dbPTM

M3K1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	M3K1_HUMAN
UniProt AC	Q13233
Protein Name	Mitogen-activated protein kinase kinase kinase 1
Gene Name	MAP3K1
Organism	Homo sapiens (Human).
Sequence Length	1512
Subcellular Localization
Protein Description	Component of a protein kinase signal transduction cascade. [PubMed: 9808624 Activates the ERK and JNK kinase pathways by phosphorylation of MAP2K1 and MAP2K4]
Protein Sequence	MAAAAGNRASSSGFPGARATSPEAGGGGGALKASSAPAAAAGLLREAGSGGRERADWRRRQLRKVRSVELDQLPEQPLFLAASPPASSTSPSPEPADAAGSGTGFQPVAVPPPHGAASRGGAHLTESVAAPDSGASSPAAAEPGEKRAPAAEPSPAAAPAGREMENKETLKGLHKMDDRPEERMIREKLKATCMPAWKHEWLERRNRRGPVVVKPIPVKGDGSEMNHLAAESPGEVQASAASPASKGRRSPSPGNSPSGRTVKSESPGVRRKRVSPVPFQSGRITPPRRAPSPDGFSPYSPEETNRRVNKVMRARLYLLQQIGPNSFLIGGDSPDNKYRVFIGPQNCSCARGTFCIHLLFVMLRVFQLEPSDPMLWRKTLKNFEVESLFQKYHSRRSSRIKAPSRNTIQKFVSRMSNSHTLSSSSTSTSSSENSIKDEEEQMCPICLLGMLDEESLTVCEDGCRNKLHHHCMSIWAEECRRNREPLICPLCRSKWRSHDFYSHELSSPVDSPSSLRAAQQQTVQQQPLAGSRRNQESNFNLTHYGTQQIPPAYKDLAEPWIQVFGMELVGCLFSRNWNVREMALRRLSHDVSGALLLANGESTGNSGGSSGSSPSGGATSGSSQTSISGDVVEACCSVLSMVCADPVYKVYVAALKTLRAMLVYTPCHSLAERIKLQRLLQPVVDTILVKCADANSRTSQLSISTLLELCKGQAGELAVGREILKAGSIGIGGVDYVLNCILGNQTESNNWQELLGRLCLIDRLLLEFPAEFYPHIVSTDVSQAEPVEIRYKKLLSLLTFALQSIDNSHSMVGKLSRRIYLSSARMVTTVPHVFSKLLEMLSVSSSTHFTRMRRRLMAIADEVEIAEAIQLGVEDTLDGQQDSFLQASVPNNYLETTENSSPECTVHLEKTGKGLCATKLSASSEDISERLASISVGPSSSTTTTTTTTEQPKPMVQTKGRPHSQCLNSSPLSHHSQLMFPALSTPSSSTPSVPAGTATDVSKHRLQGFIPCRIPSASPQTQRKFSLQFHRNCPENKDSDKLSPVFTQSRPLPSSNIHRPKPSRPTPGNTSKQGDPSKNSMTLDLNSSSKCDDSFGCSSNSSNAVIPSDETVFTPVEEKCRLDVNTELNSSIEDLLEASMPSSDTTVTFKSEVAVLSPEKAENDDTYKDDVNHNQKCKEKMEAEEEEALAIAMAMSASQDALPIVPQLQVENGEDIIIIQQDTPETLPGHTKAKQPYREDTEWLKGQQIGLGAFSSCYQAQDVGTGTLMAVKQVTYVRNTSSEQEEVVEALREEIRMMSHLNHPNIIRMLGATCEKSNYNLFIEWMAGGSVAHLLSKYGAFKESVVINYTEQLLRGLSYLHENQIIHRDVKGANLLIDSTGQRLRIADFGAAARLASKGTGAGEFQGQLLGTIAFMAPEVLRGQQYGRSCDVWSVGCAIIEMACAKPPWNAEKHSNHLALIFKIASATTAPSIPSHLSPGLRDVALRCLELQPQDRPPSRELLKHPVFRTTW

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAAAGNRA ------CCCCCCCCC	19.67	19413330
11	Phosphorylation	AAGNRASSSGFPGAR CCCCCCCCCCCCCCC	33.23	24173317
12	Phosphorylation	AGNRASSSGFPGARA CCCCCCCCCCCCCCC	41.79	24173317
20	Phosphorylation	GFPGARATSPEAGGG CCCCCCCCCCCCCCC	38.98	23401153
21	Phosphorylation	FPGARATSPEAGGGG CCCCCCCCCCCCCCC	21.54	23401153
34	Phosphorylation	GGGALKASSAPAAAA CCCCCCCCCHHHHHH	25.99	28450419
35	Phosphorylation	GGALKASSAPAAAAG CCCCCCCCHHHHHHH	43.03	21082442
67	Phosphorylation	RQLRKVRSVELDQLP HHHHHHHCEEHHHCC	23.96	22817900
