dbPTM

JMY_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	JMY_MOUSE
UniProt AC	Q9QXM1
Protein Name	Junction-mediating and -regulatory protein
Gene Name	Jmy
Organism	Mus musculus (Mouse).
Sequence Length	983
Subcellular Localization	Nucleus . Cytoplasm, cytoskeleton. Localizes to the nucleus in most cell types. In primary neutrophils, it colocalizes with actin filaments at the leading edge and is excluded from the nucleus. Localization correlates with motility, because it moves
Protein Description	Acts both as a nuclear p53/TP53-cofactor and a cytoplasmic regulator of actin dynamics depending on conditions. In nucleus, acts as a cofactor that increases p53/TP53 response via its interaction with p300/EP300. Increases p53/TP53-dependent transcription and apoptosis, suggesting an important role in p53/TP53 stress response such as DNA damage. In cytoplasm, acts as a nucleation-promoting factor for both branched and unbranched actin filaments. Activates the Arp2/3 complex to induce branched actin filament networks. Also catalyzes actin polymerization in the absence of Arp2/3, creating unbranched filaments. Contributes to cell motility by controlling actin dynamics. May promote the rapid formation of a branched actin network by first nucleating new mother filaments and then activating Arp2/3 to branch off these filaments. The p53/TP53-cofactor and actin activator activities are regulated via its subcellular location..
Protein Sequence	MSFALEETLESDWVAVRPHVFDEREKHKFVFIVAWNEIEGKFAITCHNRTAQRQRSGSREQAGTPASDGSRGPGSPAARGRSEAAASATAALRSPGPRKSQAWAEGGSPRSARSLKGDPPRGPAGRGPESPLRSPARAKASPLRRSAESRDAIASATPVPPAPPVPPVSSVRVVSASGAVSEEIEVLEMVREDEAPQPLPDSEQPPSAAELESSAEECSWAGLFSFQDLRAVHQQLCSVNSQLEPCLPVFPEEPSGMWTVLFGGAPEMTEQEIDALCYQLQVYLGHGLDTCGWKILSQVLFTETDDPEEYYESLSELRQKGYEEVLQRARRRIQELLDKHKTIESMVELLDLYQMEDEAYSSLAEATTELYQYLLQPFRDMRELAMLRRQQIKISMENDYLGPRRIESLQKEDADWQRKAHMAVLSIQDLTVKYFEITAKAQKAVYDRMRADQKKFGKASWAAAAERMEKLQYAVSKETLQMMRAKEICLEQKKHALKEEMQSLQGGTEAIARLDQLESDYYDLQLQLYEVQFEILKCEELLLTAQLESIKRLISEKRDEVVYYDTYESMEAMLEKEEMAASVHAQREELQKLQQKARQLEARRGRVSAKKAYLRNKKEICIAKHHEKFQQRFQSEDEYRAHHTIQIKRDKLHDEEERKSAWVSQERQRTLDRLRTFKQRYPGQVILKSTRLRVAHSRRKSTASPVPCEEQCHSLPTVLQGQEKTEVGGGGSQLGPSQTAEPQSLVQLEDTSSEQLESTSLPPRAVVSSELPPPQSAPLLTSIDPKPCSVTIDPLPPPLPPTPPPPPPPPPPPPPPLPVAKDNGASTTAETLEKDALRTEGNERSIPKSASAPAAHLFDSSQLVSARKKLRKTVEGLQRRRVSSPMDEVLASLKRGSFHLKKVEQRTLPPFPDEDDSNNILAQIRKGVKLKKVQKEVLRESFTLLPDTDPLTRSIHEALRRIKEASPESEDEEEALPCTDWEN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSFALEETL ------CCCCCHHHH	21.16	26643407
56	Phosphorylation	RTAQRQRSGSREQAG HHHHCCCCCCHHHCC	32.55	27087446
58	Phosphorylation	AQRQRSGSREQAGTP HHCCCCCCHHHCCCC	33.61	27087446
64	Phosphorylation	GSREQAGTPASDGSR CCHHHCCCCCCCCCC	20.78	29472430
75	Phosphorylation	DGSRGPGSPAARGRS CCCCCCCCCCCCCCH	17.94	30352176
