dbPTM

MTA2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MTA2_HUMAN
UniProt AC	O94776
Protein Name	Metastasis-associated protein MTA2
Gene Name	MTA2
Organism	Homo sapiens (Human).
Sequence Length	668
Subcellular Localization	Nucleus .
Protein Description	May be involved in the regulation of gene expression as repressor and activator. The repression might be related to covalent modification of histone proteins..
Protein Sequence	MAANMYRVGDYVYFENSSSNPYLVRRIEELNKTANGNVEAKVVCLFRRRDISSSLNSLADSNAREFEEESKQPGVSEQQRHQLKHRELFLSRQFESLPATHIRGKCSVTLLNETDILSQYLEKEDCFFYSLVFDPVQKTLLADQGEIRVGCKYQAEIPDRLVEGESDNRNQQKMEMKVWDPDNPLTDRQIDQFLVVARAVGTFARALDCSSSIRQPSLHMSAAAASRDITLFHAMDTLQRNGYDLAKAMSTLVPQGGPVLCRDEMEEWSASEAMLFEEALEKYGKDFNDIRQDFLPWKSLASIVQFYYMWKTTDRYIQQKRLKAAEADSKLKQVYIPTYTKPNPNQIISVGSKPGMNGAGFQKGLTCESCHTTQSAQWYAWGPPNMQCRLCASCWIYWKKYGGLKTPTQLEGATRGTTEPHSRGHLSRPEAQSLSPYTTSANRAKLLAKNRQTFLLQTTKLTRLARRMCRDLLQPRRAARRPYAPINANAIKAECSIRLPKAAKTPLKIHPLVRLPLATIVKDLVAQAPLKPKTPRGTKTPINRNQLSQNRGLGGIMVKRAYETMAGAGVPFSANGRPLASGIRSSSQPAAKRQKLNPADAPNPVVFVATKDTRALRKALTHLEMRRAARRPNLPLKVKPTLIAVRPPVPLPAPSHPASTNEPIVLED

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MAANMYRVGDYVY --CCCCCEEECCEEE	11.27	24043423
11	Phosphorylation	NMYRVGDYVYFENSS CCEEECCEEEEECCC	7.36	22817900
13	Phosphorylation	YRVGDYVYFENSSSN EEECCEEEEECCCCC	10.03	24719451
17	Phosphorylation	DYVYFENSSSNPYLV CEEEEECCCCCHHHH	28.13	24043423
18	Phosphorylation	YVYFENSSSNPYLVR EEEEECCCCCHHHHH	45.79	24043423
19	Phosphorylation	VYFENSSSNPYLVRR EEEECCCCCHHHHHH	41.46	24719451
22	Phosphorylation	ENSSSNPYLVRRIEE ECCCCCHHHHHHHHH	23.29	17360941
32	Acetylation	RRIEELNKTANGNVE HHHHHHHHHCCCCEE	62.73	25953088
32	Ubiquitination	RRIEELNKTANGNVE HHHHHHHHHCCCCEE	62.73	21890473
41	Acetylation	ANGNVEAKVVCLFRR CCCCEEEEEEEEEEC	22.99	26051181
41	Ubiquitination	ANGNVEAKVVCLFRR CCCCEEEEEEEEEEC	22.99	-
52	Phosphorylation	LFRRRDISSSLNSLA EEECCCCHHHHHHHH	20.40	27794612
53	Phosphorylation	FRRRDISSSLNSLAD EECCCCHHHHHHHHH	38.90	30266825
54	Phosphorylation	RRRDISSSLNSLADS ECCCCHHHHHHHHHH	25.44	30266825
57	Phosphorylation	DISSSLNSLADSNAR CCHHHHHHHHHHCHH	30.17	30266825
61	Phosphorylation	SLNSLADSNAREFEE HHHHHHHHCHHHHHH	27.12	21406692
70	Phosphorylation	AREFEEESKQPGVSE HHHHHHHHCCCCCCH	39.61	21815630
71	Acetylation	REFEEESKQPGVSEQ HHHHHHHCCCCCCHH	64.89	26051181
