dbPTM

SP16H_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SP16H_MOUSE
UniProt AC	Q920B9
Protein Name	FACT complex subunit SPT16
Gene Name	Supt16h
Organism	Mus musculus (Mouse).
Sequence Length	1047
Subcellular Localization	Nucleus. Chromosome. Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci.
Protein Description	Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II)..
Protein Sequence	MAVTLDKDAYYRRVKRLYSNWRKGEDEYASIDAIVVSVGVDEEIVYAKSTALQTWLFGYELTDTIMVFCDDKIIFMASKKKVEFLKQIANTKGNENANGAPAITLLVREKNESNKSSFDKMIDAIKESKSGKKIGVFSKDKFPGEFMKSWSDCLNKEGFDKVDISAVVAYTIAVKEDGELNLMKKAASITSEVFNKFFKERVMEIVDADEKVRHSKLAESVEKAIEEKKYLAGADPSTVEMCYPPIIQSGGNYNLKFSVVSDKNHMHFGAITCAMGIRFKSYCSNLVRTLMVDPTQEVQENYNFLLQLQEELLKELRHGVKICDVYNSVMDVVKKQKPELLNKITKNLGFGMGIEFREGSLVINSKNQYKLKKGMVFSINLGFSDLTNKEGKKPEEKTYALFIGDTVLVDEDGPATILTSVKKKVKNVGIFLKNEDDEEEEEEKDEAEDLLGRGSRAALLTERTRNEMTAEEKRRAHQKELAAQLNEEAKRRLTEQKGEQQIQKARKSNVSYKNPSLMPKEPHIREMKIYIDKKYETVIMPVFGIATPFHIATIKNISMSVEGDYTYLRINFYCPGSALGRNEGNIFPNPEATFVKEITYRASNMKAPGEQTVPALNLQNAFRIIKEVQKRYKTREAEEKEKEGIVKQDSLVINLNRSNPKLKDLYIRPNIAQKRMQGSLEAHVNGFRFTSVRGDKVDILYNNIKHALFQPCDGEMIIVLHFHLKNAVMFGKKRHTDVQFYTEVGEITTDLGKHQHMHDRDDLYAEQMEREMRHKLKTAFKNFIEKVEALTKEELEFEVPFRDLGFNGAPYRSTCLLQPTSSALVNATEWPPFVVTLDEVELIHFERVQFHLKNFDMVIVYKDYSKKVTMINAIPVASLDPIKEWLNSCDLKYTEGVQSLNWTKIMKTIVDDPEGFFEQGGWSFLEPEGEGSDAEDGDSESEIEDETFNPSEDDYEEEEEDSDEDYSSEAEESDYSKESLGSEEESGKDWDELEEEARKADRESRYEEEEEQSRSMSRKRKASVHSSGRGSNRGSRHSSAPPKKKRK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAVTLDKDA ------CCCCCCHHH	17.82	-
4	Phosphorylation	----MAVTLDKDAYY ----CCCCCCHHHHH	35.98	29176673
12	Methylation	LDKDAYYRRVKRLYS CCHHHHHHHHHHHHH	25.00	30761169
13	Methylation	DKDAYYRRVKRLYSN CHHHHHHHHHHHHHC	23.37	30761175
19	Phosphorylation	RRVKRLYSNWRKGED HHHHHHHHCCCCCCC	34.21	22006019
139	Acetylation	KKIGVFSKDKFPGEF CEEEEEECCCCCHHH	54.17	-
149	Phosphorylation	FPGEFMKSWSDCLNK CCHHHHHHHHHHCCC	21.74	28576409
156	Ubiquitination	SWSDCLNKEGFDKVD HHHHHCCCCCCCCCC	46.39	-
184	Acetylation	DGELNLMKKAASITS CCCCCHHHHHHHCHH	42.29	22826441
188	Phosphorylation	NLMKKAASITSEVFN CHHHHHHHCHHHHHH	31.12	22942356
190	Phosphorylation	MKKAASITSEVFNKF HHHHHHCHHHHHHHH	19.15	28066266
196	Ubiquitination	ITSEVFNKFFKERVM CHHHHHHHHHHHHHH	40.49	-
196	Acetylation	ITSEVFNKFFKERVM CHHHHHHHHHHHHHH	40.49	23806337
223	Acetylation	KLAESVEKAIEEKKY HHHHHHHHHHHHHHH	53.13	22826441
360	Phosphorylation	GIEFREGSLVINSKN CEEECCCEEEEECCC	18.08	29109428
365	Phosphorylation	EGSLVINSKNQYKLK CCEEEEECCCCEEEC	23.12	29109428
