RED_MOUSE - dbPTM
RED_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RED_MOUSE
UniProt AC Q9Z1M8
Protein Name Protein Red
Gene Name Ik
Organism Mus musculus (Mouse).
Sequence Length 557
Subcellular Localization Nucleus . Nucleus, nucleoplasm . Chromosome . Cytoplasm, cytoskeleton, spindle pole . Predominantly present throughout the nucleoplasm during prometaphase, metaphase and anaphase. Is also detected in nuclear foci that are not identical with Cajal bod
Protein Description Involved in pre-mRNA splicing as a component of the spliceosome. Auxiliary spliceosomal protein that regulates selection of alternative splice sites in a small set of target pre-mRNA species. Required for normal mitotic cell cycle progression. Recruits MAD1L1 and MAD2L1 to kinetochores, and is required to trigger the spindle assembly checkpoint. Required for normal accumulation of SMU1..
Protein Sequence MPERDSEPFSNPLAPDGHDVDDPHSFHQSKLTNEDFRKLLMTPRAAPTSAPPSKSRHHEMPREYNEDEDPAARRRKKKSYYAKLRQQEIERERELAEKYRDRAKERRDGVNKDYEETELISTTANYRAVGPTAEADKSAAEKRRQLIQESKFLGGDMEHTHLVKGLDFALLQKVRAEIASKEKEEEELMEKPQKETKKDEDPENKIEFKTRLGRNVYRMLFKSKSYERNELFLPGRMAYVVDLDDEYADTDIPTTLIRSKADCPTMEAQTTLTTNDIVISKLTQILSYLRQGTRNKKLKKKDKGKLEEKKPPEADMNIFEDIGDYVPSTTKTPRDKERERYRERERDRERDRDRERDRERDRERERERDREREREEEKKRHSYFEKPKVDDEPMDVDKGPGSAKELIKSINEKFAGSAGWEGTESLKKPEDKKQLGDFFGMSNSYAECYPATMDDMAVDSDEEVDYSKMDQGNKKGPLGRWDFDTQEEYSEYMNNKEALPKAAFQYGIKMSEGRKTRRFKETNDKAELDRQWKKISAIIEKRKRMEADGVEVKRPKY
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
6Phosphorylation--MPERDSEPFSNPL
--CCCCCCCCCCCCC		54.0826370283
42PhosphorylationDFRKLLMTPRAAPTS
HHHHHHCCCCCCCCC		15.0226643407
98AcetylationRERELAEKYRDRAKE
HHHHHHHHHHHHHHH		39.72-
114PhosphorylationRDGVNKDYEETELIS
HCCCCCCHHHHHHHE		19.7825367039
117PhosphorylationVNKDYEETELISTTA
CCCCHHHHHHHEEEC		24.9325367039
137AcetylationGPTAEADKSAAEKRR
CCCHHHCHHHHHHHH		49.3823806337
173UbiquitinationLDFALLQKVRAEIAS
HHHHHHHHHHHHHHC		33.39-
180PhosphorylationKVRAEIASKEKEEEE
HHHHHHHCCHHHHHH		47.1929514104
223PhosphorylationVYRMLFKSKSYERNE
HHHHHHCCCCCCCCC		21.3526643407
225PhosphorylationRMLFKSKSYERNELF
HHHHCCCCCCCCCCC		39.0425266776
226PhosphorylationMLFKSKSYERNELFL
HHHCCCCCCCCCCCC		23.7329550500
259PhosphorylationIPTTLIRSKADCPTM
CCHHHHHCCCCCCCC		25.7925777480
265PhosphorylationRSKADCPTMEAQTTL
HCCCCCCCCCCCCCC		33.6925777480
270PhosphorylationCPTMEAQTTLTTNDI
CCCCCCCCCCCCHHH		30.7125777480
271PhosphorylationPTMEAQTTLTTNDIV
CCCCCCCCCCCHHHH		15.2725777480
273PhosphorylationMEAQTTLTTNDIVIS
CCCCCCCCCHHHHHH		22.8225777480
274PhosphorylationEAQTTLTTNDIVISK
CCCCCCCCHHHHHHH		33.7225777480
280PhosphorylationTTNDIVISKLTQILS
CCHHHHHHHHHHHHH		15.6625777480
283PhosphorylationDIVISKLTQILSYLR
HHHHHHHHHHHHHHH		19.8025777480
287PhosphorylationSKLTQILSYLRQGTR
HHHHHHHHHHHHCCC		24.6125777480
288PhosphorylationKLTQILSYLRQGTRN
HHHHHHHHHHHCCCC		11.4925777480
325PhosphorylationIFEDIGDYVPSTTKT
HHHHHHHCCCCCCCC		14.7325159016
328PhosphorylationDIGDYVPSTTKTPRD
HHHHCCCCCCCCCCH		38.3725619855
329PhosphorylationIGDYVPSTTKTPRDK
HHHCCCCCCCCCCHH		26.6625619855
330PhosphorylationGDYVPSTTKTPRDKE
HHCCCCCCCCCCHHH		36.9425619855
332PhosphorylationYVPSTTKTPRDKERE
CCCCCCCCCCHHHHH		22.8225619855
402PhosphorylationDVDKGPGSAKELIKS
CCCCCCCCHHHHHHH		39.0225619855
417PhosphorylationINEKFAGSAGWEGTE
HHHHHCCCCCCCCHH		21.8528066266
442PhosphorylationLGDFFGMSNSYAECY
HHHHHCCCCCHHHHE		24.0121149613
444PhosphorylationDFFGMSNSYAECYPA
HHHCCCCCHHHHEEC		20.5721149613
445PhosphorylationFFGMSNSYAECYPAT
HHCCCCCHHHHEECC		15.6321149613
449PhosphorylationSNSYAECYPATMDDM
CCCHHHHEECCHHHC		6.3421149613
452PhosphorylationYAECYPATMDDMAVD
HHHHEECCHHHCCCC		19.3429899451
460PhosphorylationMDDMAVDSDEEVDYS
HHHCCCCCCCCCCHH		40.0821149613
466PhosphorylationDSDEEVDYSKMDQGN
CCCCCCCHHHCCCCC		18.5021149613
467PhosphorylationSDEEVDYSKMDQGNK
CCCCCCHHHCCCCCC		19.6221149613
485PhosphorylationLGRWDFDTQEEYSEY
CCCCCCCCHHHHHHH		37.56-
489PhosphorylationDFDTQEEYSEYMNNK
CCCCHHHHHHHHCCC		13.1725159016
490PhosphorylationFDTQEEYSEYMNNKE
CCCHHHHHHHHCCCC		26.0725159016
536PhosphorylationDRQWKKISAIIEKRK
HHHHHHHHHHHHHHH		23.4629176673
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 RED_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory