MBNL1_HUMAN - dbPTM
MBNL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MBNL1_HUMAN
UniProt AC Q9NR56
Protein Name Muscleblind-like protein 1
Gene Name MBNL1
Organism Homo sapiens (Human).
Sequence Length 388
Subcellular Localization Nucleus . Cytoplasm . Cytoplasmic granule . Localized with DDX1, TIAL1 and YBX1 in stress granules upon stress (PubMed:18335541). Localized in the cytoplasm of multinucleated myotubes (PubMed:18335541). Colocalizes with nuclear foci of retained expan
Protein Description Mediates pre-mRNA alternative splicing regulation. Acts either as activator or repressor of splicing on specific pre-mRNA targets. Inhibits cardiac troponin-T (TNNT2) pre-mRNA exon inclusion but induces insulin receptor (IR) pre-mRNA exon inclusion in muscle. Antagonizes the alternative splicing activity pattern of CELF proteins. Regulates the TNNT2 exon 5 skipping through competition with U2AF2. Inhibits the formation of the spliceosome A complex on intron 4 of TNNT2 pre-mRNA. Binds to the stem-loop structure within the polypyrimidine tract of TNNT2 intron 4 during spliceosome assembly. Binds to the 5'-YGCU(U/G)Y-3'consensus sequence. Binds to the IR RNA. Binds to expanded CUG repeat RNA, which folds into a hairpin structure containing GC base pairs and bulged, unpaired U residues..
Protein Sequence MAVSVTPIRDTKWLTLEVCREFQRGTCSRPDTECKFAHPSKSCQVENGRVIACFDSLKGRCSRENCKYLHPPPHLKTQLEINGRNNLIQQKNMAMLAQQMQLANAMMPGAPLQPVPMFSVAPSLATNASAAAFNPYLGPVSPSLVPAEILPTAPMLVTGNPGVPVPAAAAAAAQKLMRTDRLEVCREYQRGNCNRGENDCRFAHPADSTMIDTNDNTVTVCMDYIKGRCSREKCKYFHPPAHLQAKIKAAQYQVNQAAAAQAAATAAAMTQSAVKSLKRPLEATFDLGIPQAVLPPLPKRPALEKTNGATAVFNTGIFQYQQALANMQLQQHTAFLPPVPMVHGATPATVSAATTSATSVPFAATATANQIPIISAEHLTSHKYVTQM
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
4Phosphorylation----MAVSVTPIRDT
----CCCEECCCCCC		15.6729255136
6Phosphorylation--MAVSVTPIRDTKW
--CCCEECCCCCCCE		12.9029255136
11PhosphorylationSVTPIRDTKWLTLEV
EECCCCCCCEEEHHH		17.8029255136
12UbiquitinationVTPIRDTKWLTLEVC
ECCCCCCCEEEHHHH		44.49-
24MethylationEVCREFQRGTCSRPD
HHHHHHHCCCCCCCC		47.94115482749
35UbiquitinationSRPDTECKFAHPSKS
CCCCCCCCCCCCCCC		39.08-
41UbiquitinationCKFAHPSKSCQVENG
CCCCCCCCCCEEECC		60.7521906983
41 (in isoform 3)Ubiquitination-60.7521906983
41 (in isoform 2)Ubiquitination-60.7521906983
41 (in isoform 1)Ubiquitination-60.7521906983
41AcetylationCKFAHPSKSCQVENG
CCCCCCCCCCEEECC		60.7525953088
56PhosphorylationRVIACFDSLKGRCSR
EEEEEECCCCCCCCC		16.2427499020
58 (in isoform 3)Ubiquitination-48.5421906983
58 (in isoform 2)Ubiquitination-48.5421906983
58 (in isoform 1)Ubiquitination-48.5421906983
58UbiquitinationIACFDSLKGRCSREN
EEEECCCCCCCCCCC		48.542190698
67UbiquitinationRCSRENCKYLHPPPH
CCCCCCCCCCCCCCC		63.53-
76UbiquitinationLHPPPHLKTQLEING
