dbPTM

SPT5H_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SPT5H_HUMAN
UniProt AC	O00267
Protein Name	Transcription elongation factor SPT5
Gene Name	SUPT5H
Organism	Homo sapiens (Human).
Sequence Length	1087
Subcellular Localization	Nucleus .
Protein Description	Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A. DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter. Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme. Cleavage of blocked transcripts by RNA polymerase II promotes the resumption of transcription from the new 3' terminus and may allow repeated attempts at transcription through natural pause sites. DSIF can also positively regulate transcriptional elongation and is required for the efficient activation of transcriptional elongation by the HIV-1 nuclear transcriptional activator, Tat. DSIF acts to suppress transcriptional pausing in transcripts derived from the HIV-1 LTR and blocks premature release of HIV-1 transcripts at terminator sequences..
Protein Sequence	MSDSEDSNFSEEEDSERSSDGEEAEVDEERRSAAGSEKEEEPEDEEEEEEEEEYDEEEEEEDDDRPPKKPRHGGFILDEADVDDEYEDEDQWEDGAEDILEKEEIEASNIDNVVLDEDRSGARRLQNLWRDQREEELGEYYMKKYAKSSVGETVYGGSDELSDDITQQQLLPGVKDPNLWTVKCKIGEERATAISLMRKFIAYQFTDTPLQIKSVVAPEHVKGYIYVEAYKQTHVKQAIEGVGNLRLGYWNQQMVPIKEMTDVLKVVKEVANLKPKSWVRLKRGIYKDDIAQVDYVEPSQNTISLKMIPRIDYDRIKARMSLKDWFAKRKKFKRPPQRLFDAEKIRSLGGDVASDGDFLIFEGNRYSRKGFLFKSFAMSAVITEGVKPTLSELEKFEDQPEGIDLEVVTESTGKEREHNFQPGDNVEVCEGELINLQGKILSVDGNKITIMPKHEDLKDMLEFPAQELRKYFKMGDHVKVIAGRFEGDTGLIVRVEENFVILFSDLTMHELKVLPRDLQLCSETASGVDVGGQHEWGELVQLDPQTVGVIVRLERETFQVLNMYGKVVTVRHQAVTRKKDNRFAVALDSEQNNIHVKDIVKVIDGPHSGREGEIRHLFRSFAFLHCKKLVENGGMFVCKTRHLVLAGGSKPRDVTNFTVGGFAPMSPRISSPMHPSAGGQRGGFGSPGGGSGGMSRGRGRRDNELIGQTVRISQGPYKGYIGVVKDATESTARVELHSTCQTISVDRQRLTTVGSRRPGGMTSTYGRTPMYGSQTPMYGSGSRTPMYGSQTPLQDGSRTPHYGSQTPLHDGSRTPAQSGAWDPNNPNTPSRAEEEYEYAFDDEPTPSPQAYGGTPNPQTPGYPDPSSPQVNPQYNPQTPGTPAMYNTDQFSPYAAPSPQGSYQPSPSPQSYHQVAPSPAGYQNTHSPASYHPTPSPMAYQASPSPSPVGYSPMTPGAPSPGGYNPHTPGSGIEQNSSDWVTTDIQVKVRDTYLDTQVVGQTGVIRSVTGGMCSVYLKDSEKVVSISSEHLEPITPTKNNKVKVILGEDREATGVLLSIDGEDGIVRMDLDEQLKILNLRFLGKLLEA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSDSEDSNF ------CCCCCCCCC	62.24	24043423
4	Phosphorylation	----MSDSEDSNFSE ----CCCCCCCCCCH	53.23	24719451
7	Phosphorylation	-MSDSEDSNFSEEED -CCCCCCCCCCHHHH	35.41	20873877
10	Phosphorylation	DSEDSNFSEEEDSER CCCCCCCCHHHHHCC	48.63	24043423
15	Phosphorylation	NFSEEEDSERSSDGE CCCHHHHHCCCCCCC	37.88	24043423
18	O-linked_Glycosylation	EEEDSERSSDGEEAE HHHHHCCCCCCCCCH	28.82	30059200
18	Phosphorylation	EEEDSERSSDGEEAE HHHHHCCCCCCCCCH	28.82	24043423
19	Phosphorylation	EEDSERSSDGEEAEV HHHHCCCCCCCCCHH	56.72	28985074
32	Phosphorylation	EVDEERRSAAGSEKE HHHHHHHHHCCCCCC	28.79	30278072
36	Phosphorylation	ERRSAAGSEKEEEPE HHHHHCCCCCCCCCC	40.54	30278072
