dbPTM

MED14_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MED14_HUMAN
UniProt AC	O60244
Protein Name	Mediator of RNA polymerase II transcription subunit 14
Gene Name	MED14
Organism	Homo sapiens (Human).
Sequence Length	1454
Subcellular Localization	Nucleus .
Protein Description	Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors..
Protein Sequence	MAPVQLENHQLVPPGGGGGGSGGPPSAPAPPPPGAAVAAAAAAAASPGYRLSTLIEFLLHRAYSELMVLTDLLPRKSDVERKIEIVQFASRTRQLFVRLLALVKWANNAGKVEKCAMISSFLDQQAILFVDTADRLASLARDALVHARLPSFAIPYAIDVLTTGSYPRLPTCIRDKIIPPDPITKIEKQATLHQLNQILRHRLVTTDLPPQLANLTVANGRVKFRVEGEFEATLTVMGDDPDVPWRLLKLEILVEDKETGDGRALVHSMQISFIHQLVQSRLFADEKPLQDMYNCLHSFCLSLQLEVLHSQTLMLIRERWGDLVQVERYHAGKCLSLSVWNQQVLGRKTGTASVHKVTIKIDENDVSKPLQIFHDPPLPASDSKLVERAMKIDHLSIEKLLIDSVHARAHQKLQELKAILRGFNANENSSIETALPALVVPILEPCGNSECLHIFVDLHSGMFQLMLYGLDQATLDDMEKSVNDDMKRIIPWIQQLKFWLGQQRCKQSIKHLPTISSETLQLSNYSTHPIGNLSKNKLFIKLTRLPQYYIVVEMLEVPNKPTQLSYKYYFMSVNAADREDSPAMALLLQQFKENIQDLVFRTKTGKQTRTNAKRKLSDDPCPVESKKTKRAGEMCAFNKVLAHFVAMCDTNMPFVGLRLELSNLEIPHQGVQVEGDGFSHAIRLLKIPPCKGITEETQKALDRSLLDCTFRLQGRNNRTWVAELVFANCPLNGTSTREQGPSRHVYLTYENLLSEPVGGRKVVEMFLNDWNSIARLYECVLEFARSLPDIPAHLNIFSEVRVYNYRKLILCYGTTKGSSISIQWNSIHQKFHISLGTVGPNSGCSNCHNTILHQLQEMFNKTPNVVQLLQVLFDTQAPLNAINKLPTVPMLGLTQRTNTAYQCFSILPQSSTHIRLAFRNMYCIDIYCRSRGVVAIRDGAYSLFDNSKLVEGFYPAPGLKTFLNMFVDSNQDARRRSVNEDDNPPSPIGGDMMDSLISQLQPPPQQQPFPKQPGTSGAYPLTSPPTSYHSTVNQSPSMMHTQSPGNLHAASSPSGALRAPSPASFVPTPPPSSHGISIGPGASFASPHGTLDPSSPYTMVSPSGRAGNWPGSPQVSGPSPAARMPGMSPANPSLHSPVPDASHSPRAGTSSQTMPTNMPPPRKLPQRSWAASIPTILTHSALNILLLPSPTPGLVPGLAGSYLCSPLERFLGSVIMRRHLQRIIQQETLQLINSNEPGVIMFKTDALKCRVALSPKTNQTLQLKVTPENAGQWKPDELQVLEKFFETRVAGPPFKANTLIAFTKLLGAPTHILRDCVHIMKLELFPDQATQLKWNVQFCLTIPPSAPPIAPPGTPAVVLKSKMLFFLQLTQKTSVPPQEPVSIIVPIIYDMASGTTQQADIPRQQNSSVAAPMMVSNILKRFAEMNPPRQGECTIFAAVRDLMANLTLPPGGRP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
60	Ubiquitination	TLIEFLLHRAYSELM HHHHHHHHHHHHHHH	17.93	21890473
69	Ubiquitination	AYSELMVLTDLLPRK HHHHHHHHHHCCCCC	1.60	21890473
72	Ubiquitination	ELMVLTDLLPRKSDV HHHHHHHCCCCCCHH	6.29	21890473
111	Acetylation	KWANNAGKVEKCAMI HHHHHCCHHHHHHHH	44.82	26051181
111	Ubiquitination	KWANNAGKVEKCAMI HHHHHCCHHHHHHHH	44.82	29967540
119	Phosphorylation	VEKCAMISSFLDQQA HHHHHHHHHHCCCCE	11.27	30576142
120	Phosphorylation	EKCAMISSFLDQQAI HHHHHHHHHCCCCEE	20.92	30576142
