RBM19_HUMAN - dbPTM
RBM19_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBM19_HUMAN
UniProt AC Q9Y4C8
Protein Name Probable RNA-binding protein 19
Gene Name RBM19
Organism Homo sapiens (Human).
Sequence Length 960
Subcellular Localization Nucleus, nucleolus . Nucleus, nucleoplasm. Cytoplasm. Chromosome. In discrete foci distributed throughout the cytoplasm and nucleoplasm during the 4 to 8 cell stages and the morula stage, but not in the periphery of the nucleolar precursor body (NPB)
Protein Description Plays a role in embryo pre-implantation development..
Protein Sequence MSRLIVKNLPNGMKEERFRQLFAAFGTLTDCSLKFTKDGKFRKFGFIGFKSEEEAQKAQKHFNKSFIDTSRITVEFCKSFGDPAKPRAWSKHAQKPSQPKQPPKDSTTPEIKKDEKKKKVAGQLEKLKEDTEFQEFLSVHQRRAQAATWANDGLDAEPSKGKSKPASDYLNFDSDSGQESEEEGAGEDLEEEASLEPKAAVQKELSDMDYLKSKMVKAGSSSSSEEEESEDEAVHCDEGSEAEEEDSSATPVLQERDSKGAGQEQGMPAGKKRPPEARAETEKPANQKEPTTCHTVKLRGAPFNVTEKNVMEFLAPLKPVAIRIVRNAHGNKTGYIFVDFSNEEEVKQALKCNREYMGGRYIEVFREKNVPTTKGAPKNTTKSWQGRILGENEEEEDLAESGRLFVRNLPYTSTEEDLEKLFSKYGPLSELHYPIDSLTKKPKGFAFITFMFPEHAVKAYSEVDGQVFQGRMLHVLPSTIKKEASEDASALGSSSYKKKKEAQDKANSASSHNWNTLFMGPNAVADAIAQKYNATKSQVFDHETKGSVAVRVALGETQLVQEVRRFLIDNGVSLDSFSQAAAERSKTVILVKNLPAGTLAAQLQETFGHFGSLGRVLLPEGGITAIVEFLEPLEARKAFRHLAYSKFHHVPLYLEWAPVGVFSSTAPQKKKLQDTPSEPMEKDPAEPETVPDGETPEDENPTEEGADNSSAKMEEEEEEEEEEEESLPGCTLFIKNLNFDTTEEKLKEVFSKVGTVKSCSISKKKNKAGVLLSMGFGFVEYRKPEQAQKALKQLQGHVVDGHKLEVRISERATKPAVTLARKKQVPRKQTTSKILVRNIPFQAHSREIRELFSTFGELKTVRLPKKMTGTGTHRGFGFVDFLTKQDAKRAFNALCHSTHLYGRRLVLEWADSEVTLQALRRKTAAHFHEPPKKKRSVVLDEILEQLEGSDSDSEEQTLQL
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
27PhosphorylationQLFAAFGTLTDCSLK
HHHHHHCCCCCCCEE		21.7422210691
29PhosphorylationFAAFGTLTDCSLKFT
HHHHCCCCCCCEEEC		34.4922210691
65PhosphorylationAQKHFNKSFIDTSRI
HHHHHCHHHHCCHHC		28.6527251275
69PhosphorylationFNKSFIDTSRITVEF
HCHHHHCCHHCHHHH		18.3227251275
70PhosphorylationNKSFIDTSRITVEFC
CHHHHCCHHCHHHHH		20.2427251275
85AcetylationKSFGDPAKPRAWSKH
HHHCCCCCCCHHHHC		40.1923954790
106PhosphorylationPKQPPKDSTTPEIKK
CCCCCCCCCCCCCCH		40.0628102081
107PhosphorylationKQPPKDSTTPEIKKD
CCCCCCCCCCCCCHH		57.4125159151
108PhosphorylationQPPKDSTTPEIKKDE
CCCCCCCCCCCCHHH		23.9121815630
126UbiquitinationKVAGQLEKLKEDTEF
HHHHHHHHHHCCHHH		73.7327667366
160AcetylationGLDAEPSKGKSKPAS
CCCCCCCCCCCCCHH		79.6126051181
160UbiquitinationGLDAEPSKGKSKPAS