54	Phosphorylation	EEEEEEEYDEEEEEE HHHHHHHCCHHHHHC	31.75	25137130
86	Phosphorylation	EADVDDEYEDEDQWE CCCCCCCCCCHHHCC	35.36	28674151
104 (in isoform 2)	Phosphorylation	-	58.14	25849741
108	Phosphorylation	EKEEIEASNIDNVVL HHHHHHHCCCCCEEE	22.87	30266825
116 (in isoform 2)	Phosphorylation	-	44.11	25159151
120	Phosphorylation	VVLDEDRSGARRLQN EEECCCCHHHHHHHH	49.48	25159151
139	Ubiquitination	QREEELGEYYMKKYA HHHHHHHHHHHHHHH	46.22	32015554
139 (in isoform 2)	Ubiquitination	-	46.22	21890473
140	Phosphorylation	REEELGEYYMKKYAK HHHHHHHHHHHHHHH	13.68	17360941
140	Ubiquitination	REEELGEYYMKKYAK HHHHHHHHHHHHHHH	13.68	29967540
141	Phosphorylation	EEELGEYYMKKYAKS HHHHHHHHHHHHHHC	9.73	27642862
143	Sumoylation	ELGEYYMKKYAKSSV HHHHHHHHHHHHCCC	26.89	-
143	Sumoylation	ELGEYYMKKYAKSSV HHHHHHHHHHHHCCC	26.89	28112733
143	Ubiquitination	ELGEYYMKKYAKSSV HHHHHHHHHHHHCCC	26.89	21906983
143 (in isoform 1)	Ubiquitination	-	26.89	21890473
144	Ubiquitination	LGEYYMKKYAKSSVG HHHHHHHHHHHCCCC	33.63	29967540
147	Ubiquitination	YYMKKYAKSSVGETV HHHHHHHHCCCCCCC	39.93	33845483
148	Phosphorylation	YMKKYAKSSVGETVY HHHHHHHCCCCCCCC	23.29	25159151
149	Phosphorylation	MKKYAKSSVGETVYG HHHHHHCCCCCCCCC	33.17	25159151
153	Phosphorylation	AKSSVGETVYGGSDE HHCCCCCCCCCCCCC	17.07	25627689
155	Phosphorylation	SSVGETVYGGSDELS CCCCCCCCCCCCCCC	24.16	27732954
158	Phosphorylation	GETVYGGSDELSDDI CCCCCCCCCCCCCCC	24.45	25159151
162	Phosphorylation	YGGSDELSDDITQQQ CCCCCCCCCCCHHHH	31.05	27732954
166	Phosphorylation	DELSDDITQQQLLPG CCCCCCCHHHHCCCC	27.59	27732954
171	Ubiquitination	DITQQQLLPGVKDPN CCHHHHCCCCCCCCC	2.78	29967540
175	Acetylation	QQLLPGVKDPNLWTV HHCCCCCCCCCEEEE	73.68	23236377
175	Ubiquitination	QQLLPGVKDPNLWTV HHCCCCCCCCCEEEE	73.68	29967540
192	Phosphorylation	KIGEERATAISLMRK ECCHHHHHHHHHHHH	30.64	21406692
195	Phosphorylation	EERATAISLMRKFIA HHHHHHHHHHHHHHH	17.41	21406692
195	Ubiquitination	EERATAISLMRKFIA HHHHHHHHHHHHHHH	17.41	21890473
195 (in isoform 2)	Ubiquitination	-	17.41	21890473
199	Ubiquitination	TAISLMRKFIAYQFT HHHHHHHHHHHHHCC	27.44	21890473
199 (in isoform 1)	Ubiquitination	-	27.44	21890473
200	Ubiquitination	AISLMRKFIAYQFTD HHHHHHHHHHHHCCC	2.45	23000965
208	Phosphorylation	IAYQFTDTPLQIKSV HHHHCCCCCEEEEEE	23.88	-
209	Ubiquitination	AYQFTDTPLQIKSVV HHHCCCCCEEEEEEE	25.69	21890473
209 (in isoform 2)	Ubiquitination	-	25.69	21890473
213	Ubiquitination	TDTPLQIKSVVAPEH CCCCEEEEEEECCCH	25.00	32015554
213 (in isoform 1)	Ubiquitination	-	25.00	21890473
227	Ubiquitination	HVKGYIYVEAYKQTH HHCEEEEEEEEHHHH	2.17	21890473
227 (in isoform 2)	Ubiquitination	-	2.17	21890473
230	Phosphorylation	GYIYVEAYKQTHVKQ EEEEEEEEHHHHHHH	7.07	-
231	Ubiquitination	YIYVEAYKQTHVKQA EEEEEEEHHHHHHHH	56.63	21890473
231 (in isoform 1)	Ubiquitination	-	56.63	21890473
254	Ubiquitination	LGYWNQQMVPIKEMT ECCCCCCEEEHHHHH	2.52	32015554
