NMT2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NMT2_HUMAN
• UniProt AC: O60551
• Protein Name: Glycylpeptide N-tetradecanoyltransferase 2
• Gene Name: NMT2
• Organism: Homo sapiens (Human).
• Sequence Length: 498
• Subcellular Localization: Cytoplasm . Membrane ; Peripheral membrane protein .
• Protein Description: Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins..
• Protein Sequence: MAEDSESAASQQSLELDDQDTCGIDGDNEEETEHAKGSPGGYLGAKKKKKKQKRKKEKPNSGGTKSDSASDSQEIKIQQPSKNPSVPMQKLQDIQRAMELLSACQGPARNIDEAAKHRYQFWDTQPVPKLDEVITSHGAIEPDKDNVRQEPYSLPQGFMWDTLDLSDAEVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWLLQWHCGVRVSSNKKLVGFISAIPANIRIYDSVKKMVEINFLCVHKKLRSKRVAPVLIREITRRVNLEGIFQAVYTAGVVLPKPIATCRYWHRSLNPRKLVEVKFSHLSRNMTLQRTMKLYRLPDVTKTSGLRPMEPKDIKSVRELINTYLKQFHLAPVMDEEEVAHWFLPREHIIDTFVVESPNGKLTDFLSFYTLPSTVMHHPAHKSLKAAYSFYNIHTETPLLDLMSDALILAKSKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWRCPGTDSEKVGLVLQ

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
5	Phosphorylation	---MAEDSESAASQQ ---CCCCHHHHHHHH	25.59	27251275
7	Phosphorylation	-MAEDSESAASQQSL -CCCCHHHHHHHHCC	32.84	26471730
10	Phosphorylation	EDSESAASQQSLELD CCHHHHHHHHCCCCC	28.59	26471730
13	Phosphorylation	ESAASQQSLELDDQD HHHHHHHCCCCCCCC	19.04	26471730
21	Phosphorylation	LELDDQDTCGIDGDN CCCCCCCCCCCCCCC	13.65	27251275
38	Phosphorylation	ETEHAKGSPGGYLGA HHHHHCCCCCCHHHH	21.47	30266825
42	Phosphorylation	AKGSPGGYLGAKKKK HCCCCCCHHHHHHHH	14.10	23403867
61	Phosphorylation	RKKEKPNSGGTKSDS CCCCCCCCCCCCCCC	47.31	26846344
64	Phosphorylation	EKPNSGGTKSDSASD CCCCCCCCCCCCCCC	30.79	26846344
66	Phosphorylation	PNSGGTKSDSASDSQ CCCCCCCCCCCCCCC	36.31	26846344
68	Phosphorylation	SGGTKSDSASDSQEI CCCCCCCCCCCCCCE	36.44	26846344
70	Phosphorylation	GTKSDSASDSQEIKI CCCCCCCCCCCCEEE	41.57	26846344
72	Phosphorylation	KSDSASDSQEIKIQQ CCCCCCCCCCEEEEC	27.50	23403867
144	Ubiquitination	HGAIEPDKDNVRQEP CCCCCCCCCCCCCCC	63.02	-
182	Phosphorylation	YTLLNENYVEDDDNM HHHHHHCCCCCCCCC	10.07	22817900
229	Phosphorylation	KKLVGFISAIPANIR CEEEEEEECCCCCCE	20.20	-
254	Acetylation	INFLCVHKKLRSKRV EEEEEEHHHHCCCCC	32.86	25953088
283	Phosphorylation	EGIFQAVYTAGVVLP HHHHHHHHEECCCCC	8.22	-
302	Phosphorylation	TCRYWHRSLNPRKLV CCHHHHHCCCHHHEE	21.44	28355574
317	Phosphorylation	EVKFSHLSRNMTLQR EEECHHHCCCCCHHH	19.04	29514088
321	Phosphorylation	SHLSRNMTLQRTMKL HHHCCCCCHHHHHHH	24.24	29514088
325	Phosphorylation	RNMTLQRTMKLYRLP CCCCHHHHHHHHCCC	13.00	20068231
327	Ubiquitination	MTLQRTMKLYRLPDV CCHHHHHHHHCCCCC	41.58	-
329	Phosphorylation	LQRTMKLYRLPDVTK HHHHHHHHCCCCCCC	12.46	20068231
335	Phosphorylation	LYRLPDVTKTSGLRP HHCCCCCCCCCCCCC	35.66	20068231
337	Phosphorylation	RLPDVTKTSGLRPME CCCCCCCCCCCCCCC	20.75	20068231
338	Phosphorylation	LPDVTKTSGLRPMEP CCCCCCCCCCCCCCC	37.07	20068231
447	Ubiquitination	ALILAKSKGFDVFNA HHHHHHHCCCCHHHH	63.99	-
458	Sulfoxidation	VFNALDLMENKTFLE HHHHHHHHCCHHHHH	5.49	21406390
461	Ubiquitination	ALDLMENKTFLEKLK HHHHHCCHHHHHHHC	27.61	-
466	Acetylation	ENKTFLEKLKFGIGD CCHHHHHHHCCCCCC	60.15	26051181

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

Oops, there are no upstream regulatory protein records of NMT2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NMT2_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 NMT2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GAG_HV1H2	gag	physical	16501079
A4_HUMAN	APP	physical	21832049
TMED9_HUMAN	TMED9	physical	21988832
P53_HUMAN	TP53	physical	16530191
BCL2_HUMAN	BCL2	physical	16530191

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-38, AND MASSSPECTROMETRY.
PubMed: 19413330