YTHD2_HUMAN - dbPTM
YTHD2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YTHD2_HUMAN
UniProt AC Q9Y5A9
Protein Name YTH domain-containing family protein 2 {ECO:0000305}
Gene Name YTHDF2 {ECO:0000312|HGNC:HGNC:31675}
Organism Homo sapiens (Human).
Sequence Length 579
Subcellular Localization Cytoplasm, cytosol . Nucleus . Cytoplasm, P-body . Localizes to the cytosol and relocates to the nucleus following heat shock stress (PubMed:26458103).
Protein Description Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, and regulates mRNA stability. [PubMed: 24284625]
Protein Sequence MSASSLLEQRPKGQGNKVQNGSVHQKDGLNDDDFEPYLSPQARPNNAYTAMSDSYLPSYYSPSIGFSYSLGEAAWSTGGDTAMPYLTSYGQLSNGEPHFLPDAMFGQPGALGSTPFLGQHGFNFFPSGIDFSAWGNNSSQGQSTQSSGYSSNYAYAPSSLGGAMIDGQSAFANETLNKAPGMNTIDQGMAALKLGSTEVASNVPKVVGSAVGSGSITSNIVASNSLPPATIAPPKPASWADIASKPAKQQPKLKTKNGIAGSSLPPPPIKHNMDIGTWDNKGPVAKAPSQALVQNIGQPTQGSPQPVGQQANNSPPVAQASVGQQTQPLPPPPPQPAQLSVQQQAAQPTRWVAPRNRGSGFGHNGVDGNGVGQSQAGSGSTPSEPHPVLEKLRSINNYNPKDFDWNLKHGRVFIIKSYSEDDIHRSIKYNIWCSTEHGNKRLDAAYRSMNGKGPVYLLFSVNGSGHFCGVAEMKSAVDYNTCAGVWSQDKWKGRFDVRWIFVKDVPNSQLRHIRLENNENKPVTNSRDTQEVPLEKAKQVLKIIASYKHTTSIFDDFSHYEKRQEEEESVKKERQGRGK
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
2Phosphorylation------MSASSLLEQ
------CCHHHHHHH		36.5423401153
2Acetylation------MSASSLLEQ
------CCHHHHHHH		36.5420058876
4Phosphorylation----MSASSLLEQRP
----CCHHHHHHHCC		17.7629255136
5Phosphorylation---MSASSLLEQRPK
---CCHHHHHHHCCC		36.3729255136
12UbiquitinationSLLEQRPKGQGNKVQ
HHHHHCCCCCCCCCC		67.0822505724
17UbiquitinationRPKGQGNKVQNGSVH
CCCCCCCCCCCCCCC		52.6127667366
22PhosphorylationGNKVQNGSVHQKDGL
CCCCCCCCCCCCCCC		24.7928985074
26UbiquitinationQNGSVHQKDGLNDDD
CCCCCCCCCCCCCCC		38.60-
37PhosphorylationNDDDFEPYLSPQARP
CCCCCCCCCCCCCCC		16.7730266825
39PhosphorylationDDFEPYLSPQARPNN
CCCCCCCCCCCCCCC		14.7719664994
48PhosphorylationQARPNNAYTAMSDSY
CCCCCCCCCCCCCCC		9.3526074081
138O-linked_GlycosylationFSAWGNNSSQGQSTQ
CCCCCCCCCCCCCCC		28.2128510447
143UbiquitinationNNSSQGQSTQSSGYS
CCCCCCCCCCCCCCC		34.9321963094
143 (in isoform 2)Ubiquitination-34.9321890473
182SulfoxidationTLNKAPGMNTIDQGM
HHHCCCCCCHHHHHH		3.7821406390
193UbiquitinationDQGMAALKLGSTEVA
HHHHHHHHCCCCHHH		46.1821906983
193 (in isoform 1)Ubiquitination-46.1821890473
195AcetylationGMAALKLGSTEVASN
HHHHHHCCCCHHHHC		30.8219608861
196PhosphorylationMAALKLGSTEVASNV