254 (in isoform 2)	Ubiquitination	-	2.52	21890473
258	Ubiquitination	NQQMVPIKEMTDVLK CCCEEEHHHHHHHHH	35.05	21906983
258 (in isoform 1)	Ubiquitination	-	35.05	21890473
264	Ubiquitination	IKEMTDVLKVVKEVA HHHHHHHHHHHHHHH	3.76	33845483
265	2-Hydroxyisobutyrylation	KEMTDVLKVVKEVAN HHHHHHHHHHHHHHC	44.84	-
268	Ubiquitination	TDVLKVVKEVANLKP HHHHHHHHHHHCCCC	49.84	21890473
270	Ubiquitination	VLKVVKEVANLKPKS HHHHHHHHHCCCCCC	3.38	32015554
274	Ubiquitination	VKEVANLKPKSWVRL HHHHHCCCCCCEEEE	50.65	32015554
283	Ubiquitination	KSWVRLKRGIYKDDI CCEEEECCCCCCCCC	41.14	29967540
287	Ubiquitination	RLKRGIYKDDIAQVD EECCCCCCCCCCCCC	47.18	29967540
295	Phosphorylation	DDIAQVDYVEPSQNT CCCCCCCEECCCCCE	14.09	17360941
302	Ubiquitination	YVEPSQNTISLKMIP EECCCCCEEEEEEEC	12.33	21963094
306	Ubiquitination	SQNTISLKMIPRIDY CCCEEEEEEECCCCH	28.17	21963094
313	Ubiquitination	KMIPRIDYDRIKARM EEECCCCHHHHHHHH	12.54	23000965
317	Acetylation	RIDYDRIKARMSLKD CCCHHHHHHHHCHHH	30.73	7678493
317	Ubiquitination	RIDYDRIKARMSLKD CCCHHHHHHHHCHHH	30.73	23000965
319	Ubiquitination	DYDRIKARMSLKDWF CHHHHHHHHCHHHHH	15.38	21890473
319 (in isoform 2)	Ubiquitination	-	15.38	21890473
321	Phosphorylation	DRIKARMSLKDWFAK HHHHHHHCHHHHHHH	27.06	-
323	Acetylation	IKARMSLKDWFAKRK HHHHHCHHHHHHHCC	45.68	7678503
323	Ubiquitination	IKARMSLKDWFAKRK HHHHHCHHHHHHHCC	45.68	23000965
323 (in isoform 1)	Ubiquitination	-	45.68	21890473
324	Ubiquitination	KARMSLKDWFAKRKK HHHHCHHHHHHHCCC	51.52	23000965
328	Acetylation	SLKDWFAKRKKFKRP CHHHHHHHCCCCCCC	56.10	19608861
328	Ubiquitination	SLKDWFAKRKKFKRP CHHHHHHHCCCCCCC	56.10	23000965
340	Ubiquitination	KRPPQRLFDAEKIRS CCCCHHHCCHHHHHH	10.22	33845483
344	Acetylation	QRLFDAEKIRSLGGD HHHCCHHHHHHCCCC	45.18	25953088
344	Ubiquitination	QRLFDAEKIRSLGGD HHHCCHHHHHHCCCC	45.18	33845483
354	Phosphorylation	SLGGDVASDGDFLIF HCCCCCCCCCCEEEE	41.81	28348404
375	Phosphorylation	RKGFLFKSFAMSAVI CCCCHHHHHHHHHHH	15.76	20068231
379	Phosphorylation	LFKSFAMSAVITEGV HHHHHHHHHHHHCCC	18.89	24719451
383	Phosphorylation	FAMSAVITEGVKPTL HHHHHHHHCCCCCCH	21.79	20068231
383	Ubiquitination	FAMSAVITEGVKPTL HHHHHHHHCCCCCCH	21.79	32015554
387	Ubiquitination	AVITEGVKPTLSELE HHHHCCCCCCHHHHH	43.04	32015554
391	Phosphorylation	EGVKPTLSELEKFED CCCCCCHHHHHHCCC	42.48	24719451
410	Ubiquitination	IDLEVVTESTGKERE CCEEEEECCCCCCCC	34.39	32015554
414	Ubiquitination	VVTESTGKEREHNFQ EEECCCCCCCCCCCC	54.40	32015554
435	Ubiquitination	VCEGELINLQGKILS ECCCEEEECCCEEEE	38.65	29967540
439	Ubiquitination	ELINLQGKILSVDGN EEEECCCEEEEECCC	27.75	29967540
443	Ubiquitination	LQGKILSVDGNKITI CCCEEEEECCCEEEE	11.08	33845483
447	Ubiquitination	ILSVDGNKITIMPKH EEEECCCEEEEECCC	46.91	33845483
453	Sumoylation	NKITIMPKHEDLKDM CEEEEECCCHHHHHH	42.10	-
453	Sumoylation	NKITIMPKHEDLKDM CEEEEECCCHHHHHH	42.10	-
454	Ubiquitination	KITIMPKHEDLKDML EEEEECCCHHHHHHH	28.12	32015554
