NEB1_RAT - dbPTM
NEB1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NEB1_RAT
UniProt AC O35867
Protein Name Neurabin-1
Gene Name Ppp1r9a
Organism Rattus norvegicus (Rat).
Sequence Length 1095
Subcellular Localization Cytoplasm, cytoskeleton. Cell junction, synapse, synaptosome.
Protein Description Binds to actin filaments (F-actin) and shows cross-linking activity. Binds along the sides of the F-actin. May be involved in neurite formation. Inhibits protein phosphatase 1-alpha activity. May play an important role in linking the actin cytoskeleton to the plasma membrane at the synaptic junction..
Protein Sequence MLKAESSGERTTLRSASPHRNAYRTEFQALKSTFDKPKPDGEQKTKEGEGSQQSRGRKYGSNVNRIKNLFMQMGMEPNENAAIIAKTRGKGRPSSPQKRMKPKEFVEKTDGSVVKLESSVSERISRFDTMHDGPSYAKFTETRKMFERSGHESGQNNRHSPKKEKAGEAEPQDEWGGSKSNRGSSDSLDSLSPRTEAVSPTVSQLSAVFENSESPGAITPGKAENSNYSVTGHYPLNLPSVTVTNLDTFGRLKDSNSRPSSNKQATDTEEPEKSEAVPVPEVAQKGTSLASLPSEERQLSTEAEDVTAQPDTPDSTDKDSPGEPSAESQAMPKSNTLSRPKEPLEDAEANVVGSEAEQPQRRDLTGGGDLTSPDASASSCGKEVPEDSNSFEGSHVYMHSDYNVYRVRSRYNSDWGETGTEQDEGDDSDENNYYQPDMEYSEIVGLPQEEEIPANRKIKFSCAPIKVFNTYSNEDYDRRNDDVDPVAASAEYELEKRVEKLELFPVELEKDEDGLGISIIGMGVGADAGLEKLGIFVKTVTEGGAAQRDGRIQVNDQIVEVDGISLVGVTQNFAATVLRNTKGNVRFVIGREKPGQVSEVAQLISQTLEQERRQRELLERHYAQYDADDDETGEYATDEEEDEVGPILPGGDMAIEVFELPENEDMFSPSDLDTSKLSHKFKELQIKHAVTEAEIQKLKTKLQAAENEKVRWELEKNQLQQNIEENKERMVKLESYWIEAQTLCHTVNEHLKETQSQYQALEKKYNKAKKLIKDFQQKELDFIRRQEVERKKLEEVEKAHLVEVQGLQVRIRDLEAEVFRLLKQNGTQVNNNNNIFERRPSPGEVSKGDTMENVEVKQTSCQDGLSQDLNEAVPETERLDSKALKTRAQLSVKNRRQRPTRTRLYDSVSSTDGEDSLERKNFTFNDDFSPSSTSSADLSGLGAEPKTPGLSQSLALSSDESLDMIDDEILDDGQSPKHTQSQSRAVHEWSVQQVSHWLVGLSLDQYVSEFSAQNISGEQLLQLDGNKLKALGMTSSQDRALVKKKLKEMKMSLEKARKAQEKMEKQREKLRRKEQEQMQRKSKKSEKMTSTTEQP
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
17PhosphorylationRTTLRSASPHRNAYR
CCCCCCCCCCCCHHH
23.6125403869
94PhosphorylationTRGKGRPSSPQKRMK
CCCCCCCCCCCCCCC
53.9725403869
95PhosphorylationRGKGRPSSPQKRMKP
CCCCCCCCCCCCCCC
33.7527115346
160PhosphorylationSGQNNRHSPKKEKAG
CCCCCCCCCCHHCCC
34.8725403869
180PhosphorylationDEWGGSKSNRGSSDS
CCCCCCCCCCCCCCC
33.1927097102
184PhosphorylationGSKSNRGSSDSLDSL
CCCCCCCCCCCHHHC
27.9528432305
185PhosphorylationSKSNRGSSDSLDSLS
CCCCCCCCCCHHHCC
33.7628432305
187PhosphorylationSNRGSSDSLDSLSPR
CCCCCCCCHHHCCCC
35.7027097102
190PhosphorylationGSSDSLDSLSPRTEA
CCCCCHHHCCCCCHH
35.7227097102
192PhosphorylationSDSLDSLSPRTEAVS
CCCHHHCCCCCHHCC
19.1127097102
195PhosphorylationLDSLSPRTEAVSPTV
HHHCCCCCHHCCCCH
31.5127097102
199PhosphorylationSPRTEAVSPTVSQLS
CCCCHHCCCCHHHHH
23.1527097102
201PhosphorylationRTEAVSPTVSQLSAV
CCHHCCCCHHHHHHH
25.8627097102
203PhosphorylationEAVSPTVSQLSAVFE
HHCCCCHHHHHHHHC
28.0728432305
206PhosphorylationSPTVSQLSAVFENSE
CCCHHHHHHHHCCCC
18.1028432305
212PhosphorylationLSAVFENSESPGAIT
HHHHHCCCCCCCCCC
32.0527097102
214PhosphorylationAVFENSESPGAITPG
HHHCCCCCCCCCCCC
28.5827097102
291PhosphorylationQKGTSLASLPSEERQ
HCCCCHHCCCHHHHH
46.2128432305
294PhosphorylationTSLASLPSEERQLST
CCHHCCCHHHHHCCC
58.3328432305
300PhosphorylationPSEERQLSTEAEDVT
CHHHHHCCCCCHHCC
18.8327097102
301PhosphorylationSEERQLSTEAEDVTA
HHHHHCCCCCHHCCC
48.0527097102
307PhosphorylationSTEAEDVTAQPDTPD
CCCCHHCCCCCCCCC
31.7127097102
312PhosphorylationDVTAQPDTPDSTDKD
HCCCCCCCCCCCCCC
35.3627097102
315PhosphorylationAQPDTPDSTDKDSPG
CCCCCCCCCCCCCCC
39.4422673903
316PhosphorylationQPDTPDSTDKDSPGE
CCCCCCCCCCCCCCC
