NEB2_HUMAN - dbPTM
NEB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NEB2_HUMAN
UniProt AC Q96SB3
Protein Name Neurabin-2
Gene Name PPP1R9B
Organism Homo sapiens (Human).
Sequence Length 815
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 (By similarity). Required for hepatocyte growth factor (HGF)-induced cell migration..
Protein Sequence MMKTEPRGPGGPLRSASPHRSAYEAGIQALKPPDAPGPDEAPKGAHHKKYGSNVHRIKSMFLQMGTTAGPSGEAGGGAGLAEAPRASERGVRLSLPRASSLNENVDHSALLKLGTSVSERVSRFDSKPAPSAQPAPPPHPPSRLQETRKLFERSAPAAGGDKEAARRLLRQERAGLQDRKLDVVVRFNGSTEALDKLDADAVSPTVSQLSAVFEKADSRTGLHRGPGLPRAAGVPQVNSKLVSKRSRVFQPPPPPPPAPSGDAPAEKERCPAGQQPPQHRVAPARPPPKPREVRKIKPVEVEESGESEAESAPGEVIQAEVTVHAALENGSTVATAASPAPEEPKAQAAPEKEAAAVAPPERGVGNGRAPDVAPEEVDESKKEDFSEADLVDVSAYSGLGEDSAGSALEEDDEDDEEDGEPPYEPESGCVEIPGLSEEEDPAPSRKIHFSTAPIQVFSTYSNEDYDRRNEDVDPMAASAEYELEKRVERLELFPVELEKDSEGLGISIIGMGAGADMGLEKLGIFVKTVTEGGAAHRDGRIQVNDLLVEVDGTSLVGVTQSFAASVLRNTKGRVRFMIGRERPGEQSEVAQLIQQTLEQERWQREMMEQRYAQYGEDDEETGEYATDEDEELSPTFPGGEMAIEVFELAENEDALSPVDMEPEKLVHKFKELQIKHAVTEAEIQQLKRKLQSLEQEKGRWRVEKAQLEQSVEENKERMEKLEGYWGEAQSLCQAVDEHLRETQAQYQALERKYSKAKRLIKDYQQKEIEFLKKETAQRRVLEESELARKEEMDKLLDKISELEGNLQTLRNSNST
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 Orthologous
Protein Cluster
4Phosphorylation----MMKTEPRGPGG
----CCCCCCCCCCC		33.0726074081
14MethylationRGPGGPLRSASPHRS
CCCCCCCCCCCCCHH		33.05115917581
15PhosphorylationGPGGPLRSASPHRSA
CCCCCCCCCCCCHHH		40.5628450419
17PhosphorylationGGPLRSASPHRSAYE
CCCCCCCCCCHHHHH		23.6130576142
21PhosphorylationRSASPHRSAYEAGIQ
CCCCCCHHHHHHHHH		31.9728450419
23PhosphorylationASPHRSAYEAGIQAL
CCCCHHHHHHHHHHC		13.9328450419
59PhosphorylationSNVHRIKSMFLQMGT
CCHHHHHHHHHHCCC		16.6428857561
66PhosphorylationSMFLQMGTTAGPSGE
HHHHHCCCCCCCCCC		14.2320068231
67PhosphorylationMFLQMGTTAGPSGEA
HHHHCCCCCCCCCCC		24.7227251275
71PhosphorylationMGTTAGPSGEAGGGA
CCCCCCCCCCCCCCC		48.6320068231
87PhosphorylationLAEAPRASERGVRLS
CCCCCCHHHCCCCCC		29.16-
94PhosphorylationSERGVRLSLPRASSL
HHCCCCCCCCCCHHC		26.2630266825
99PhosphorylationRLSLPRASSLNENVD
CCCCCCCHHCCCCCC		36.3223927012
100PhosphorylationLSLPRASSLNENVDH
CCCCCCHHCCCCCCH		33.9425159151
108PhosphorylationLNENVDHSALLKLGT
CCCCCCHHHHHHHCC		19.0223927012
115PhosphorylationSALLKLGTSVSERVS
HHHHHHCCCHHHHHH		36.0720068231
116PhosphorylationALLKLGTSVSERVSR
HHHHHCCCHHHHHHC		23.1120068231
118PhosphorylationLKLGTSVSERVSRFD
HHHCCCHHHHHHCCC		21.3229514088
122PhosphorylationTSVSERVSRFDSKPA
CCHHHHHHCCCCCCC		33.1929514088
126PhosphorylationERVSRFDSKPAPSAQ
HHHHCCCCCCCCCCC		37.5129514088
127AcetylationRVSRFDSKPAPSAQP
HHHCCCCCCCCCCCC		47.2226051181
190PhosphorylationVVVRFNGSTEALDKL
EEEEECCCHHHHHHC		24.9529255136
191PhosphorylationVVRFNGSTEALDKLD
EEEECCCHHHHHHCC		27.0329255136
192PhosphorylationVRFNGSTEALDKLDA
EEECCCHHHHHHCCC		49.2724719451
193PhosphorylationRFNGSTEALDKLDAD
EECCCHHHHHHCCCC		22.5823186163
203PhosphorylationKLDADAVSPTVSQLS
HCCCCCCCCCHHHHH		19.3029255136
205PhosphorylationDADAVSPTVSQLSAV
CCCCCCCCHHHHHHH		25.8629255136
207PhosphorylationDAVSPTVSQLSAVFE
CCCCCCHHHHHHHHH		28.0724732914
210PhosphorylationSPTVSQLSAVFEKAD
CCCHHHHHHHHHHHC		18.1024732914
243PhosphorylationQVNSKLVSKRSRVFQ
CCCCHHHCCCCCCCC		32.56-
246PhosphorylationSKLVSKRSRVFQPPP
CHHHCCCCCCCCCCC		36.2130387612
260PhosphorylationPPPPPAPSGDAPAEK
CCCCCCCCCCCCCHH		51.9530387612
267AcetylationSGDAPAEKERCPAGQ
CCCCCCHHHCCCCCC		53.1926051181
