FL2D_HUMAN - dbPTM
FL2D_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FL2D_HUMAN
UniProt AC Q15007
Protein Name Pre-mRNA-splicing regulator WTAP {ECO:0000305}
Gene Name WTAP {ECO:0000303|PubMed:11001926, ECO:0000312|HGNC:HGNC:16846}
Organism Homo sapiens (Human).
Sequence Length 396
Subcellular Localization Nucleus speckle . Nucleus, nucleoplasm . Cytoplasm . Mainly nuclear with some fraction located in the cytoplasm. ZC3H13 is required to anchor component of the MACOM subcomplex, such as VIRMA, in the nucleus.
Protein Description Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing. [PubMed: 29507755 Required for accumulation of METTL3 and METTL14 to nuclear speckle]
Protein Sequence MTNEEPLPKKVRLSETDFKVMARDELILRWKQYEAYVQALEGKYTDLNSNDVTGLRESEEKLKQQQQESARRENILVMRLATKEQEMQECTTQIQYLKQVQQPSVAQLRSTMVDPAINLFFLKMKGELEQTKDKLEQAQNELSAWKFTPDSQTGKKLMAKCRMLIQENQELGRQLSQGRIAQLEAELALQKKYSEELKSSQDELNDFIIQLDEEVEGMQSTILVLQQQLKETRQQLAQYQQQQSQASAPSTSRTTASEPVEQSEATSKDCSRLTNGPSNGSSSRQRTSGSGFHREGNTTEDDFPSSPGNGNKSSNSSEERTGRGGSGYVNQLSAGYESVDSPTGSENSLTHQSNDTDSSHDPQEEKAVSGKGNRTVGSRHVQNGLDSSVNVQGSVL
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-------MTNEEPLP
-------CCCCCCCC		9.0722814378
2Phosphorylation------MTNEEPLPK
------CCCCCCCCC		51.8720068231
2Acetylation------MTNEEPLPK
------CCCCCCCCC		51.8720068231
9UbiquitinationTNEEPLPKKVRLSET
CCCCCCCCCCCCCCC		72.14-
10UbiquitinationNEEPLPKKVRLSETD
CCCCCCCCCCCCCCC		30.55-
14PhosphorylationLPKKVRLSETDFKVM
CCCCCCCCCCCHHHE		28.0829255136
16PhosphorylationKKVRLSETDFKVMAR
CCCCCCCCCHHHEEC		43.2829255136
19 (in isoform 1)Ubiquitination-33.6321890473
19UbiquitinationRLSETDFKVMARDEL
CCCCCCHHHEECCHH		33.6321890473
19 (in isoform 2)Ubiquitination-33.6321890473
19UbiquitinationRLSETDFKVMARDEL
CCCCCCHHHEECCHH		33.6321890473
31UbiquitinationDELILRWKQYEAYVQ
CHHHHHHHHHHHHHH		36.2521906983
31 (in isoform 2)Ubiquitination-36.2521890473
31 (in isoform 1)Ubiquitination-36.2521890473
43 (in isoform 2)Ubiquitination-35.2921890473
43UbiquitinationYVQALEGKYTDLNSN
HHHHHCCCCCCCCCC		35.2921906983
43 (in isoform 1)Ubiquitination-35.2921890473
44PhosphorylationVQALEGKYTDLNSND
HHHHCCCCCCCCCCC		19.1528152594
45PhosphorylationQALEGKYTDLNSNDV
HHHCCCCCCCCCCCC		37.1828152594
49PhosphorylationGKYTDLNSNDVTGLR
CCCCCCCCCCCCCHH		41.52-
53PhosphorylationDLNSNDVTGLRESEE
CCCCCCCCCHHHHHH		33.1028985074
58PhosphorylationDVTGLRESEEKLKQQ
CCCCHHHHHHHHHHH		44.6225159151
61UbiquitinationGLRESEEKLKQQQQE
CHHHHHHHHHHHHHH		57.86-
63 (in isoform 1)Ubiquitination-58.0721890473
63 (in isoform 2)Ubiquitination-58.0721890473