HHHHHCCCCHHHHCC		31.6525159151
197PhosphorylationAALKLGSTEVASNVP
HHHHCCCCHHHHCCC		32.4523186163
231 (in isoform 2)Ubiquitination-6.1821890473
231UbiquitinationNSLPPATIAPPKPAS
CCCCCCCCCCCCCCC		6.1822817900
236UbiquitinationATIAPPKPASWADIA
CCCCCCCCCCHHHHH		36.9822817900
238PhosphorylationIAPPKPASWADIASK
CCCCCCCCHHHHHCC		31.1825159151
245AcetylationSWADIASKPAKQQPK
CHHHHHCCCHHHCCC		39.7223954790
263PhosphorylationKNGIAGSSLPPPPIK
CCCCCCCCCCCCCCC		43.9328555341
277PhosphorylationKHNMDIGTWDNKGPV
CCCCCCCCCCCCCCC		29.9430576142
281 (in isoform 1)Ubiquitination-63.2221890473
281UbiquitinationDIGTWDNKGPVAKAP
CCCCCCCCCCCCCCC		63.2222817900
286UbiquitinationDNKGPVAKAPSQALV
CCCCCCCCCCCHHHH		62.1522817900
326PhosphorylationQASVGQQTQPLPPPP
CCCCCCCCCCCCCCC		25.0228464451
341UbiquitinationPQPAQLSVQQQAAQP
CCCCCCCHHHHHCCC		8.9423000965
350MethylationQQAAQPTRWVAPRNR
HHHCCCCCEECCCCC		32.33115389591
351UbiquitinationQAAQPTRWVAPRNRG
HHCCCCCEECCCCCC		7.9721890473
351 (in isoform 2)Ubiquitination-7.9721890473
357MethylationRWVAPRNRGSGFGHN
CEECCCCCCCCCCCC		41.77115920233
358UbiquitinationWVAPRNRGSGFGHNG
EECCCCCCCCCCCCC		35.3521890473
358 (in isoform 2)Ubiquitination-35.3521890473
359PhosphorylationVAPRNRGSGFGHNGV
ECCCCCCCCCCCCCC		27.9325159151
374PhosphorylationDGNGVGQSQAGSGST
CCCCCCCCCCCCCCC		18.9729978859
378UbiquitinationVGQSQAGSGSTPSEP
CCCCCCCCCCCCCCC		32.3629967540
380PhosphorylationQSQAGSGSTPSEPHP
CCCCCCCCCCCCCCH		38.5528555341
381PhosphorylationSQAGSGSTPSEPHPV
CCCCCCCCCCCCCHH		34.0728555341
383PhosphorylationAGSGSTPSEPHPVLE
CCCCCCCCCCCHHHH		64.94-
391UbiquitinationEPHPVLEKLRSINNY
CCCHHHHHHHCCCCC		45.0723000965
391AcetylationEPHPVLEKLRSINNY
CCCHHHHHHHCCCCC		45.0726051181
393MethylationHPVLEKLRSINNYNP
CHHHHHHHCCCCCCC		46.70115920237
394PhosphorylationPVLEKLRSINNYNPK
HHHHHHHCCCCCCCC		39.8525159151
398PhosphorylationKLRSINNYNPKDFDW
HHHCCCCCCCCCCCC		28.4924117733
401 (in isoform 1)Ubiquitination-68.3521890473
401AcetylationSINNYNPKDFDWNLK
CCCCCCCCCCCCCCC		68.3591215
401UbiquitinationSINNYNPKDFDWNLK
CCCCCCCCCCCCCCC		68.3522817900
408AcetylationKDFDWNLKHGRVFII
CCCCCCCCCCEEEEE		40.5826822725
408 (in isoform 1)Ubiquitination-40.5821890473
408UbiquitinationKDFDWNLKHGRVFII
CCCCCCCCCCEEEEE		40.5822817900
416UbiquitinationHGRVFIIKSYSEDDI
CCEEEEEEECCHHHH		38.23-
417PhosphorylationGRVFIIKSYSEDDIH
CEEEEEEECCHHHHH		24.3928152594
418PhosphorylationRVFIIKSYSEDDIHR