83	Phosphorylation	QPLFLAASPPASSTS CCEEEEECCCCCCCC	26.30	25921289
92	Phosphorylation	PASSTSPSPEPADAA CCCCCCCCCCCCCCC	41.48	25921289
133	Phosphorylation	ESVAAPDSGASSPAA CCCCCCCCCCCCCCC	34.89	25159151
136	Phosphorylation	AAPDSGASSPAAAEP CCCCCCCCCCCCCCC	40.14	25159151
137	Phosphorylation	APDSGASSPAAAEPG CCCCCCCCCCCCCCC	20.30	25159151
154	Phosphorylation	RAPAAEPSPAAAPAG CCCCCCCCCCCCCCC	20.76	25159151
169	Phosphorylation	REMENKETLKGLHKM CCCCCHHHHHHHHCC	35.07	18767875
223	Phosphorylation	IPVKGDGSEMNHLAA EECCCCCHHHCCCCC	38.11	27732954
232	Phosphorylation	MNHLAAESPGEVQAS HCCCCCCCCCCCCCC	33.22	25159151
239	Phosphorylation	SPGEVQASAASPASK CCCCCCCCCCCCCCC	13.79	22199227
242	Phosphorylation	EVQASAASPASKGRR CCCCCCCCCCCCCCC	22.25	25159151
245	Phosphorylation	ASAASPASKGRRSPS CCCCCCCCCCCCCCC	38.74	27732954
250	Phosphorylation	PASKGRRSPSPGNSP CCCCCCCCCCCCCCC	28.50	27794612
252	Phosphorylation	SKGRRSPSPGNSPSG CCCCCCCCCCCCCCC	46.84	27794612
256	Phosphorylation	RSPSPGNSPSGRTVK CCCCCCCCCCCCCCC	26.76	30576142
258	Phosphorylation	PSPGNSPSGRTVKSE CCCCCCCCCCCCCCC	40.50	30576142
264	Phosphorylation	PSGRTVKSESPGVRR CCCCCCCCCCCCCCC	38.68	25159151
266	Phosphorylation	GRTVKSESPGVRRKR CCCCCCCCCCCCCCC	33.76	25850435
275	Phosphorylation	GVRRKRVSPVPFQSG CCCCCCCCCCCCCCC	24.98	30266825
281	Phosphorylation	VSPVPFQSGRITPPR CCCCCCCCCCCCCCC	30.34	23403867
285	Phosphorylation	PFQSGRITPPRRAPS CCCCCCCCCCCCCCC	26.36	23403867
292	Phosphorylation	TPPRRAPSPDGFSPY CCCCCCCCCCCCCCC	34.34	23401153
297	O-linked_Glycosylation	APSPDGFSPYSPEET CCCCCCCCCCCHHHH	28.58	29351928
297	Phosphorylation	APSPDGFSPYSPEET CCCCCCCCCCCHHHH	28.58	30266825
299	Phosphorylation	SPDGFSPYSPEETNR CCCCCCCCCHHHHHH	35.34	28450419
300	Phosphorylation	PDGFSPYSPEETNRR CCCCCCCCHHHHHHH	29.26	25159151
304	Phosphorylation	SPYSPEETNRRVNKV CCCCHHHHHHHHHHH	32.15	25850435
317	Phosphorylation	KVMRARLYLLQQIGP HHHHHHHHHHHHHCC	10.38	24300666
326	Phosphorylation	LQQIGPNSFLIGGDS HHHHCCCCEECCCCC	25.27	24300666
333	Phosphorylation	SFLIGGDSPDNKYRV CEECCCCCCCCCEEE	37.11	24300666
338	Phosphorylation	GDSPDNKYRVFIGPQ CCCCCCCEEEEECCC	20.47	24300666
391	Ubiquitination	EVESLFQKYHSRRSS CHHHHHHHHHHCCCC	37.28	29967540
397	Phosphorylation	QKYHSRRSSRIKAPS HHHHHCCCCCCCCCC	23.90	24719451
398	Phosphorylation	KYHSRRSSRIKAPSR HHHHCCCCCCCCCCH	35.89	24719451
431	Phosphorylation	SSTSTSSSENSIKDE CCCCCCCCCCCCCHH	40.33	-
436	Sumoylation	SSSENSIKDEEEQMC CCCCCCCCHHHHHHC	59.93	-
436	Sumoylation	SSSENSIKDEEEQMC CCCCCCCCHHHHHHC	59.93	-
497	Phosphorylation	LCRSKWRSHDFYSHE HHCCCCCCCCCCCCC	26.71	23186163
501	Phosphorylation	KWRSHDFYSHELSSP CCCCCCCCCCCCCCC	18.38	28450419
