dbPTM

MLF1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MLF1_HUMAN
UniProt AC	P58340
Protein Name	Myeloid leukemia factor 1
Gene Name	MLF1
Organism	Homo sapiens (Human).
Sequence Length	268
Subcellular Localization	Cytoplasm . Nucleus . Shuttles between the cytoplasm and nucleus.
Protein Description	Involved in lineage commitment of primary hemopoietic progenitors by restricting erythroid formation and enhancing myeloid formation. Interferes with erythropoietin-induced erythroid terminal differentiation by preventing cells from exiting the cell cycle through suppression of CDKN1B/p27Kip1 levels. Suppresses COP1 activity via CSN3 which activates p53 and induces cell cycle arrest. Binds DNA and affects the expression of a number of genes so may function as a transcription factor in the nucleus..
Protein Sequence	MFRMLNSSFEDDPFFSESILAHRENMRQMIRSFSEPFGRDLLSISDGRGRAHNRRGHNDGEDSLTHTDVSSFQTMDQMVSNMRNYMQKLERNFGQLSVDPNGHSFCSSSVMTYSKIGDEPPKVFQASTQTRRAPGGIKETRKAMRDSDSGLEKMAIGHHIHDRAHVIKKSKNKKTGDEEVNQEFINMNESDAHAFDEEWQSEVLKYKPGRHNLGNTRMRSVGHENPGSRELKRREKPQQSPAIEHGRRSNVLGDKLHIKGSSVKSNKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MFRMLNSSFEDDPF -CCCCCCCCCCCCCC	32.23	29978859
8	Phosphorylation	MFRMLNSSFEDDPFF CCCCCCCCCCCCCCC	31.42	25106551
16	Phosphorylation	FEDDPFFSESILAHR CCCCCCCCHHHHHHH	30.71	23186163
18	Phosphorylation	DDPFFSESILAHREN CCCCCCHHHHHHHHH	23.00	23186163
23	Dimethylation	SESILAHRENMRQMI CHHHHHHHHHHHHHH	31.23	-
23	Methylation	SESILAHRENMRQMI CHHHHHHHHHHHHHH	31.23	30762609
27	Dimethylation	LAHRENMRQMIRSFS HHHHHHHHHHHHHCC	34.20	-
27	Methylation	LAHRENMRQMIRSFS HHHHHHHHHHHHHCC	34.20	30762615
32	Phosphorylation	NMRQMIRSFSEPFGR HHHHHHHHCCCCCCC	23.38	30266825
34	Phosphorylation	RQMIRSFSEPFGRDL HHHHHHCCCCCCCCC	45.68	30266825
43	Phosphorylation	PFGRDLLSISDGRGR CCCCCCCCCCCCCCC	27.61	23090842
45	Phosphorylation	GRDLLSISDGRGRAH CCCCCCCCCCCCCCC	30.54	23090842
48	Methylation	LLSISDGRGRAHNRR CCCCCCCCCCCCCCC	36.09	30988097
48	Phosphorylation	LLSISDGRGRAHNRR CCCCCCCCCCCCCCC	36.09	27251275
50	Methylation	SISDGRGRAHNRRGH CCCCCCCCCCCCCCC	31.17	97812407
50	Phosphorylation	SISDGRGRAHNRRGH CCCCCCCCCCCCCCC	31.17	27251275
63	Phosphorylation	GHNDGEDSLTHTDVS CCCCCCCCCCCCCHH	30.75	30622161
65	Phosphorylation	NDGEDSLTHTDVSSF CCCCCCCCCCCHHHH	27.04	30622161
67	Phosphorylation	GEDSLTHTDVSSFQT CCCCCCCCCHHHHHH	32.62	25693802
70	Phosphorylation	SLTHTDVSSFQTMDQ CCCCCCHHHHHHHHH	28.39	25693802
71	Phosphorylation	LTHTDVSSFQTMDQM CCCCCHHHHHHHHHH	22.63	25954137
74	Phosphorylation	TDVSSFQTMDQMVSN CCHHHHHHHHHHHHH	22.24	25954137
