GRIP1_MOUSE - dbPTM
GRIP1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GRIP1_MOUSE
UniProt AC Q925T6
Protein Name Glutamate receptor-interacting protein 1
Gene Name Grip1
Organism Mus musculus (Mouse).
Sequence Length 1127
Subcellular Localization Cytoplasmic vesicle. Endoplasmic reticulum. Cell junction, synapse, postsynaptic cell membrane. Cytoplasmic and membrane-associated with vesicles, peri-Golgi complexes and endoplasmic reticulum. Enriched in postsynaptic plasma membrane and postsynapt
Protein Description May play a role as a localized scaffold for the assembly of a multiprotein signaling complex and as mediator of the trafficking of its binding partners at specific subcellular location in neurons (By similarity). Through complex formation with NSG1, GRIA2 and STX12 controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting (By similarity)..
Protein Sequence MIAVSFKCRCQILRRLTKDESPYTKSASQTKPPDGALAVRRQSIPEEFKGSTVVELMKKEGTTLGLTVSGGIDKDGKPRVSNLRQGGIAARSDQLDVGDYIKAVNGINLAKFRHDEIISLLKNVGERVVLEVEYELPPVSVQGSSVMFRTVEVTLHKEGNTFGFVIRGGAHDDRNKSRPVVITCVRPGGPADREGTIKPGDRLLSVDGIRLLGTTHAEAMSILKQCGQEATLLIEYDVSVMDSVATASGPLLVEVAKTPGASLGVALTTSVCCNKQVIVIDKIKSASIADRCGALHVGDHILSIDGTSMEYCTLAEATQFLANTTDQVKLEILPHHQTRLALKGPDHVKIQRSDRQHPWDAWASNQCGVHTNHHHNTYHPDHCRVPALTFPKALPPNSPPAMVPSSSPTSMSAYSLSSLNMGTLPRSLYSTSPRGTMMRRRLKKKDFKSSLSLASSTVGLAGQVVHTETTEVVLTADPVTGFGIQLQGSVFATETLSSPPLISYIEADSPAERCGVLQIGDRVMAINGIPTEDSTFEEANQLLRDSSITSKVTLEIEFDVAESVIPSSGTFHVKLPKKHSVELGITISSPSSRKPGDPLVISDIKKGSVAHRTGTLELGDKLLAIDNIRLDNCSMEDAVQILQQCEDLVKLKIRKDEDNSDEQESSGAIIYTVELKRYGGPLGITISGTEEPFDPIIISSLTKGGLAERTGAIHIGDRILAINSSSLKGKPLSEAIHLLQMAGETVTLKIKKQTDAQSASSPKKFPIPGHSGDLGDGEEDPSPIQKPGKLSDAYPSTVPSVDSAVDSWDGSGIDASYGSQGSTFQTSGYNYNTYDWRSPKQRTSLSPVPKPRSQTYPDVGLSNEDWDRSTASGFVGASDSADAEQEENFWSQALEDLETCGQSGILRELEEKADRRVSLRNMTLLATIMSGSTMSLNHEAPMARSQLGRQASFQERSSSRPHYSQTTRSNTLPSDVGRKSVTLRKMKQEIKEIMSPTPVELHKVTLYKDSGMEDFGFSVADGLLEKGVYVKNIRPAGPGDVGGLKPYDRLLQVNHVRTRDFDCCLVVPLIAESGNKLDLVISRNPLASQKSIEQPALPSDWSEQNSAFFQQPSHGGNLETREPTNTL
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
11 (in isoform 2)S-palmitoylation-20.57-
11S-palmitoylationVSFKCRCQILRRLTK
EEEHHHHHHHHHHCC
20.5722325201
43PhosphorylationALAVRRQSIPEEFKG
CEEEECCCCCHHHCC
38.0025521595
51PhosphorylationIPEEFKGSTVVELMK
CCHHHCCCCEEEHHH
20.7229899451
52PhosphorylationPEEFKGSTVVELMKK
CHHHCCCCEEEHHHC
36.9229899451
344 (in isoform 3)Phosphorylation-33.45-
345 (in isoform 2)Phosphorylation-27.26-
423PhosphorylationLSSLNMGTLPRSLYS
HHHCCCCCCCHHHHC
23.87-
427PhosphorylationNMGTLPRSLYSTSPR
CCCCCCHHHHCCCCC
29.7129899451
430PhosphorylationTLPRSLYSTSPRGTM
CCCHHHHCCCCCHHH
27.9228066266
431PhosphorylationLPRSLYSTSPRGTMM
CCHHHHCCCCCHHHH
