dbPTM

NEB2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NEB2_MOUSE
UniProt AC	Q6R891
Protein Name	Neurabin-2
Gene Name	Ppp1r9b
Organism	Mus musculus (Mouse).
Sequence Length	817
Subcellular Localization	Cytoplasm, cytoskeleton. Nucleus. Cell projection, dendritic spine. Cell junction, synapse. Cell junction, adherens junction. Cytoplasm. Cell membrane. Cell projection, lamellipodium. Cell projection, filopodium. Cell projection, ruffle membrane. Enr
Protein Description	Seems to act as a scaffold protein in multiple signaling pathways. Modulates excitatory synaptic transmission and dendritic spine morphology. Binds to actin filaments (F-actin) and shows cross-linking activity. Binds along the sides of the F-actin. May play an important role in linking the actin cytoskeleton to the plasma membrane at the synaptic junction. Believed to target protein phosphatase 1/PP1 to dendritic spines, which are rich in F-actin, and regulates its specificity toward ion channels and other substrates, such as AMPA-type and NMDA-type glutamate receptors. Plays a role in regulation of G-protein coupled receptor signaling, including dopamine D2 receptors and alpha-adrenergic receptors. May establish a signaling complex for dopaminergic neurotransmission through D2 receptors by linking receptors downstream signaling molecules and the actin cytoskeleton. Binds to ADRA1B and RGS2 and mediates regulation of ADRA1B signaling. May confer to Rac signaling specificity by binding to both, RacGEFs and Rac effector proteins. Probably regulates p70 S6 kinase activity by forming a complex with TIAM1. Required for hepatocyte growth factor (HGF)-induced cell migration (By similarity)..
Protein Sequence	MMKTEPRGPGGPLRSASPHRSAYEAGIQALKPPDAPGPDEAPKAAHHKKYGSNVHRIKSMFLQMGTTAGPPGEAGGGAGMAEAPRASDRGVRLSLPRASSLNENVDHSALLKLGTSVSERVSRFDSKPAPSAQPAPPPHPPSRLQETRKLFERSVPAASGGDKEAVARRLLRQERAGLQDRKLDVVVRFNGSTEALDKLDADAVSPTVSQLSAVFEKADSRTGLHRAPGPPRAAGAPQVNSKLVTKRSRVFQPPPPPPAPSGDGATEKERGPGGQQPPQHRVAPARPPPKPREVRKIKPVEVEESGESEAESAPGEVIQAEVTVHAALENGSTPATTASPAPEEPKAEAVPEEEAAASVATLERGVDNGRAPDMAPEEVDESKKEDFSEADLVDVSAYSGLGEDSGGSALEEDDEEDEEDGEPPYEPESGCVEIPGLSEEEDPAPSRKIHFSTAPIQVFSTYSNEDYDRRNEDVDPMAASAEYELEKRVERLELFPVELEKDSEGLGISIIGMGAGADMGLEKLGIFVKTVTEGGAAHRDGRIQVNDLLVEVDGTSLVGVTQSFAASVLRNTKGRVRFMIGRERPGEQSEVAQLIQQTLEQERWQREMMEQRYAQYGEDDEETGEYATDEDEELSPTFPGGEMAIEVFELAENEDALSPVEMEPEKLVHKFKELQIKHAVTEAEIQQLKRKLQSLEQEKGRWRVEKAQLEQSVEENKERMEKLEGYWGEAQSLCQAVDEHLRETQAQYQALERKYSKAKRLIKDYQQKEIEFLKKETAQRRVLEESELARKEEMDKLLDKISELEGNLQTLRNSNST

