RBM42_HUMAN - dbPTM
RBM42_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBM42_HUMAN
UniProt AC Q9BTD8
Protein Name RNA-binding protein 42
Gene Name RBM42
Organism Homo sapiens (Human).
Sequence Length 480
Subcellular Localization Nucleus. Cytoplasm. Upon stress response, localizes with HNRNPK in cytoplasmic aggregates of stalled translational preinitiation complexes called stress granules..
Protein Description Binds (via the RRM domain) to the 3'-untranslated region (UTR) of CDKN1A mRNA..
Protein Sequence MAGAGPAPGLPGAGGPVVPGPGAGIPGKSGEERLKEMEAEMALFEQEVLGAPVPGIPTAVPAVPTVPTVPTVEAMQVPAAPVIRPIIATNTYQQVQQTLEARAAAAATVVPPMVGGPPFVGPVGFGPGDRSHLDSPEAREAMFLRRAAVAPQRAPILRPAFVPHVLQRADSALSSAAAGPRPMALRPPHQALVGPPLPGPPGPPMMLPPMARAPGPPLGSMAALRPPLEEPAAPRELGLGLGLGLKEKEEAVVAAAAGLEEASAAVAVGAGGAPAGPAVIGPSLPLALAMPLPEPEPLPLPLEVVRGLLPPLRIPELLSLRPRPRPPRPEPPPGLMALEVPEPLGEDKKKGKPEKLKRCIRTAAGSSWEDPSLLEWDADDFRIFCGDLGNEVNDDILARAFSRFPSFLKAKVIRDKRTGKTKGYGFVSFKDPSDYVRAMREMNGKYVGSRPIKLRKSMWKDRNLDVVRKKQKEKKKLGLR
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------MAGAGPAPG
------CCCCCCCCC		19.2822814378
28UbiquitinationPGAGIPGKSGEERLK
CCCCCCCCCHHHHHH		50.3524816145
130MethylationVGFGPGDRSHLDSPE
CCCCCCCHHHCCCHH		31.7180702737
131PhosphorylationGFGPGDRSHLDSPEA
CCCCCCHHHCCCHHH		32.8924732914
135PhosphorylationGDRSHLDSPEAREAM
CCHHHCCCHHHHHHH		30.8823401153
135 (in isoform 4)Phosphorylation-30.8825849741
139MethylationHLDSPEAREAMFLRR
HCCCHHHHHHHHHHH		30.46115388401
145MethylationAREAMFLRRAAVAPQ
HHHHHHHHHHHHCCC		18.2254558643
146MethylationREAMFLRRAAVAPQR
HHHHHHHHHHHCCCC		29.1097816529
153MethylationRAAVAPQRAPILRPA
HHHHCCCCCCCCCHH		41.0724129315
153Asymmetric dimethylarginineRAAVAPQRAPILRPA
HHHHCCCCCCCCCHH		41.07-
158Asymmetric dimethylargininePQRAPILRPAFVPHV
CCCCCCCCHHHHHHH		22.63-
158MethylationPQRAPILRPAFVPHV
CCCCCCCCHHHHHHH		22.6324129315
168Asymmetric dimethylarginineFVPHVLQRADSALSS
HHHHHHHHHHHHHHH		35.88-
168MethylationFVPHVLQRADSALSS
HHHHHHHHHHHHHHH		35.8824129315
181Asymmetric dimethylarginineSSAAAGPRPMALRPP
HHHHCCCCCCCCCCC		32.48-
181MethylationSSAAAGPRPMALRPP
HHHHCCCCCCCCCCC		32.4824129315
186MethylationGPRPMALRPPHQALV
CCCCCCCCCCCCCCC		32.9252718025
186DimethylationGPRPMALRPPHQALV
CCCCCCCCCCCCCCC		32.92-
217UbiquitinationMARAPGPPLGSMAAL
CCCCCCCCCCCCCCC		56.0933845483
225MethylationLGSMAALRPPLEEPA
CCCCCCCCCCCCCCC		26.5182797377
246UbiquitinationLGLGLGLKEKEEAVV
CCCCCCCHHHHHHHH		66.0133845483
306MethylationPLPLEVVRGLLPPLR
CCCHHHHHCCCCCCC		34.91115388409
396 (in isoform 4)Ubiquitination-3.4621890473
400 (in isoform 2)Ubiquitination-10.9321890473
401UbiquitinationDDILARAFSRFPSFL
HHHHHHHHHHCHHHH		4.4821890473
401 (in isoform 3)Ubiquitination-4.4821890473
406PhosphorylationRAFSRFPSFLKAKVI
HHHHHCHHHHEEEEE		40.2624719451
416UbiquitinationKAKVIRDKRTGKTKG
EEEEEECCCCCCCCC		41.8524816145