71	Ubiquitination	REFEEESKQPGVSEQ HHHHHHHCCCCCCHH	64.89	21890473
105	Acetylation	PATHIRGKCSVTLLN CCCEECCCCEEEEEC	17.31	26051181
152	Acetylation	GEIRVGCKYQAEIPD CCEEECEEEEEECCC	34.17	19608861
152	Malonylation	GEIRVGCKYQAEIPD CCEEECEEEEEECCC	34.17	26320211
152	Ubiquitination	GEIRVGCKYQAEIPD CCEEECEEEEEECCC	34.17	19608861
160	Methylation	YQAEIPDRLVEGESD EEEECCCCCCCCCCC	34.97	115483943
169	Methylation	VEGESDNRNQQKMEM CCCCCCCHHHHCEEE	47.53	115483951
173	Acetylation	SDNRNQQKMEMKVWD CCCHHHHCEEEEECC	27.36	25953088
173	Methylation	SDNRNQQKMEMKVWD CCCHHHHCEEEEECC	27.36	115483959
173	Ubiquitination	SDNRNQQKMEMKVWD CCCHHHHCEEEEECC	27.36	-
177	Ubiquitination	NQQKMEMKVWDPDNP HHHCEEEEECCCCCC	27.20	-
188	Methylation	PDNPLTDRQIDQFLV CCCCCCHHHHHHHHH	30.07	115483935
217	Phosphorylation	SSSIRQPSLHMSAAA CCCCCCCCHHHHHHH	23.67	21406692
221	Phosphorylation	RQPSLHMSAAAASRD CCCCHHHHHHHHHCC	12.19	21406692
226	Phosphorylation	HMSAAAASRDITLFH HHHHHHHHCCHHHHH	26.26	21406692
237	Phosphorylation	TLFHAMDTLQRNGYD HHHHHHHHHHHCCHH	16.23	24945436
282	Ubiquitination	LFEEALEKYGKDFND HHHHHHHHHCCCHHH	61.22	-
285	Ubiquitination	EALEKYGKDFNDIRQ HHHHHHCCCHHHHHH	56.93	-
320	Ubiquitination	TDRYIQQKRLKAAEA HHHHHHHHHHHHHHH	43.24	-
332	Acetylation	AEADSKLKQVYIPTY HHHCHHCCEEECCCC	41.26	20167786
335	Phosphorylation	DSKLKQVYIPTYTKP CHHCCEEECCCCCCC	9.93	-
339	Phosphorylation	KQVYIPTYTKPNPNQ CEEECCCCCCCCCCC	13.86	-
341	Acetylation	VYIPTYTKPNPNQII EECCCCCCCCCCCEE	32.17	20167786
341	Ubiquitination	VYIPTYTKPNPNQII EECCCCCCCCCCCEE	32.17	-
352	Phosphorylation	NQIISVGSKPGMNGA CCEEEECCCCCCCCC	33.26	25159151
353	Acetylation	QIISVGSKPGMNGAG CEEEECCCCCCCCCC	39.39	25953088
393	Phosphorylation	MQCRLCASCWIYWKK HHCCHHHHHHHHHHH	14.69	20860994
397	Phosphorylation	LCASCWIYWKKYGGL HHHHHHHHHHHCCCC	6.15	20860994
399	Acetylation	ASCWIYWKKYGGLKT HHHHHHHHHCCCCCC	21.10	26051181
401	Phosphorylation	CWIYWKKYGGLKTPT HHHHHHHCCCCCCCC	16.82	23186163
405	Ubiquitination	WKKYGGLKTPTQLEG HHHCCCCCCCCCCCC	56.59	-
406	Phosphorylation	KKYGGLKTPTQLEGA HHCCCCCCCCCCCCC	36.29	25159151
408	Phosphorylation	YGGLKTPTQLEGATR CCCCCCCCCCCCCCC	51.52	23186163
414	Phosphorylation	PTQLEGATRGTTEPH CCCCCCCCCCCCCCC	40.25	23186163
427	Phosphorylation	PHSRGHLSRPEAQSL CCCCCCCCCHHHHCC	39.86	25159151
433	Phosphorylation	LSRPEAQSLSPYTTS CCCHHHHCCCCCCCC	37.55	25159151