458	Ubiquitination	MPKHEDLKDMLEFPA ECCCHHHHHHHHCCH	54.11	32015554
469	Ubiquitination	EFPAQELRKYFKMGD HCCHHHHHHHHHCCC	30.76	29967540
473	Ubiquitination	QELRKYFKMGDHVKV HHHHHHHHCCCEEEE	38.59	29967540
479	Acetylation	FKMGDHVKVIAGRFE HHCCCEEEEEEEEEE	25.22	25953088
508	Ubiquitination	ILFSDLTMHELKVLP EEEECCCHHHHCCCH	2.76	33845483
512	Ubiquitination	DLTMHELKVLPRDLQ CCCHHHHCCCHHHHH	38.45	33845483
557	Phosphorylation	IVRLERETFQVLNMY EEEEEHHHHHHHCCC	26.11	28509920
562	Ubiquitination	RETFQVLNMYGKVVT HHHHHHHCCCCEEEE	23.83	33845483
564	Phosphorylation	TFQVLNMYGKVVTVR HHHHHCCCCEEEEEE	16.84	20068231
566	Ubiquitination	QVLNMYGKVVTVRHQ HHHCCCCEEEEEEEE	18.95	33845483
569	Phosphorylation	NMYGKVVTVRHQAVT CCCCEEEEEEEEEEC	18.14	28509920
593	Ubiquitination	ALDSEQNNIHVKDIV EEECCCCCEEHHHEE	25.99	32015554
597	Ubiquitination	EQNNIHVKDIVKVID CCCCEEHHHEEEEEC	27.81	32015554
601	Acetylation	IHVKDIVKVIDGPHS EEHHHEEEEECCCCC	33.53	26051181
601	Ubiquitination	IHVKDIVKVIDGPHS EEHHHEEEEECCCCC	33.53	33845483
624	Ubiquitination	LFRSFAFLHCKKLVE HHHHHHHHHHHHHHH	4.09	24816145
627	2-Hydroxyisobutyrylation	SFAFLHCKKLVENGG HHHHHHHHHHHHCCC	38.09	-
627	Acetylation	SFAFLHCKKLVENGG HHHHHHHHHHHHCCC	38.09	25953088
639	Acetylation	NGGMFVCKTRHLVLA CCCEEEEECCCEEEC	43.20	25953088
646	Ubiquitination	KTRHLVLAGGSKPRD ECCCEEECCCCCCCC	16.90	23000965
649	Phosphorylation	HLVLAGGSKPRDVTN CEEECCCCCCCCCCC	38.27	29052541
650	Ubiquitination	LVLAGGSKPRDVTNF EEECCCCCCCCCCCE	47.55	23000965
655	Phosphorylation	GSKPRDVTNFTVGGF CCCCCCCCCEEECCC	28.98	23927012
658	O-linked_Glycosylation	PRDVTNFTVGGFAPM CCCCCCEEECCCCCC	21.95	30059200
658	Phosphorylation	PRDVTNFTVGGFAPM CCCCCCEEECCCCCC	21.95	29255136
662	Phosphorylation	TNFTVGGFAPMSPRI CCEEECCCCCCCCCC	5.92	32142685
665	Sulfoxidation	TVGGFAPMSPRISSP EECCCCCCCCCCCCC	8.48	21406390
666	Phosphorylation	VGGFAPMSPRISSPM ECCCCCCCCCCCCCC	15.23	29255136
667	Phosphorylation	GGFAPMSPRISSPMH CCCCCCCCCCCCCCC	31.22	32142685
668	Methylation	GFAPMSPRISSPMHP CCCCCCCCCCCCCCC	33.83	80702713
670	Phosphorylation	APMSPRISSPMHPSA CCCCCCCCCCCCCCC	29.66	23401153
671	Phosphorylation	PMSPRISSPMHPSAG CCCCCCCCCCCCCCC	24.70	23401153
676	Phosphorylation	ISSPMHPSAGGQRGG CCCCCCCCCCCCCCC	25.52	23927012
677	Methylation	SSPMHPSAGGQRGGF CCCCCCCCCCCCCCC	30.50	12718890
681	Asymmetric dimethylarginine	HPSAGGQRGGFGSPG CCCCCCCCCCCCCCC	50.94	-
681	Methylation	HPSAGGQRGGFGSPG CCCCCCCCCCCCCCC	50.94	12718890
686	Phosphorylation	GQRGGFGSPGGGSGG CCCCCCCCCCCCCCC	20.36	30576142
691	Phosphorylation	FGSPGGGSGGMSRGR CCCCCCCCCCCCCCC	35.13	20068231
692	Methylation	GSPGGGSGGMSRGRG CCCCCCCCCCCCCCC	38.81	12718890
694	Methylation	PGGGSGGMSRGRGRR CCCCCCCCCCCCCCC	2.55	12718890
695	Phosphorylation	GGGSGGMSRGRGRRD CCCCCCCCCCCCCCC	34.55	20068231
696	Asymmetric dimethylarginine	GGSGGMSRGRGRRDN CCCCCCCCCCCCCCC	29.90	-
