RBM28_HUMAN - dbPTM
RBM28_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBM28_HUMAN
UniProt AC Q9NW13
Protein Name RNA-binding protein 28
Gene Name RBM28
Organism Homo sapiens (Human).
Sequence Length 759
Subcellular Localization Nucleus, nucleolus .
Protein Description Nucleolar component of the spliceosomal ribonucleoprotein complexes..
Protein Sequence MAGLTLFVGRLPPSARSEQLEELFSQVGPVKQCFVVTEKGSKACRGFGYVTFSMLEDVQRALKEITTFEGCKINVTVAKKKLRNKTKEKGKNENSECPKKEPKAKKAKVADKKARLIIRNLSFKCSEDDLKTVFAQFGAVLEVNIPRKPDGKMRGFGFVQFKNLLEAGKALKGMNMKEIKGRTVAVDWAVAKDKYKDTQSVSAIGEEKSHESKHQESVKKKGREEEDMEEEENDDDDDDDDEEDGVFDDEDEEEENIESKVTKPVQIQKRAVKRPAPAKSSDHSEEDSDLEESDSIDDGEELAQSDTSTEEQEDKAVQVSNKKKRKLPSDVNEGKTVFIRNLSFDSEEEELGELLQQFGELKYVRIVLHPDTEHSKGCAFAQFMTQEAAQKCLLAASPENEAGGLKLDGRQLKVDLAVTRDEAAKLQTTKVKKPTGTRNLYLAREGLIRAGTKAAEGVSAADMAKRERFELLKHQKLKDQNIFVSRTRLCLHNLPKAVDDKQLRKLLLSATSGEKGVRIKECRVMRDLKGVHGNMKGQSLGYAFAEFQEHEHALKALRLINNNPEIFGPLKRPIVEFSLEDRRKLKMKELRIQRSLQKMRSKPATGEPQKGQPEPAKDQQQKAAQHHTEEQSKVPPEQKRKAGSTSWTGFQTKAEVEQVELPDGKKRRKVLALPSHRGPKIRLRDKGKVKPVHPKKPKPQINQWKQEKQQLSSEQVSRKKAKGNKTETRFNQLVEQYKQKLLGPSKGAPLAKRSKWFDS
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
2Acetylation------MAGLTLFVG
------CCCCEEEEE		23.00-
39UbiquitinationQCFVVTEKGSKACRG
EEEEEEECCCHHCCC		60.15-
39AcetylationQCFVVTEKGSKACRG
EEEEEEECCCHHCCC		60.1526051181
66PhosphorylationQRALKEITTFEGCKI
HHHHHHCCCCCCCCE		26.9023401153
792-HydroxyisobutyrylationKINVTVAKKKLRNKT
CEEEEHHHHHHHHHH		46.21-
79AcetylationKINVTVAKKKLRNKT
CEEEEHHHHHHHHHH		46.2125953088
95PhosphorylationEKGKNENSECPKKEP
HCCCCCCCCCCCCCC		34.10-
122PhosphorylationRLIIRNLSFKCSEDD
HHHHHCCCCCCCHHH		26.6321712546
124AcetylationIIRNLSFKCSEDDLK
HHHCCCCCCCHHHHH		33.2126051181
132PhosphorylationCSEDDLKTVFAQFGA
CCHHHHHHHHHHHCC		28.3120068231
147MethylationVLEVNIPRKPDGKMR
EEEEECCCCCCCCCC		60.3824381713
154MethylationRKPDGKMRGFGFVQF
CCCCCCCCCEEEEEH		40.5524381721
162UbiquitinationGFGFVQFKNLLEAGK
CEEEEEHHHHHHHHH		29.60-
162AcetylationGFGFVQFKNLLEAGK
CEEEEEHHHHHHHHH		29.6026051181
172UbiquitinationLEAGKALKGMNMKEI
HHHHHHHCCCCHHHH		62.06-
195PhosphorylationWAVAKDKYKDTQSVS
HHHHHHHCCCCCCCH		24.9923186163
1962-HydroxyisobutyrylationAVAKDKYKDTQSVSA
HHHHHHCCCCCCCHH		61.10-
198PhosphorylationAKDKYKDTQSVSAIG
HHHHCCCCCCCHHHC		20.7025850435
200PhosphorylationDKYKDTQSVSAIGEE
HHCCCCCCCHHHCCH		21.8225850435
202PhosphorylationYKDTQSVSAIGEEKS
CCCCCCCHHHCCHHC		21.2925159151
263AcetylationNIESKVTKPVQIQKR
CHHHCCCCCHHHHHH		46.2926051181
280PhosphorylationKRPAPAKSSDHSEED
CCCCCCCCCCCCCCC		43.0024144214
281PhosphorylationRPAPAKSSDHSEEDS
CCCCCCCCCCCCCCC		38.3424144214
284PhosphorylationPAKSSDHSEEDSDLE
CCCCCCCCCCCCCCC		47.9024144214
288PhosphorylationSDHSEEDSDLEESDS
CCCCCCCCCCCCCCC		47.5830576142
293PhosphorylationEDSDLEESDSIDDGE
CCCCCCCCCCCCCHH		27.5530576142
295PhosphorylationSDLEESDSIDDGEEL
CCCCCCCCCCCHHHH		36.8830576142
305PhosphorylationDGEELAQSDTSTEEQ
CHHHHHHCCCCCHHH		36.9318452278
307PhosphorylationEELAQSDTSTEEQED
HHHHHCCCCCHHHHH		42.6818452278
308PhosphorylationELAQSDTSTEEQEDK
HHHHCCCCCHHHHHH		38.5224461736
329PhosphorylationKKKRKLPSDVNEGKT
CCCCCCCCCCCCCCE		65.7028555341
343PhosphorylationTVFIRNLSFDSEEEE
EEEEEECCCCCCHHH		30.4728464451
346PhosphorylationIRNLSFDSEEEELGE
