MIF_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MIF_HUMAN
• UniProt AC: P14174
• Protein Name: Macrophage migration inhibitory factor
• Gene Name: MIF
• Organism: Homo sapiens (Human).
• Sequence Length: 115
• Subcellular Localization: Secreted . Cytoplasm . Does not have a cleavable signal sequence and is secreted via a specialized, non-classical pathway. Secreted by macrophages upon stimulation by bacterial lipopolysaccharide (LPS), or by M.tuberculosis antigens.
• Protein Description: Pro-inflammatory cytokine. Involved in the innate immune response to bacterial pathogens. The expression of MIF at sites of inflammation suggests a role as mediator in regulating the function of macrophages in host defense. Counteracts the anti-inflammatory activity of glucocorticoids. Has phenylpyruvate tautomerase and dopachrome tautomerase activity (in vitro), but the physiological substrate is not known. It is not clear whether the tautomerase activity has any physiological relevance, and whether it is important for cytokine activity..
• Protein Sequence: MPMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLMAFGGSSEPCALCSLHSIGKIGGAQNRSYSKLLCGLLAERLRISPDRVYINYYDMNAANVGWNNSTFA

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
3	Sulfoxidation	-----MPMFIVNTNV -----CCEEEEECCC	3.28	21406390
8	Phosphorylation	MPMFIVNTNVPRASV CCEEEEECCCCCCCC	27.05	29978859
12	Methylation	IVNTNVPRASVPDGF EEECCCCCCCCCCCH	34.90	54557361
14	Phosphorylation	NTNVPRASVPDGFLS ECCCCCCCCCCCHHH	35.15	26074081
21	Phosphorylation	SVPDGFLSELTQQLA CCCCCHHHHHHHHHH	28.44	24275569
37	Phosphorylation	ATGKPPQYIAVHVVP HHCCCCCEEEEEECC	9.16	21253578
54	O-linked_Glycosylation	LMAFGGSSEPCALCS HHHCCCCCCCCHHHH	49.16	OGP
60	S-nitrosylation	SSEPCALCSLHSIGK CCCCCHHHHHHHHCC	1.85	24105792
74	Methylation	KIGGAQNRSYSKLLC CCCCCCCCCHHHHHH	25.54	115483259
75	Phosphorylation	IGGAQNRSYSKLLCG CCCCCCCCHHHHHHH	41.11	25849741
76	Phosphorylation	GGAQNRSYSKLLCGL CCCCCCCHHHHHHHH	13.44	28102081
77	Phosphorylation	GAQNRSYSKLLCGLL CCCCCCHHHHHHHHH	20.34	28102081
78	Succinylation	AQNRSYSKLLCGLLA CCCCCHHHHHHHHHH	36.93	-
78	Ubiquitination	AQNRSYSKLLCGLLA CCCCCHHHHHHHHHH	36.93	21890473
78	Malonylation	AQNRSYSKLLCGLLA CCCCCHHHHHHHHHH	36.93	26320211
78	2-Hydroxyisobutyrylation	AQNRSYSKLLCGLLA CCCCCHHHHHHHHHH	36.93	-
78	Phosphoglycerylation	AQNRSYSKLLCGLLA CCCCCHHHHHHHHHH	36.93	-
78	Succinylation	AQNRSYSKLLCGLLA CCCCCHHHHHHHHHH	36.93	-
78	Acetylation	AQNRSYSKLLCGLLA CCCCCHHHHHHHHHH	36.93	19608861
81	Glutathionylation	RSYSKLLCGLLAERL CCHHHHHHHHHHHHH	5.38	22555962
81	S-nitrosylation	RSYSKLLCGLLAERL CCHHHHHHHHHHHHH	5.38	19483679
81	S-palmitoylation	RSYSKLLCGLLAERL CCHHHHHHHHHHHHH	5.38	29575903
81	S-nitrosocysteine	RSYSKLLCGLLAERL CCHHHHHHHHHHHHH	5.38	-
87	Methylation	LCGLLAERLRISPDR HHHHHHHHHCCCCCC	24.53	115483275
89	Methylation	GLLAERLRISPDRVY HHHHHHHCCCCCCEE	33.29	115483283
91	Phosphorylation	LAERLRISPDRVYIN HHHHHCCCCCCEEEE	17.83	11069294
94	Methylation	RLRISPDRVYINYYD HHCCCCCCEEEEEEC	26.90	115483267
99	Phosphorylation	PDRVYINYYDMNAAN CCCEEEEEECCCCCC	7.41	-
100	Phosphorylation	DRVYINYYDMNAANV CCEEEEEECCCCCCC	12.29	-
112	O-linked_Glycosylation	ANVGWNNSTFA---- CCCCCCCCCCC----	22.99	97979813
113	O-linked_Glycosylation	NVGWNNSTFA----- CCCCCCCCCC-----	26.21	26280537

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MIF_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 MIF_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GORS2_HUMAN	GORASP2	physical	16189514
CSN5_HUMAN	COPS5	physical	11089976
CHIP_HUMAN	STUB1	physical	22271573
HS90A_HUMAN	HSP90AA1	physical	22271573
NDKA_HUMAN	NME1	physical	18815136
P53_HUMAN	TP53	physical	18815136
CSN5_HUMAN	COPS5	physical	15757663
BEX3_HUMAN	NGFRAP1	physical	21988832
MIF_HUMAN	MIF	physical	25416956
NTAQ1_HUMAN	WDYHV1	physical	25416956
UFM1_HUMAN	UFM1	physical	26344197
EGFR_HUMAN	EGFR	physical	26280537

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 604302: Rheumatoid arthritis systemic juvenile (RASJ)
• 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

Acetylation

"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-78, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-37, AND MASSSPECTROMETRY.
PubMed: 15592455