696	Methylation	GGSGGMSRGRGRRDN CCCCCCCCCCCCCCC	29.90	12718890
698	Asymmetric dimethylarginine	SGGMSRGRGRRDNEL CCCCCCCCCCCCCCC	34.04	-
698	Methylation	SGGMSRGRGRRDNEL CCCCCCCCCCCCCCC	34.04	12718890
700	Dimethylation	GMSRGRGRRDNELIG CCCCCCCCCCCCCCC	41.22	-
700	Methylation	GMSRGRGRRDNELIG CCCCCCCCCCCCCCC	41.22	116195835
709	Phosphorylation	DNELIGQTVRISQGP CCCCCCCEEEECCCC	13.41	17924679
713	Phosphorylation	IGQTVRISQGPYKGY CCCEEEECCCCCCCE	20.65	24667141
714	Ubiquitination	GQTVRISQGPYKGYI CCEEEECCCCCCCEE	55.28	21890473
714 (in isoform 2)	Ubiquitination	-	55.28	21890473
717	Phosphorylation	VRISQGPYKGYIGVV EEECCCCCCCEEEEE	24.70	17924679
718	Acetylation	RISQGPYKGYIGVVK EECCCCCCCEEEEEE	48.66	26051181
718	Ubiquitination	RISQGPYKGYIGVVK EECCCCCCCEEEEEE	48.66	23000965
718 (in isoform 1)	Ubiquitination	-	48.66	21890473
720	Phosphorylation	SQGPYKGYIGVVKDA CCCCCCCEEEEEEEC	7.14	24667141
728	Phosphorylation	IGVVKDATESTARVE EEEEEECCCCCEEEE	40.37	21712546
730	Phosphorylation	VVKDATESTARVELH EEEECCCCCEEEEEE	24.02	24667141
731	Phosphorylation	VKDATESTARVELHS EEECCCCCEEEEEEC	16.55	24667141
738	Phosphorylation	TARVELHSTCQTISV CEEEEEECEEEEEEE	43.43	21712546
739	Phosphorylation	ARVELHSTCQTISVD EEEEEECEEEEEEEC	9.63	21712546
740	Glutathionylation	RVELHSTCQTISVDR EEEEECEEEEEEECC	3.63	22555962
742	Phosphorylation	ELHSTCQTISVDRQR EEECEEEEEEECCEE	19.84	29214152
744	Phosphorylation	HSTCQTISVDRQRLT ECEEEEEEECCEEEE	22.73	20068231
747	Methylation	CQTISVDRQRLTTVG EEEEEECCEEEEECC	22.74	115917605
749	Methylation	TISVDRQRLTTVGSR EEEECCEEEEECCCC	34.59	115917609
751	Phosphorylation	SVDRQRLTTVGSRRP EECCEEEEECCCCCC	22.94	26434776
752	Phosphorylation	VDRQRLTTVGSRRPG ECCEEEEECCCCCCC	27.71	26434776
755	Phosphorylation	QRLTTVGSRRPGGMT EEEEECCCCCCCCCC	22.30	23401153
757	Methylation	LTTVGSRRPGGMTST EEECCCCCCCCCCCC	35.59	115917613
762	Phosphorylation	SRRPGGMTSTYGRTP CCCCCCCCCCCCCCC	22.61	24275569
763	O-linked_Glycosylation	RRPGGMTSTYGRTPM CCCCCCCCCCCCCCC	15.67	30059200
763	Phosphorylation	RRPGGMTSTYGRTPM CCCCCCCCCCCCCCC	15.67	28555341
764	Phosphorylation	RPGGMTSTYGRTPMY CCCCCCCCCCCCCCC	22.34	26434776
765	Phosphorylation	PGGMTSTYGRTPMYG CCCCCCCCCCCCCCC	12.36	26434776
768	Phosphorylation	MTSTYGRTPMYGSQT CCCCCCCCCCCCCCC	14.19	21945579
771	Phosphorylation	TYGRTPMYGSQTPMY CCCCCCCCCCCCCCC	18.15	21945579
773	Phosphorylation	GRTPMYGSQTPMYGS CCCCCCCCCCCCCCC	17.25	21945579
775	Phosphorylation	TPMYGSQTPMYGSGS CCCCCCCCCCCCCCC	16.24	21945579
778	Phosphorylation	YGSQTPMYGSGSRTP CCCCCCCCCCCCCCC	14.89	21945579
780	Phosphorylation	SQTPMYGSGSRTPMY CCCCCCCCCCCCCCC	18.99	21945579
782	Phosphorylation	TPMYGSGSRTPMYGS CCCCCCCCCCCCCCC	34.38	21945579
783	Methylation	PMYGSGSRTPMYGSQ CCCCCCCCCCCCCCC	46.50	115917617
784	Phosphorylation	MYGSGSRTPMYGSQT CCCCCCCCCCCCCCC	17.69	29255136