EEECCCCCCHHHHHH		44.9228464451
376AcetylationHPDTEHSKGCAFAQF
CCCCCCCCCCHHHHH		60.9726051181
397PhosphorylationQKCLLAASPENEAGG
HHHHHHCCCCCCCCC		27.4328112733
406AcetylationENEAGGLKLDGRQLK
CCCCCCEEECCCEEE		48.0526051181
419PhosphorylationLKVDLAVTRDEAAKL
EEEEEEECHHHHHHH		27.1320068231
459PhosphorylationTKAAEGVSAADMAKR
CHHHCCCCHHHHHHH		28.70-
4652-HydroxyisobutyrylationVSAADMAKRERFELL
CCHHHHHHHHHHHHH		48.42-
473MethylationRERFELLKHQKLKDQ
HHHHHHHHHCCCCCC		57.52115976435
478MalonylationLLKHQKLKDQNIFVS
HHHHCCCCCCCEEEC		65.3926320211
496AcetylationLCLHNLPKAVDDKQL
HHHHCCCCCCCHHHH		65.3026051181
509PhosphorylationQLRKLLLSATSGEKG
HHHHHHHHCCCCCCC		29.4820068231
511PhosphorylationRKLLLSATSGEKGVR
HHHHHHCCCCCCCCE		33.6120068231
512PhosphorylationKLLLSATSGEKGVRI
HHHHHCCCCCCCCEE		44.6725627689
515AcetylationLSATSGEKGVRIKEC
HHCCCCCCCCEEEEE		67.2525953088
5712-HydroxyisobutyrylationPEIFGPLKRPIVEFS
CCCCCCCCCCEEECC		60.30-
595PhosphorylationKELRIQRSLQKMRSK
HHHHHHHHHHHHHCC		20.8327134283
622AcetylationPAKDQQQKAAQHHTE
CCHHHHHHHHHHHCH		41.1520167786
639AcetylationSKVPPEQKRKAGSTS
HCCCHHHHCCCCCCC		54.9620167786
644PhosphorylationEQKRKAGSTSWTGFQ
HHHCCCCCCCCCCCC		24.9125159151
645PhosphorylationQKRKAGSTSWTGFQT
HHCCCCCCCCCCCCC		27.6325627689
646PhosphorylationKRKAGSTSWTGFQTK
HCCCCCCCCCCCCCC		25.0825159151
653SumoylationSWTGFQTKAEVEQVE
CCCCCCCCEEEEEEE		31.5928112733
6652-HydroxyisobutyrylationQVELPDGKKRRKVLA
EEECCCCCCEEEEEE		50.95-
665AcetylationQVELPDGKKRRKVLA
EEECCCCCCEEEEEE		50.9526051181
675PhosphorylationRKVLALPSHRGPKIR
EEEEECCCCCCCCEE		27.0228555341
705SumoylationKPQINQWKQEKQQLS
CCCHHHHHHHHHHHC		38.52-
705MethylationKPQINQWKQEKQQLS
CCCHHHHHHHHHHHC		38.52110873973
705SumoylationKPQINQWKQEKQQLS
CCCHHHHHHHHHHHC		38.52-
708UbiquitinationINQWKQEKQQLSSEQ
HHHHHHHHHHHCHHH		40.63-
712PhosphorylationKQEKQQLSSEQVSRK
HHHHHHHCHHHHHHH		27.7329743597
713PhosphorylationQEKQQLSSEQVSRKK
HHHHHHCHHHHHHHH		40.4129255136
717PhosphorylationQLSSEQVSRKKAKGN
HHCHHHHHHHHHCCC		37.7729255136
738UbiquitinationNQLVEQYKQKLLGPS
HHHHHHHHHHHHCCC		40.42-
745PhosphorylationKQKLLGPSKGAPLAK
HHHHHCCCCCCCHHH		41.7629396449
746MalonylationQKLLGPSKGAPLAKR
HHHHCCCCCCCHHHH		63.3332601280
755MethylationAPLAKRSKWFDS---
CCHHHHCCCCCC---		56.78115976447
759PhosphorylationKRSKWFDS-------
HHCCCCCC-------		32.4221712546
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 RBM28_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBM28_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 RBM28_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RL5_HUMANRPL5physical
22939629
RS17_HUMANRPS17physical
22939629
RRP12_HUMANRRP12physical
22939629
RPC6_HUMANPOLR3Fphysical
22939629
RPC7_HUMANPOLR3Gphysical
22939629
ZN622_HUMANZNF622physical
22939629
NOP2_HUMANNOP2physical
26344197
PESC_HUMANPES1physical
26344197
SDA1_HUMANSDAD1physical
26344197
TOP1_HUMANTOP1physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612079Alopecia, neurologic defects, and endocrinopathy syndrome (ANES)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RBM28_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-122, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND MASSSPECTROMETRY.

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