55.2222673903
328PhosphorylationPGEPSAESQAMPKSN
CCCCCHHHHCCCCCC
23.9726022182
338PhosphorylationMPKSNTLSRPKEPLE
CCCCCCCCCCCCCHH
44.49-
365PhosphorylationQPQRRDLTGGGDLTS
CCCCCCCCCCCCCCC
37.7628551015
371PhosphorylationLTGGGDLTSPDASAS
CCCCCCCCCCCCCHH
42.8427097102
372PhosphorylationTGGGDLTSPDASASS
CCCCCCCCCCCCHHH
28.2530411139
376PhosphorylationDLTSPDASASSCGKE
CCCCCCCCHHHCCCC
35.7428432305
418PhosphorylationYNSDWGETGTEQDEG
CCCCCCCCCCCCCCC
45.5322673903
420PhosphorylationSDWGETGTEQDEGDD
CCCCCCCCCCCCCCC
37.5822673903
428PhosphorylationEQDEGDDSDENNYYQ
CCCCCCCCCCCCCCC
52.1122673903
433PhosphorylationDDSDENNYYQPDMEY
CCCCCCCCCCCCCCH
18.3022673903
434PhosphorylationDSDENNYYQPDMEYS
CCCCCCCCCCCCCHH
18.7222673903
440PhosphorylationYYQPDMEYSEIVGLP
CCCCCCCHHHHCCCC
12.6422673903
441PhosphorylationYQPDMEYSEIVGLPQ
CCCCCCHHHHCCCCC
13.9322673903
461PhosphorylationANRKIKFSCAPIKVF
CCCCCEEEECEEEEE
12.3612052877
841PhosphorylationNIFERRPSPGEVSKG
CCCCCCCCCCCCCCC
43.6630240740
850PhosphorylationGEVSKGDTMENVEVK
CCCCCCCCCCCEEEE
34.7428432305
866PhosphorylationTSCQDGLSQDLNEAV
EECCCCCCCHHHHHC
27.46-
891PhosphorylationLKTRAQLSVKNRRQR
HHHHHHHHHCCCCCC
20.9722108457
905PhosphorylationRPTRTRLYDSVSSTD
CCCCCCCCCCCCCCC
11.6828432305
907PhosphorylationTRTRLYDSVSSTDGE
CCCCCCCCCCCCCCC
15.4428432305
909PhosphorylationTRLYDSVSSTDGEDS
CCCCCCCCCCCCCCC
31.3228432305
910PhosphorylationRLYDSVSSTDGEDSL
CCCCCCCCCCCCCCH
28.5028432305
911PhosphorylationLYDSVSSTDGEDSLE
CCCCCCCCCCCCCHH
40.2828432305
916PhosphorylationSSTDGEDSLERKNFT
CCCCCCCCHHHCCEE
28.0327097102
923PhosphorylationSLERKNFTFNDDFSP
CHHHCCEECCCCCCC
30.8128551015
929PhosphorylationFTFNDDFSPSSTSSA
EECCCCCCCCCCCCC
30.7628551015
931PhosphorylationFNDDFSPSSTSSADL
CCCCCCCCCCCCCCC
45.0828551015
932PhosphorylationNDDFSPSSTSSADLS
CCCCCCCCCCCCCCC
35.3728551015
933PhosphorylationDDFSPSSTSSADLSG
CCCCCCCCCCCCCCC
30.9128551015
934PhosphorylationDFSPSSTSSADLSGL
CCCCCCCCCCCCCCC
26.0228551015
935PhosphorylationFSPSSTSSADLSGLG
CCCCCCCCCCCCCCC
26.3728551015
939PhosphorylationSTSSADLSGLGAEPK
CCCCCCCCCCCCCCC
32.3028551015
947PhosphorylationGLGAEPKTPGLSQSL
CCCCCCCCCCCCHHH
33.0516641100
951PhosphorylationEPKTPGLSQSLALSS
CCCCCCCCHHHCCCC
24.5216641100
953PhosphorylationKTPGLSQSLALSSDE
CCCCCCHHHCCCCCC
16.5416641100
957PhosphorylationLSQSLALSSDESLDM
CCHHHCCCCCCCCCC
30.0928551015
958PhosphorylationSQSLALSSDESLDMI
CHHHCCCCCCCCCCC
46.3728551015
961PhosphorylationLALSSDESLDMIDDE
HCCCCCCCCCCCCHH
34.3628551015
975PhosphorylationEILDDGQSPKHTQSQ
HHCCCCCCCCCCCHH
41.2528551015

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
461SPhosphorylationKinasePRKACAP27791
GPS
461SPhosphorylationKinasePKA-FAMILY-GPS
461SPhosphorylationKinasePKA-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NEB1_RAT !!

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 NEB1_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TGON3_RATTgoln2physical
10514494

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NEB1_RAT

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Regulation of neurabin I interaction with protein phosphatase 1 byphosphorylation.";
McAvoy T., Allen P.B., Obaishi H., Nakanishi H., Takai Y.,Greengard P., Nairn A.C., Hemmings H.C. Jr.;
Biochemistry 38:12943-12949(1999).
Cited for: INTERACTION WITH PP1, PHOSPHORYLATION AT SER-461, AND MUTAGENESIS.

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