DI3L2_HUMAN - dbPTM
DI3L2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DI3L2_HUMAN
UniProt AC Q8IYB7
Protein Name DIS3-like exonuclease 2 {ECO:0000255|HAMAP-Rule:MF_03045}
Gene Name DIS3L2 {ECO:0000255|HAMAP-Rule:MF_03045}
Organism Homo sapiens (Human).
Sequence Length 885
Subcellular Localization Cytoplasm . Cytoplasm, P-body.
Protein Description 3'-5'-exoribonuclease that specifically recognizes RNAs polyuridylated at their 3' end and mediates their degradation. Component of an exosome-independent RNA degradation pathway that mediates degradation of both mRNAs and miRNAs that have been polyuridylated by a terminal uridylyltransferase, such as ZCCHC11/TUT4. Mediates degradation of cytoplasmic mRNAs that have been deadenylated and subsequently uridylated at their 3'. Mediates degradation of uridylated pre-let-7 miRNAs, contributing to the maintenance of embryonic stem (ES) cells. Essential for correct mitosis, and negatively regulates cell proliferation..
Protein Sequence MSHPDYRMNLRPLGTPRGVSAVAGPHDIGASPGDKKSKNRSTRGKKKSIFETYMSKEDVSEGLKRGTLIQGVLRINPKKFHEAFIPSPDGDRDIFIDGVVARNRALNGDLVVVKLLPEEHWKVVKPESNDKETEAAYESDIPEELCGHHLPQQSLKSYNDSPDVIVEAQFDGSDSEDGHGITQNVLVDGVKKLSVCVSEKGREDGDAPVTKDETTCISQDTRALSEKSLQRSAKVVYILEKKHSRAATGFLKLLADKNSELFRKYALFSPSDHRVPRIYVPLKDCPQDFVARPKDYANTLFICRIVDWKEDCNFALGQLAKSLGQAGEIEPETEGILTEYGVDFSDFSSEVLECLPQGLPWTIPPEEFSKRRDLRKDCIFTIDPSTARDLDDALSCKPLADGNFKVGVHIADVSYFVPEGSDLDKVAAERATSVYLVQKVVPMLPRLLCEELCSLNPMSDKLTFSVIWTLTPEGKILDEWFGRTIIRSCTKLSYEHAQSMIESPTEKIPAKELPPISPEHSSEEVHQAVLNLHGIAKQLRQQRFVDGALRLDQLKLAFTLDHETGLPQGCHIYEYRESNKLVEEFMLLANMAVAHKIHRAFPEQALLRRHPPPQTRMLSDLVEFCDQMGLPVDFSSAGALNKSLTQTFGDDKYSLARKEVLTNMCSRPMQMALYFCSGLLQDPAQFRHYALNVPLYTHFTSPIRRFADVLVHRLLAAALGYRERLDMAPDTLQKQADHCNDRRMASKRVQELSTSLFFAVLVKESGPLESEAMVMGILKQAFDVLVLRYGVQKRIYCNALALRSHHFQKVGKKPELTLVWEPEDMEQEPAQQVITIFSLVEVVLQAESTALKYSAILKRPGTQGHLGPEKEEEESDGEPEDSSTS
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
15PhosphorylationMNLRPLGTPRGVSAV
CCCCCCCCCCCCCCC		19.9322199227
17MethylationLRPLGTPRGVSAVAG
CCCCCCCCCCCCCCC		58.96-
20PhosphorylationLGTPRGVSAVAGPHD
CCCCCCCCCCCCCCC		21.6129396449
31PhosphorylationGPHDIGASPGDKKSK
CCCCCCCCCCCCCCC		24.9729255136
36AcetylationGASPGDKKSKNRSTR
CCCCCCCCCCCCCCC		71.987960547
38MethylationSPGDKKSKNRSTRGK
CCCCCCCCCCCCCCC		66.32-
46AcetylationNRSTRGKKKSIFETY
CCCCCCCCHHHHHHH		55.367960557
56AcetylationIFETYMSKEDVSEGL
HHHHHCCHHHHCHHH		41.217960567
60PhosphorylationYMSKEDVSEGLKRGT
HCCHHHHCHHHHHCC		37.96-
128PhosphorylationWKVVKPESNDKETEA
CEEECCCCCCHHHHH		59.8829978859
133PhosphorylationPESNDKETEAAYESD
CCCCCHHHHHHHHCC		36.3427050516
137PhosphorylationDKETEAAYESDIPEE
CHHHHHHHHCCCCHH		24.0223898821
139PhosphorylationETEAAYESDIPEELC
HHHHHHHCCCCHHHC		28.3225159151
154PhosphorylationGHHLPQQSLKSYNDS
CCCCCHHHHHHCCCC		32.3025850435
157PhosphorylationLPQQSLKSYNDSPDV
CCHHHHHHCCCCCCE		34.1728122231
158PhosphorylationPQQSLKSYNDSPDVI
CHHHHHHCCCCCCEE		22.7728122231
161PhosphorylationSLKSYNDSPDVIVEA
HHHHCCCCCCEEEEE		21.2527732954
173PhosphorylationVEAQFDGSDSEDGHG
EEEEECCCCCCCCCC		39.5525159151
175PhosphorylationAQFDGSDSEDGHGIT
EEECCCCCCCCCCCC		39.0125159151
182PhosphorylationSEDGHGITQNVLVDG
CCCCCCCCCCEEECC		20.7728450419
192UbiquitinationVLVDGVKKLSVCVSE
EEECCEEEEEEEEEC		43.52-