502	Phosphorylation	WRSHDFYSHELSSPV CCCCCCCCCCCCCCC	15.52	28450419
506	Phosphorylation	DFYSHELSSPVDSPS CCCCCCCCCCCCCHH	29.61	21712546
507	Phosphorylation	FYSHELSSPVDSPSS CCCCCCCCCCCCHHH	41.38	25159151
511	Phosphorylation	ELSSPVDSPSSLRAA CCCCCCCCHHHHHHH	27.24	25159151
513	Phosphorylation	SSPVDSPSSLRAAQQ CCCCCCHHHHHHHHH	46.05	28450419
514	Phosphorylation	SPVDSPSSLRAAQQQ CCCCCHHHHHHHHHH	25.84	23663014
522	Phosphorylation	LRAAQQQTVQQQPLA HHHHHHHHHHHCCCC	18.88	22210691
531	Phosphorylation	QQQPLAGSRRNQESN HHCCCCCCCCCCCCC	23.59	26434776
542	Phosphorylation	QESNFNLTHYGTQQI CCCCCCCCCCCCCCC	17.73	-
657	Phosphorylation	VYVAALKTLRAMLVY HHHHHHHHHHHHHHH	23.48	22817900
665	Phosphorylation	LRAMLVYTPCHSLAE HHHHHHHCCCCHHHH	16.38	22817900
686	Phosphorylation	LLQPVVDTILVKCAD HHHHHCHHHHHECCC	12.47	22964224
690	Ubiquitination	VVDTILVKCADANSR HCHHHHHECCCCCCH	21.91	-
796	Phosphorylation	IRYKKLLSLLTFALQ HHHHHHHHHHHHHHH	31.59	-
829	Phosphorylation	SSARMVTTVPHVFSK HCCCHHHCHHHHHHH	22.19	30576142
844	Phosphorylation	LLEMLSVSSSTHFTR HHHHHCCCCCHHHHH	18.39	-
850	Phosphorylation	VSSSTHFTRMRRRLM CCCCHHHHHHHHHHH	18.89	-
919	Ubiquitination	GKGLCATKLSASSED CCCEEEEECCCCCCH	23.17	29967540
921	Phosphorylation	GLCATKLSASSEDIS CEEEEECCCCCCHHH	27.88	23927012
923	Phosphorylation	CATKLSASSEDISER EEEECCCCCCHHHHH	30.77	19664994
924	Phosphorylation	ATKLSASSEDISERL EEECCCCCCHHHHHH	38.72	29255136
928	Phosphorylation	SASSEDISERLASIS CCCCCHHHHHHHHCE	29.05	23403867
999	Phosphorylation	SVPAGTATDVSKHRL CCCCCCCCCCHHHHH	36.45	-
1013	Ubiquitination	LQGFIPCRIPSASPQ HCCCCCEECCCCCHH	38.20	21963094
1015	Ubiquitination	GFIPCRIPSASPQTQ CCCCEECCCCCHHHH	12.42	22817900
1016	Phosphorylation	FIPCRIPSASPQTQR CCCEECCCCCHHHHH	38.72	21082442
1017	Ubiquitination	IPCRIPSASPQTQRK CCEECCCCCHHHHHH	21.63	22817900
1018	Phosphorylation	PCRIPSASPQTQRKF CEECCCCCHHHHHHE	23.13	29255136
1021	Phosphorylation	IPSASPQTQRKFSLQ CCCCCHHHHHHEEEE	33.45	28450419
1026	Phosphorylation	PQTQRKFSLQFHRNC HHHHHHEEEEEHHCC	25.05	28152594
1039	Phosphorylation	NCPENKDSDKLSPVF CCCCCCCCCCCCCCC	37.95	29449344
1039	Ubiquitination	NCPENKDSDKLSPVF CCCCCCCCCCCCCCC	37.95	21963094
1041	Ubiquitination	PENKDSDKLSPVFTQ CCCCCCCCCCCCCCC	55.61	22817900
1043	Phosphorylation	NKDSDKLSPVFTQSR CCCCCCCCCCCCCCC	25.43	25849741
1043	Ubiquitination	NKDSDKLSPVFTQSR CCCCCCCCCCCCCCC	25.43	22817900
1047	Phosphorylation	DKLSPVFTQSRPLPS CCCCCCCCCCCCCCC	26.35	27732954
1080	Phosphorylation	QGDPSKNSMTLDLNS CCCCCCCCEEEECCC	19.51	22210691
1082	Phosphorylation	DPSKNSMTLDLNSSS CCCCCCEEEECCCCC	19.55	28857561
