MSI2H_HUMAN - dbPTM
MSI2H_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MSI2H_HUMAN
UniProt AC Q96DH6
Protein Name RNA-binding protein Musashi homolog 2
Gene Name MSI2
Organism Homo sapiens (Human).
Sequence Length 328
Subcellular Localization Cytoplasm. Associated with polysomes..
Protein Description RNA binding protein that regulates the expression of target mRNAs at the translation level. May play a role in the proliferation and maintenance of stem cells in the central nervous system (By similarity)..
Protein Sequence MEANGSQGTSGSANDSQHDPGKMFIGGLSWQTSPDSLRDYFSKFGEIRECMVMRDPTTKRSRGFGFVTFADPASVDKVLGQPHHELDSKTIDPKVAFPRRAQPKMVTRTKKIFVGGLSANTVVEDVKQYFEQFGKVEDAMLMFDKTTNRHRGFGFVTFENEDVVEKVCEIHFHEINNKMVECKKAQPKEVMFPPGTRGRARGLPYTMDAFMLGMGMLGYPNFVATYGRGYPGFAPSYGYQFPGFPAAAYGPVAAAAVAAARGSGSNPARPGGFPGANSPGPVADLYGPASQDSGVGNYISAASPQPGSGFGHGIAGPLIATAFTNGYH
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
1Acetylation-------MEANGSQG
-------CCCCCCCC		11.2219413330
2 (in isoform 2)Acetylation-51.3320068231
5 (in isoform 2)Phosphorylation-28.5221406692
6 (in isoform 2)Phosphorylation-25.8321406692
6Phosphorylation--MEANGSQGTSGSA
--CCCCCCCCCCCCC		25.8328450419
9PhosphorylationEANGSQGTSGSANDS
CCCCCCCCCCCCCCC		23.4428450419
9 (in isoform 2)Phosphorylation-23.4424719451
10 (in isoform 2)Phosphorylation-37.2620068231
10PhosphorylationANGSQGTSGSANDSQ
CCCCCCCCCCCCCCC		37.2628450419
12PhosphorylationGSQGTSGSANDSQHD
CCCCCCCCCCCCCCC		24.5423186163
14 (in isoform 2)Phosphorylation-51.6825159151
16PhosphorylationTSGSANDSQHDPGKM
CCCCCCCCCCCCCCE		29.2628450419
16 (in isoform 2)Phosphorylation-29.2620068231
17 (in isoform 2)Phosphorylation-48.1120068231
25 (in isoform 2)Phosphorylation-3.7021406692
28 (in isoform 2)Phosphorylation-3.8721406692
29 (in isoform 2)Phosphorylation-22.0321406692
29PhosphorylationKMFIGGLSWQTSPDS
CEEECEECCCCCCHH		22.0327251275
32 (in isoform 2)Phosphorylation-35.6521406692
32PhosphorylationIGGLSWQTSPDSLRD
ECEECCCCCCHHHHH		35.6520873877
33PhosphorylationGGLSWQTSPDSLRDY
CEECCCCCCHHHHHH		16.1723401153
36PhosphorylationSWQTSPDSLRDYFSK
CCCCCCHHHHHHHHH		28.7827251275
39 (in isoform 2)Ubiquitination-54.8721890473
41 (in isoform 3)Ubiquitination-8.2021890473
42PhosphorylationDSLRDYFSKFGEIRE
HHHHHHHHHHCCEEE		22.3525944883
43AcetylationSLRDYFSKFGEIREC
HHHHHHHHHCCEEEE		47.7125825284
43 (in isoform 1)Ubiquitination-47.7121890473
43UbiquitinationSLRDYFSKFGEIREC
HHHHHHHHHCCEEEE		47.7121890473
432-HydroxyisobutyrylationSLRDYFSKFGEIREC
HHHHHHHHHCCEEEE		47.71-
59UbiquitinationVMRDPTTKRSRGFGF
EEECCCCCCCCCCEE		51.35-
68PhosphorylationSRGFGFVTFADPASV
