THOC2_MOUSE - dbPTM
THOC2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID THOC2_MOUSE
UniProt AC B1AZI6
Protein Name THO complex subunit 2
Gene Name Thoc2
Organism Mus musculus (Mouse).
Sequence Length 1594
Subcellular Localization Nucleus . Nucleus speckle.
Protein Description Required for efficient export of polyadenylated RNA and spliced mRNA. Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. Plays a role for proper neuronal development..
Protein Sequence MAAAAVVVPAEWIKNWEKSGRGEFLHLCRILSENKSHDSSTYRDFQQALYELSYHVIKGNLKHEQASSVLNDISEFREDMPSILADVFCILDIETNCLEEKSKRDYFTQLVLACLYLVSDTVLKERLDPETLESLGLIKQSQQFNQKSVKIKTKLFYKQQKFNLLREENEGYAKLIAELGQDLSGNITSDLILENIKSLIGCFNLDPNRVLDVILEVFECRPEHDDFFISLLESYMSMCEPQTLCHILGFKFKFYQEPSGETPSSLYRVAAVLLQFNLIDLDDLYVHLLPADNCIMDEYKREIVEAKQIVRKLTMVVLSSEKLDERDKEKDKDDEKVEKPPDNQKLGLLEALLKVGDWQHAQNIMDQMPPYYAASHKLIALAICKLIHITVEPLYRRVGVPKGAKGSPVSALQNKRAPKQVESFEDLRRDVFNMFCYLGPHLSHDPILFAKVVRIGKSFMKEFQSDGSKQEDKEKTEVILSCLLSITDQVLLPSLSLMDCNACMSEELWGMFKTFPYQHRYRLYGQWKNETYNGHPLLVKVKAQTIDRAKYIMKRLTKENVKPSGRQIGKLSHSNPTILFDYILSQIQKYDNLITPVVDSLKYLTSLNYDVLAYCIIEALANPEKERMKHDDTTISSWLQSLASFCGAVFRKYPIDLAGLLQYVANQLKAGKSFDLLILKEVVQKMAGIEITEEMTMEQLEAMTGGEQLKAEGGYFGQIRNTKKSSQRLKDALLDHDLALPLCLLMAQQRNGVIFQEGGEKHLKLVGKLYDQCHDTLVQFGGFLASNLSTEDYIKRVPSIDVLCNEFHTPHDAAFFLSRPMYAHHISSKYDELKKSEKGSKQQHKVHKYITSCEMVMAPVHEAVVSLHVSKVWDDISPQFYATFWSLTMYDLAVPHTSYEREVNKLKVQMKAIDDNQEMPPNKKKKEKERCTALQDKLLEEEKKQMEHVQRVLQRLKLEKDNWLLAKSTKNETITKFLQLCIFPRCIFSAIDAVYCARFVELVHQQKTPNFSTLLCYDRVFSDIIYTVASCTENEASRYGRFLCCMLETVTRWHSDRATYEKECGNYPGFLTILRATGFDGGNKADQLDYENFRHVVHKWHYKLTKASVHCLETGEYTHIRNILIVLTKILPWYPKVLNLGQALERRVNKICQEEKEKRPDLYALAMGYSGQLKSRKSHMIPENEFHHKDPPPRNAVASVQNGPGGGTSSSSIGNASKSDESGAEETDKSRERSQCGTKAVNKASSTTPKGNSSNGNSGSNSNKAVKENDKEKVKEKEKEKKEKTPATTPEARALGKDSKEKPKEERPNKEDKARETKERTPKSDKEKEKFKKEEKAKDEKFKTTVPIVESKSTQEREREKEPSRERDVAKEMKSKENVKGGEKTPVSGSLKSPVPRSDISEPDREQKRRKIDSHPSPSHSSTVKDSLIDLKDSSAKLYINHNPPPLSKSKEREMDKKDLDKSRERSREREKKDEKDRKERKRDHSNNDREVPPDITKRRKEENGTMGVSKHKSESPCESQYPNEKDKEKNKSKSSGKEKSSSDSFKSEKMDKISSGGKKESRHDKEKIEKKEKRDSSGGKEEKKHHKSSDKHR
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
158MalonylationIKTKLFYKQQKFNLL
HHHHHHHHHHHHHHH		38.6326320211
253AcetylationHILGFKFKFYQEPSG
HHHCCEEEEEECCCC		43.6922826441
314PhosphorylationKQIVRKLTMVVLSSE
HHHHHHHHHHHHCHH		15.7927600695
320PhosphorylationLTMVVLSSEKLDERD
HHHHHHCHHHCCHHH		34.2928059163
407PhosphorylationVPKGAKGSPVSALQN
CCCCCCCCCCHHHCC		22.7929514104
410PhosphorylationGAKGSPVSALQNKRA
CCCCCCCHHHCCCCC		27.0128066266
457AcetylationAKVVRIGKSFMKEFQ
HHHHHHCHHHHHHHH		37.8423576753
663PhosphorylationDLAGLLQYVANQLKA
CHHHHHHHHHHHHHC		11.0829514104
1199PhosphorylationPPRNAVASVQNGPGG
CCCCCEEECCCCCCC		20.0325619855
1208PhosphorylationQNGPGGGTSSSSIGN
CCCCCCCCCHHHCCC		28.8025619855
1209PhosphorylationNGPGGGTSSSSIGNA
CCCCCCCCHHHCCCC		31.3423684622
1210PhosphorylationGPGGGTSSSSIGNAS
