dbPTM

TMF1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TMF1_HUMAN
UniProt AC	P82094
Protein Name	TATA element modulatory factor
Gene Name	TMF1
Organism	Homo sapiens (Human).
Sequence Length	1093
Subcellular Localization	Cytoplasm. Nucleus. Golgi apparatus membrane. Concentrated at the budding structures localized at the tips of cisternae.
Protein Description	Potential coactivator of the androgen receptor. Mediates STAT3 degradation. May play critical roles in two RAB6-dependent retrograde transport processes: one from endosomes to the Golgi and the other from the Golgi to the ER. This protein binds the HIV-1 TATA element and inhibits transcriptional activation by the TATA-binding protein (TBP)..
Protein Sequence	MSWFNASQLSSFAKQALSQAQKSIDRVLDIQEEEPSIWAETIPYGEPGISSPVSGGWDTSTWGLKSNTEPQSPPIASPKAITKPVRRTVVDESENFFSAFLSPTDVQTIQKSPVVSKPPAKSQRPEEEVKSSLHESLHIGQSRTPETTESQVKDSSLCVSGETLAAGTSSPKTEGKHEETVNKESDMKVPTVSLKVSESVIDVKTTMESISNTSTQSLTAETKDIALEPKEQKHEDRQSNTPSPPVSTFSSGTSTTSDIEVLDHESVISESSASSRQETTDSKSSLHLMQTSFQLLSASACPEYNRLDDFQKLTESCCSSDAFERIDSFSVQSLDSRSVSEINSDDELSGKGYALVPIIVNSSTPKSKTVESAEGKSEEVNETLVIPTEEAEMEESGRSATPVNCEQPDILVSSTPINEGQTVLDKVAEQCEPAESQPEALSEKEDVCKTVEFLNEKLEKREAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKEELATRLNSSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANAAKDSEAQEAALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEIGELQQRLQEAENRNQELSQSVSSTTRPLLRQIENLQATLGSQTSSWEKLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSMESQNSLLRQENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDEYVRTLEETRKEKTLLNSQLEMERMKVEQERKKAIFTQETIKEKERKPFSVSSTPTMSRSSSISGVDMAGLQTSFLSQDESHDHSFGPMPISANGSNLYDAVRMGAGSSIIENLQSQLKLREGEITHLQLEIGNLEKTRSIMAEELVKLTNQNDELEEKVKEIPKLRTQLRDLDQRYNTILQMYGEKAEEAEELRLDLEDVKNMYKTQIDELLRQSLS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	WFNASQLSSFAKQAL CCCHHHHHHHHHHHH	18.77	-
22	Acetylation	QALSQAQKSIDRVLD HHHHHHHHHHHHHHH	53.01	25953088
22	Ubiquitination	QALSQAQKSIDRVLD HHHHHHHHHHHHHHH	53.01	-
23	Phosphorylation	ALSQAQKSIDRVLDI HHHHHHHHHHHHHHC	20.03	24719451
50	Phosphorylation	PYGEPGISSPVSGGW CCCCCCCCCCCCCCC	34.21	27251275
51	Phosphorylation	YGEPGISSPVSGGWD CCCCCCCCCCCCCCC	27.66	27251275
66	Phosphorylation	TSTWGLKSNTEPQSP CCCCCCCCCCCCCCC	54.77	23403867
68	Phosphorylation	TWGLKSNTEPQSPPI CCCCCCCCCCCCCCC	57.01	25159151
72	Phosphorylation	KSNTEPQSPPIASPK CCCCCCCCCCCCCCC	43.27	25159151
77	Phosphorylation	PQSPPIASPKAITKP CCCCCCCCCCCCCCC	27.87	25159151
82	Phosphorylation	IASPKAITKPVRRTV CCCCCCCCCCCCCCE	33.87	-
93	Phosphorylation	RRTVVDESENFFSAF CCCEECCCCCCHHHH	33.12	21712546
98	Phosphorylation	DESENFFSAFLSPTD CCCCCCHHHHCCCCC	17.61	27251275
102	Phosphorylation	NFFSAFLSPTDVQTI CCHHHHCCCCCHHHH	21.21	25159151
104	Phosphorylation	FSAFLSPTDVQTIQK HHHHCCCCCHHHHHC	45.48	18669648
108	Phosphorylation	LSPTDVQTIQKSPVV CCCCCHHHHHCCCCC	25.81	29496963
112	Phosphorylation	DVQTIQKSPVVSKPP CHHHHHCCCCCCCCC	13.42	25159151
116	Phosphorylation	IQKSPVVSKPPAKSQ HHCCCCCCCCCCCCC	39.41	29396449