1087	Phosphorylation	SMTLDLNSSSKCDDS CEEEECCCCCCCCCC	43.20	18691976
1088	Phosphorylation	MTLDLNSSSKCDDSF EEEECCCCCCCCCCC	32.51	25627689
1089	Phosphorylation	TLDLNSSSKCDDSFG EEECCCCCCCCCCCC	36.80	-
1114	Phosphorylation	PSDETVFTPVEEKCR CCCCCEECCCHHHHC	23.30	27251275
1157	Phosphorylation	KSEVAVLSPEKAEND EEEEEEECHHHCCCC	25.14	25159151
1160	Ubiquitination	VAVLSPEKAENDDTY EEEECHHHCCCCCCC	65.47	33845483
1166	Phosphorylation	EKAENDDTYKDDVNH HHCCCCCCCHHCCCH	35.02	27732954
1167	Phosphorylation	KAENDDTYKDDVNHN HCCCCCCCHHCCCHH	21.29	27732954
1168	Ubiquitination	AENDDTYKDDVNHNQ CCCCCCCHHCCCHHH	49.93	-
1176	Ubiquitination	DDVNHNQKCKEKMEA HCCCHHHHHHHHHHH	53.22	21963094
1178	Ubiquitination	VNHNQKCKEKMEAEE CCHHHHHHHHHHHHH	68.36	22817900
1180	Ubiquitination	HNQKCKEKMEAEEEE HHHHHHHHHHHHHHH	27.77	22817900
1235	Ubiquitination	PGHTKAKQPYREDTE CCCCCCCCCCCCCCH	45.15	22053931
1261	Ubiquitination	FSSCYQAQDVGTGTL CCCCEEEECCCCCCE	30.32	22053931
1338	Phosphorylation	VAHLLSKYGAFKESV HHHHHHHCCCCCCEE	15.43	-
1371	Ubiquitination	QIIHRDVKGANLLID CEECCCCCCCCEEEC	57.50	-
1379	Phosphorylation	GANLLIDSTGQRLRI CCCEEECCCCCEEEE	27.69	27174698
1380	Phosphorylation	ANLLIDSTGQRLRIA CCEEECCCCCEEEEH	33.32	27174698
1397	Phosphorylation	GAAARLASKGTGAGE HHHHHHHHCCCCCHH	35.89	27251275
1398	Ubiquitination	AAARLASKGTGAGEF HHHHHHHCCCCCHHH	55.68	21906983
1400	Phosphorylation	ARLASKGTGAGEFQG HHHHHCCCCCHHHHH	27.82	27251275
1412	Phosphorylation	FQGQLLGTIAFMAPE HHHHHHHHHHHHCHH	14.76	-
1455	Phosphorylation	PWNAEKHSNHLALIF CCCCCCCCCHHHHHH	36.69	25850435
1504	Ubiquitination	PPSRELLKHPVFRTT CCCHHHHCCCCCCCC	59.49	32015554

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
67	S	Phosphorylation	Kinase	PAK1	Q13153	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	DTX1	Q86Y01	PMID:9590294

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of M3K1_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 M3K1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CDC37_HUMAN	CDC37	physical	14743216
FKBP5_HUMAN	FKBP5	physical	14743216
DCAF7_HUMAN	DCAF7	physical	14743216
RL30_HUMAN	RPL30	physical	14743216
RL4_HUMAN	RPL4	physical	14743216
RS13_HUMAN	RPS13	physical	14743216
MK08_HUMAN	MAPK8	physical	9405400
AXIN1_HUMAN	AXIN1	physical	11884395
DVL2_HUMAN	DVL2	physical	10829020
AXIN1_HUMAN	AXIN1	physical	10829020
RAF1_HUMAN	RAF1	physical	10969079
MP2K1_HUMAN	MAP2K1	physical	10969079
MK01_HUMAN	MAPK1	physical	10969079
TRAF2_HUMAN	TRAF2	physical	10346818
MP2K4_HUMAN	MAP2K4	physical	10713157
IKKB_HUMAN	IKBKB	physical	11057907
RHOA_HUMAN	RHOA	physical	14581471
ACTN1_HUMAN	ACTN1	physical	14581471