CCCCCCCHHHCCCCC		28.1325619855
1211PhosphorylationPGGGTSSSSIGNASK
CCCCCCHHHCCCCCC		26.2425619855
1212PhosphorylationGGGTSSSSIGNASKS
CCCCCHHHCCCCCCC		36.1425619855
1217PhosphorylationSSSIGNASKSDESGA
HHHCCCCCCCCCCCC		36.3723684622
1219PhosphorylationSIGNASKSDESGAEE
HCCCCCCCCCCCCCC		44.0825521595
1222PhosphorylationNASKSDESGAEETDK
CCCCCCCCCCCCCHH		48.5825521595
1227PhosphorylationDESGAEETDKSRERS
CCCCCCCCHHHHHHH		39.9920469934
1230PhosphorylationGAEETDKSRERSQCG
CCCCCHHHHHHHHHC		42.0325159016
1285PhosphorylationEKEKKEKTPATTPEA
HHHHHCCCCCCCHHH		21.1725521595
1288PhosphorylationKKEKTPATTPEARAL
HHCCCCCCCHHHHHC		44.0525521595
1289PhosphorylationKEKTPATTPEARALG
HCCCCCCCHHHHHCC		22.6525521595
1321PhosphorylationARETKERTPKSDKEK
HHHHHHHCCCCHHHH		35.8423684622
1364PhosphorylationREREKEPSRERDVAK
HHHHCCCCHHHHHHH		48.1126824392
1385PhosphorylationNVKGGEKTPVSGSLK
CCCCCCCCCCCCCCC		25.3126824392
1388PhosphorylationGGEKTPVSGSLKSPV
CCCCCCCCCCCCCCC		24.7022942356
1390PhosphorylationEKTPVSGSLKSPVPR
CCCCCCCCCCCCCCH		25.7228833060
1393PhosphorylationPVSGSLKSPVPRSDI
CCCCCCCCCCCHHHC		36.1025521595
1401PhosphorylationPVPRSDISEPDREQK
CCCHHHCCCCCHHHH		48.3323684622
1414PhosphorylationQKRRKIDSHPSPSHS
HHHHHCCCCCCCCCC		40.5527742792
1417PhosphorylationRKIDSHPSPSHSSTV
HHCCCCCCCCCCCCC		33.3427087446
1419PhosphorylationIDSHPSPSHSSTVKD
CCCCCCCCCCCCCCH		40.1027742792
1421PhosphorylationSHPSPSHSSTVKDSL
CCCCCCCCCCCCHHH		31.8527742792
1422PhosphorylationHPSPSHSSTVKDSLI
CCCCCCCCCCCHHHE		31.6227742792
1423PhosphorylationPSPSHSSTVKDSLID
CCCCCCCCCCHHHEE		34.2927742792
1427PhosphorylationHSSTVKDSLIDLKDS
CCCCCCHHHEECCCC		22.8525367039
1439PhosphorylationKDSSAKLYINHNPPP
CCCCCEEEECCCCCC		10.0425367039
1448PhosphorylationNHNPPPLSKSKEREM
CCCCCCCCHHHHHHC		40.4325159016
1450PhosphorylationNPPPLSKSKEREMDK
CCCCCCHHHHHHCCH		36.0525159016
1486PhosphorylationKERKRDHSNNDREVP
HHHHHHCCCCCCCCC		41.4327087446
1514PhosphorylationMGVSKHKSESPCESQ
CCCCCCCCCCCCHHC		42.9225521595
1516PhosphorylationVSKHKSESPCESQYP
CCCCCCCCCCHHCCC		41.7725521595
1520PhosphorylationKSESPCESQYPNEKD
CCCCCCHHCCCCHHH		41.5525159016
1522PhosphorylationESPCESQYPNEKDKE
CCCCHHCCCCHHHHH		19.8025159016
1542PhosphorylationSSGKEKSSSDSFKSE
CCCCCCCCCCHHHHH		49.5930635358
1543PhosphorylationSGKEKSSSDSFKSEK
CCCCCCCCCHHHHHH		44.3530635358
1545PhosphorylationKEKSSSDSFKSEKMD
CCCCCCCHHHHHHHH		36.2030635358
1548PhosphorylationSSSDSFKSEKMDKIS
CCCCHHHHHHHHHHC		40.2030635358
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 THOC2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of THOC2_MOUSE !!
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 THOC2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of THOC2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of THOC2_MOUSE

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Related Literatures of Post-Translational Modification

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