80	Phosphorylation	QTMDQMVSNMRNYMQ HHHHHHHHHHHHHHH	21.40	25954137
85	Phosphorylation	MVSNMRNYMQKLERN HHHHHHHHHHHHHHH	7.20	25954137
88	Ubiquitination	NMRNYMQKLERNFGQ HHHHHHHHHHHHHCC	35.47	-
97	Phosphorylation	ERNFGQLSVDPNGHS HHHHCCCCCCCCCCC	19.31	25693802
108	Phosphorylation	NGHSFCSSSVMTYSK CCCCCCCCCCEEHHH	28.29	28985074
109	Phosphorylation	GHSFCSSSVMTYSKI CCCCCCCCCEEHHHC	10.30	25693802
112	Phosphorylation	FCSSSVMTYSKIGDE CCCCCCEEHHHCCCC	23.61	28985074
113	Phosphorylation	CSSSVMTYSKIGDEP CCCCCEEHHHCCCCC	7.00	28985074
114	Phosphorylation	SSSVMTYSKIGDEPP CCCCEEHHHCCCCCC	14.50	29496907
122	Acetylation	KIGDEPPKVFQASTQ HCCCCCCCEEEECCC	67.41	25038526
122	Ubiquitination	KIGDEPPKVFQASTQ HCCCCCCCEEEECCC	67.41	21906983
147	Phosphorylation	TRKAMRDSDSGLEKM HHHHHHHCCCHHHHH	24.26	24173317
149	Phosphorylation	KAMRDSDSGLEKMAI HHHHHCCCHHHHHHH	49.59	30622161
153	Acetylation	DSDSGLEKMAIGHHI HCCCHHHHHHHCHHH	38.38	25038526
168	Acetylation	HDRAHVIKKSKNKKT HHHHHHHHHCCCCCC	50.32	24888395
169	Acetylation	DRAHVIKKSKNKKTG HHHHHHHHCCCCCCC	56.38	24888403
174	Ubiquitination	IKKSKNKKTGDEEVN HHHCCCCCCCCHHHH	68.11	21906983
205	Acetylation	EWQSEVLKYKPGRHN HHHHHHHHCCCCCCC	57.30	25038526
206	Phosphorylation	WQSEVLKYKPGRHNL HHHHHHHCCCCCCCC	20.46	18083107
219	Methylation	NLGNTRMRSVGHENP CCCCCCCCCCCCCCC	25.54	24395539
220	Phosphorylation	LGNTRMRSVGHENPG CCCCCCCCCCCCCCC	24.09	25394399
228	Phosphorylation	VGHENPGSRELKRRE CCCCCCCCHHHHHCC	24.68	30622161
236	Ubiquitination	RELKRREKPQQSPAI HHHHHCCCCCCCHHH	46.44	21906983
240	Phosphorylation	RREKPQQSPAIEHGR HCCCCCCCHHHHHCC	15.85	24702127
249	Phosphorylation	AIEHGRRSNVLGDKL HHHHCCCCCCCCCCC	29.90	30622161
255	Acetylation	RSNVLGDKLHIKGSS CCCCCCCCCEECCCC	39.92	25038526
261	Phosphorylation	DKLHIKGSSVKSNKK CCCEECCCCCCCCCC	27.27	30622161
262	Phosphorylation	KLHIKGSSVKSNKK- CCEECCCCCCCCCC-	42.08	30622161

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 MLF1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MLF1_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 MLF1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GRIK5_HUMAN	GRIK5	physical	16169070
CSN3_HUMAN	COPS3	physical	15861129
CENPU_HUMAN	CENPU	physical	15116101
DNJB6_HUMAN	DNAJB6	physical	26186194
MAP1B_HUMAN	MAP1B	physical	26186194
ERC6L_HUMAN	ERCC6L	physical	26186194
TROP_HUMAN	TRO	physical	26186194
AKA11_HUMAN	AKAP11	physical	26186194
BRCA2_HUMAN	BRCA2	physical	26186194
SYNRG_HUMAN	SYNRG	physical	26186194
FA83H_HUMAN	FAM83H	physical	26186194
ZWINT_HUMAN	ZWINT	physical	26186194
SPC24_HUMAN	SPC24	physical	26186194
