JMY_HUMAN - dbPTM
JMY_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID JMY_HUMAN
UniProt AC Q8N9B5
Protein Name Junction-mediating and -regulatory protein
Gene Name JMY
Organism Homo sapiens (Human).
Sequence Length 988
Subcellular Localization Nucleus. Cytoplasm, cytoskeleton . Localizes to the nucleus in most cell types. Accumulates in nucleus under DNA damage conditions, increasing p53/TP53 transcription response and reducing its influence on cell motility (By similarity). In primary neu
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 (By similarity)..
Protein Sequence MSFALEETLESDWVAVRPHVFDEREKHKFVFIVAWNEIEGKFAITCHNRTAQRQRSGSREQAGARGGAEAGGAASDGSRGPGSPAGRGRPEATASATLVRSPGPRRSSAWAEGGSPRSTRSLLGDPRLRSPGSKGAESRLRSPVRAKPIPGQKTSEADDAAGAAAAAARPAPREAQVSSVRIVSASGTVSEEIEVLEMVKEDEAPLALSDAEQPPPATELESPAEECSWAGLFSFQDLRAVHQQLCSVNSQLEPCLPVFPEEPSGMWTVLFGGAPEMTEQEIDTLCYQLQVYLGHGLDTCGWKILSQVLFTETDDPEEYYESLSELRQKGYEEVLQRARKRIQELLDKHKNTESMVELLDLYQMEDEAYSSLAEATTELYQYLLQPFRDMRELAMLRRQQIKISMENDYLGPRRIESLQKEDADWQRKAHMAVLSIQDLTVKYFEITAKAQKAVYDRMRADQKKFGKASWAAAAERMEKLQYAVSKETLQMMRAKEICLEQRKHALKEEMQSLRGGTEAIARLDQLEADYYDLQLQLYEVQFEILKCEELLLTAQLESIKRLISEKRDEVVYYDTYESMEAMLEKEEMAASAYLQREELQKLQQKARQLEARRGRVSAKKSYLRNKKEICIAKHNEKIQQRTRIEDEYRTHHTVQLKREKLHDEEERKSAWVSQERQRTLDRLRTFKQRYPGQVILKSTRLRLAHARRKGAASPVLQEDHCDSLPSVLQVEEKTEEVGEGRVKRGPSQTTEPQSLVQLEDTSLTQLEATSLPLSGVTSELPPTISLPLLNNNLEPCSVTINPLPSPLPPTPPPPPPPPPPPPPPPLPVAKDSGPETLEKDLPRKEGNEKRIPKSASAPSAHLFDSSQLVSARKKLRKTAEGLQRRRVSSPMDEVLASLKRGSFHLKKVEQRTLPPFPDEDDSNNILAQIRKGVKLKKVQKDVLRESFTLLPDTDPLTRSIHEALRRIKEASPESEDEEEALPCTDWEN
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
2Phosphorylation------MSFALEETL
------CCCCCHHHH		21.1628348404
56PhosphorylationRTAQRQRSGSREQAG
HHHHCHHCCCHHHHH		32.55-
58PhosphorylationAQRQRSGSREQAGAR
HHCHHCCCHHHHHHC		33.61-
65MethylationSREQAGARGGAEAGG
CHHHHHHCCCCCCCC		43.06115387713
83PhosphorylationDGSRGPGSPAGRGRP
CCCCCCCCCCCCCCC		18.0823532336
87MethylationGPGSPAGRGRPEATA
CCCCCCCCCCCCCCC		39.80115480745
89MethylationGSPAGRGRPEATASA
CCCCCCCCCCCCCEE		25.23115480751
93PhosphorylationGRGRPEATASATLVR
CCCCCCCCCEEEEEE		21.3430576142
95PhosphorylationGRPEATASATLVRSP
CCCCCCCEEEEEECC		19.8930576142
101PhosphorylationASATLVRSPGPRRSS
CEEEEEECCCCCCCC		27.0826074081
107PhosphorylationRSPGPRRSSAWAEGG
ECCCCCCCCCCCCCC		26.2023403867
108PhosphorylationSPGPRRSSAWAEGGS
CCCCCCCCCCCCCCC		26.4723403867
115PhosphorylationSAWAEGGSPRSTRSL
CCCCCCCCCCCHHHH		28.1723401153
118PhosphorylationAEGGSPRSTRSLLGD
CCCCCCCCHHHHHCC		31.4026074081
119PhosphorylationEGGSPRSTRSLLGDP
CCCCCCCHHHHHCCC		26.0926074081
121PhosphorylationGSPRSTRSLLGDPRL
CCCCCHHHHHCCCCC		28.2123401153
130PhosphorylationLGDPRLRSPGSKGAE
HCCCCCCCCCCCCHH		37.9023403867
133PhosphorylationPRLRSPGSKGAESRL
CCCCCCCCCCHHHHC		31.1623403867
142PhosphorylationGAESRLRSPVRAKPI
CHHHHCCCCCCCCCC		32.1325159151
155PhosphorylationPIPGQKTSEADDAAG
CCCCCCCCCHHHHHH		37.5128555341
319PhosphorylationETDDPEEYYESLSEL
CCCCHHHHHHHHHHH		15.7528796482
320PhosphorylationTDDPEEYYESLSELR
CCCHHHHHHHHHHHH		11.4328796482
322PhosphorylationDPEEYYESLSELRQK
