SHSA7_MOUSE - dbPTM
SHSA7_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SHSA7_MOUSE
UniProt AC Q8C3Q5
Protein Name Protein shisa-7 {ECO:0000305}
Gene Name Shisa7 {ECO:0000303|PubMed:29199957, ECO:0000312|MGI:MGI:3605641}
Organism Mus musculus (Mouse).
Sequence Length 558
Subcellular Localization Cell junction, synapse, postsynaptic cell membrane, postsynaptic density
Single-pass type I membrane protein .
Protein Description Regulator of long-term synaptic potentiation specifically involved in the formation and retrieval of hippocampus-dependent contextual fear memory. Probably regulates induction and maintenance of long-term potentiation at Schaffer collaterals/CA3-CA1 excitatory synapses by affecting the recruitment of AMPA-type glutamate receptor (AMPAR) at postsynaptic density..
Protein Sequence MPALLLLGTVALLASAAGPAGARPSNDTSSVAPGPLPALLAHLRRLTGALAGGGSAAGTSANATKTSPASGTGAAARAPPPAELCHGYYDVMGQYDATFNCSTGSYRFCCGTCHYRFCCEHRHMRLAQASCSNYDTPRWATTPPPLAGGAGGAGGAGGGPGPGQAGWLEGGRAGGAGGRGGEGPGGSTAYVVCGVISFALAVGVGAKVAFSKASRAPRAHREINVPRALVDILRHQAGPATRPDRARSSSLTPGLGGPDSMAPRTPKNLYNTMKPSNLDNLHYNVNSPKHHAATLDWRAMPPPSPSLHYSTLSCSRSFHNLSHLPPSYEAAVKSELNRYSSLKRLAEKDLDEAYLKRRQLEMPRGTLPLHALRRPGTGGGYRMDGWGGPEELGLAPAPNPRRVMSQEHLLGDGSRASRYEFTLPRARLVSQEHLLLSSPEALRQSREHLLSPPRSPALPPDPTTRASLAASHSNLLLGPGGPPTPLHGLPPSGLHAHHHHALHGSPQPAWMSDAGGGGGTLARRPPFQRQGTLEQLQFIPGHHLPQHLRTASKNEVTV
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
26N-linked_GlycosylationPAGARPSNDTSSVAP
CCCCCCCCCCCCCCC		60.30-
47PhosphorylationLAHLRRLTGALAGGG
HHHHHHHHHHHHCCC		20.7129899451
60PhosphorylationGGSAAGTSANATKTS
CCCCCCCCCCCCCCC		20.7129899451
188UbiquitinationGEGPGGSTAYVVCGV
CCCCCCCHHHHHHHH		25.8627667366
212UbiquitinationGAKVAFSKASRAPRA
CHHHHHHHHHCCCHH		43.8827667366
243UbiquitinationQAGPATRPDRARSSS
CCCCCCCCCCHHHCC		30.9627667366
248PhosphorylationTRPDRARSSSLTPGL
CCCCCHHHCCCCCCC		24.2425521595
249PhosphorylationRPDRARSSSLTPGLG
CCCCHHHCCCCCCCC		24.6622817900
250PhosphorylationPDRARSSSLTPGLGG
CCCHHHCCCCCCCCC		37.1925521595
252PhosphorylationRARSSSLTPGLGGPD
CHHHCCCCCCCCCCC		19.7725521595
260PhosphorylationPGLGGPDSMAPRTPK
CCCCCCCCCCCCCCC		21.7020415495
260UbiquitinationPGLGGPDSMAPRTPK
CCCCCCCCCCCCCCC		21.7027667366
265PhosphorylationPDSMAPRTPKNLYNT
CCCCCCCCCCCHHHC		37.2429899451
267 (in isoform 2)Ubiquitination-60.0022790023
267UbiquitinationSMAPRTPKNLYNTMK
CCCCCCCCCHHHCCC		60.0022790023
272PhosphorylationTPKNLYNTMKPSNLD
CCCCHHHCCCCCCCC		17.0218056256
274 (in isoform 2)Ubiquitination-43.16-
287PhosphorylationNLHYNVNSPKHHAAT
CCEECCCCCCCCEEC		30.9222817900
304PhosphorylationWRAMPPPSPSLHYST
CCCCCCCCCCCEEEE		32.6629899451
306PhosphorylationAMPPPSPSLHYSTLS
CCCCCCCCCEEEEEE		31.9229899451
316 (in isoform 2)Ubiquitination-47.90-
317PhosphorylationSTLSCSRSFHNLSHL
EEEEECCCCCCHHCC		17.9829899451
322PhosphorylationSRSFHNLSHLPPSYE
CCCCCCHHCCCCCHH		28.4426804993
331 (in isoform 2)Ubiquitination-9.42-
333 (in isoform 2)Ubiquitination-33.2222790023
333UbiquitinationPSYEAAVKSELNRYS
CCHHHHHHHHHHHHH		33.2222790023
339 (in isoform 2)Ubiquitination-11.09-
348 (in isoform 2)Ubiquitination-58.9722790023
348UbiquitinationSLKRLAEKDLDEAYL
HHHHHHHCCCCHHHH		58.9722790023
354PhosphorylationEKDLDEAYLKRRQLE
HCCCCHHHHHHHCCC		15.6522817900
356 (in isoform 2)Ubiquitination-32.6222790023
356UbiquitinationDLDEAYLKRRQLEMP
CCCHHHHHHHCCCCC		32.6222790023
405PhosphorylationPNPRRVMSQEHLLGD
CCHHCCCCCHHHCCC		29.5629899451
430PhosphorylationLPRARLVSQEHLLLS
CCCHHHCCHHHHHHC		34.1524925903
437PhosphorylationSQEHLLLSSPEALRQ
CHHHHHHCCHHHHHH		43.7622324799
438PhosphorylationQEHLLLSSPEALRQS
HHHHHHCCHHHHHHH		27.0825521595
445PhosphorylationSPEALRQSREHLLSP
CHHHHHHHHHHHCCC		32.9529899451
451PhosphorylationQSREHLLSPPRSPAL
HHHHHHCCCCCCCCC		38.9425521595
455PhosphorylationHLLSPPRSPALPPDP
HHCCCCCCCCCCCCC		21.9425521595
463PhosphorylationPALPPDPTTRASLAA
CCCCCCCCHHHHHHH		35.9720415495
464PhosphorylationALPPDPTTRASLAAS
CCCCCCCHHHHHHHH		29.6220415495
532PhosphorylationPPFQRQGTLEQLQFI
CCCCCCCCHHHHHCC		20.8425521595
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 SHSA7_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SHSA7_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 SHSA7_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SHSA7_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SHSA7_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Proteomic analysis of in vivo phosphorylated synaptic proteins.";
Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,Blackstock W.P., Choudhary J.S., Grant S.G.;
J. Biol. Chem. 280:5972-5982(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-532, AND MASSSPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-354, AND MASSSPECTROMETRY.

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