RBM23_HUMAN - dbPTM
RBM23_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBM23_HUMAN
UniProt AC Q86U06
Protein Name Probable RNA-binding protein 23
Gene Name RBM23
Organism Homo sapiens (Human).
Sequence Length 439
Subcellular Localization Nucleus .
Protein Description Probable RNA-binding protein. May be involved in pre-mRNA splicing process..
Protein Sequence MASDDFDIVIEAMLEAPYKKEEDEQQRKEVKKDYPSNTTSSTSNSGNETSGSSTIGETSKKKRSRSHNKSRDRKRSRSRDRDRYRRRNSRSRSPGRQCRHRSRSWDRRHGSESRSRDHRREDRVHYRSPPLATGYRYGHSKSPHFREKSPVREPVDNLSPEERDARTVFCMQLAARIRPRDLEDFFSAVGKVRDVRIISDRNSRRSKGIAYVEFCEIQSVPLAIGLTGQRLLGVPIIVQASQAEKNRLAAMANNLQKGNGGPMRLYVGSLHFNITEDMLRGIFEPFGKIDNIVLMKDSDTGRSKGYGFITFSDSECARRALEQLNGFELAGRPMRVGHVTERLDGGTDITFPDGDQELDLGSAGGRFQLMAKLAEGAGIQLPSTAAAAAAAAAQAAALQLNGAVPLGALNPAALTALSPALNLASQCFQLSSLFTPQTM
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
19SumoylationAMLEAPYKKEEDEQQ
HHHHCCCCCHHHHHH		53.28-
34PhosphorylationRKEVKKDYPSNTTSS
HHHHHHHCCCCCCCC		19.90-
36PhosphorylationEVKKDYPSNTTSSTS
HHHHHCCCCCCCCCC		40.35-
40PhosphorylationDYPSNTTSSTSNSGN
HCCCCCCCCCCCCCC		29.58-
50PhosphorylationSNSGNETSGSSTIGE
CCCCCCCCCCCCCCC		30.42-
50 (in isoform 4)Phosphorylation-30.42-
50 (in isoform 2)Phosphorylation-30.42-
52 (in isoform 2)Phosphorylation-24.87-
52PhosphorylationSGNETSGSSTIGETS
CCCCCCCCCCCCCCC		24.87-
52 (in isoform 4)Phosphorylation-24.87-
53 (in isoform 2)Phosphorylation-27.80-
53PhosphorylationGNETSGSSTIGETSK
CCCCCCCCCCCCCCC		27.80-
53 (in isoform 4)Phosphorylation-27.80-
62 (in isoform 2)Phosphorylation-60.38-
62 (in isoform 4)Phosphorylation-60.38-
76PhosphorylationKSRDRKRSRSRDRDR
HHHHHHHHHHHHHHH		37.3320068231
78PhosphorylationRDRKRSRSRDRDRYR
HHHHHHHHHHHHHHH		39.5220068231
89PhosphorylationDRYRRRNSRSRSPGR
HHHHHHHHCCCCCCC		29.8030576142
91PhosphorylationYRRRNSRSRSPGRQC
HHHHHHCCCCCCCCC		36.6130576142
93PhosphorylationRRNSRSRSPGRQCRH
HHHHCCCCCCCCCCC		32.7130576142
102PhosphorylationGRQCRHRSRSWDRRH
CCCCCCCCCCCHHHC		25.2529449344
104PhosphorylationQCRHRSRSWDRRHGS
CCCCCCCCCHHHCCC		34.2829449344
112 (in isoform 4)Phosphorylation-55.5527050516
113PhosphorylationDRRHGSESRSRDHRR
HHHCCCCCCCCCCCC		36.93-
126PhosphorylationRREDRVHYRSPPLAT
CCCCCCCCCCCCCCC		15.2123927012
128PhosphorylationEDRVHYRSPPLATGY
CCCCCCCCCCCCCCC		24.5723927012
133PhosphorylationYRSPPLATGYRYGHS
CCCCCCCCCCCCCCC		42.2923403867
135PhosphorylationSPPLATGYRYGHSKS
CCCCCCCCCCCCCCC		9.0523403867
137PhosphorylationPLATGYRYGHSKSPH
CCCCCCCCCCCCCCC		15.6530177828
140PhosphorylationTGYRYGHSKSPHFRE
CCCCCCCCCCCCCCC		30.3926055452
142PhosphorylationYRYGHSKSPHFREKS