138	Phosphorylation	DTADRLASLARDALV EHHHHHHHHHHHHHH	27.44	30576142
151	Phosphorylation	LVHARLPSFAIPYAI HHHCCCCCCCCCCEE	31.72	-
176	Acetylation	LPTCIRDKIIPPDPI CCCCCCCCCCCCCCC	32.46	26051181
176	Ubiquitination	LPTCIRDKIIPPDPI CCCCCCCCCCCCCCC	32.46	23000965
184	Phosphorylation	IIPPDPITKIEKQAT CCCCCCCCHHHHHHH	31.21	20068231
185	Ubiquitination	IPPDPITKIEKQATL CCCCCCCHHHHHHHH	49.98	21906983
188	Ubiquitination	DPITKIEKQATLHQL CCCCHHHHHHHHHHH	49.02	22817900
191	O-linked_Glycosylation	TKIEKQATLHQLNQI CHHHHHHHHHHHHHH	23.44	30379171
233	Phosphorylation	VEGEFEATLTVMGDD EEEEEEEEEEEECCC	18.76	29759185
235	Phosphorylation	GEFEATLTVMGDDPD EEEEEEEEEECCCCC	12.23	29759185
268	Ubiquitination	DGRALVHSMQISFIH CCCHHHHHHHHHHHH	12.61	22817900
283	Ubiquitination	QLVQSRLFADEKPLQ HHHHHHCCCCCCCHH	8.60	21890473
296	Ubiquitination	LQDMYNCLHSFCLSL HHHHHHHHHHHHHHH	3.18	22817900
301	Ubiquitination	NCLHSFCLSLQLEVL HHHHHHHHHHHHHHH	5.58	21963094
351	Phosphorylation	VLGRKTGTASVHKVT HCCCCCCCCEEEEEE	22.46	25599653
356	Ubiquitination	TGTASVHKVTIKIDE CCCCEEEEEEEEECC	38.63	29967540
360	Acetylation	SVHKVTIKIDENDVS EEEEEEEEECCCCCC	34.44	23236377
367	Phosphorylation	KIDENDVSKPLQIFH EECCCCCCCCEEECC	31.27	24719451
368	Ubiquitination	IDENDVSKPLQIFHD ECCCCCCCCEEECCC	49.98	29967540
381	Phosphorylation	HDPPLPASDSKLVER CCCCCCCCCCHHHHH	40.24	23898821
383	Phosphorylation	PPLPASDSKLVERAM CCCCCCCCHHHHHHH	25.95	23898821
384	Ubiquitination	PLPASDSKLVERAMK CCCCCCCHHHHHHHH	62.64	21906983
390	Ubiquitination	SKLVERAMKIDHLSI CHHHHHHHHCCCCCH	4.97	22817900
391	Ubiquitination	KLVERAMKIDHLSIE HHHHHHHHCCCCCHH	43.95	29967540
394	Ubiquitination	ERAMKIDHLSIEKLL HHHHHCCCCCHHHHH	25.58	21890473
396	Phosphorylation	AMKIDHLSIEKLLID HHHCCCCCHHHHHHH	25.86	22210691
399	"N6,N6-dimethyllysine"	IDHLSIEKLLIDSVH CCCCCHHHHHHHHHH	47.09	-
399	Methylation	IDHLSIEKLLIDSVH CCCCCHHHHHHHHHH	47.09	23644510
399	Ubiquitination	IDHLSIEKLLIDSVH CCCCCHHHHHHHHHH	47.09	22817900
412	Ubiquitination	VHARAHQKLQELKAI HHHHHHHHHHHHHHH	42.12	22817900
417	Ubiquitination	HQKLQELKAILRGFN HHHHHHHHHHHHCCC	32.40	21963094
487	Ubiquitination	KSVNDDMKRIIPWIQ HHCCHHHHHHHHHHH	47.65	-
506	Ubiquitination	WLGQQRCKQSIKHLP HHCHHHHHHHHHCCC	49.63	22817900
510	Ubiquitination	QRCKQSIKHLPTISS HHHHHHHHCCCCCCH	44.32	21906983
535	Ubiquitination	HPIGNLSKNKLFIKL CCCCCCCCCCEEEEC	62.36	29967540
568	Phosphorylation	PTQLSYKYYFMSVNA CCEEEEEEEEEECCH	8.16	22817900