786	Sulfoxidation	GSGSRTPMYGSQTPL CCCCCCCCCCCCCCC	6.14	21406390
787	Phosphorylation	SGSRTPMYGSQTPLQ CCCCCCCCCCCCCCC	18.15	23927012
789	Phosphorylation	SRTPMYGSQTPLQDG CCCCCCCCCCCCCCC	17.25	23927012
791	Phosphorylation	TPMYGSQTPLQDGSR CCCCCCCCCCCCCCC	27.88	23401153
797	Phosphorylation	QTPLQDGSRTPHYGS CCCCCCCCCCCCCCC	41.07	23401153
799	Phosphorylation	PLQDGSRTPHYGSQT CCCCCCCCCCCCCCC	19.00	23401153
802	Phosphorylation	DGSRTPHYGSQTPLH CCCCCCCCCCCCCCC	21.48	23927012
804	Phosphorylation	SRTPHYGSQTPLHDG CCCCCCCCCCCCCCC	24.58	23927012
806	Phosphorylation	TPHYGSQTPLHDGSR CCCCCCCCCCCCCCC	29.52	23927012
812	Phosphorylation	QTPLHDGSRTPAQSG CCCCCCCCCCCCCCC	38.75	23927012
814	Phosphorylation	PLHDGSRTPAQSGAW CCCCCCCCCCCCCCC	25.36	25850435
818	Phosphorylation	GSRTPAQSGAWDPNN CCCCCCCCCCCCCCC	32.36	29978859
828	Phosphorylation	WDPNNPNTPSRAEEE CCCCCCCCCCHHHHH	24.73	25849741
830	Phosphorylation	PNNPNTPSRAEEEYE CCCCCCCCHHHHHHH	41.92	27732954
845	Phosphorylation	YAFDDEPTPSPQAYG HCCCCCCCCCCCCCC	34.06	25137130
847	Phosphorylation	FDDEPTPSPQAYGGT CCCCCCCCCCCCCCC	31.93	25137130
854	Phosphorylation	SPQAYGGTPNPQTPG CCCCCCCCCCCCCCC	18.61	26074081
859	Phosphorylation	GGTPNPQTPGYPDPS CCCCCCCCCCCCCCC	21.67	26074081
862	Phosphorylation	PNPQTPGYPDPSSPQ CCCCCCCCCCCCCCC	12.98	26074081
866	Phosphorylation	TPGYPDPSSPQVNPQ CCCCCCCCCCCCCCC	63.13	26074081
867	Phosphorylation	PGYPDPSSPQVNPQY CCCCCCCCCCCCCCC	25.41	26074081
874	Phosphorylation	SPQVNPQYNPQTPGT CCCCCCCCCCCCCCC	30.02	26074081
878	Phosphorylation	NPQYNPQTPGTPAMY CCCCCCCCCCCCCCC	25.58	26074081
881	Phosphorylation	YNPQTPGTPAMYNTD CCCCCCCCCCCCCCC	14.74	26074081
897	Phosphorylation	FSPYAAPSPQGSYQP CCCCCCCCCCCCCCC	25.73	26074081
901	Phosphorylation	AAPSPQGSYQPSPSP CCCCCCCCCCCCCCC	18.49	26074081
917	O-linked_Glycosylation	SYHQVAPSPAGYQNT CCCCCCCCCCCCCCC	20.04	55821385
917	Phosphorylation	SYHQVAPSPAGYQNT CCCCCCCCCCCCCCC	20.04	26074081
951	Phosphorylation	SPSPVGYSPMTPGAP CCCCCCCCCCCCCCC	11.41	26074081
954	Phosphorylation	PVGYSPMTPGAPSPG CCCCCCCCCCCCCCC	23.19	26074081
959	Phosphorylation	PMTPGAPSPGGYNPH CCCCCCCCCCCCCCC	35.33	26074081
963	Phosphorylation	GAPSPGGYNPHTPGS CCCCCCCCCCCCCCC	31.28	26074081
967	Phosphorylation	PGGYNPHTPGSGIEQ CCCCCCCCCCCCCCC	30.51	26074081
970	Phosphorylation	YNPHTPGSGIEQNSS CCCCCCCCCCCCCCC	37.49	26074081
976	Phosphorylation	GSGIEQNSSDWVTTD CCCCCCCCCCCEEEE	29.39	26074081
977	Phosphorylation	SGIEQNSSDWVTTDI CCCCCCCCCCEEEEE	42.94	26074081
1013	Ubiquitination	SVTGGMCSVYLKDSE ECCCCEEEEEECCCC	12.61	33845483
1017	Acetylation	GMCSVYLKDSEKVVS CEEEEEECCCCCEEE	41.33	26051181
1017	Ubiquitination	GMCSVYLKDSEKVVS CEEEEEECCCCCEEE	41.33	33845483
1021	Acetylation	VYLKDSEKVVSISSE EEECCCCCEEEEECC	52.46	26051181
1024	Phosphorylation	KDSEKVVSISSEHLE CCCCCEEEEECCCCC	21.53	23403867
1026	Phosphorylation	SEKVVSISSEHLEPI CCCEEEEECCCCCCC	23.36	23403867