CCCCCCCEEEEEECC		31.06-
141PhosphorylationNPYLGPVSPSLVPAE
CCCCCCCCCCCCCCH		16.3526074081
143PhosphorylationYLGPVSPSLVPAEIL
CCCCCCCCCCCCHHH		34.2026074081
158PhosphorylationPTAPMLVTGNPGVPV
CCCCEEECCCCCCCH		27.5523879269
175UbiquitinationAAAAAAQKLMRTDRL
HHHHHHHHHHCCCHH		39.25-
188PhosphorylationRLEVCREYQRGNCNR
HHHHHHHHHCCCCCC		5.55-
208PhosphorylationRFAHPADSTMIDTND
CCCCCCCCCEEECCC		23.21-
213PhosphorylationADSTMIDTNDNTVTV
CCCCEEECCCCEEEE		33.2830576142
219PhosphorylationDTNDNTVTVCMDYIK
ECCCCEEEEEHHHHC		13.1230576142
224PhosphorylationTVTVCMDYIKGRCSR
EEEEEHHHHCCCCCH		4.2530576142
246UbiquitinationPPAHLQAKIKAAQYQ
CCHHHHHHHHHHHHH		31.60-
246MalonylationPPAHLQAKIKAAQYQ
CCHHHHHHHHHHHHH		31.6026320211
248UbiquitinationAHLQAKIKAAQYQVN
HHHHHHHHHHHHHHH		36.64-
265PhosphorylationAAAQAAATAAAMTQS
HHHHHHHHHHHHHHH		16.4724043423
270PhosphorylationAATAAAMTQSAVKSL
HHHHHHHHHHHHHHC		18.0424043423
272PhosphorylationTAAAMTQSAVKSLKR
HHHHHHHHHHHHCCC		26.3425159151
275AcetylationAMTQSAVKSLKRPLE
HHHHHHHHHCCCCHH		50.1925953088
276PhosphorylationMTQSAVKSLKRPLEA
HHHHHHHHCCCCHHH		32.3124719451
278UbiquitinationQSAVKSLKRPLEATF
HHHHHHCCCCHHHHC		60.09-
281 (in isoform 5)Ubiquitination-8.97-
284PhosphorylationLKRPLEATFDLGIPQ
CCCCHHHHCCCCCCH		14.3326434776
287 (in isoform 5)Ubiquitination-6.14-
299UbiquitinationAVLPPLPKRPALEKT
HHCCCCCCCCCHHCC		77.89-
315O-linked_GlycosylationGATAVFNTGIFQYQQ
CCEEEECCCHHHHHH		21.8623301498
349O-linked_GlycosylationVHGATPATVSAATTS
CCCCCCCCCCCCCCC		19.05OGP
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 MBNL1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MBNL1_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 MBNL1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DHX9_HUMANDHX9physical
21900255
DDX5_HUMANDDX5physical
21900255
DDX17_HUMANDDX17physical
21900255
HNRH1_HUMANHNRNPH1physical
21900255
HNRH2_HUMANHNRNPH2physical
21900255
HNRH3_HUMANHNRNPH3physical
21900255
HNRPF_HUMANHNRNPFphysical
21900255
ROA2_HUMANHNRNPA2B1physical
21900255
HNRPL_HUMANHNRNPLphysical
21900255
HNRPK_HUMANHNRNPKphysical
21900255
BIN1_HUMANBIN1physical
21623381
A4_HUMANAPPphysical
21832049
TIAR_HUMANTIAL1physical
22939629
ZNHI3_HUMANZNHIT3physical
21988832
AEN_HUMANAENphysical
25416956
MBNL2_HUMANMBNL2physical
26186194
MBNL3_HUMANMBNL3physical
26186194
MBNL3_HUMANMBNL3physical
28514442
MBNL2_HUMANMBNL2physical
28514442
SYIM_HUMANIARS2physical
28514442
ZN143_HUMANZNF143physical
27173435
I2BP1_HUMANIRF2BP1physical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
160900Dystrophia myotonica 1 (DM1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MBNL1_HUMAN

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Related Literatures of Post-Translational Modification

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