121	Methylation	VVSKPPAKSQRPEEE CCCCCCCCCCCCHHH	53.55	115979867
136	Phosphorylation	VKSSLHESLHIGQSR HHHHHHHHHHCCCCC	17.94	25159151
142	Phosphorylation	ESLHIGQSRTPETTE HHHHCCCCCCCCCCH	32.67	25627689
144	Phosphorylation	LHIGQSRTPETTESQ HHCCCCCCCCCCHHH	30.62	29255136
155	Phosphorylation	TESQVKDSSLCVSGE CHHHCCCCCEEEECC	21.35	23663014
156	Phosphorylation	ESQVKDSSLCVSGET HHHCCCCCEEEECCE	35.60	23663014
160	Phosphorylation	KDSSLCVSGETLAAG CCCCEEEECCEECCC	29.89	23663014
163	Phosphorylation	SLCVSGETLAAGTSS CEEEECCEECCCCCC	25.81	23663014
168	Phosphorylation	GETLAAGTSSPKTEG CCEECCCCCCCCCCC	22.70	23663014
169	Phosphorylation	ETLAAGTSSPKTEGK CEECCCCCCCCCCCC	43.66	23663014
170	Phosphorylation	TLAAGTSSPKTEGKH EECCCCCCCCCCCCC	30.19	30278072
173	Phosphorylation	AGTSSPKTEGKHEET CCCCCCCCCCCCCCC	54.04	28450419
197	Phosphorylation	PTVSLKVSESVIDVK CEEEEEEECCEEEHH	23.67	30108239
199	Phosphorylation	VSLKVSESVIDVKTT EEEEEECCEEEHHHH	19.50	25159151
206	Phosphorylation	SVIDVKTTMESISNT CEEEHHHHHHHHHCC	17.14	30576142
209	Phosphorylation	DVKTTMESISNTSTQ EHHHHHHHHHCCCCC	22.09	25159151
211	Phosphorylation	KTTMESISNTSTQSL HHHHHHHHCCCCCCC	43.25	27251275
213	Phosphorylation	TMESISNTSTQSLTA HHHHHHCCCCCCCCE	26.76	22199227
214	Phosphorylation	MESISNTSTQSLTAE HHHHHCCCCCCCCEE	28.79	21815630
215	Phosphorylation	ESISNTSTQSLTAET HHHHCCCCCCCCEEC	21.82	25159151
217	Phosphorylation	ISNTSTQSLTAETKD HHCCCCCCCCEECCC	27.98	25159151
219	Phosphorylation	NTSTQSLTAETKDIA CCCCCCCCEECCCCC	27.91	27251275
222	Phosphorylation	TQSLTAETKDIALEP CCCCCEECCCCCCCC	31.39	23090842
239	Phosphorylation	QKHEDRQSNTPSPPV HHCCCCCCCCCCCCC	43.49	27251275
241	Phosphorylation	HEDRQSNTPSPPVST CCCCCCCCCCCCCEE	30.32	27251275
243	Phosphorylation	DRQSNTPSPPVSTFS CCCCCCCCCCCEECC	39.54	27251275
247	Phosphorylation	NTPSPPVSTFSSGTS CCCCCCCEECCCCCC	29.52	26471730
248	Phosphorylation	TPSPPVSTFSSGTST CCCCCCEECCCCCCC	27.98	27251275
250	Phosphorylation	SPPVSTFSSGTSTTS CCCCEECCCCCCCCC	28.13	27251275
251	Phosphorylation	PPVSTFSSGTSTTSD CCCEECCCCCCCCCC	41.73	27251275
253	Phosphorylation	VSTFSSGTSTTSDIE CEECCCCCCCCCCEE	25.50	27251275
254	Phosphorylation	STFSSGTSTTSDIEV EECCCCCCCCCCEEE	32.96	27251275
255	Phosphorylation	TFSSGTSTTSDIEVL ECCCCCCCCCCEEEE	30.11	27251275
256	Phosphorylation	FSSGTSTTSDIEVLD CCCCCCCCCCEEEEC	24.95	27251275
257	Phosphorylation	SSGTSTTSDIEVLDH CCCCCCCCCEEEECC	36.36	27251275
291	Phosphorylation	SSLHLMQTSFQLLSA HHHHHHHHHHHHHHH	19.97	28348404
292	Phosphorylation	SLHLMQTSFQLLSAS HHHHHHHHHHHHHHH	8.29	28348404
299	Phosphorylation	SFQLLSASACPEYNR HHHHHHHHCCCCCCC	27.33	-
304	Phosphorylation	SASACPEYNRLDDFQ HHHCCCCCCCHHHHH	7.25	27259358
316	Phosphorylation	DFQKLTESCCSSDAF HHHHHHHHHCCCHHH	18.39	30108239
319	Phosphorylation	KLTESCCSSDAFERI HHHHHHCCCHHHHHH	35.26	25159151
320	Phosphorylation	LTESCCSSDAFERID HHHHHCCCHHHHHHH	21.02	23401153
328	Phosphorylation	DAFERIDSFSVQSLD HHHHHHHHCEECCCC	19.63	23401153
330	Phosphorylation	FERIDSFSVQSLDSR HHHHHHCEECCCCCC	24.17	30266825