EEEEEEECCHHHHHH		15.8628152594
419PhosphorylationVFIIKSYSEDDIHRS
EEEEEECCHHHHHHH		41.4625159151
428AcetylationDDIHRSIKYNIWCST
HHHHHHHEEEEEEEC		33.2325953088
428UbiquitinationDDIHRSIKYNIWCST
HHHHHHHEEEEEEEC		33.2329967540
440AcetylationCSTEHGNKRLDAAYR
EECCCCCHHHHHHHH		59.9525953088
440UbiquitinationCSTEHGNKRLDAAYR
EECCCCCHHHHHHHH		59.9529967540
446PhosphorylationNKRLDAAYRSMNGKG
CHHHHHHHHHHCCCC		12.63-
471UbiquitinationSGHFCGVAEMKSAVD
CCCCCEEEEHHCCCC		9.1029967540
486UbiquitinationYNTCAGVWSQDKWKG
CCCCCCCCCCCCCCC		6.8632015554
488UbiquitinationTCAGVWSQDKWKGRF
CCCCCCCCCCCCCCE		40.3630230243
490UbiquitinationAGVWSQDKWKGRFDV
CCCCCCCCCCCCEEE		43.0729967540
490AcetylationAGVWSQDKWKGRFDV
CCCCCCCCCCCCEEE		43.0726051181
492UbiquitinationVWSQDKWKGRFDVRW
CCCCCCCCCCEEEEE		46.04-
498UbiquitinationWKGRFDVRWIFVKDV
CCCCEEEEEEEEECC		23.7129967540
512UbiquitinationVPNSQLRHIRLENNE
CCCHHHEEEEEECCC		20.3629967540
521UbiquitinationRLENNENKPVTNSRD
EEECCCCCCCCCCCC		34.3924816145
524PhosphorylationNNENKPVTNSRDTQE
CCCCCCCCCCCCCCC		35.6829978859
526PhosphorylationENKPVTNSRDTQEVP
CCCCCCCCCCCCCCC		23.3629978859
536UbiquitinationTQEVPLEKAKQVLKI
CCCCCHHHHHHHHHH		69.4432015554
538UbiquitinationEVPLEKAKQVLKIIA
CCCHHHHHHHHHHHH		52.5930230243
548UbiquitinationLKIIASYKHTTSIFD
HHHHHHCCCCCCCCC		31.7929967540
550PhosphorylationIIASYKHTTSIFDDF
HHHHCCCCCCCCCCC		20.3420068231
551PhosphorylationIASYKHTTSIFDDFS
HHHCCCCCCCCCCCH		21.3920068231
552PhosphorylationASYKHTTSIFDDFSH
HHCCCCCCCCCCCHH		23.5520068231
558PhosphorylationTSIFDDFSHYEKRQE
CCCCCCCHHHHHHHH		31.9628152594
560PhosphorylationIFDDFSHYEKRQEEE
CCCCCHHHHHHHHHH		23.1928796482
562UbiquitinationDDFSHYEKRQEEEES
CCCHHHHHHHHHHHH		52.8229967540
562AcetylationDDFSHYEKRQEEEES
CCCHHHHHHHHHHHH		52.8226051181
569PhosphorylationKRQEEEESVKKERQG
HHHHHHHHHHHHHCC		42.3828348404
571UbiquitinationQEEEESVKKERQGRG
HHHHHHHHHHHCCCC		59.1924816145
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 YTHD2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YTHD2_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 YTHD2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
GDE_HUMANAGLphysical
26344197
HEM3_HUMANHMBSphysical
26344197
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 YTHD2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-37, AND MASSSPECTROMETRY.

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