CCCCCCCCCCCCCHH		79.6133845483
163PhosphorylationAEPSKGKSKPASDYL
CCCCCCCCCCHHHCC		53.1725137130
167PhosphorylationKGKSKPASDYLNFDS
CCCCCCHHHCCCCCC		35.0025137130
169PhosphorylationKSKPASDYLNFDSDS
CCCCHHHCCCCCCCC		10.8925137130
174PhosphorylationSDYLNFDSDSGQESE
HHCCCCCCCCCCCCC		29.5526503892
176PhosphorylationYLNFDSDSGQESEEE
CCCCCCCCCCCCCCC		46.4526503892
180PhosphorylationDSDSGQESEEEGAGE
CCCCCCCCCCCCCCC		42.2826503892
194PhosphorylationEDLEEEASLEPKAAV
CCHHHHHCCCHHHHH		36.2226552605
203AcetylationEPKAAVQKELSDMDY
CHHHHHHHHHCCHHH		54.7626051181
206PhosphorylationAAVQKELSDMDYLKS
HHHHHHHCCHHHHHH		31.79-
220PhosphorylationSKMVKAGSSSSSEEE
HHHHHCCCCCCCCCC		31.7225137130
221PhosphorylationKMVKAGSSSSSEEEE
HHHHCCCCCCCCCCC		33.0625137130
222PhosphorylationMVKAGSSSSSEEEES
HHHCCCCCCCCCCCC		39.3125137130
223PhosphorylationVKAGSSSSSEEEESE
HHCCCCCCCCCCCCC		43.6525137130
224PhosphorylationKAGSSSSSEEEESED
HCCCCCCCCCCCCCC		51.4825137130
229PhosphorylationSSSEEEESEDEAVHC
CCCCCCCCCCCCCCC		54.3425137130
240PhosphorylationAVHCDEGSEAEEEDS
CCCCCCCCCCCCCCC		31.4225137130
271AcetylationEQGMPAGKKRPPEAR
CCCCCCCCCCCHHHH		47.9526051181
288UbiquitinationTEKPANQKEPTTCHT
CCCCCCCCCCCCCEE		66.5224816145
356PhosphorylationALKCNREYMGGRYIE
HHHCCHHHHCCCEEE		9.60-
382UbiquitinationGAPKNTTKSWQGRIL
CCCCCCCCCCCCCCC		47.8929967540
414PhosphorylationRNLPYTSTEEDLEKL
ECCCCCCCHHHHHHH		35.2827067055
420UbiquitinationSTEEDLEKLFSKYGP
CCHHHHHHHHHHHCC		63.2329967540
423PhosphorylationEDLEKLFSKYGPLSE
HHHHHHHHHHCCHHH		35.0924719451
425PhosphorylationLEKLFSKYGPLSELH
HHHHHHHHCCHHHCC		23.83-
433PhosphorylationGPLSELHYPIDSLTK
CCHHHCCCCHHHCCC		17.95-
441UbiquitinationPIDSLTKKPKGFAFI
CHHHCCCCCCCEEEE		46.8833845483
443UbiquitinationDSLTKKPKGFAFITF
HHCCCCCCCEEEEEE		75.4533845483
479PhosphorylationMLHVLPSTIKKEASE
EEEECHHHHCHHHCC		34.57-
481SumoylationHVLPSTIKKEASEDA
EECHHHHCHHHCCCH		44.6528112733
485PhosphorylationSTIKKEASEDASALG
HHHCHHHCCCHHHHC		36.7823401153
489PhosphorylationKEASEDASALGSSSY
HHHCCCHHHHCCHHH		36.0323401153
493PhosphorylationEDASALGSSSYKKKK
CCHHHHCCHHHHHHH		19.5723401153
494PhosphorylationDASALGSSSYKKKKE
CHHHHCCHHHHHHHH		35.5723401153
495PhosphorylationASALGSSSYKKKKEA
HHHHCCHHHHHHHHH		42.5423401153
496PhosphorylationSALGSSSYKKKKEAQ
HHHCCHHHHHHHHHH		28.8623401153
536MethylationAQKYNATKSQVFDHE
HHHHCCCHHHCCCCC		36.16115976375
544PhosphorylationSQVFDHETKGSVAVR