1027	Phosphorylation	EKVVSISSEHLEPIT CCEEEEECCCCCCCC	27.63	21082442
1030	Phosphorylation	VSISSEHLEPITPTK EEEECCCCCCCCCCC	8.01	32142685
1033	Ubiquitination	SSEHLEPITPTKNNK ECCCCCCCCCCCCCE	5.42	32015554
1033 (in isoform 2)	Ubiquitination	-	5.42	21890473
1034	Phosphorylation	SEHLEPITPTKNNKV CCCCCCCCCCCCCEE	35.30	22167270
1036	Phosphorylation	HLEPITPTKNNKVKV CCCCCCCCCCCEEEE	37.44	30266825
1037	Acetylation	LEPITPTKNNKVKVI CCCCCCCCCCEEEEE	60.78	25953088
1037	Sumoylation	LEPITPTKNNKVKVI CCCCCCCCCCEEEEE	60.78	28112733
1037	Ubiquitination	LEPITPTKNNKVKVI CCCCCCCCCCEEEEE	60.78	33845483
1037 (in isoform 1)	Ubiquitination	-	60.78	21890473
1040	Ubiquitination	ITPTKNNKVKVILGE CCCCCCCEEEEEECC	53.48	-
1067	Sulfoxidation	GEDGIVRMDLDEQLK CCCCEEECCHHHHHH	4.09	21406390
1070	Ubiquitination	GIVRMDLDEQLKILN CEEECCHHHHHHHHC	37.01	24816145
1074	Ubiquitination	MDLDEQLKILNLRFL CCHHHHHHHHCHHHH	44.86	24816145

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
666	S	Phosphorylation	Kinase	CDK1	P06493	PSP
666	S	Phosphorylation	Kinase	CDK9	P50750	PSP
666	S	Phosphorylation	Kinase	CDK2	P24941	PSP
768	T	Phosphorylation	Kinase	CDK9	P50750	PSP
773	S	Phosphorylation	Kinase	CDK9	P50750	PSP
773	S	Phosphorylation	Kinase	CDK7	P50613	PSP
775	T	Phosphorylation	Kinase	CDK2	P24941	PSP
775	T	Phosphorylation	Kinase	CDK9	P50750	Uniprot
775	T	Phosphorylation	Kinase	CDK7	P50613	PSP
782	S	Phosphorylation	Kinase	CDK7	P50613	PSP
782	S	Phosphorylation	Kinase	CDK9	P50750	PSP
784	T	Phosphorylation	Kinase	CDK9	P50750	Uniprot
784	T	Phosphorylation	Kinase	CDK7	P50613	PSP
791	T	Phosphorylation	Kinase	CDK9	P50750	PSP
791	T	Phosphorylation	Kinase	CDK2	P24941	PSP
799	T	Phosphorylation	Kinase	CDK9	P50750	PSP
806	T	Phosphorylation	Kinase	CDK9	P50750	PSP
814	T	Phosphorylation	Kinase	CDK9	P50750	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SPT5H_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 SPT5H_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ANM5_HUMAN	PRMT5	physical	12718890
SPT4H_HUMAN	SUPT4H1	physical	12718890
ANM1_HUMAN	PRMT1	physical	12718890
RPB1_HUMAN	POLR2A	physical	10454543
HTSF1_HUMAN	HTATSF1	physical	10454543
PIN1_HUMAN	PIN1	physical	11575923
CDK9_HUMAN	CDK9	physical	10958691
CCNT1_HUMAN	CCNT1	physical	10958691
CDK7_HUMAN	CDK7	physical	10958691
CCNH_HUMAN	CCNH	physical	10958691
NEMO_HUMAN	IKBKG	physical	20211142
SSBP3_HUMAN	SSBP3	physical	20211142
MAML3_HUMAN	MAML3	physical	20211142
ZBTB3_HUMAN	ZBTB3	physical	20211142
ZN496_HUMAN	ZNF496	physical	20211142
RPB1_HUMAN	POLR2A	physical	21880767
SPT4H_HUMAN	SUPT4H1	physical	12653964
T2FB_HUMAN	GTF2F2	physical	22939629
SPT4H_HUMAN	SUPT4H1	physical	10075709
RPB1_HUMAN	POLR2A	physical	10075709
TAT_HV1H2	tat	physical	11112772
CARM1_HUMAN	CARM1	physical	22863883
RANB3_HUMAN	RANBP3	physical	22863883
SC24C_HUMAN	SEC24C	physical	22863883