87	Phosphorylation	GRSEAAASATAALRS CCHHHHHHHHHHHHC	22.79	26643407
89	Phosphorylation	SEAAASATAALRSPG HHHHHHHHHHHHCCC	15.23	26643407
94	Phosphorylation	SATAALRSPGPRKSQ HHHHHHHCCCCCHHH	34.75	24899341
108	Phosphorylation	QAWAEGGSPRSARSL HHHHCCCCCCCHHHC	28.17	25521595
111	Phosphorylation	AEGGSPRSARSLKGD HCCCCCCCHHHCCCC	31.27	26643407
114	Phosphorylation	GSPRSARSLKGDPPR CCCCCHHHCCCCCCC	33.86	26643407
130	Phosphorylation	PAGRGPESPLRSPAR CCCCCCCCCCCCHHH	32.16	26824392
134	Phosphorylation	GPESPLRSPARAKAS CCCCCCCCHHHHCCC	30.51	26824392
141	Phosphorylation	SPARAKASPLRRSAE CHHHHCCCCCCCCHH	24.62	26824392
146	Phosphorylation	KASPLRRSAESRDAI CCCCCCCCHHHHHHH	29.92	29514104
395	Phosphorylation	RRQQIKISMENDYLG HHHHHHHHCCCCCCC	18.29	-
408	Phosphorylation	LGPRRIESLQKEDAD CCHHHHHHHHHCCCH	33.46	23140645
473	Phosphorylation	ERMEKLQYAVSKETL HHHHHHHHHHCHHHH	21.29	-
493	Ubiquitination	KEICLEQKKHALKEE HHHHHHHHHHHHHHH	36.83	22790023
569	Phosphorylation	VYYDTYESMEAMLEK EEEECHHHHHHHHHH	16.12	29514104
701	Phosphorylation	VAHSRRKSTASPVPC EECCCCCCCCCCCCH	27.65	25521595
702	Phosphorylation	AHSRRKSTASPVPCE ECCCCCCCCCCCCHH	33.90	27742792
704	Phosphorylation	SRRKSTASPVPCEEQ CCCCCCCCCCCHHHH	26.90	25521595
714	Phosphorylation	PCEEQCHSLPTVLQG CHHHHHHCCCCEECC	43.61	22324799
717	Phosphorylation	EQCHSLPTVLQGQEK HHHHCCCCEECCCCC	38.86	29472430
802	Phosphorylation	LPPPLPPTPPPPPPP CCCCCCCCCCCCCCC	46.62	26643407
845	Phosphorylation	RTEGNERSIPKSASA HCCCCCCCCCCCCCC	36.74	30635358
849	Phosphorylation	NERSIPKSASAPAAH CCCCCCCCCCCCHHH	23.31	29899451
851	Phosphorylation	RSIPKSASAPAAHLF CCCCCCCCCCHHHHC	41.71	29472430
860	Phosphorylation	PAAHLFDSSQLVSAR CHHHHCCHHHHHHHH	16.79	25293948
861	Phosphorylation	AAHLFDSSQLVSARK HHHHCCHHHHHHHHH	29.40	25293948
865	Phosphorylation	FDSSQLVSARKKLRK CCHHHHHHHHHHHHH	30.83	30635358
883	Phosphorylation	GLQRRRVSSPMDEVL HHHHHCCCCCHHHHH	27.23	26824392
884	Phosphorylation	LQRRRVSSPMDEVLA HHHHCCCCCHHHHHH	22.76	26824392
897	Phosphorylation	LASLKRGSFHLKKVE HHHHHHCCEEEEEEH	17.33	29899451
941	Phosphorylation	QKEVLRESFTLLPDT HHHHHHHHHCCCCCC	19.66	26824392
966	Phosphorylation	LRRIKEASPESEDEE HHHHHHHCCCCCCHH	30.23	23737553
969	Phosphorylation	IKEASPESEDEEEAL HHHHCCCCCCHHHHC	54.45	27087446
979	Phosphorylation	EEEALPCTDWEN--- HHHHCCCCCCCC---	42.05	24759943

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
-	K	Ubiquitination	E3 ubiquitin ligase	Mdm2	P23804	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of JMY_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 JMY_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of JMY_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of JMY_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells."; Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.; J. Proteome Res. 6:3174-3186(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-64 AND SER-75, AND MASSSPECTROMETRY.	17622165 [Abstract]