HHCCCCCCCCCEEHH		36.9728555341
547PhosphorylationFDHETKGSVAVRVAL
CCCCCCCCEEHHHHC		14.4128555341
557PhosphorylationVRVALGETQLVQEVR
HHHHCCCCHHHHHHH		25.9624719451
606PhosphorylationLAAQLQETFGHFGSL
HHHHHHHHHCCCCCH		23.19-
675PhosphorylationQKKKLQDTPSEPMEK
CCCCCCCCCCCCCCC		18.7621815630
677PhosphorylationKKLQDTPSEPMEKDP
CCCCCCCCCCCCCCC		57.32-
695PhosphorylationETVPDGETPEDENPT
CCCCCCCCCCCCCCC		37.1925850435
702PhosphorylationTPEDENPTEEGADNS
CCCCCCCCCCCCCCC		59.2425002506
709PhosphorylationTEEGADNSSAKMEEE
CCCCCCCCCCCCHHH		32.0225850435
710PhosphorylationEEGADNSSAKMEEEE
CCCCCCCCCCCHHHH		37.8625850435
741PhosphorylationIKNLNFDTTEEKLKE
EECCCCCCCHHHHHH		31.78-
752AcetylationKLKEVFSKVGTVKSC
HHHHHHHHHCCEEEC		32.9726051181
752UbiquitinationKLKEVFSKVGTVKSC
HHHHHHHHHCCEEEC		32.97-
813PhosphorylationVRISERATKPAVTLA
EEEECCCCCCCCHHH		43.7221406692
818PhosphorylationRATKPAVTLARKKQV
CCCCCCCHHHHHCCC		19.4621406692
830PhosphorylationKQVPRKQTTSKILVR
CCCCCCCCCCCCHHH		35.7520068231
831PhosphorylationQVPRKQTTSKILVRN
CCCCCCCCCCCHHHC		26.0620068231
832PhosphorylationVPRKQTTSKILVRNI
CCCCCCCCCCHHHCC		22.5320068231
845PhosphorylationNIPFQAHSREIRELF
CCCHHHCHHHHHHHH		34.32-
860PhosphorylationSTFGELKTVRLPKKM
HHHCCEEEEECCCCC		24.3920164059
872PhosphorylationKKMTGTGTHRGFGFV
CCCCCCCCCCCCCHH		14.29-
884UbiquitinationGFVDFLTKQDAKRAF
CHHHCCCHHHHHHHH		48.61-
888AcetylationFLTKQDAKRAFNALC
CCCHHHHHHHHHHHH		53.187481227
936PhosphorylationEPPKKKRSVVLDEIL
CCCCCCCCHHHHHHH		26.0028450419
949PhosphorylationILEQLEGSDSDSEEQ
HHHHHCCCCCCCHHH		25.2717081983
951PhosphorylationEQLEGSDSDSEEQTL
HHHCCCCCCCHHHHC		44.7411230166
953PhosphorylationLEGSDSDSEEQTLQL
HCCCCCCCHHHHCCC		47.1617081983
957PhosphorylationDSDSEEQTLQL----
CCCCHHHHCCC----		21.5425137130
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 RBM19_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBM19_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 RBM19_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPB1_HUMANFTSJ3physical
22939629
TSR1_HUMANTSR1physical
26344197
UTP15_HUMANUTP15physical
26344197
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 RBM19_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-174; SER-176 ANDSER-180, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-949; SER-951 ANDTHR-957, AND MASS SPECTROMETRY.

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