29.2428066266
432PhosphorylationPRSLYSTSPRGTMMR
CHHHHCCCCCHHHHH
13.4722817900
432 (in isoform 4)Phosphorylation-13.4725293948
435 (in isoform 4)Phosphorylation-22.7325293948
437 (in isoform 4)Phosphorylation-1.8825293948
438 (in isoform 4)Phosphorylation-2.7925293948
440 (in isoform 4)Phosphorylation-30.3225293948
660PhosphorylationIRKDEDNSDEQESSG
EECCCCCCCCHHHCC
55.6429899451
665PhosphorylationDNSDEQESSGAIIYT
CCCCCHHHCCEEEEE
33.4929899451
700PhosphorylationFDPIIISSLTKGGLA
CCCEEEEECCCCCHH
29.65-
758PhosphorylationKKQTDAQSASSPKKF
EECCCCCCCCCCCCC
31.6623335269
760PhosphorylationQTDAQSASSPKKFPI
CCCCCCCCCCCCCCC
53.0423335269
761PhosphorylationTDAQSASSPKKFPIP
CCCCCCCCCCCCCCC
40.2225521595
771PhosphorylationKFPIPGHSGDLGDGE
CCCCCCCCCCCCCCC
39.6622817900
782PhosphorylationGDGEEDPSPIQKPGK
CCCCCCCCCCCCCCC
47.1322817900
833 (in isoform 3)Phosphorylation-16.7025293948
834 (in isoform 2)Phosphorylation-15.1825293948
836 (in isoform 3)Phosphorylation-7.7025293948
837 (in isoform 2)Phosphorylation-39.9425293948
838 (in isoform 3)Phosphorylation-31.9925293948
839 (in isoform 3)Phosphorylation-28.3825293948
839 (in isoform 2)Phosphorylation-28.3825293948
840 (in isoform 2)Phosphorylation-54.3725293948
841 (in isoform 3)Phosphorylation-58.2125293948
842 (in isoform 2)Phosphorylation-32.2025293948
843PhosphorylationWRSPKQRTSLSPVPK
CCCCCCCCCCCCCCC
31.3721454597
844PhosphorylationRSPKQRTSLSPVPKP
CCCCCCCCCCCCCCC
29.1021454597
846PhosphorylationPKQRTSLSPVPKPRS
CCCCCCCCCCCCCCC
24.5021454597
952PhosphorylationSQLGRQASFQERSSS
HHHHHHHHHHHHHCC
21.0822324799
969PhosphorylationHYSQTTRSNTLPSDV
CCCCCCCCCCCCCCC
31.8825521595
971PhosphorylationSQTTRSNTLPSDVGR
CCCCCCCCCCCCCCC
41.0923527152
974PhosphorylationTRSNTLPSDVGRKSV
CCCCCCCCCCCCCHH
48.3023984901
995PhosphorylationQEIKEIMSPTPVELH
HHHHHHCCCCCCEEE
31.1428066266
997PhosphorylationIKEIMSPTPVELHKV
HHHHCCCCCCEEEEE
32.4325521595
1088PhosphorylationISRNPLASQKSIEQP
EECCCCCCCCCCCCC
45.9128066266
1091PhosphorylationNPLASQKSIEQPALP
CCCCCCCCCCCCCCC
24.5829899451

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

Oops, there are no upstream regulatory protein records of GRIP1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GRIP1_MOUSE !!

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 GRIP1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NRIP1_MOUSENrip1physical
17389641
KAT2B_MOUSEKat2bphysical
17389641
ACTN2_MOUSEActn2physical
15072553
ALS2_MOUSEAls2physical
17093100
ESR1_MOUSEEsr1physical
8643509
ANDR_MOUSEArphysical
8643509

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GRIP1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND MASSSPECTROMETRY.

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