583	Ubiquitination	ADREDSPAMALLLQQ HCCCCCHHHHHHHHH	10.38	21890473
604	O-linked_Glycosylation	DLVFRTKTGKQTRTN HHHHHCCCCCCCCCC	49.34	30379171
615	Acetylation	TRTNAKRKLSDDPCP CCCCCHHHCCCCCCC	52.19	25953088
617	Phosphorylation	TNAKRKLSDDPCPVE CCCHHHCCCCCCCCC	42.90	29255136
625	Phosphorylation	DDPCPVESKKTKRAG CCCCCCCCCCCCCHH	39.42	30266825
626	Acetylation	DPCPVESKKTKRAGE CCCCCCCCCCCCHHH	51.46	25953088
626	Ubiquitination	DPCPVESKKTKRAGE CCCCCCCCCCCCHHH	51.46	33845483
627	Ubiquitination	PCPVESKKTKRAGEM CCCCCCCCCCCHHHH	69.43	-
691	Ubiquitination	LLKIPPCKGITEETQ HCCCCCCCCCCHHHH	60.15	29967540
699	Ubiquitination	GITEETQKALDRSLL CCCHHHHHHHHHHHH	59.33	22817900
798	Phosphorylation	PAHLNIFSEVRVYNY CHHHCCCCCEEEEEC	31.24	24719451
832	Ubiquitination	NSIHQKFHISLGTVG CCCCCEEEEEECCCC	18.76	21963094
901	Phosphorylation	TQRTNTAYQCFSILP ECCCCCHHHHHHHCC	12.08	-
927	Phosphorylation	NMYCIDIYCRSRGVV CEEEEEEEECCCCEE	4.32	-
941	Phosphorylation	VAIRDGAYSLFDNSK EEEECCCEECCCCCC	16.07	-
948	Ubiquitination	YSLFDNSKLVEGFYP EECCCCCCCCCEEEC	63.91	21906983
977	Phosphorylation	NQDARRRSVNEDDNP CHHHHHHCCCCCCCC	27.73	30278072
986	Phosphorylation	NEDDNPPSPIGGDMM CCCCCCCCCCCHHHH	30.33	30278072
995	Phosphorylation	IGGDMMDSLISQLQP CCHHHHHHHHHHCCC	15.09	23663014
998	Phosphorylation	DMMDSLISQLQPPPQ HHHHHHHHHCCCCCC	30.08	28464451
1061	Phosphorylation	SGALRAPSPASFVPT CCCCCCCCCCCCCCC	31.92	23401153
1064	Phosphorylation	LRAPSPASFVPTPPP CCCCCCCCCCCCCCC	30.11	23401153
1083	Phosphorylation	ISIGPGASFASPHGT EEECCCCCCCCCCCC	27.53	26074081
1086	Phosphorylation	GPGASFASPHGTLDP CCCCCCCCCCCCCCC	18.54	26074081
1090	Phosphorylation	SFASPHGTLDPSSPY CCCCCCCCCCCCCCC	25.59	26074081
1094	Phosphorylation	PHGTLDPSSPYTMVS CCCCCCCCCCCEEEC	43.54	26074081
1095	Phosphorylation	HGTLDPSSPYTMVSP CCCCCCCCCCEEECC	27.58	26074081
1097	Phosphorylation	TLDPSSPYTMVSPSG CCCCCCCCEEECCCC	14.93	26074081
1098	Phosphorylation	LDPSSPYTMVSPSGR CCCCCCCEEECCCCC	17.93	23401153
1101	Phosphorylation	SSPYTMVSPSGRAGN CCCCEEECCCCCCCC	11.52	23401153
1112	Phosphorylation	RAGNWPGSPQVSGPS CCCCCCCCCCCCCCC	14.21	25159151
1116	Phosphorylation	WPGSPQVSGPSPAAR CCCCCCCCCCCHHHC	39.47	25159151
1119	Phosphorylation	SPQVSGPSPAARMPG CCCCCCCCHHHCCCC	30.60	25159151
1123	Methylation	SGPSPAARMPGMSPA CCCCHHHCCCCCCCC	33.66	115367503
1127	Ubiquitination	PAARMPGMSPANPSL HHHCCCCCCCCCCCC	3.41	21963094
