MISSL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MISSL_HUMAN
• UniProt AC: Q8NDC0
• Protein Name: MAPK-interacting and spindle-stabilizing protein-like
• Gene Name: MAPK1IP1L
• Organism: Homo sapiens (Human).
• Sequence Length: 245
• Protein Sequence: MSDEFSLADALPEHSPAKTSAVSNTKPGQPPQGWPGSNPWNNPSAPSSVPSGLPPSATPSTVPFGPAPTGMYPSVPPTGPPPGPPAPFPPSGPSCPPPGGPYPAPTVPGPGPTGPYPTPNMPFPELPRPYGAPTDPAAAGPLGPWGSMSSGPWAPGMGGQYPTPNMPYPSPGPYPAPPPPQAPGAAPPVPWGTVPPGAWGPPAPYPAPTGSYPTPGLYPTPSNPFQVPSGPSGAPPMPGGPHSYH

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
2	Phosphorylation	------MSDEFSLAD ------CCCCCCHHH	45.94	25159151
2	Acetylation	------MSDEFSLAD ------CCCCCCHHH	45.94	21406692
6	Phosphorylation	--MSDEFSLADALPE --CCCCCCHHHHCCC	22.17	25159151
15	Phosphorylation	ADALPEHSPAKTSAV HHHCCCCCCCCCCCC	25.54	29255136
18	Ubiquitination	LPEHSPAKTSAVSNT CCCCCCCCCCCCCCC	46.53	33845483
19	Phosphorylation	PEHSPAKTSAVSNTK CCCCCCCCCCCCCCC	24.83	26074081
20	O-linked_Glycosylation	EHSPAKTSAVSNTKP CCCCCCCCCCCCCCC	26.43	29485866
20	Phosphorylation	EHSPAKTSAVSNTKP CCCCCCCCCCCCCCC	26.43	26074081
23	Phosphorylation	PAKTSAVSNTKPGQP CCCCCCCCCCCCCCC	38.20	26074081
25	Phosphorylation	KTSAVSNTKPGQPPQ CCCCCCCCCCCCCCC	30.98	26074081
44	O-linked_Glycosylation	SNPWNNPSAPSSVPS CCCCCCCCCCCCCCC	55.74	29485866
47	O-linked_Glycosylation	WNNPSAPSSVPSGLP CCCCCCCCCCCCCCC	43.62	29485866
48	O-linked_Glycosylation	NNPSAPSSVPSGLPP CCCCCCCCCCCCCCC	36.67	29485866
51	O-linked_Glycosylation	SAPSSVPSGLPPSAT CCCCCCCCCCCCCCC	51.29	29485866
56	O-linked_Glycosylation	VPSGLPPSATPSTVP CCCCCCCCCCCCCCC	42.72	29485866
58	O-linked_Glycosylation	SGLPPSATPSTVPFG CCCCCCCCCCCCCCC	23.31	29485866
60	O-linked_Glycosylation	LPPSATPSTVPFGPA CCCCCCCCCCCCCCC	37.37	29485866
61	O-linked_Glycosylation	PPSATPSTVPFGPAP CCCCCCCCCCCCCCC	33.14	29485866
161	Phosphorylation	APGMGGQYPTPNMPY CCCCCCCCCCCCCCC	16.61	-
174	Phosphorylation	PYPSPGPYPAPPPPQ CCCCCCCCCCCCCCC	20.24	-
232	O-linked_Glycosylation	FQVPSGPSGAPPMPG CCCCCCCCCCCCCCC	51.63	OGP

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MISSL_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 MISSL_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MISSL_HUMAN	MAPK1IP1L	physical	16189514
MISSL_HUMAN	MAPK1IP1L	physical	25416956

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

"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-2 AND SER-15, AND MASSSPECTROMETRY.
PubMed: 19413330

"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-15, AND MASSSPECTROMETRY.
PubMed: 18691976

"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-15, AND MASSSPECTROMETRY.
PubMed: 17081983