SF01_HUMAN	SF1	physical	22863883
BRCA1_HUMAN	BRCA1	physical	18197258
RPB1_HUMAN	POLR2A	physical	18197258
CSK2B_HUMAN	CSNK2B	physical	26344197
CTR9_HUMAN	CTR9	physical	26344197
PAF1_HUMAN	PAF1	physical	26344197
RPB2_HUMAN	POLR2B	physical	26344197
SPT4H_HUMAN	SUPT4H1	physical	26344197
RPB1_HUMAN	POLR2A	physical	26496610
RPB2_HUMAN	POLR2B	physical	26496610
RPB3_HUMAN	POLR2C	physical	26496610
RPB4_HUMAN	POLR2D	physical	26496610
RPAB1_HUMAN	POLR2E	physical	26496610
RPB7_HUMAN	POLR2G	physical	26496610
RPAB3_HUMAN	POLR2H	physical	26496610
RPB9_HUMAN	POLR2I	physical	26496610
RPB11_HUMAN	POLR2J	physical	26496610
RPAB5_HUMAN	POLR2L	physical	26496610
SPT4H_HUMAN	SUPT4H1	physical	26496610
SPT6H_HUMAN	SUPT6H	physical	26496610
WIPF1_HUMAN	WIPF1	physical	26496610
NOLC1_HUMAN	NOLC1	physical	26496610
MED14_HUMAN	MED14	physical	26496610
SETX_HUMAN	SETX	physical	26496610
SYNE2_HUMAN	SYNE2	physical	26496610
RPRD2_HUMAN	RPRD2	physical	26496610
PHF3_HUMAN	PHF3	physical	26496610
POC1A_HUMAN	POC1A	physical	26496610
PAF1_HUMAN	PAF1	physical	26496610
MCM10_HUMAN	MCM10	physical	26496610
IWS1_HUMAN	IWS1	physical	26496610
RPR1B_HUMAN	RPRD1B	physical	26496610
CDC73_HUMAN	CDC73	physical	26496610
JADE1_HUMAN	JADE1	physical	26496610
WDR61_HUMAN	WDR61	physical	26496610
LEO1_HUMAN	LEO1	physical	26496610
RN214_HUMAN	RNF214	physical	26496610
AIPL1_HUMAN	AIPL1	physical	27173435
PDE5A_HUMAN	PDE5A	physical	27173435

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 SPT5H_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-328, AND MASS SPECTROMETRY.	19608861 [Abstract]
Methylation
Reference	PubMed
"Methylation of SPT5 regulates its interaction with RNA polymerase IIand transcriptional elongation properties."; Kwak Y.T., Guo J., Prajapati S., Park K.-J., Surabhi R.M., Miller B.,Gehrig P., Gaynor R.B.; Mol. Cell 11:1055-1066(2003). Cited for: FUNCTION, INTERACTION WITH CDK9; PRMT1; RNA POLYMERASE II; PRMT5 ANDSUPT4H1, METHYLATION AT ARG-681; ARG-696 AND ARG-698, AND MUTAGENESISOF ARG-681; ARG-696 AND ARG-698.	12718890 [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-666, AND MASSSPECTROMETRY.	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-666 AND THR-791, ANDMASS 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-666 AND THR-1034, ANDMASS 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-666, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666; THR-709; TYR-717AND THR-1034, AND MASS SPECTROMETRY.	17924679 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Domains in the SPT5 protein that modulate its transcriptionalregulatory properties."; Ivanov D., Kwak Y.T., Guo J., Gaynor R.B.; Mol. Cell. Biol. 20:2970-2983(2000). Cited for: FUNCTION, INTERACTION WITH RNA POLYMERASE II AND SUPT4H1, ANDPHOSPHORYLATION AT THR-775 AND THR-784.	10757782 [Abstract]