1128	Phosphorylation	AARMPGMSPANPSLH HHCCCCCCCCCCCCC	27.12	23927012
1132	Ubiquitination	PGMSPANPSLHSPVP CCCCCCCCCCCCCCC	40.13	22817900
1133	Phosphorylation	GMSPANPSLHSPVPD CCCCCCCCCCCCCCC	38.22	23401153
1136	Phosphorylation	PANPSLHSPVPDASH CCCCCCCCCCCCCCC	32.65	23927012
1140	Ubiquitination	SLHSPVPDASHSPRA CCCCCCCCCCCCCCC	62.02	21890473
1142	Phosphorylation	HSPVPDASHSPRAGT CCCCCCCCCCCCCCC	31.70	23401153
1144	Phosphorylation	PVPDASHSPRAGTSS CCCCCCCCCCCCCCC	17.37	23927012
1146	Methylation	PDASHSPRAGTSSQT CCCCCCCCCCCCCCC	48.98	115918925
1149	Phosphorylation	SHSPRAGTSSQTMPT CCCCCCCCCCCCCCC	24.99	22210691
1150	Phosphorylation	HSPRAGTSSQTMPTN CCCCCCCCCCCCCCC	21.38	22210691
1151	Phosphorylation	SPRAGTSSQTMPTNM CCCCCCCCCCCCCCC	29.52	26552605
1153	Phosphorylation	RAGTSSQTMPTNMPP CCCCCCCCCCCCCCC	27.37	23186163
1156	Phosphorylation	TSSQTMPTNMPPPRK CCCCCCCCCCCCCCC	33.07	26552605
1179	Ubiquitination	SIPTILTHSALNILL CCCHHHHHCHHHECC	13.97	21890473
1188	Ubiquitination	ALNILLLPSPTPGLV HHHECCCCCCCCCCC	37.93	21963094
1243	Ubiquitination	EPGVIMFKTDALKCR CCCEEEEECCCCEEE	28.28	21963094
1248	Ubiquitination	MFKTDALKCRVALSP EEECCCCEEEEEECC	23.01	22817900
1254	Phosphorylation	LKCRVALSPKTNQTL CEEEEEECCCCCCEE	18.02	24719451
1256	Ubiquitination	CRVALSPKTNQTLQL EEEEECCCCCCEEEE	57.65	22817900
1264	Ubiquitination	TNQTLQLKVTPENAG CCCEEEEEECCCCCC	30.97	29967540
1274	Ubiquitination	PENAGQWKPDELQVL CCCCCCCCHHHHHHH	34.40	29967540
1283	Ubiquitination	DELQVLEKFFETRVA HHHHHHHHHHHHHCC	51.71	29967540
1295	Ubiquitination	RVAGPPFKANTLIAF HCCCCCCCHHHHHHH	46.64	21906983
1304	Ubiquitination	NTLIAFTKLLGAPTH HHHHHHHHHHCCCHH	34.95	21963094
1354	Phosphorylation	PPIAPPGTPAVVLKS CCCCCCCCCEEEECC	17.53	-
1360	Ubiquitination	GTPAVVLKSKMLFFL CCCEEEECCHHHHEH	36.10	-
1361	Phosphorylation	TPAVVLKSKMLFFLQ CCEEEECCHHHHEHH	21.09	-
1373	Phosphorylation	FLQLTQKTSVPPQEP EHHHHCCCCCCCCCC	25.74	24043423
1374	Phosphorylation	LQLTQKTSVPPQEPV HHHHCCCCCCCCCCE	39.40	24043423
1382	Phosphorylation	VPPQEPVSIIVPIIY CCCCCCEEEEEEEEE	19.81	24043423
1389	Phosphorylation	SIIVPIIYDMASGTT EEEEEEEEECCCCCC	10.61	24043423
1393	Phosphorylation	PIIYDMASGTTQQAD EEEEECCCCCCCCCC	29.99	24043423
1395	Phosphorylation	IYDMASGTTQQADIP EEECCCCCCCCCCCC	20.95	24043423
1396	Phosphorylation	YDMASGTTQQADIPR EECCCCCCCCCCCCC	23.39	24043423
1416	Phosphorylation	VAAPMMVSNILKRFA CHHHHHHHHHHHHHH	10.56	28450419