CHHHHHHHHHHHHHC		22.5228796482
324PhosphorylationEEYYESLSELRQKGY
HHHHHHHHHHHHCCH		43.8128796482
329UbiquitinationSLSELRQKGYEEVLQ
HHHHHHHCCHHHHHH		57.9624816145
348UbiquitinationRIQELLDKHKNTESM
HHHHHHHHCCCCHHH		57.3529967540
409PhosphorylationKISMENDYLGPRRIE
HHHCCCCCCCHHHHH		25.7425159151
420UbiquitinationRRIESLQKEDADWQR
HHHHHHHHCCCHHHH		63.9629967540
427MethylationKEDADWQRKAHMAVL
HCCCHHHHHHHHHHH		33.6024377421
427DimethylationKEDADWQRKAHMAVL
HCCCHHHHHHHHHHH		33.60-
467UbiquitinationADQKKFGKASWAAAA
HHHHHHCHHHHHHHH		42.24-
479UbiquitinationAAAERMEKLQYAVSK
HHHHHHHHHHHHHCH		31.3929967540
495UbiquitinationTLQMMRAKEICLEQR
HHHHHHHHHHHHHHH		36.9329967540
530PhosphorylationLDQLEADYYDLQLQL
HHHHHCHHHHHHHHH		13.1124043423
531PhosphorylationDQLEADYYDLQLQLY
HHHHCHHHHHHHHHH		15.6624043423
538PhosphorylationYDLQLQLYEVQFEIL
HHHHHHHHHHHHHHH		10.9024043423
560UbiquitinationTAQLESIKRLISEKR
HHHHHHHHHHHHCCC		50.8929967540
564PhosphorylationESIKRLISEKRDEVV
HHHHHHHHCCCCCEE		41.4824719451
572PhosphorylationEKRDEVVYYDTYESM
CCCCCEEEEECHHHH		10.78-
576PhosphorylationEVVYYDTYESMEAML
CEEEEECHHHHHHHH		11.78-
601UbiquitinationLQREELQKLQQKARQ
HCHHHHHHHHHHHHH		61.9729967540
648PhosphorylationRTRIEDEYRTHHTVQ
HHHCHHHHHHHHHHH		32.8827642862
657UbiquitinationTHHTVQLKREKLHDE
HHHHHHHHHHHCCCH		41.2329967540
668UbiquitinationLHDEEERKSAWVSQE
CCCHHHHHHHHHHHH		48.0529967540
713PhosphorylationARRKGAASPVLQEDH
HHHCCCCCCCCCCHH		18.2729255136
723PhosphorylationLQEDHCDSLPSVLQV
CCCHHCCCCCCEEEE		47.8022167270
726PhosphorylationDHCDSLPSVLQVEEK
HHCCCCCCEEEEECC		40.5325850435
734PhosphorylationVLQVEEKTEEVGEGR
EEEEECCCCCCCCCC		40.4323312004
832O-linked_GlycosylationPLPVAKDSGPETLEK
CCCCCCCCCCCCHHH		56.3830379171
854PhosphorylationNEKRIPKSASAPSAH
CCCCCCCCCCCCCCC		23.3128857561
856PhosphorylationKRIPKSASAPSAHLF
CCCCCCCCCCCCCCC		48.0528857561
859PhosphorylationPKSASAPSAHLFDSS
CCCCCCCCCCCCCHH		28.2128464451
865PhosphorylationPSAHLFDSSQLVSAR
CCCCCCCHHHHHHHH		16.7923186163
866PhosphorylationSAHLFDSSQLVSARK
CCCCCCHHHHHHHHH		29.4023312004
870PhosphorylationFDSSQLVSARKKLRK
CCHHHHHHHHHHHHH		30.8325159151
888PhosphorylationGLQRRRVSSPMDEVL
HHHHHHCCCCHHHHH		27.2325159151
889PhosphorylationLQRRRVSSPMDEVLA
HHHHHCCCCHHHHHH		22.7623927012
897PhosphorylationPMDEVLASLKRGSFH
CHHHHHHHHHHCCEE		30.2022912867
902PhosphorylationLASLKRGSFHLKKVE
HHHHHHCCEEEEEEH		17.3326546556
946PhosphorylationQKDVLRESFTLLPDT
HHHHHHHHHCCCCCC		19.6625159151
948PhosphorylationDVLRESFTLLPDTDP
HHHHHHHCCCCCCCH		36.3427251275
957PhosphorylationLPDTDPLTRSIHEAL
CCCCCHHHHHHHHHH		27.97-
959PhosphorylationDTDPLTRSIHEALRR
CCCHHHHHHHHHHHH		24.06-
971PhosphorylationLRRIKEASPESEDEE
HHHHHHHCCCCCCHH		30.2328102081
974PhosphorylationIKEASPESEDEEEAL
HHHHCCCCCCHHHHC		54.4522617229
984PhosphorylationEEEALPCTDWEN---
HHHHCCCCCCCC---		42.0522210691
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
-KUbiquitinationE3 ubiquitin ligaseMDM2Q00987
PMID:17170761
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115 AND SER-974, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-974, AND MASSSPECTROMETRY.

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