333	Phosphorylation	IDSFSVQSLDSRSVS HHHCEECCCCCCCHH	31.80	30266825
336	Phosphorylation	FSVQSLDSRSVSEIN CEECCCCCCCHHHCC	31.57	30266825
338	Phosphorylation	VQSLDSRSVSEINSD ECCCCCCCHHHCCCC	33.67	29255136
340	Phosphorylation	SLDSRSVSEINSDDE CCCCCCHHHCCCCCC	33.72	30266825
344	Phosphorylation	RSVSEINSDDELSGK CCHHHCCCCCCCCCC	52.69	19664994
349	Phosphorylation	INSDDELSGKGYALV CCCCCCCCCCCEEEE	36.09	30266825
353	Phosphorylation	DELSGKGYALVPIIV CCCCCCCEEEEEEEE	10.55	25159151
362	Phosphorylation	LVPIIVNSSTPKSKT EEEEEEECCCCCCCC	25.37	25159151
363	Phosphorylation	VPIIVNSSTPKSKTV EEEEEECCCCCCCCC	43.45	25159151
364	Phosphorylation	PIIVNSSTPKSKTVE EEEEECCCCCCCCCC	34.26	25159151
367	Phosphorylation	VNSSTPKSKTVESAE EECCCCCCCCCCCCC	34.46	26074081
369	Phosphorylation	SSTPKSKTVESAEGK CCCCCCCCCCCCCCC	36.27	26074081
388	Phosphorylation	NETLVIPTEEAEMEE CCEEEEECHHHHHHH	35.02	26471730
396	Phosphorylation	EEAEMEESGRSATPV HHHHHHHHCCCCCCC	26.63	26074081
399	Phosphorylation	EMEESGRSATPVNCE HHHHHCCCCCCCCCC	39.77	29255136
401	Phosphorylation	EESGRSATPVNCEQP HHHCCCCCCCCCCCC	29.08	29255136
413	Phosphorylation	EQPDILVSSTPINEG CCCCEEEECCCCCCC	25.67	30278072
414	Phosphorylation	QPDILVSSTPINEGQ CCCEEEECCCCCCCC	30.62	23403867
415	Phosphorylation	PDILVSSTPINEGQT CCEEEECCCCCCCCC	22.23	30278072
422	Phosphorylation	TPINEGQTVLDKVAE CCCCCCCCHHHHHHH	33.61	23403867
436	Phosphorylation	EQCEPAESQPEALSE HHCCCCCCCHHHHHC	53.81	28348404
442	Phosphorylation	ESQPEALSEKEDVCK CCCHHHHHCCHHHHH	54.38	25849741
449	Ubiquitination	SEKEDVCKTVEFLNE HCCHHHHHHHHHHHH	56.29	-
457	Ubiquitination	TVEFLNEKLEKREAQ HHHHHHHHHHHHHHH	61.95	-
467	Phosphorylation	KREAQLLSLSKEKAL HHHHHHHHHHHHHHH	38.91	24719451
470	Acetylation	AQLLSLSKEKALLEE HHHHHHHHHHHHHHH	69.40	20167786
470	Ubiquitination	AQLLSLSKEKALLEE HHHHHHHHHHHHHHH	69.40	-
472	Ubiquitination	LLSLSKEKALLEEAF HHHHHHHHHHHHHHH	48.33	-
490	Ubiquitination	KDEMFRVKEESSSIS HHHHHHHHHCCCCHH	52.05	-
497	Phosphorylation	KEESSSISSLKDEFT HHCCCCHHHHHHHHH	31.40	24719451
500	Ubiquitination	SSSISSLKDEFTQRI CCCHHHHHHHHHHHH	58.10	-
519	Acetylation	KKVQLACKERDAAKK HHHHHHHHHHHHHHH	50.61	19608861
541	Phosphorylation	ELATRLNSSETADLL HHHHHCCCHHHHHHH	33.86	30266825
542	Phosphorylation	LATRLNSSETADLLK HHHHCCCHHHHHHHH	37.58	30266825
544	Phosphorylation	TRLNSSETADLLKEK HHCCCHHHHHHHHHH	27.67	30266825
564	Acetylation	GLMEEGEKLSKQQLH HHHHHHHHHCHHHHH	69.76	18530477
630	Phosphorylation	ENIKKLNSMVERQEK HHHHHHHHHHHHHHH	34.34	27251275
637	Acetylation	SMVERQEKDLGRLQV HHHHHHHHHHCCCCC	50.33	7377529
655	Phosphorylation	ELEEKNRSIQAALDS HHHHHHHHHHHHHHH	28.57	28555341
679	Phosphorylation	KANAAKDSEAQEAAL HHHHCCCHHHHHHHH	33.84	-
687	Phosphorylation	EAQEAALSREMKAKE HHHHHHHHHHHHHHH	22.82	-
763	Phosphorylation	RNQELSQSVSSTTRP HHHHHHHHHHHCHHH	22.16	28555341
843	Phosphorylation	SLLRQENSRFQAQLE HHHHHHHHHHHHHHH	33.45	30242111
851	Phosphorylation	RFQAQLESEKNRLCK HHHHHHHHHHCCCCC	63.56	30242111
853	Ubiquitination	QAQLESEKNRLCKLE HHHHHHHHCCCCCCH	57.56	-
