NOE2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NOE2_HUMAN
• UniProt AC: O95897
• Protein Name: Noelin-2
• Gene Name: OLFM2
• Organism: Homo sapiens (Human).
• Sequence Length: 454
• Subcellular Localization: Secreted . Cell junction, synapse . Membrane . Nucleus . Cytoplasm . Nuclear localization is induced by TGF-beta.
• Protein Description: Involved in transforming growth factor beta (TGF-beta)-induced smooth muscle differentiation. TGF-beta induces expression and translocation of OLFM2 to the nucleus where it binds to SRF, causing its dissociation from the transcriptional repressor HEY2/HERP1 and facilitating binding of SRF to target genes. [PubMed: 25298399 Plays a role in AMPAR complex organization (By similarity Is a regulator of vascular smooth-muscle cell (SMC) phenotypic switching, that acts by promoting RUNX2 and inhibiting MYOCD binding to SRF. SMC phenotypic switching is the process through which vascular SMCs undergo transition between a quiescent contractile phenotype and a proliferative synthetic phenotype in response to pathological stimuli. SMC phenotypic plasticity is essential for vascular development and remodeling (By similarity]
• Protein Sequence: MWPLTVPPPLLLLLCSGLAGQTLFQNPEEGWQLYTSAQAPDGKCICTAVIPAQSTCSRDGRSRELRQLMEKVQNVSQSMEVLELRTYRDLQYVRGMETLMRSLDARLRAADGSLSAKSFQELKDRMTELLPLSSVLEQYKADTRTIVRLREEVRNLSGSLAAIQEEMGAYGYEDLQQRVMALEARLHACAQKLGCGKLTGVSNPITVRAMGSRFGSWMTDTMAPSADSRVWYMDGYYKGRRVLEFRTLGDFIKGQNFIQHLLPQPWAGTGHVVYNGSLFYNKYQSNVVVKYHFRSRSVLVQRSLPGAGYNNTFPYSWGGFSDMDFMVDESGLWAVYTTNQNAGNIVVSRLDPHTLEVMRSWDTGYPKRSAGEAFMICGVLYVTNSHLAGAKVYFAYFTNTSSYEYTDVPFHNQYSHISMLDYNPRERALYTWNNGHQVLYNVTLFHVISTSGDP

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
74	N-linked_Glycosylation	QLMEKVQNVSQSMEV HHHHHHHHHHHHHHH	38.09	UniProtKB CARBOHYD
113	Phosphorylation	RLRAADGSLSAKSFQ HHHHCCCCCCHHHHH	21.50	-
115	Phosphorylation	RAADGSLSAKSFQEL HHCCCCCCHHHHHHH	35.03	-
118	Phosphorylation	DGSLSAKSFQELKDR CCCCCHHHHHHHHHH	31.70	-
123	Ubiquitination	AKSFQELKDRMTELL HHHHHHHHHHHHHHH	42.40	-
147	Ubiquitination	KADTRTIVRLREEVR CCCCHHHHHHHHHHH	4.69	-
155	N-linked_Glycosylation	RLREEVRNLSGSLAA HHHHHHHHCCHHHHH	43.67	UniProtKB CARBOHYD
172	Phosphorylation	EEMGAYGYEDLQQRV HHHHCCCHHHHHHHH	8.13	-
206	Phosphorylation	TGVSNPITVRAMGSR CCCCCCEEEEECHHH	12.75	-
212	Phosphorylation	ITVRAMGSRFGSWMT EEEEECHHHCCCCCC	16.02	24275569
219	Phosphorylation	SRFGSWMTDTMAPSA HHCCCCCCCCCCCCC	23.28	24275569
232	Phosphorylation	SADSRVWYMDGYYKG CCCCCEEEECCEECC	5.18	24275569
275	N-linked_Glycosylation	GTGHVVYNGSLFYNK CCCEEEEECEEEEEE	23.20	UniProtKB CARBOHYD
310	N-linked_Glycosylation	SLPGAGYNNTFPYSW ECCCCCCCCCCCCCC	39.90	UniProtKB CARBOHYD
348	Phosphorylation	NAGNIVVSRLDPHTL CCCEEEEEECCHHHH	19.07	24719451
399	N-linked_Glycosylation	VYFAYFTNTSSYEYT EEEEEEECCCCCEEC	28.23	UniProtKB CARBOHYD
441	N-linked_Glycosylation	NGHQVLYNVTLFHVI CCCEEEEEEEEEEEE	19.01	UniProtKB CARBOHYD

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

Oops, there are no upstream regulatory protein records of NOE2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NOE2_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 NOE2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SRSF5_HUMAN	SRSF5	physical	16169070
F10A1_HUMAN	ST13	physical	16169070
BL1S6_HUMAN	BLOC1S6	physical	21988832
KR103_HUMAN	KRTAP10-3	physical	25416956
ZFHX4_HUMAN	ZFHX4	physical	28514442
BRE1B_HUMAN	RNF40	physical	28514442
TBB1_HUMAN	TUBB1	physical	28514442
DVL2_HUMAN	DVL2	physical	28514442
FEM1B_HUMAN	FEM1B	physical	28514442
KDM5C_HUMAN	KDM5C	physical	28514442
MSTO1_HUMAN	MSTO1	physical	28514442
LRIF1_HUMAN	LRIF1	physical	28514442
ZSWM8_HUMAN	ZSWIM8	physical	28514442
CBY1_HUMAN	CBY1	physical	28514442
EGFL7_HUMAN	EGFL7	physical	28514442
DTNB_HUMAN	DTNB	physical	28514442
SDF2L_HUMAN	SDF2L1	physical	28514442
DPYL4_HUMAN	DPYSL4	physical	28514442
MTA70_HUMAN	METTL3	physical	28514442
PEX6_HUMAN	PEX6	physical	28514442
GALNS_HUMAN	GALNS	physical	28514442
BMP7_HUMAN	BMP7	physical	28514442
ZN507_HUMAN	ZNF507	physical	28514442
CO039_HUMAN	C15orf39	physical	28514442
FUT11_HUMAN	FUT11	physical	28514442
NCOR1_HUMAN	NCOR1	physical	28514442
CNEP1_HUMAN	CTDNEP1	physical	28514442
BANP_HUMAN	BANP	physical	28514442
VCIP1_HUMAN	VCPIP1	physical	28514442
UBP54_HUMAN	USP54	physical	28514442
GPTC8_HUMAN	GPATCH8	physical	28514442
N42L2_HUMAN	N4BP2L2	physical	28514442
DNJB9_HUMAN	DNAJB9	physical	28514442
HAUS8_HUMAN	HAUS8	physical	28514442

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.