KAPCB_HUMAN	PRKACB	physical	26186194
WAC2A_HUMAN	FAM21A	physical	26186194
HTR5B_HUMAN	HEATR5B	physical	26186194
CK5P2_HUMAN	CDK5RAP2	physical	26186194
RIPK1_HUMAN	RIPK1	physical	26186194
KIF11_HUMAN	KIF11	physical	26186194
KNL1_HUMAN	CASC5	physical	26186194
ATG2B_HUMAN	ATG2B	physical	26186194
HAUS6_HUMAN	HAUS6	physical	26186194
MYOME_HUMAN	PDE4DIP	physical	26186194
ALMS1_HUMAN	ALMS1	physical	26186194
RGPD5_HUMAN	RGPD5	physical	26186194
HAUS8_HUMAN	HAUS8	physical	26186194
HERC1_HUMAN	HERC1	physical	26186194
KAP1_HUMAN	PRKAR1B	physical	26186194
GRDN_HUMAN	CCDC88A	physical	26186194
APOB_HUMAN	APOB	physical	26186194
P73_HUMAN	TP73	physical	26186194
CRBG3_HUMAN	CRYBG3	physical	26186194
BUB1_HUMAN	BUB1	physical	26186194
DSN1_HUMAN	DSN1	physical	26186194
TRBP2_HUMAN	TARBP2	physical	26186194
SYNRG_HUMAN	SYNRG	physical	28514442
WAC2A_HUMAN	FAM21A	physical	28514442
CRBG3_HUMAN	CRYBG3	physical	28514442
TROP_HUMAN	TRO	physical	28514442
CE295_HUMAN	CEP295	physical	28514442
BRCA2_HUMAN	BRCA2	physical	28514442
ERC6L_HUMAN	ERCC6L	physical	28514442
MYOME_HUMAN	PDE4DIP	physical	28514442
BUB1_HUMAN	BUB1	physical	28514442
AKA11_HUMAN	AKAP11	physical	28514442
KAPCB_HUMAN	PRKACB	physical	28514442
ATG2B_HUMAN	ATG2B	physical	28514442
GRDN_HUMAN	CCDC88A	physical	28514442
DSN1_HUMAN	DSN1	physical	28514442
KNL1_HUMAN	CASC5	physical	28514442
CK5P2_HUMAN	CDK5RAP2	physical	28514442
KAP1_HUMAN	PRKAR1B	physical	28514442
KIF11_HUMAN	KIF11	physical	28514442
FA83H_HUMAN	FAM83H	physical	28514442
ZWINT_HUMAN	ZWINT	physical	28514442
HAUS8_HUMAN	HAUS8	physical	28514442
KI20B_HUMAN	KIF20B	physical	28514442
ALMS1_HUMAN	ALMS1	physical	28514442
NDC80_HUMAN	NDC80	physical	28514442
PLEC_HUMAN	PLEC	physical	28514442
PMF1_HUMAN	PMF1	physical	28514442
WNK1_HUMAN	WNK1	physical	28514442
SPC24_HUMAN	SPC24	physical	28514442
E41L2_HUMAN	EPB41L2	physical	28514442
HAUS6_HUMAN	HAUS6	physical	28514442
KAPCG_HUMAN	PRKACG	physical	28514442
RIPK1_HUMAN	RIPK1	physical	28514442
TBCE_HUMAN	TBCE	physical	27173435
DJC13_HUMAN	DNAJC13	physical	27173435
EDRF1_HUMAN	EDRF1	physical	27173435
FYB2_HUMAN	C1orf168	physical	27173435
I2BP1_HUMAN	IRF2BP1	physical	27173435
NMT1_HUMAN	NMT1	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 MLF1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Structural insights of the MLF1/14-3-3 interaction."; Molzan M., Weyand M., Rose R., Ottmann C.; FEBS J. 279:563-571(2012). Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 29-42 IN COMPLEX WITH YWHAE,AND PHOSPHORYLATION AT SER-34.	22151054 [Abstract]