866	Phosphorylation	LEDENNRYQVELENL CHHCCCCEEEEHHHH	21.02	18669648
877	Phosphorylation	LENLKDEYVRTLEET HHHHHHHHHHHHHHH	12.83	18669648
889	Phosphorylation	EETRKEKTLLNSQLE HHHHHHHHHHHHHHH	37.25	18691976
893	Phosphorylation	KEKTLLNSQLEMERM HHHHHHHHHHHHHHH	35.79	20068231
897	Sulfoxidation	LLNSQLEMERMKVEQ HHHHHHHHHHHHHHH	5.56	21406390
912	Phosphorylation	ERKKAIFTQETIKEK HHHHHHHCHHHHHHH	21.27	-
915	Phosphorylation	KAIFTQETIKEKERK HHHHCHHHHHHHHCC	27.77	28555341
925	Phosphorylation	EKERKPFSVSSTPTM HHHCCCCCCCCCCCC	29.62	23927012
927	Phosphorylation	ERKPFSVSSTPTMSR HCCCCCCCCCCCCCC	27.57	25159151
928	Phosphorylation	RKPFSVSSTPTMSRS CCCCCCCCCCCCCCC	35.93	23927012
929	Phosphorylation	KPFSVSSTPTMSRSS CCCCCCCCCCCCCCC	18.44	23927012
931	Phosphorylation	FSVSSTPTMSRSSSI CCCCCCCCCCCCCCC	28.06	25159151
933	Phosphorylation	VSSTPTMSRSSSISG CCCCCCCCCCCCCCC	31.33	25159151
935	Phosphorylation	STPTMSRSSSISGVD CCCCCCCCCCCCCCC	22.56	27251275
936	Phosphorylation	TPTMSRSSSISGVDM CCCCCCCCCCCCCCC	30.49	28348404
937	Phosphorylation	PTMSRSSSISGVDMA CCCCCCCCCCCCCCC	23.24	23898821
939	Phosphorylation	MSRSSSISGVDMAGL CCCCCCCCCCCCCCC	34.41	28348404
960	Phosphorylation	QDESHDHSFGPMPIS CCCCCCCCCCCCCCC	37.65	26074081
971	Phosphorylation	MPISANGSNLYDAVR CCCCCCCCCHHHHHH	24.38	-
974	Phosphorylation	SANGSNLYDAVRMGA CCCCCCHHHHHHHCC	13.20	25884760
984	Phosphorylation	VRMGAGSSIIENLQS HHHCCCHHHHHHHHH	27.03	28555341
1015	Phosphorylation	GNLEKTRSIMAEELV CCHHHHHHHHHHHHH	23.19	20860994
1070	Methylation	AEEAEELRLDLEDVK HHHHHHHCCCHHHHH	29.45	115918649
1080	Phosphorylation	LEDVKNMYKTQIDEL HHHHHHHHHHHHHHH	21.93	30206219
1082	Phosphorylation	DVKNMYKTQIDELLR HHHHHHHHHHHHHHH	17.17	30206219
1091	Phosphorylation	IDELLRQSLS----- HHHHHHHHCC-----	24.93	22199227
1093	Phosphorylation	ELLRQSLS------- HHHHHHCC-------	43.34	22199227

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 TMF1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TMF1_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 TMF1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
ANDR_HUMAN	AR	physical	10428808

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 TMF1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-519, AND MASS SPECTROMETRY.	19608861 [Abstract]
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-77; SER-199; SER-328 ANDSER-344, AND MASS SPECTROMETRY.	19690332 [Abstract]
"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-72; SER-77; SER-344 ANDSER-349, AND MASS SPECTROMETRY.	19413330 [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-72; SER-77; SER-112;SER-328; SER-338; SER-344; TYR-866; TYR-877; SER-925; THR-929 ANDSER-933, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-144; SER-328; SER-344;THR-364 AND SER-542, AND MASS SPECTROMETRY.	18691976 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASSSPECTROMETRY.	19007248 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-77, AND MASSSPECTROMETRY.	16964243 [Abstract]