RBM22_HUMAN - dbPTM
RBM22_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBM22_HUMAN
UniProt AC Q9NW64
Protein Name Pre-mRNA-splicing factor RBM22
Gene Name RBM22
Organism Homo sapiens (Human).
Sequence Length 420
Subcellular Localization Nucleus. Cytoplasm. Mainly located in the nucleus. Translocated from the nucleus to the cytoplasm after heat shock cell treatment. May be shuttling between the nucleus and the cytosol.
Protein Description Involved in the first step of pre-mRNA splicing. Binds directly to the internal stem-loop (ISL) domain of the U6 snRNA and to the pre-mRNA intron near the 5' splice site during the activation and catalytic phases of the spliceosome cycle. Involved in both translocations of the nuclear SLU7 to the cytoplasm and the cytosolic calcium-binding protein PDCD6 to the nucleus upon cellular stress responses..
Protein Sequence MATSLGSNTYNRQNWEDADFPILCQTCLGENPYIRMTKEKYGKECKICARPFTVFRWCPGVRMRFKKTEVCQTCSKLKNVCQTCLLDLEYGLPIQVRDAGLSFKDDMPKSDVNKEYYTQNMEREISNSDGTRPVGMLGKATSTSDMLLKLARTTPYYKRNRPHICSFWVKGECKRGEECPYRHEKPTDPDDPLADQNIKDRYYGINDPVADKLLKRASTMPRLDPPEDKTITTLYVGGLGDTITETDLRNHFYQFGEIRTITVVQRQQCAFIQFATRQAAEVAAEKSFNKLIVNGRRLNVKWGRSQAARGKEKEKDGTTDSGIKLEPVPGLPGALPPPPAAEEEASANYFNLPPSGPPAVVNIALPPPPGIAPPPPPGFGPHMFHPMGPPPPFMRAPGPIHYPSQDPQRMGAHAGKHSSP
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------MATSLGSNT
------CCCCCCCCC		13.0922223895
3Phosphorylation-----MATSLGSNTY
-----CCCCCCCCCC		24.1620068231
4Phosphorylation----MATSLGSNTYN
----CCCCCCCCCCC		22.6120068231
7Phosphorylation-MATSLGSNTYNRQN
-CCCCCCCCCCCCCC		31.1520873877
9PhosphorylationATSLGSNTYNRQNWE
CCCCCCCCCCCCCCC		24.7020068231
10PhosphorylationTSLGSNTYNRQNWED
CCCCCCCCCCCCCCC		16.7620068231
26PhosphorylationDFPILCQTCLGENPY
CCCCHHHHHCCCCCC		14.5422210691
33PhosphorylationTCLGENPYIRMTKEK
HHCCCCCCEEECHHH		16.85-
43UbiquitinationMTKEKYGKECKICAR
ECHHHHCCCCCCCCC		57.7724816145
65 (in isoform 2)Ubiquitination-7.5121890473
762-HydroxyisobutyrylationEVCQTCSKLKNVCQT
HHHHHHHHHHHHHHH		66.67-
76AcetylationEVCQTCSKLKNVCQT
HHHHHHHHHHHHHHH		66.6725953088
76UbiquitinationEVCQTCSKLKNVCQT
HHHHHHHHHHHHHHH		66.6733845483
78UbiquitinationCQTCSKLKNVCQTCL
HHHHHHHHHHHHHHH		51.5833845483
83PhosphorylationKLKNVCQTCLLDLEY
HHHHHHHHHHHHCCC		10.4526552605
90PhosphorylationTCLLDLEYGLPIQVR
HHHHHCCCCCCEEEE		31.1228796482
102PhosphorylationQVRDAGLSFKDDMPK
EEEECCCCCCCCCCH		29.3621815630
104UbiquitinationRDAGLSFKDDMPKSD
EECCCCCCCCCCHHH		49.8232015554
109SumoylationSFKDDMPKSDVNKEY
CCCCCCCHHHCCHHH		53.29-
109SumoylationSFKDDMPKSDVNKEY
CCCCCCCHHHCCHHH		53.29-
109UbiquitinationSFKDDMPKSDVNKEY
CCCCCCCHHHCCHHH		53.2922817900
110PhosphorylationFKDDMPKSDVNKEYY
CCCCCCHHHCCHHHH		40.7025348954
114UbiquitinationMPKSDVNKEYYTQNM
CCHHHCCHHHHHHHH		47.1122817900
114 (in isoform 1)Ubiquitination-47.1121890473
116PhosphorylationKSDVNKEYYTQNMER
HHHCCHHHHHHHHHH		17.2728796482
117PhosphorylationSDVNKEYYTQNMERE
HHCCHHHHHHHHHHH		11.7128796482
118PhosphorylationDVNKEYYTQNMEREI
HCCHHHHHHHHHHHH		16.7428796482