CCCCEEEEECCHHHH		15.7330301811
74PhosphorylationVTFADPASVDKVLGQ
EEECCHHHHHHHCCC		35.9221712546
77AcetylationADPASVDKVLGQPHH
CCHHHHHHHCCCCCC		36.8826051181
77UbiquitinationADPASVDKVLGQPHH
CCHHHHHHHCCCCCC		36.88-
89UbiquitinationPHHELDSKTIDPKVA
CCCCCCCCCCCHHHC		49.52-
94UbiquitinationDSKTIDPKVAFPRRA
CCCCCCHHHCCCCCC		42.31-
104UbiquitinationFPRRAQPKMVTRTKK
CCCCCCCCCEECCEE		33.64-
129PhosphorylationVVEDVKQYFEQFGKV
HHHHHHHHHHHHCCH		11.90-
135UbiquitinationQYFEQFGKVEDAMLM
HHHHHHCCHHHEEEE		43.68-
141 (in isoform 2)Ubiquitination-3.1121890473
145UbiquitinationDAMLMFDKTTNRHRG
HEEEEEECCCCCCCC		46.0821890473
145 (in isoform 1)Ubiquitination-46.0821890473
145AcetylationDAMLMFDKTTNRHRG
HEEEEEECCCCCCCC		46.0827452117
146PhosphorylationAMLMFDKTTNRHRGF
EEEEEECCCCCCCCE		31.0220068231
147PhosphorylationMLMFDKTTNRHRGFG
EEEEECCCCCCCCEE		35.6820068231
166UbiquitinationENEDVVEKVCEIHFH
CCHHHHHHHHEEEEE		40.34-
178UbiquitinationHFHEINNKMVECKKA
EEEEECCEEEECCCC		39.57-
196PhosphorylationEVMFPPGTRGRARGL
CCCCCCCCCCCCCCC		35.4128348404
197MethylationVMFPPGTRGRARGLP
CCCCCCCCCCCCCCC		38.2254557447
199MethylationFPPGTRGRARGLPYT
CCCCCCCCCCCCCCC		20.1654557441
201MethylationPGTRGRARGLPYTMD
CCCCCCCCCCCCCHH		45.9154557453
205PhosphorylationGRARGLPYTMDAFML
CCCCCCCCCHHHHHH		21.5328176443
206PhosphorylationRARGLPYTMDAFMLG
CCCCCCCCHHHHHHC		13.4628176443
219PhosphorylationLGMGMLGYPNFVATY
HCCHHHCCCCHHEEC		7.3428176443
225PhosphorylationGYPNFVATYGRGYPG
CCCCHHEECCCCCCC		22.6228176443
226PhosphorylationYPNFVATYGRGYPGF
CCCHHEECCCCCCCC		8.6228176443
228MethylationNFVATYGRGYPGFAP
CHHEECCCCCCCCCC		30.9324129315
261MethylationAAAVAAARGSGSNPA
HHHHHHHHCCCCCCC		34.7724129315
300PhosphorylationSGVGNYISAASPQPG
CCCCCCEEECCCCCC		13.8626074081
303PhosphorylationGNYISAASPQPGSGF
CCCEEECCCCCCCCC		24.6326074081
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 MSI2H_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MSI2H_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 MSI2H_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ICK_HUMANICKphysical
26186194
ANX13_HUMANANXA13physical
26186194
T10B_HUMANTIMM10Bphysical
26186194
FKB1A_HUMANFKBP1Aphysical
26344197
RAB7A_HUMANRAB7Aphysical
26344197
UB2L3_HUMANUBE2L3physical
26344197
RHBT2_HUMANRHOBTB2physical
27941885
T10B_HUMANTIMM10Bphysical
28514442
ICK_HUMANICKphysical
28514442
ANX13_HUMANANXA13physical
28514442
ANR40_HUMANANKRD40physical
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 MSI2H_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 MET-1, AND MASS SPECTROMETRY.

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