MLF2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MLF2_HUMAN
• UniProt AC: Q15773
• Protein Name: Myeloid leukemia factor 2
• Gene Name: MLF2
• Organism: Homo sapiens (Human).
• Sequence Length: 248
• Subcellular Localization: Cytoplasm. Nucleus.
• Protein Sequence: MFRFMRDVEPEDPMFLMDPFAIHRQHMSRMLSGGFGYSPFLSITDGNMPGTRPASRRMQQAGAVSPFGMLGMSGGFMDMFGMMNDMIGNMEHMTAGGNCQTFSSSTVISYSNTGDGAPKVYQETSEMRSAPGGIRETRRTVRDSDSGLEQMSIGHHIRDRAHILQRSRNHRTGDQEERQDYINLDESEAAAFDDEWRRETSRFRQQRPLEFRRLESSGAGGRRAEGPPRLAIQGPEDSPSRQSRRYDW

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
28	Phosphorylation	AIHRQHMSRMLSGGF HHHHHHHHHHHCCCC	16.65	20044836
32	Phosphorylation	QHMSRMLSGGFGYSP HHHHHHHCCCCCCCC	27.77	28450419
37	Phosphorylation	MLSGGFGYSPFLSIT HHCCCCCCCCCEECC	15.77	20090780
38	Phosphorylation	LSGGFGYSPFLSITD HCCCCCCCCCEECCC	15.00	19835603
42	Phosphorylation	FGYSPFLSITDGNMP CCCCCCEECCCCCCC	24.66	27251275
44	Phosphorylation	YSPFLSITDGNMPGT CCCCEECCCCCCCCC	34.18	19835603
51	Phosphorylation	TDGNMPGTRPASRRM CCCCCCCCCCCHHHH	27.84	28857561
55	Phosphorylation	MPGTRPASRRMQQAG CCCCCCCHHHHHHCC	24.09	28857561
121	Phosphorylation	GDGAPKVYQETSEMR CCCCCCCHHHHHHHH	13.52	28796482
140	Phosphorylation	GIRETRRTVRDSDSG CHHHCHHHHCCCCCC	19.32	30108239
144	Phosphorylation	TRRTVRDSDSGLEQM CHHHHCCCCCCCCCH	24.10	17287340
146	Phosphorylation	RTVRDSDSGLEQMSI HHHCCCCCCCCCHHH	49.59	30108239
152	Phosphorylation	DSGLEQMSIGHHIRD CCCCCCHHHHHHHHH	25.72	23401153
167	Phosphorylation	RAHILQRSRNHRTGD HHHHHHHHHCCCCCC	25.19	24719451
172	Phosphorylation	QRSRNHRTGDQEERQ HHHHCCCCCCHHHHH	37.24	27470641
181	Phosphorylation	DQEERQDYINLDESE CHHHHHHHCCCCHHH	5.38	27642862
212	Methylation	QQRPLEFRRLESSGA HHCCCHHHHHHCCCC	32.66	115483345
216	Phosphorylation	LEFRRLESSGAGGRR CHHHHHHCCCCCCCC	38.37	30266825
217	Phosphorylation	EFRRLESSGAGGRRA HHHHHHCCCCCCCCC	24.24	30266825
238	Phosphorylation	AIQGPEDSPSRQSRR EEECCCCCCCCCCCC	24.10	19664994
240	Phosphorylation	QGPEDSPSRQSRRYD ECCCCCCCCCCCCCC	47.07	29255136
243	Phosphorylation	EDSPSRQSRRYDW-- CCCCCCCCCCCCC--	20.02	30266825
246	Phosphorylation	PSRQSRRYDW----- CCCCCCCCCC-----	22.48	26074081

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of MLF2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MLF2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of MLF2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MMS19_HUMAN	MMS19	physical	17353931
BAG2_HUMAN	BAG2	physical	17353931
AIFM1_HUMAN	AIFM1	physical	17353931
ABCD3_HUMAN	ABCD3	physical	17353931
RGS20_HUMAN	RGS20	physical	17353931
CIAO1_HUMAN	CIAO1	physical	17353931
MIP18_HUMAN	FAM96B	physical	17353931
PMVK_HUMAN	PMVK	physical	17353931
GCN1_HUMAN	GCN1L1	physical	22863883
KIF15_HUMAN	KIF15	physical	22863883
POP1_HUMAN	POP1	physical	22863883
RPP30_HUMAN	RPP30	physical	22863883
UBP19_HUMAN	USP19	physical	22863883
DNJB6_HUMAN	DNAJB6	physical	25036637
HSP76_HUMAN	HSPA6	physical	25036637
DNJB1_HUMAN	DNAJB1	physical	25036637
BAG3_HUMAN	BAG3	physical	25036637
BAG2_HUMAN	BAG2	physical	25036637
DNJB4_HUMAN	DNAJB4	physical	25036637

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-238, AND MASSSPECTROMETRY.
PubMed: 19690332

"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-238, AND MASSSPECTROMETRY.
PubMed: 19369195

"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-238, AND MASSSPECTROMETRY.
PubMed: 19413330

"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-238, AND MASSSPECTROMETRY.
PubMed: 18669648

"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-238, AND MASSSPECTROMETRY.
PubMed: 18691976

"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144; SER-152 ANDSER-238, AND MASS SPECTROMETRY.
PubMed: 17287340

"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND MASSSPECTROMETRY.
PubMed: 16565220