CCCCCCCCCCCCCCC		26.9926055452
149PhosphorylationSPHFREKSPVREPVD
CCCCCCCCCCCCCCC		24.7129255136
157 (in isoform 4)Ubiquitination-42.5221890473
159PhosphorylationREPVDNLSPEERDAR
CCCCCCCCHHHHHHH		36.2023927012
167PhosphorylationPEERDARTVFCMQLA
HHHHHHHHHHHHHHH		21.4720068231
169 (in isoform 5)Ubiquitination-2.5821890473
170GlutathionylationRDARTVFCMQLAARI
HHHHHHHHHHHHHHC		1.1522555962
175 (in isoform 2)Ubiquitination-18.9421890473
191UbiquitinationDFFSAVGKVRDVRII
HHHHHHCCEEEEEEE		27.7421890473
191 (in isoform 1)Ubiquitination-27.7421890473
191 (in isoform 3)Ubiquitination-27.7421890473
199PhosphorylationVRDVRIISDRNSRRS
EEEEEEEECCCCCCC		28.31-
219PhosphorylationVEFCEIQSVPLAIGL
EEEEECCCCCEEEEC		31.22-
241PhosphorylationVPIIVQASQAEKNRL
CCEEEECHHHHHHHH		16.90-
245UbiquitinationVQASQAEKNRLAAMA
EECHHHHHHHHHHHH		50.84-
257UbiquitinationAMANNLQKGNGGPMR
HHHHHHHCCCCCCCE		58.47-
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 RBM23_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBM23_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 RBM23_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TBA4A_HUMANTUBA4Aphysical
16169070
TF3C1_HUMANGTF3C1physical
16169070
DPOA2_HUMANPOLA2physical
16169070
PTN_HUMANPTNphysical
16169070
RFA1_HUMANRPA1physical
16169070
MED31_HUMANMED31physical
16169070
CE126_HUMANKIAA1377physical
16169070
ESR1_HUMANESR1physical
15694343
PRGR_HUMANPGRphysical
15694343
RBM25_HUMANRBM25physical
22365833
CHERP_HUMANCHERPphysical
22365833
RBM39_HUMANRBM39physical
22365833
RBM4_HUMANRBM4physical
22365833
ANM5_HUMANPRMT5physical
22365833
QKI_HUMANQKIphysical
22365833
RFOX2_HUMANRBFOX2physical
22365833
SRPK2_HUMANSRPK2physical
22365833
ANM5_HUMANPRMT5physical
23455924
FAM9B_HUMANFAM9Bphysical
25416956
LRRC1_HUMANLRRC1physical
26186194
SCRIB_HUMANSCRIBphysical
26186194
RRP44_HUMANDIS3physical
26186194
ANKH1_HUMANANKHD1physical
26186194
ANR17_HUMANANKRD17physical
26186194
ACOT2_HUMANACOT2physical
26186194
NAA10_HUMANNAA10physical
26186194
DBNL_HUMANDBNLphysical
26186194
SAHH3_HUMANAHCYL2physical
26186194
ZN579_HUMANZNF579physical
26186194
SCRIB_HUMANSCRIBphysical
28514442
RRP44_HUMANDIS3physical
28514442
SAHH3_HUMANAHCYL2physical
28514442
DBNL_HUMANDBNLphysical
28514442
ZN579_HUMANZNF579physical
28514442
NAA10_HUMANNAA10physical
28514442
ANKH1_HUMANANKHD1physical
28514442
LRRC1_HUMANLRRC1physical
28514442
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 RBM23_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-149, AND MASSSPECTROMETRY.

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