455	Phosphorylation	EDLLGRGSRAALLTE HHHHCHHHHHHHHHH	19.86	29514104
479	Acetylation	EKRRAHQKELAAQLN HHHHHHHHHHHHHHC	44.84	22826441
504	Acetylation	KGEQQIQKARKSNVS HHHHHHHHHHHCCCC	52.36	23806337
508	Phosphorylation	QIQKARKSNVSYKNP HHHHHHHCCCCCCCC	36.59	-
513	Acetylation	RKSNVSYKNPSLMPK HHCCCCCCCCCCCCC	55.67	23806337
520	Acetylation	KNPSLMPKEPHIREM CCCCCCCCCCCCCEE	70.66	22826441
596	Ubiquitination	NPEATFVKEITYRAS CCCCEEEEEEEEECC	38.93	-
650	Phosphorylation	EGIVKQDSLVINLNR CCCCCCCEEEEECCC	23.26	25266776
658	Phosphorylation	LVINLNRSNPKLKDL EEEECCCCCCCHHHE	57.31	27841257
666	Phosphorylation	NPKLKDLYIRPNIAQ CCCHHHEEECCHHHH	12.67	-
674	Acetylation	IRPNIAQKRMQGSLE ECCHHHHHHHHCCEE	40.59	23236377
696	Acetylation	FTSVRGDKVDILYNN EEEECCCCEEEEECC	44.63	23806337
732	Acetylation	KNAVMFGKKRHTDVQ CCCHHHCCCCCCCCC	35.06	-
741	Phosphorylation	RHTDVQFYTEVGEIT CCCCCCEEEEECEEE	5.72	21454597
748	Phosphorylation	YTEVGEITTDLGKHQ EEEECEEEECCCCCC	15.23	21454597
749	Phosphorylation	TEVGEITTDLGKHQH EEECEEEECCCCCCC	34.58	21454597
786	Acetylation	AFKNFIEKVEALTKE HHHHHHHHHHHHCHH	40.33	23806337
792	Acetylation	EKVEALTKEELEFEV HHHHHHCHHHCEEEC	50.47	8275939
899	Phosphorylation	KYTEGVQSLNWTKIM CCCCCCCCCCHHHHH	22.67	28066266
903	Phosphorylation	GVQSLNWTKIMKTIV CCCCCCHHHHHHHHC	15.04	28066266
904	Acetylation	VQSLNWTKIMKTIVD CCCCCHHHHHHHHCC	32.20	-
979	Phosphorylation	ESDYSKESLGSEEES HCCCCHHHHCCCCHH	41.59	28973931
982	Phosphorylation	YSKESLGSEEESGKD CCHHHHCCCCHHCCC	47.32	27818261
986	Phosphorylation	SLGSEEESGKDWDEL HHCCCCHHCCCHHHH	55.19	27818261
1004	Phosphorylation	ARKADRESRYEEEEE HHHHHHHHHHHHHHH	40.85	29550500
1006	Phosphorylation	KADRESRYEEEEEQS HHHHHHHHHHHHHHH	36.65	22871156
1013	Phosphorylation	YEEEEEQSRSMSRKR HHHHHHHHHHHCHHH	29.60	23684622
1015	Phosphorylation	EEEEQSRSMSRKRKA HHHHHHHHHCHHHHH	26.76	29899451
1023	Phosphorylation	MSRKRKASVHSSGRG HCHHHHHHHCCCCCC	24.33	25266776
1026	Phosphorylation	KRKASVHSSGRGSNR HHHHHHCCCCCCCCC	32.12	26824392
1027	Phosphorylation	RKASVHSSGRGSNRG HHHHHCCCCCCCCCC	20.03	30635358

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 SP16H_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SP16H_MOUSE !!

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 SP16H_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of SP16H_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SP16H_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-979; SER-982 ANDSER-986, AND MASS SPECTROMETRY.	19367708 [Abstract]