435	Phosphorylation	RPEAQSLSPYTTSAN CHHHHCCCCCCCCHH	22.55	20201521
437	Phosphorylation	EAQSLSPYTTSANRA HHHCCCCCCCCHHHH	21.19	30266825
438	Phosphorylation	AQSLSPYTTSANRAK HHCCCCCCCCHHHHH	20.05	30266825
439	Phosphorylation	QSLSPYTTSANRAKL HCCCCCCCCHHHHHH	21.72	30266825
440	Phosphorylation	SLSPYTTSANRAKLL CCCCCCCCHHHHHHH	18.75	30266825
453	Phosphorylation	LLAKNRQTFLLQTTK HHHHCCCHHHHHHHH	17.02	28555341
458	Phosphorylation	RQTFLLQTTKLTRLA CCHHHHHHHHHHHHH	26.35	-
459	Phosphorylation	QTFLLQTTKLTRLAR CHHHHHHHHHHHHHH	15.87	-
460	Acetylation	TFLLQTTKLTRLARR HHHHHHHHHHHHHHH	51.77	-
460	Ubiquitination	TFLLQTTKLTRLARR HHHHHHHHHHHHHHH	51.77	21890473
460	Ubiquitination	TFLLQTTKLTRLARR HHHHHHHHHHHHHHH	51.77	21890473
483	Phosphorylation	RRAARRPYAPINANA HHHHCCCCCCCCHHH	24.17	28152594
492	Acetylation	PINANAIKAECSIRL CCCHHHEEEEEEEEC	35.40	25953088
496	Phosphorylation	NAIKAECSIRLPKAA HHEEEEEEEECCCCC	11.40	25159151
504	Ubiquitination	IRLPKAAKTPLKIHP EECCCCCCCCCCCCC	56.38	-
505	Phosphorylation	RLPKAAKTPLKIHPL ECCCCCCCCCCCCCC	29.18	23927012
508	Acetylation	KAAKTPLKIHPLVRL CCCCCCCCCCCCCCC	39.92	26051181
508	Sumoylation	KAAKTPLKIHPLVRL CCCCCCCCCCCCCCC	39.92	28112733
508	Ubiquitination	KAAKTPLKIHPLVRL CCCCCCCCCCCCCCC	39.92	21890473
508	Ubiquitination	KAAKTPLKIHPLVRL CCCCCCCCCCCCCCC	39.92	21890473
519	Phosphorylation	LVRLPLATIVKDLVA CCCCCHHHHHHHHHH	33.70	20068231
522	Acetylation	LPLATIVKDLVAQAP CCHHHHHHHHHHCCC	41.30	-
522	Ubiquitination	LPLATIVKDLVAQAP CCHHHHHHHHHHCCC	41.30	21890473
522	Ubiquitination	LPLATIVKDLVAQAP CCHHHHHHHHHHCCC	41.30	21890473
531	Acetylation	LVAQAPLKPKTPRGT HHHCCCCCCCCCCCC	43.33	23954790
531	Ubiquitination	LVAQAPLKPKTPRGT HHHCCCCCCCCCCCC	43.33	-
534	Phosphorylation	QAPLKPKTPRGTKTP CCCCCCCCCCCCCCC	27.09	25159151
538	Phosphorylation	KPKTPRGTKTPINRN CCCCCCCCCCCCCHH	32.78	30576142
539	Ubiquitination	PKTPRGTKTPINRNQ CCCCCCCCCCCCHHH	55.94	-
540	Phosphorylation	KTPRGTKTPINRNQL CCCCCCCCCCCHHHH	29.28	20068231
548	Phosphorylation	PINRNQLSQNRGLGG CCCHHHHHCCCCCCH	18.69	25159151
551	Methylation	RNQLSQNRGLGGIMV HHHHHCCCCCCHHHH	33.79	115483927
559	Acetylation	GLGGIMVKRAYETMA CCCHHHHHHHHHHHC	17.58	25953088
559	Methylation	GLGGIMVKRAYETMA CCCHHHHHHHHHHHC	17.58	7614655
559	Sumoylation	GLGGIMVKRAYETMA CCCHHHHHHHHHHHC	17.58	28112733
559	Ubiquitination	GLGGIMVKRAYETMA CCCHHHHHHHHHHHC	17.58	-