63UbiquitinationRESEEKLKQQQQESA
HHHHHHHHHHHHHHH		58.0721906983
69PhosphorylationLKQQQQESARRENIL
HHHHHHHHHHHHHHH		23.8020164059
83AcetylationLVMRLATKEQEMQEC
HHHHCCCHHHHHHHH		52.3626051181
83UbiquitinationLVMRLATKEQEMQEC
HHHHCCCHHHHHHHH		52.36-
91PhosphorylationEQEMQECTTQIQYLK
HHHHHHHHHHHHHHH		22.4529759185
92PhosphorylationQEMQECTTQIQYLKQ
HHHHHHHHHHHHHHH		35.0229759185
98UbiquitinationTTQIQYLKQVQQPSV
HHHHHHHHHCCCCCH		43.41-
104PhosphorylationLKQVQQPSVAQLRST
HHHCCCCCHHHHHHH		26.2524043423
123 (in isoform 2)Ubiquitination-33.1521890473
123UbiquitinationAINLFFLKMKGELEQ
HHHHHHHHHHHHHHH		33.1521890473
123UbiquitinationAINLFFLKMKGELEQ
HHHHHHHHHHHHHHH		33.1521890473
123 (in isoform 1)Ubiquitination-33.1521890473
125SumoylationNLFFLKMKGELEQTK
HHHHHHHHHHHHHHH		47.87-
125 (in isoform 1)Ubiquitination-47.8721890473
125SumoylationNLFFLKMKGELEQTK
HHHHHHHHHHHHHHH		47.87-
125UbiquitinationNLFFLKMKGELEQTK
HHHHHHHHHHHHHHH		47.8721906983
125 (in isoform 2)Ubiquitination-47.8721890473
134 (in isoform 1)Ubiquitination-56.3221890473
134UbiquitinationELEQTKDKLEQAQNE
HHHHHHHHHHHHHHH		56.322190698
134 (in isoform 2)Ubiquitination-56.3221890473
146 (in isoform 2)Ubiquitination-38.7921890473
146UbiquitinationQNELSAWKFTPDSQT
HHHHHHCCCCCCCHH		38.79-
148PhosphorylationELSAWKFTPDSQTGK
HHHHCCCCCCCHHHH		23.5921815630
155AcetylationTPDSQTGKKLMAKCR
CCCCHHHHHHHHHHH		46.2325953088
163SulfoxidationKLMAKCRMLIQENQE
HHHHHHHHHHHHHHH		5.6121406390
191UbiquitinationEAELALQKKYSEELK
HHHHHHHHHHHHHHH		55.30-
239PhosphorylationTRQQLAQYQQQQSQA
HHHHHHHHHHHHHHC		11.5926714015
244PhosphorylationAQYQQQQSQASAPST
HHHHHHHHHCCCCCC		24.3117525332
250PhosphorylationQSQASAPSTSRTTAS
HHHCCCCCCCCCCCC		38.4428555341
254PhosphorylationSAPSTSRTTASEPVE
CCCCCCCCCCCCCCC		26.8723312004
255PhosphorylationAPSTSRTTASEPVEQ
CCCCCCCCCCCCCCC		27.3823312004
257PhosphorylationSTSRTTASEPVEQSE
CCCCCCCCCCCCCCC		40.1023312004
263PhosphorylationASEPVEQSEATSKDC
CCCCCCCCCCCCCCH		18.7223312004
266PhosphorylationPVEQSEATSKDCSRL
CCCCCCCCCCCHHHH		32.0523312004
267PhosphorylationVEQSEATSKDCSRLT
CCCCCCCCCCHHHHC		33.2821712546
268AcetylationEQSEATSKDCSRLTN
CCCCCCCCCHHHHCC		59.4025953088
271PhosphorylationEATSKDCSRLTNGPS
CCCCCCHHHHCCCCC		40.2226074081
274PhosphorylationSKDCSRLTNGPSNGS
CCCHHHHCCCCCCCC		36.7022199227
278PhosphorylationSRLTNGPSNGSSSRQ
HHHCCCCCCCCCCCC		56.0426074081
281PhosphorylationTNGPSNGSSSRQRTS
CCCCCCCCCCCCCCC		29.4122199227
282PhosphorylationNGPSNGSSSRQRTSG
CCCCCCCCCCCCCCC		30.8226074081
283PhosphorylationGPSNGSSSRQRTSGS
CCCCCCCCCCCCCCC		33.8426074081