RHG04_HUMAN	ARHGAP4	physical	14581471
MK09_HUMAN	MAPK9	physical	14581471
MK01_HUMAN	MAPK1	physical	14581471
MP2K4_HUMAN	MAP2K4	physical	14581471
IKKA_HUMAN	CHUK	physical	9689078
FLNB_HUMAN	FLNB	physical	19270716
UBC9_HUMAN	UBE2I	physical	21336309
IKKA_HUMAN	CHUK	physical	9819420
IKKB_HUMAN	IKBKB	physical	9819420
MP2K4_HUMAN	MAP2K4	physical	15299005
P53_HUMAN	TP53	physical	20923779
M4K2_HUMAN	MAP4K2	physical	11784851
M3K1_HUMAN	MAP3K1	physical	11784851
RHOA_HUMAN	RHOA	physical	21129722
DCAF7_HUMAN	DCAF7	physical	20940704
HIPK2_HUMAN	HIPK2	physical	20940704
DYR1A_HUMAN	DYRK1A	physical	20940704
DYR1B_HUMAN	DYRK1B	physical	20940704
MK08_HUMAN	MAPK8	physical	14500727
IKBA_HUMAN	NFKBIA	physical	14500727
MK01_HUMAN	MAPK1	physical	14500727
MP2K4_HUMAN	MAP2K4	physical	14500727
MP2K7_HUMAN	MAP2K7	physical	14500727
MP2K1_HUMAN	MAP2K1	physical	14500727
NR4A1_HUMAN	NR4A1	physical	16434970
MP2K4_HUMAN	MAP2K4	physical	9808624
JUN_HUMAN	JUN	physical	12796506
CRTC1_HUMAN	CRTC1	physical	18784253
GSTP1_HUMAN	GSTP1	physical	16636664
MK08_HUMAN	MAPK8	physical	21152872
MK08_HUMAN	MAPK8	physical	12228228
MP2K4_HUMAN	MAP2K4	physical	12228228
STK38_HUMAN	STK38	physical	17906693
IKKA_HUMAN	CHUK	physical	16286467
IKKB_HUMAN	IKBKB	physical	16286467
MP2K4_HUMAN	MAP2K4	physical	16472679
RHOA_HUMAN	RHOA	physical	24135036
FRAT1_HUMAN	FRAT1	physical	24135036
MK01_HUMAN	MAPK1	physical	24135036
MK03_HUMAN	MAPK3	physical	24135036
AXIN1_HUMAN	AXIN1	physical	24135036
BAP1_HUMAN	BAP1	physical	25260751
FKBP6_HUMAN	FKBP6	physical	25260751
NPL4_HUMAN	NPLOC4	physical	25260751
ASCC2_HUMAN	ASCC2	physical	25260751
UB2V1_HUMAN	UBE2V1	physical	25260751
UBAC1_HUMAN	UBAC1	physical	25260751
DNJB6_HUMAN	DNAJB6	physical	25260751
TM1L2_HUMAN	TOM1L2	physical	25260751
CUED1_HUMAN	CUEDC1	physical	25260751
HBS1L_HUMAN	HBS1L	physical	25260751
DP13A_HUMAN	APPL1	physical	25260751
ZFAN5_HUMAN	ZFAND5	physical	25260751
TRAF2_HUMAN	TRAF2	physical	25260751
TOM1_HUMAN	TOM1	physical	25260751
RD23A_HUMAN	RAD23A	physical	25260751
STAM1_HUMAN	STAM	physical	25260751
HG2A_HUMAN	CD74	physical	25260751
HIP1_HUMAN	HIP1	physical	25260751
UBXN7_HUMAN	UBXN7	physical	25260751
HGS_HUMAN	HGS	physical	25260751
CF106_HUMAN	C6orf106	physical	25260751
R3GEF_HUMAN	RAB3IL1	physical	25260751
UBS3B_HUMAN	UBASH3B	physical	25260751
TAB1_HUMAN	TAB1	physical	25260751
DNJB2_HUMAN	DNAJB2	physical	25260751
RN141_HUMAN	RNF141	physical	25260751
MINY3_HUMAN	FAM188A	physical	25260751
UBAP1_HUMAN	UBAP1	physical	25260751
DCNL1_HUMAN	DCUN1D1	physical	25260751
NEK10_HUMAN	NEK10	physical	25260751
