVG ECCCCCCCCCEEEEE	55.32	29449344
924	Ubiquitination	DKESSDKKIAVGTEW CCCCCCCEEEEECCC	40.67	-
938	O-linked_Glycosylation	WDIPRNESSDSALGD CCCCCCCCCCCCCCC	42.89	30699359
938	Phosphorylation	WDIPRNESSDSALGD CCCCCCCCCCCCCCC	42.89	30108239
939	Phosphorylation	DIPRNESSDSALGDS CCCCCCCCCCCCCCC	29.43	30108239
941	Phosphorylation	PRNESSDSALGDSES CCCCCCCCCCCCCCC	27.60	23663014
946	Phosphorylation	SDSALGDSESEDTGH CCCCCCCCCCCCCCC	41.02	22167270
948	Phosphorylation	SALGDSESEDTGHDM CCCCCCCCCCCCCCC	44.73	23663014
951	Phosphorylation	GDSESEDTGHDMTRQ CCCCCCCCCCCCHHH	32.15	23663014
956	Phosphorylation	EDTGHDMTRQVSSYY CCCCCCCHHHHHHHH	24.81	23663014
960	Phosphorylation	HDMTRQVSSYYGGEQ CCCHHHHHHHHCCCC	12.32	24719451
961	Phosphorylation	DMTRQVSSYYGGEQE CCHHHHHHHHCCCCC	24.42	27251275

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
938	S	Phosphorylation	Kinase	CK2A1	P68400	PSP
938	S	Phosphorylation	Kinase	ALTERNATE	-	Uniprot
939	S	Phosphorylation	Kinase	CK2A1	P68400	PSP
939	S	Phosphorylation	Kinase	CK2	-	Uniprot
941	S	Phosphorylation	Kinase	CK2A1	P68400	PSP
941	S	Phosphorylation	Kinase	CK2	-	Uniprot
946	S	Phosphorylation	Kinase	CK2A1	P68400	PSP
946	S	Phosphorylation	Kinase	CK2	-	Uniprot
948	S	Phosphorylation	Kinase	CK2A1	P68400	PSP
948	S	Phosphorylation	Kinase	CK2	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
11	K	Glycosylation	30699359
Ubiquitinated through 'Lys-11' linkage of ubiquitin moieties at Lys-1119 following glycosylation by OGT, leading to its degradation by the proteasome.
11	K	ubiquitylation	30699359
Ubiquitinated through 'Lys-11' linkage of ubiquitin moieties at Lys-1119 following glycosylation by OGT, leading to its degradation by the proteasome.
938	S	Phosphorylation	30699359
GlcNAcylation at Ser-938 by OGT following dephosphorylation by protein phosphatase 5 (PP5) promotes ubiquitination and degradation by the proteasome.
938	S	Phosphorylation	30699359
Priming phosphorylation at Ser-938 is followed by relay phosphorylation at Ser-939, Ser-941, Ser-946 and Ser-948, promoting its gradual interaction with HSP90AA1/Hsp90.
938	S	ubiquitylation	30699359
GlcNAcylation at Ser-938 by OGT following dephosphorylation by protein phosphatase 5 (PP5) promotes ubiquitination and degradation by the proteasome.
939	S	Phosphorylation	30699359
Priming phosphorylation at Ser-938 is followed by relay phosphorylation at Ser-939, Ser-941, Ser-946 and Ser-948, promoting its gradual interaction with HSP90AA1/Hsp90.
941	S	Phosphorylation	30699359
Priming phosphorylation at Ser-938 is followed by relay phosphorylation at Ser-939, Ser-941, Ser-946 and Ser-948, promoting its gradual interaction with HSP90AA1/Hsp90.
946	S	Phosphorylation	30699359
Priming phosphorylation at Ser-938 is followed by relay phosphorylation at Ser-939, Ser-941, Ser-946 and Ser-948, promoting its gradual interaction with HSP90AA1/Hsp90.
948	S	Phosphorylation	30699359
Priming phosphorylation at Ser-938 is followed by relay phosphorylation at Ser-939, Ser-941, Ser-946 and Ser-948, promoting its gradual interaction with HSP90AA1/Hsp90.
1119	K	Glycosylation	30699359
Ubiquitinated through 'Lys-11' linkage of ubiquitin moieties at Lys-1119 following glycosylation by OGT, leading to its degradation by the proteasome.
1119	K	ubiquitylation	30699359
Ubiquitinated through 'Lys-11' linkage of ubiquitin moieties at Lys-1119 following glycosylation by OGT, leading to its degradation by the proteasome.

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 FNIP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HS90A_HUMAN	HSP90AA1	physical	17028174
AAPK1_HUMAN	PRKAA1	physical	17028174
AAKB1_HUMAN	PRKAB1	physical	17028174
AAKG1_HUMAN	PRKAG1	physical	17028174
FLCN_HUMAN	FLCN	physical	17028174
FLCN_RAT	Flcn	physical	19914239
HS90A_HUMAN	HSP90AA1	physical	27353360
STIP1_HUMAN	STIP1	physical	27353360
CDC37_HUMAN	CDC37	physical	27353360
TEBP_HUMAN	PTGES3	physical	27353360
FLCN_HUMAN	FLCN	physical	27353360
GCR_HUMAN	NR3C1	physical	27353360
CDK4_HUMAN	CDK4	physical	27353360
BRAF_HUMAN	BRAF	physical	27353360
FNIP1_HUMAN	FNIP1	physical	27353360
FNIP2_HUMAN	FNIP2	physical	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 FNIP1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-760 AND SER-763, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"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-593; SER-594; SER-760AND SER-763, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-593, AND MASSSPECTROMETRY.	18220336 [Abstract]

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