418PhosphorylationKVIRDKRTGKTKGYG
EEEECCCCCCCCCCC		49.09-
421PhosphorylationRDKRTGKTKGYGFVS
ECCCCCCCCCCCEEE		30.9228387310
423UbiquitinationKRTGKTKGYGFVSFK
CCCCCCCCCCEEEEC		32.7821890473
424UbiquitinationRTGKTKGYGFVSFKD
CCCCCCCCCEEEECC		14.6732015554
424PhosphorylationRTGKTKGYGFVSFKD
CCCCCCCCCEEEECC		14.6720393185
428PhosphorylationTKGYGFVSFKDPSDY
CCCCCEEEECCHHHH		25.0728387310
430 (in isoform 1)Ubiquitination-62.3121890473
430UbiquitinationGYGFVSFKDPSDYVR
CCCEEEECCHHHHHH		62.3123000965
438UbiquitinationDPSDYVRAMREMNGK
CHHHHHHHHHHHCCE		7.4324816145
445UbiquitinationAMREMNGKYVGSRPI
HHHHHCCEECCCCCC		31.5824816145
446PhosphorylationMREMNGKYVGSRPIK
HHHHCCEECCCCCCC		16.0829496907
449PhosphorylationMNGKYVGSRPIKLRK
HCCEECCCCCCCCCH		25.4925954137
453UbiquitinationYVGSRPIKLRKSMWK
ECCCCCCCCCHHHHH		44.9432015554
467UbiquitinationKDRNLDVVRKKQKEK
HCCCHHHHHHHHHHH		8.0824816145
474UbiquitinationVRKKQKEKKKLGLR-
HHHHHHHHHHHCCC-		63.3424816145
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
406SPhosphorylationKinaseCHEK1O14757
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBM42_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 RBM42_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
SF3B2_HUMANSF3B2physical
22939629
SNRPA_HUMANSNRPAphysical
22365833
PPIL1_HUMANPPIL1physical
22365833
HNRPK_HUMANHNRNPKphysical
22365833
RBM4_HUMANRBM4physical
22365833
RFOX2_HUMANRBFOX2physical
22365833
RAM_HUMANFAM103A1physical
26344197
MAP11_HUMANMETAP1physical
26344197
KCC2G_HUMANCAMK2Gphysical
28514442
KCC2B_HUMANCAMK2Bphysical
28514442
KCC2D_HUMANCAMK2Dphysical
28514442
SNR27_HUMANSNRNP27physical
28514442
RBM45_HUMANRBM45physical
28514442
RB11B_HUMANRAB11Bphysical
28514442
NGRN_HUMANNGRNphysical
28514442
PTCD1_HUMANPTCD1physical
28514442
TRUB2_HUMANTRUB2physical
28514442
QKI_HUMANQKIphysical
28514442
RUSD4_HUMANRPUSD4physical
28514442
RT09_HUMANMRPS9physical
28514442
RUSD3_HUMANRPUSD3physical
28514442
MTEF3_HUMANMTERF3physical
28514442
SNUT1_HUMANSART1physical
28514442
RT07_HUMANMRPS7physical
28514442
SYYM_HUMANYARS2physical
28514442
RT05_HUMANMRPS5physical
28514442
SUV3_HUMANSUPV3L1physical
28514442
NADK_HUMANNADKphysical
28514442
PTCD3_HUMANPTCD3physical
28514442
RCC1L_HUMANWBSCR16physical
28514442
RT02_HUMANMRPS2physical
28514442
MASU1_HUMANMALSU1physical
28514442
FAKD2_HUMANFASTKD2physical
28514442
RT35_HUMANMRPS35physical
28514442
F120A_HUMANFAM120Aphysical
28514442
RT14_HUMANMRPS14physical
28514442
RT33_HUMANMRPS33physical
28514442
RT31_HUMANMRPS31physical
28514442
RT26_HUMANMRPS26physical
28514442
RT21_HUMANMRPS21physical
28514442
PRP6_HUMANPRPF6physical
28514442
RT24_HUMANMRPS24physical
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 RBM42_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.

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