STAM2_HUMAN	STAM2	physical	25260751
GRAP1_HUMAN	GRIPAP1	physical	25260751
EPHA1_HUMAN	EPHA1	physical	25260751
RAD18_HUMAN	RAD18	physical	25260751
HOIL1_HUMAN	RBCK1	physical	25260751
IMPCT_HUMAN	IMPACT	physical	25260751
PSMD4_HUMAN	PSMD4	physical	25260751
SPART_HUMAN	SPG20	physical	25260751
ZFAN3_HUMAN	ZFAND3	physical	25260751
EPN1_HUMAN	EPN1	physical	25260751
RN114_HUMAN	RNF114	physical	25260751
UB2G1_HUMAN	UBE2G1	physical	25260751
DCNL2_HUMAN	DCUN1D2	physical	25260751
UCHL5_HUMAN	UCHL5	physical	25260751
CREL1_HUMAN	CRELD1	physical	25260751
ATX3_HUMAN	ATXN3	physical	25260751
FAF2_HUMAN	FAF2	physical	25260751
CEP85_HUMAN	CEP85	physical	25260751
UFD1_HUMAN	UFD1L	physical	25260751
UBE2K_HUMAN	UBE2K	physical	25260751
UBP28_HUMAN	USP28	physical	25260751
F184A_HUMAN	FAM184A	physical	25260751
GGA2_HUMAN	GGA2	physical	25260751
PKHB2_HUMAN	PLEKHB2	physical	25260751
KRT36_HUMAN	KRT36	physical	25260751
RN126_HUMAN	RNF126	physical	25260751
APEX2_HUMAN	APEX2	physical	25260751
ODFP2_HUMAN	ODF2	physical	25260751
DEN6B_HUMAN	DENND6B	physical	25260751
CAR14_HUMAN	CARD14	physical	25260751
UBQL1_HUMAN	UBQLN1	physical	25260751
CCD69_HUMAN	CCDC69	physical	25260751
RABE2_HUMAN	RABEP2	physical	25260751
R51A1_HUMAN	RAD51AP1	physical	25260751
TNIP1_HUMAN	TNIP1	physical	25260751
P53_HUMAN	TP53	physical	26018553
MBP_HUMAN	MBP	physical	12624112
M3K1_HUMAN	MAP3K1	physical	12624112
VHL_HUMAN	VHL	genetic	28319113
MP2K4_HUMAN	MAP2K4	physical	27806347
NOTC1_HUMAN	NOTCH1	physical	27806347
GRB2_HUMAN	GRB2	physical	15192046
BAALC_HUMAN	BAALC	physical	26050649

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613762	46,XY sex reversal 6 (SRXY6)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of M3K1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-21 AND SER-923, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"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 THR-20; SER-21; SER-35;SER-133; SER-136; SER-252; SER-275; SER-292; SER-507; SER-923;SER-1016; SER-1018 AND SER-1157, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-21 AND SER-923, 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-292; SER-297; SER-300;SER-507; SER-511 AND SER-1018, 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-21; SER-35; SER-154;SER-232; SER-242; SER-292; SER-297; SER-300; SER-507; SER-511;SER-923; SER-1018; SER-1043 AND SER-1157, AND MASS SPECTROMETRY.	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-292, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-657 AND THR-665, ANDMASS SPECTROMETRY.	18187866 [Abstract]