562	Phosphorylation	GIMVKRAYETMAGAG HHHHHHHHHHHCCCC	18.90	-
564	Phosphorylation	MVKRAYETMAGAGVP HHHHHHHHHCCCCCC	10.31	20068231
573	Phosphorylation	AGAGVPFSANGRPLA CCCCCCCCCCCCCCC	18.11	29978859
581	Phosphorylation	ANGRPLASGIRSSSQ CCCCCCCCCCCCCCC	42.30	20068231
586	Phosphorylation	LASGIRSSSQPAAKR CCCCCCCCCCHHHHH	24.12	28555341
587	Phosphorylation	ASGIRSSSQPAAKRQ CCCCCCCCCHHHHHH	41.24	26853621
592	Acetylation	SSSQPAAKRQKLNPA CCCCHHHHHHCCCCC	58.42	30585581
595	Acetylation	QPAAKRQKLNPADAP CHHHHHHCCCCCCCC	55.02	25953088
595	Sumoylation	QPAAKRQKLNPADAP CHHHHHHCCCCCCCC	55.02	28112733
610	Phosphorylation	NPVVFVATKDTRALR CCEEEEEECCHHHHH	24.93	22210691
611	Acetylation	PVVFVATKDTRALRK CEEEEEECCHHHHHH	47.57	25953088
611	Ubiquitination	PVVFVATKDTRALRK CEEEEEECCHHHHHH	47.57	21890473
611	Ubiquitination	PVVFVATKDTRALRK CEEEEEECCHHHHHH	47.57	21890473
621	Phosphorylation	RALRKALTHLEMRRA HHHHHHHHHHHHHHH	29.31	-
655	Phosphorylation	PVPLPAPSHPASTNE CCCCCCCCCCCCCCC	44.18	28555341
659	Phosphorylation	PAPSHPASTNEPIVL CCCCCCCCCCCCCCC	35.90	27251275
660	Phosphorylation	APSHPASTNEPIVLE CCCCCCCCCCCCCCC	45.79	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
Oops, there are no upstream regulatory protein records of MTA2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MTA2_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 MTA2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CHD4_HUMAN	CHD4	physical	12920132
SIN3A_HUMAN	SIN3A	physical	12920132
MTA1_HUMAN	MTA1	physical	12920132
HDAC1_HUMAN	HDAC1	physical	12920132
HDAC2_HUMAN	HDAC2	physical	12920132
RBBP4_HUMAN	RBBP4	physical	12920132
RBBP7_HUMAN	RBBP7	physical	12920132
TOP2B_HUMAN	TOP2B	physical	11062478
HDAC1_HUMAN	HDAC1	physical	10444591
HDAC2_HUMAN	HDAC2	physical	10444591
RBBP4_HUMAN	RBBP4	physical	10444591
RBBP7_HUMAN	RBBP7	physical	10444591
MBD3_HUMAN	MBD3	physical	10444591
CHD3_HUMAN	CHD3	physical	10444591
HDAC1_HUMAN	HDAC1	physical	19686092
HDAC2_HUMAN	HDAC2	physical	19686092
RBBP4_HUMAN	RBBP4	physical	19686092
MED30_HUMAN	MED30	physical	20211142
ESR1_HUMAN	ESR1	physical	16645043
HDAC1_HUMAN	HDAC1	physical	16645043
BC11B_HUMAN	BCL11B	physical	16091750
CHD3_HUMAN	CHD3	physical	11297506
HDAC1_HUMAN	HDAC1	physical	11297506
HDAC2_HUMAN	HDAC2	physical	11297506
RBBP7_HUMAN	RBBP7	physical	11297506
RBBP4_HUMAN	RBBP4	physical	11297506