287PhosphorylationGSSSRQRTSGSGFHR
CCCCCCCCCCCCCCC		29.1520068231
288PhosphorylationSSSRQRTSGSGFHRE
CCCCCCCCCCCCCCC		32.9025159151
290PhosphorylationSRQRTSGSGFHREGN
CCCCCCCCCCCCCCC		37.7428985074
298PhosphorylationGFHREGNTTEDDFPS
CCCCCCCCCCCCCCC		42.2822167270
299PhosphorylationFHREGNTTEDDFPSS
CCCCCCCCCCCCCCC		41.2222167270
305PhosphorylationTTEDDFPSSPGNGNK
CCCCCCCCCCCCCCC		49.5129255136
306PhosphorylationTEDDFPSSPGNGNKS
CCCCCCCCCCCCCCC		36.7419664994
313PhosphorylationSPGNGNKSSNSSEER
CCCCCCCCCCCCCCC		38.4623312004
314PhosphorylationPGNGNKSSNSSEERT
CCCCCCCCCCCCCCC		42.2023312004
316PhosphorylationNGNKSSNSSEERTGR
CCCCCCCCCCCCCCC		40.8623312004
317PhosphorylationGNKSSNSSEERTGRG
CCCCCCCCCCCCCCC		47.9623312004
326PhosphorylationERTGRGGSGYVNQLS
CCCCCCCCCHHHHHH		29.7623663014
328PhosphorylationTGRGGSGYVNQLSAG
CCCCCCCHHHHHHCC		9.6423663014
333PhosphorylationSGYVNQLSAGYESVD
CCHHHHHHCCEECCC		15.1923663014
336PhosphorylationVNQLSAGYESVDSPT
HHHHHCCEECCCCCC		12.5423663014
338PhosphorylationQLSAGYESVDSPTGS
HHHCCEECCCCCCCC		23.8123663014
341PhosphorylationAGYESVDSPTGSENS
CCEECCCCCCCCCCC		23.3923927012
343PhosphorylationYESVDSPTGSENSLT
EECCCCCCCCCCCCC		58.2423927012
345PhosphorylationSVDSPTGSENSLTHQ
CCCCCCCCCCCCCCC		35.7623927012
348PhosphorylationSPTGSENSLTHQSND
CCCCCCCCCCCCCCC		30.5023927012
350PhosphorylationTGSENSLTHQSNDTD
CCCCCCCCCCCCCCC		20.0723663014
353PhosphorylationENSLTHQSNDTDSSH
CCCCCCCCCCCCCCC		29.1223663014
356PhosphorylationLTHQSNDTDSSHDPQ
CCCCCCCCCCCCCHH		41.8723663014
358PhosphorylationHQSNDTDSSHDPQEE
CCCCCCCCCCCHHHH		31.5023663014
359PhosphorylationQSNDTDSSHDPQEEK
CCCCCCCCCCHHHHH		34.4223663014
387PhosphorylationHVQNGLDSSVNVQGS
HHCCCCCCCEECCCC		41.0320068231
388PhosphorylationVQNGLDSSVNVQGSV
HCCCCCCCEECCCCC		19.8520068231
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 FL2D_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FL2D_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 FL2D_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WT1_HUMANWT1physical
11001926
MPPB_HUMANPMPCBphysical
22939629
IKZF1_HUMANIKZF1physical
25416956
VIR_HUMANKIAA1429physical
26344197
ZC3HD_HUMANZC3H13physical
26344197
CAH4_HUMANCA4physical
26071132
WT1_HUMANWT1physical
26071132
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 FL2D_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305 AND SER-306, ANDMASS SPECTROMETRY.
"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-306, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND MASSSPECTROMETRY.

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