126PhosphorylationQNMEREISNSDGTRP
HHHHHHHCCCCCCCC		26.0620068231
126O-linked_GlycosylationQNMEREISNSDGTRP
HHHHHHHCCCCCCCC		26.0630379171
128PhosphorylationMEREISNSDGTRPVG
HHHHHCCCCCCCCCC		30.5420068231
131PhosphorylationEISNSDGTRPVGMLG
HHCCCCCCCCCCCCE		36.4720068231
136SulfoxidationDGTRPVGMLGKATST
CCCCCCCCCEEEECH		4.5521406390
139SumoylationRPVGMLGKATSTSDM
CCCCCCEEEECHHHH		44.5228112733
139UbiquitinationRPVGMLGKATSTSDM
CCCCCCEEEECHHHH		44.5229967540
139MethylationRPVGMLGKATSTSDM
CCCCCCEEEECHHHH		44.5230792361
141PhosphorylationVGMLGKATSTSDMLL
CCCCEEEECHHHHHH		35.7023403867
142PhosphorylationGMLGKATSTSDMLLK
CCCEEEECHHHHHHH		30.6723401153
143PhosphorylationMLGKATSTSDMLLKL
CCEEEECHHHHHHHH		25.1323898821
144PhosphorylationLGKATSTSDMLLKLA
CEEEECHHHHHHHHH		22.3123403867
149UbiquitinationSTSDMLLKLARTTPY
CHHHHHHHHHHCCCH		35.8232015554
149SumoylationSTSDMLLKLARTTPY
CHHHHHHHHHHCCCH		35.8225218447
149SumoylationSTSDMLLKLARTTPY
CHHHHHHHHHHCCCH		35.82-
149MethylationSTSDMLLKLARTTPY
CHHHHHHHHHHCCCH		35.8282987753
154PhosphorylationLLKLARTTPYYKRNR
HHHHHHCCCHHHCCC		12.0721815630
156PhosphorylationKLARTTPYYKRNRPH
HHHHCCCHHHCCCCC		21.3722817900
157PhosphorylationLARTTPYYKRNRPHI
HHHCCCHHHCCCCCC		12.5022817900
163 (in isoform 2)Ubiquitination-30.3721890473
170UbiquitinationHICSFWVKGECKRGE
CCCEEEECCCCCCCC		39.32-
185MethylationECPYRHEKPTDPDDP
CCCCCCCCCCCCCCC		47.28116265247
199UbiquitinationPLADQNIKDRYYGIN
CCCCCCHHHHHCCCC		43.6433845483
202PhosphorylationDQNIKDRYYGINDPV
CCCHHHHHCCCCCHH		19.0427642862
203PhosphorylationQNIKDRYYGINDPVA
CCHHHHHCCCCCHHH		16.6627642862
212UbiquitinationINDPVADKLLKRAST
CCCHHHHHHHHHHCC		46.0821890473
212AcetylationINDPVADKLLKRAST
CCCHHHHHHHHHHCC		46.0819608861
212 (in isoform 1)Ubiquitination-46.0821890473
219PhosphorylationKLLKRASTMPRLDPP
HHHHHHCCCCCCCCC		30.1528555341
286AcetylationAAEVAAEKSFNKLIV
HHHHHHHHHCCEEEE		56.4725953088
286UbiquitinationAAEVAAEKSFNKLIV
HHHHHHHHHCCEEEE		56.47-
290SumoylationAAEKSFNKLIVNGRR
HHHHHCCEEEECCEE		37.2625218447
290AcetylationAAEKSFNKLIVNGRR
HHHHHCCEEEECCEE		37.2625953088
290SumoylationAAEKSFNKLIVNGRR
HHHHHCCEEEECCEE		37.26-
324SumoylationGTTDSGIKLEPVPGL
CCCCCCCEEEECCCC		50.77-
395MethylationGPPPPFMRAPGPIHY
CCCCCCCCCCCCCCC		37.7030763003
395DimethylationGPPPPFMRAPGPIHY
CCCCCCCCCCCCCCC		37.70-
404PhosphorylationPGPIHYPSQDPQRMG
CCCCCCCCCCHHHCC		39.80-
418PhosphorylationGAHAGKHSSP-----
CCCCCCCCCC-----		48.0326270265
419PhosphorylationAHAGKHSSP------
CCCCCCCCC------		34.0624719451
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 RBM22_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBM22_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 RBM22_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AQR_HUMANAQRphysical
22365833
HNRL1_HUMANHNRNPUL1physical
22365833
RBM4_HUMANRBM4physical
22365833
RFOX2_HUMANRBFOX2physical
22365833
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 RBM22_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-212, AND MASS SPECTROMETRY.

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