1420	Ubiquitination	MMVSNILKRFAEMNP HHHHHHHHHHHHHCC	41.49	-
1425	Sulfoxidation	ILKRFAEMNPPRQGE HHHHHHHHCCCCCCC	9.05	21406390

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
986	S	Phosphorylation	Kinase	ERK2	P28482	PSP
986	S	Phosphorylation	Kinase	MAPK3	P27361	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MED14_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 MED14_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
STAT2_HUMAN	STAT2	physical	12509459
MED23_HUMAN	MED23	physical	9989412
MED7_HUMAN	MED7	physical	9989412
MED1_HUMAN	MED1	physical	9989412
MED24_HUMAN	MED24	physical	9989412
MED17_HUMAN	MED17	physical	9989412
MED26_HUMAN	MED26	physical	9989412
MED27_HUMAN	MED27	physical	9989412
ACTN1_HUMAN	ACTN1	physical	15604093
ACTN2_HUMAN	ACTN2	physical	15604093
DCTN1_HUMAN	DCTN1	physical	15604093
UACA_HUMAN	UACA	physical	15604093
NECA2_HUMAN	NECAB2	physical	15604093
MED29_HUMAN	MED29	physical	22939629
MED1_HUMAN	MED1	physical	22939629
MED17_HUMAN	MED17	physical	22939629
MED16_HUMAN	MED16	physical	22939629
MED21_HUMAN	MED21	physical	22939629
MED24_HUMAN	MED24	physical	22939629
MED4_HUMAN	MED4	physical	22939629
MED27_HUMAN	MED27	physical	22939629
MED8_HUMAN	MED8	physical	22939629
MED18_HUMAN	MED18	physical	22939629
PP6R1_HUMAN	PPP6R1	physical	22939629
PPARG_HUMAN	PPARG	physical	20194623
MED1_HUMAN	MED1	physical	26344197
MED10_HUMAN	MED10	physical	26344197
MED11_HUMAN	MED11	physical	26344197
MED12_HUMAN	MED12	physical	26344197
MED17_HUMAN	MED17	physical	26344197
MED19_HUMAN	MED19	physical	26344197
MED24_HUMAN	MED24	physical	26344197
MED27_HUMAN	MED27	physical	26344197
MED4_HUMAN	MED4	physical	26344197

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 MED14_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-1112; SER-1128 ANDSER-1136, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617; SER-986; SER-1112;SER-1133 AND SER-1142, AND MASS SPECTROMETRY.	19369195 [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-1112 AND SER-1119, 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-1128; SER-1133; SER-1136AND SER-1144, 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 SER-617 AND SER-1119, ANDMASS SPECTROMETRY.	18691976 [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-1128, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-986, AND MASSSPECTROMETRY.	15302935 [Abstract]