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
15	Phosphorylation	GPGGPLRSASPHRSA CCCCCCCCCCCCHHH	40.56	26643407
17	Phosphorylation	GGPLRSASPHRSAYE CCCCCCCCCCHHHHH	23.61	26643407
21	Phosphorylation	RSASPHRSAYEAGIQ CCCCCCHHHHHHHHH	31.97	26643407
23	Phosphorylation	ASPHRSAYEAGIQAL CCCCHHHHHHHHHHC	13.93	24759943
87	Phosphorylation	MAEAPRASDRGVRLS CCCCCCCCCCCCCCC	29.17	29899451
94	Phosphorylation	SDRGVRLSLPRASSL CCCCCCCCCCCCHHC	26.26	22324799
99	Phosphorylation	RLSLPRASSLNENVD CCCCCCCHHCCCCCC	36.32	25521595
100	Phosphorylation	LSLPRASSLNENVDH CCCCCCHHCCCCCCH	33.94	24925903
108	Phosphorylation	LNENVDHSALLKLGT CCCCCCHHHHHHHCC	19.02	25619855
116	Phosphorylation	ALLKLGTSVSERVSR HHHHHCCCHHHHHHC	23.11	29176673
118	Phosphorylation	LKLGTSVSERVSRFD HHHCCCHHHHHHCCC	21.32	29176673
192	Phosphorylation	VVVRFNGSTEALDKL EEEEECCCHHHHHHC	24.95	27087446
193	Phosphorylation	VVRFNGSTEALDKLD EEEECCCHHHHHHCC	27.03	26824392
205	Phosphorylation	KLDADAVSPTVSQLS HCCCCCCCCCHHHHH	19.30	24925903
207	Phosphorylation	DADAVSPTVSQLSAV CCCCCCCCHHHHHHH	25.86	25619855
209	Phosphorylation	DAVSPTVSQLSAVFE CCCCCCHHHHHHHHH	28.07	25619855
212	Phosphorylation	SPTVSQLSAVFEKAD CCCHHHHHHHHHHHC	18.10	18779572
220	Phosphorylation	AVFEKADSRTGLHRA HHHHHHCCCCCCCCC	36.28	29899451
358	Phosphorylation	PEEEAAASVATLERG CHHHHHHHHHHHHHC	13.93	28066266
361	Phosphorylation	EAAASVATLERGVDN HHHHHHHHHHHCCCC	27.31	28066266
382	Phosphorylation	APEEVDESKKEDFSE CHHHCCHHHCCCCCC	44.56	25521595
398	Phosphorylation	DLVDVSAYSGLGEDS CCEEHHHCCCCCCCC	8.86	22210881
438	Phosphorylation	CVEIPGLSEEEDPAP CEECCCCCCCCCCCC	49.21	-
483	Phosphorylation	PMAASAEYELEKRVE HHHHHHHHHHHHHHH	26.07	22210881
658	Phosphorylation	AENEDALSPVEMEPE HCCCCCCCCCCCCHH	28.72	-
800	Ubiquitination	EMDKLLDKISELEGN HHHHHHHHHHHHHHH	48.37	22790023

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
15	S	Phosphorylation	Kinase	MK01	P63085	PhosphoELM
17	S	Phosphorylation	Kinase	CDK5	P49615	Uniprot
94	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
94	S	Phosphorylation	Kinase	KAPCA	P05132	PhosphoELM
94	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
94	S	Phosphorylation	Kinase	PKA	-	Uniprot
205	S	Phosphorylation	Kinase	MK01	P63085	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
94	S	Phosphorylation	16300646
Dephosphorylation of Ser-94 is mediated mainly by PP1 and to a lesser extent by PP2A.
94	S	Phosphorylation	16300646
Stimulation of D1 (but not D2) dopamine receptors induces Ser-94 phosphorylation.

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of NEB2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
DCX_MOUSE	Dcx	physical	14550532

Drug and Disease Associations

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

Regulatory Network of NEB2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphorylation of spinophilin by ERK and cyclin-dependent PK 5(Cdk5)."; Futter M., Uematsu K., Bullock S.A., Kim Y., Hemmings H.C. Jr.,Nishi A., Greengard P., Nairn A.C.; Proc. Natl. Acad. Sci. U.S.A. 102:3489-3494(2005). Cited for: PHOSPHORYLATION BY MAPK1 AND CDK5, PHOSPHORYLATION AT SER-15; SER-17AND SER-205, AND MUTAGENESIS OF SER-15.	15728359 [Abstract]
"Regulation of spinophilin Ser94 phosphorylation in neostriatalneurons involves both DARPP-32-dependent and independent pathways."; Uematsu K., Futter M., Hsieh-Wilson L.C., Higashi H., Maeda H.,Nairn A.C., Greengard P., Nishi A.; J. Neurochem. 95:1642-1652(2005). Cited for: PHOSPHORYLATION BY PKA, PHOSPHORYLATION AT SER-94, ANDDEPHOSPHORYLATION BY PP1 AND PP2A.	16300646 [Abstract]

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