194PhosphorylationVDGVKKLSVCVSEKG
ECCEEEEEEEEECCC		23.5026657352
198PhosphorylationKKLSVCVSEKGREDG
EEEEEEEECCCCCCC		28.5929978859
200UbiquitinationLSVCVSEKGREDGDA
EEEEEECCCCCCCCC		56.62-
211UbiquitinationDGDAPVTKDETTCIS
CCCCCCCCCCCEEEC		54.5224816145
227UbiquitinationDTRALSEKSLQRSAK
HHHHHCHHHHHHHHE		53.7629967540
252AcetylationRAATGFLKLLADKNS
HHHHHHHHHHHHCCC		38.9119608861
264MalonylationKNSELFRKYALFSPS
CCCHHHHHHCCCCCC		27.7832601280
269PhosphorylationFRKYALFSPSDHRVP
HHHHCCCCCCCCCCC		25.0923312004
271PhosphorylationKYALFSPSDHRVPRI
HHCCCCCCCCCCCEE		44.8723312004
283UbiquitinationPRIYVPLKDCPQDFV
CEEEEEHHCCCCCCC		51.74-
283MalonylationPRIYVPLKDCPQDFV
CEEEEEHHCCCCCCC		51.7432601280
376UbiquitinationSKRRDLRKDCIFTID
HCCHHCCHHCEEEEC		65.3429967540
397UbiquitinationLDDALSCKPLADGNF
HHHHHCCEECCCCCE		39.4229967540
454PhosphorylationLLCEELCSLNPMSDK
HHHHHHHCCCCCCCC		43.7529396449
459PhosphorylationLCSLNPMSDKLTFSV
HHCCCCCCCCEEEEE		32.6229396449
488PhosphorylationFGRTIIRSCTKLSYE
HHHHHHHHHHHCCHH		18.7429759185
490PhosphorylationRTIIRSCTKLSYEHA
HHHHHHHHHCCHHHH		35.9529759185
499PhosphorylationLSYEHAQSMIESPTE
CCHHHHHHHHHCCCC		23.6329759185
503PhosphorylationHAQSMIESPTEKIPA
HHHHHHHCCCCCCCH		26.6325627689
505PhosphorylationQSMIESPTEKIPAKE
HHHHHCCCCCCCHHH		60.2229759185
507 (in isoform 3)Ubiquitination-57.3721906983
507 (in isoform 2)Ubiquitination-57.3721906983
507 (in isoform 1)Ubiquitination-57.3721906983
507UbiquitinationMIESPTEKIPAKELP
HHHCCCCCCCHHHCC		57.372190698
511UbiquitinationPTEKIPAKELPPISP
CCCCCCHHHCCCCCC		55.2029967540
517PhosphorylationAKELPPISPEHSSEE
HHHCCCCCCCCCHHH		29.9725627689
596UbiquitinationANMAVAHKIHRAFPE
HHHHHHHHHHHHCHH		30.3933845483
643PhosphorylationSAGALNKSLTQTFGD
CCCCCCHHHHHHHCC		35.2625159151
652UbiquitinationTQTFGDDKYSLARKE
HHHHCCCHHHHHHHH		41.2927667366
653PhosphorylationQTFGDDKYSLARKEV
HHHCCCHHHHHHHHH		18.8627642862
662PhosphorylationLARKEVLTNMCSRPM
HHHHHHHHHHCCCHH		26.5322817900
721PhosphorylationLLAAALGYRERLDMA
HHHHHHCHHHHHCCC		15.34-
796PhosphorylationYGVQKRIYCNALALR
HCCCHHHHHCHHHHH		5.4520068231
858UbiquitinationLKYSAILKRPGTQGH
HHHHHHHCCCCCCCC		50.8929967540
862PhosphorylationAILKRPGTQGHLGPE
HHHCCCCCCCCCCCC		33.7823927012
875PhosphorylationPEKEEEESDGEPEDS
CCCCCCCCCCCCCCC		54.9529255136
882PhosphorylationSDGEPEDSSTS----
CCCCCCCCCCC----		33.5823927012
883PhosphorylationDGEPEDSSTS-----
CCCCCCCCCC-----		45.0223927012
884PhosphorylationGEPEDSSTS------
CCCCCCCCC------		42.2723927012
885PhosphorylationEPEDSSTS-------
CCCCCCCC-------		39.9223927012
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 DI3L2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DI3L2_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 DI3L2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CSN6_HUMANCOPS6physical
16169070
FEZ1_HUMANFEZ1physical
16169070
VIME_HUMANVIMphysical
16169070
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
267000Perlman syndrome (PRLMNS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DI3L2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-252, AND MASS SPECTROMETRY.
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-875, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-662, AND MASSSPECTROMETRY.

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