MBD2_HUMAN	MBD2	physical	11297506
MBD3_HUMAN	MBD3	physical	11297506
HDAC1_HUMAN	HDAC1	physical	11102443
HDAC2_HUMAN	HDAC2	physical	11102443
MBD2_HUMAN	MBD2	physical	11102443
TRX1_HHV11	UL38	physical	20585571
BRCA1_HUMAN	BRCA1	physical	19703393
CHD3_HUMAN	CHD3	physical	19703393
CHD4_HUMAN	CHD4	physical	19703393
KDM1A_HUMAN	KDM1A	physical	19703393
HDAC1_HUMAN	HDAC1	physical	19703393
HDAC2_HUMAN	HDAC2	physical	19703393
RBBP7_HUMAN	RBBP7	physical	19703393
RBBP4_HUMAN	RBBP4	physical	19703393
MBD3_HUMAN	MBD3	physical	19703393
RBBP7_HUMAN	RBBP7	physical	20714342
HDAC2_HUMAN	HDAC2	physical	20714342
TWST1_HUMAN	TWIST1	physical	22457607
RBBP4_HUMAN	RBBP4	physical	22939629
RBBP7_HUMAN	RBBP7	physical	22939629
P66B_HUMAN	GATAD2B	physical	22939629
P66A_HUMAN	GATAD2A	physical	22939629
T22D3_HUMAN	TSC22D3	physical	21988832
UBE3C_HUMAN	UBE3C	physical	21988832
BRCC3_HUMAN	BRCC3	physical	22863883
CD2AP_HUMAN	CD2AP	physical	22863883
EH1L1_HUMAN	EHBP1L1	physical	22863883
GEPH_HUMAN	GPHN	physical	22863883
JIP4_HUMAN	SPAG9	physical	22863883
LARP7_HUMAN	LARP7	physical	22863883
MAP4_HUMAN	MAP4	physical	22863883
LSM8_HUMAN	LSM8	physical	22863883
RPB1_HUMAN	POLR2A	physical	22863883
RPB3_HUMAN	POLR2C	physical	22863883
PP4R1_HUMAN	PPP4R1	physical	22863883
RABE2_HUMAN	RABEP2	physical	22863883
ROCK2_HUMAN	ROCK2	physical	22863883
NACC2_HUMAN	NACC2	physical	22926524
DNMT1_HUMAN	DNMT1	physical	23708667
P66A_HUMAN	GATAD2A	physical	26344197
MTA1_HUMAN	MTA1	physical	26344197
RBBP4_HUMAN	RBBP4	physical	28179136
RBBP7_HUMAN	RBBP7	physical	28179136
IMA1_HUMAN	KPNA2	physical	28179136
IMB1_HUMAN	KPNB1	physical	28179136
ZN827_HUMAN	ZNF827	physical	25150861

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 MTA2_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-152, 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-435, AND MASSSPECTROMETRY.	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-433; SER-435; THR-505AND THR-534, 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-435, AND MASSSPECTROMETRY.	18691976 [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-435, AND MASSSPECTROMETRY.	18220336 [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-57, AND MASSSPECTROMETRY.	17081983 [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 THR-540, AND MASSSPECTROMETRY.	17924679 [Abstract]