304PhosphorylationKPVEVEESGESEAES
CCEEEECCCCCCCCC		34.0620058876
307PhosphorylationEVEESGESEAESAPG
EEECCCCCCCCCCCC		45.7028348404
311PhosphorylationSGESEAESAPGEVIQ
CCCCCCCCCCCCEEE		46.9728348404
331PhosphorylationHAALENGSTVATAAS
EEHHHCCCEEEEECC		31.1526074081
332PhosphorylationAALENGSTVATAASP
EHHHCCCEEEEECCC		18.6326074081
335PhosphorylationENGSTVATAASPAPE
HCCCEEEEECCCCCC		20.5826074081
338PhosphorylationSTVATAASPAPEEPK
CEEEEECCCCCCCCH		21.0926657352
380PhosphorylationAPEEVDESKKEDFSE
CHHHCCHHHCCCCCC		44.5622199227
436PhosphorylationCVEIPGLSEEEDPAP
CEECCCCCCCCCCCC		49.2120058876
438PhosphorylationEIPGLSEEEDPAPSR
ECCCCCCCCCCCCCC		65.4124275569
444PhosphorylationEEEDPAPSRKIHFST
CCCCCCCCCCEEEEC		48.5924275569
478PhosphorylationDVDPMAASAEYELEK
CCCHHHHHHHHHHHH		16.4622461510
481PhosphorylationPMAASAEYELEKRVE
HHHHHHHHHHHHHHH		26.0727642862
507PhosphorylationDSEGLGISIIGMGAG
CCCCCCEEEEECCCC		13.3230257219
633PhosphorylationTDEDEELSPTFPGGE
CCCCCCCCCCCCCCC		25.7724275569
656PhosphorylationAENEDALSPVDMEPE
HCCCCCCCCCCCCHH		25.2926657352
658PhosphorylationNEDALSPVDMEPEKL
CCCCCCCCCCCHHHH		11.1324275569
675UbiquitinationKFKELQIKHAVTEAE
HHHHHHHHHHCCHHH		16.7321890473
677UbiquitinationKELQIKHAVTEAEIQ
HHHHHHHHCCHHHHH		12.6221890473
677UbiquitinationKELQIKHAVTEAEIQ
HHHHHHHHCCHHHHH		12.62-
687UbiquitinationEAEIQQLKRKLQSLE
HHHHHHHHHHHHHHH		43.0521890473
689UbiquitinationEIQQLKRKLQSLEQE
HHHHHHHHHHHHHHH		49.65-
689UbiquitinationEIQQLKRKLQSLEQE
HHHHHHHHHHHHHHH		49.6521890473
692PhosphorylationQLKRKLQSLEQEKGR
HHHHHHHHHHHHHCC		44.2926852163
710PhosphorylationEKAQLEQSVEENKER
HHHHHHHHHHHHHHH		23.3220068231
717UbiquitinationSVEENKERMEKLEGY
HHHHHHHHHHHHHHH		39.9230230243
742PhosphorylationVDEHLRETQAQYQAL
HHHHHHHHHHHHHHH		23.8328796482
746PhosphorylationLRETQAQYQALERKY
HHHHHHHHHHHHHHH		9.9628796482
808PhosphorylationELEGNLQTLRNSNST
HHHHHHHHHHCCCCC		30.7430576142
812PhosphorylationNLQTLRNSNST----
HHHHHHCCCCC----		26.2330576142
814PhosphorylationQTLRNSNST------
HHHHCCCCC------		35.0028555341
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
94SPhosphorylationKinasePKA-FAMILY-GPS
94SPhosphorylationKinasePKA_GROUP-PhosphoELM
100SPhosphorylationKinasePKA-FAMILY-GPS
100SPhosphorylationKinasePKA_GROUP-PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
94SPhosphorylation

-
94SPhosphorylation

-
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDN2A_HUMANCDKN2Aphysical
11278317
ARF_HUMANCDKN2Aphysical
11278317
TIAM1_HUMANTIAM1physical
12531897
IPP2_HUMANPPP1R2physical
12270929
PP1A_HUMANPPP1CAphysical
10194355
PP1B_HUMANPPP1CBphysical
10194355
PP1G_HUMANPPP1CCphysical
10194355
DRD2_HUMANDRD2physical
10391935
PP1G_HUMANPPP1CCphysical
10391935
RGRF1_HUMANRASGRF1physical
12531897
ADA2C_HUMANADRA2Cphysical
11154706
ADA2B_HUMANADRA2Bphysical
11154706
ADA2A_HUMANADRA2Aphysical
11154706
ACTS_HUMANACTA1physical
12417592
PP1A_HUMANPPP1CAphysical
19094064
DCX_HUMANDCXphysical
19094064
DCX_HUMANDCXphysical
17178868
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.
Regulatory Network of NEB2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASSSPECTROMETRY.
"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-203, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND THR-205, ANDMASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, AND MASSSPECTROMETRY.

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