PATL1_HUMAN - dbPTM
PATL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PATL1_HUMAN
UniProt AC Q86TB9
Protein Name Protein PAT1 homolog 1
Gene Name PATL1
Organism Homo sapiens (Human).
Sequence Length 770
Subcellular Localization Cytoplasm, P-body. Nucleus. Nucleus, PML body. Nucleus speckle. Predominantly cytoplasmic. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner. Enriched in splicing speckles. Localization to nuclear foci and speckles requires ac
Protein Description RNA-binding protein involved in deadenylation-dependent decapping of mRNAs, leading to the degradation of mRNAs. Acts as a scaffold protein that connects deadenylation and decapping machinery. Required for cytoplasmic mRNA processing body (P-body) assembly. In case of infection, required for translation and replication of hepatitis C virus (HCV)..
Protein Sequence MFRYESLEDCPLDEDEDAFQGLGEEDEEIDQFNDDTFGSGAVDDDWQEAHERLAELEEKLPVAVNEQTGNGERDEMDLLGDHEENLAERLSKMVIENELEDPAIMRAVQTRPVLQPQPGSLNSSIWDGSEVLRRIRGPLLAQEMPTVSVLEYALPQRPPQGPEDDRDLSERALPRRSTSPIIGSPPVRAVPIGTPPKQMAVPSFTQQILCPKPVHVRPPMPPRYPAPYGERMSPNQLCSVPNSSLLGHPFPPSVPPVLSPLQRAQLLGGAQLQPGRMSPSQFARVPGFVGSPLAAMNPKLLQGRVGQMLPPAPGFRAFFSAPPSATPPPQQHPPGPGPHLQNLRSQAPMFRPDTTHLHPQHRRLLHQRQQQNRSQHRNLNGAGDRGSHRSSHQDHLRKDPYANLMLQREKDWVSKIQMMQLQSTDPYLDDFYYQNYFEKLEKLSAAEEIQGDGPKKERTKLITPQVAKLEHAYKPVQFEGSLGKLTVSSVNNPRKMIDAVVTSRSEDDETKEKQVRDKRRKTLVIIEKTYSLLLDVEDYERRYLLSLEEERPALMDDRKHKICSMYDNLRGKLPGQERPSDDHFVQIMCIRKGKRMVARILPFLSTEQAADILMTTARNLPFLIKKDAQDEVLPCLLSPFSLLLYHLPSVSITSLLRQLMNLPQSAATPALSNPHLTAVLQNKFGLSLLLILLSRGEDLQSSDPATESTQNNQWTEVMFMATRELLRIPQAALAKPISIPTNLVSLFSRYVDRQKLNLLETKLQLVQGIR
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
6Phosphorylation--MFRYESLEDCPLD
--CCCCCCCCCCCCC		28.2928348404
59UbiquitinationRLAELEEKLPVAVNE
HHHHHHHHCCEEEEC		49.0329967540
68PhosphorylationPVAVNEQTGNGERDE
CEEEECCCCCCCCCH		26.8328555341
73MethylationEQTGNGERDEMDLLG
CCCCCCCCCHHHHHC		46.73115486517
91PhosphorylationENLAERLSKMVIENE
HHHHHHHHHHHHHCC		25.5628555341
92UbiquitinationNLAERLSKMVIENEL
HHHHHHHHHHHHCCC		41.6024816145
93SulfoxidationLAERLSKMVIENELE
HHHHHHHHHHHCCCC		3.0921406390
120PhosphorylationVLQPQPGSLNSSIWD
CCCCCCCCCCCCCCC		30.9425850435
123PhosphorylationPQPGSLNSSIWDGSE
CCCCCCCCCCCCHHH		28.6125850435
124PhosphorylationQPGSLNSSIWDGSEV
CCCCCCCCCCCHHHH		26.9929978859
129PhosphorylationNSSIWDGSEVLRRIR
CCCCCCHHHHHHHHC		23.2729523821
146PhosphorylationLLAQEMPTVSVLEYA
HHHCCCCCEEEEHHH		24.8928796482
148PhosphorylationAQEMPTVSVLEYALP
HCCCCCEEEEHHHCC		24.3828796482
152PhosphorylationPTVSVLEYALPQRPP
CCEEEEHHHCCCCCC		14.8528796482
169PhosphorylationPEDDRDLSERALPRR
CCCCCCHHHHCCCCC		29.3524719451
177PhosphorylationERALPRRSTSPIIGS
HHCCCCCCCCCCCCC		34.2229255136
178PhosphorylationRALPRRSTSPIIGSP
HCCCCCCCCCCCCCC		36.3929255136
179PhosphorylationALPRRSTSPIIGSPP
CCCCCCCCCCCCCCC		18.4919664994
184PhosphorylationSTSPIIGSPPVRAVP
CCCCCCCCCCCEEEC		18.6723927012
194PhosphorylationVRAVPIGTPPKQMAV
CEEECCCCCCHHHCC		36.8230266825
203PhosphorylationPKQMAVPSFTQQILC
CHHHCCCCCCEEECC		34.0430576142
205PhosphorylationQMAVPSFTQQILCPK
HHCCCCCCEEECCCC		24.7330576142
217Asymmetric dimethylarginineCPKPVHVRPPMPPRY
CCCCCCCCCCCCCCC		18.09-
217MethylationCPKPVHVRPPMPPRY
CCCCCCCCCCCCCCC		18.0924129315
223Asymmetric dimethylarginineVRPPMPPRYPAPYGE
CCCCCCCCCCCCCCC		44.17-
223MethylationVRPPMPPRYPAPYGE
CCCCCCCCCCCCCCC		44.1724129315
233PhosphorylationAPYGERMSPNQLCSV
CCCCCCCCHHHCCCC		27.2428450419
233 (in isoform 4)Phosphorylation-27.2425849741
239PhosphorylationMSPNQLCSVPNSSLL
CCHHHCCCCCCHHHC		49.5628450419
239 (in isoform 4)Phosphorylation-49.5626552605
243PhosphorylationQLCSVPNSSLLGHPF
HCCCCCCHHHCCCCC		19.1228450419
244PhosphorylationLCSVPNSSLLGHPFP
CCCCCCHHHCCCCCC		33.9628450419
248 (in isoform 4)Phosphorylation-22.3128634298
250 (in isoform 4)Phosphorylation-13.2628634298
253PhosphorylationLGHPFPPSVPPVLSP
CCCCCCCCCCCCCCH		47.7128450419
259PhosphorylationPSVPPVLSPLQRAQL
CCCCCCCCHHHHHHH		24.65-
263Asymmetric dimethylargininePVLSPLQRAQLLGGA
CCCCHHHHHHHHCCC		31.80-
263MethylationPVLSPLQRAQLLGGA
CCCCHHHHHHHHCCC		31.8024129315
276MethylationGAQLQPGRMSPSQFA
CCCCCCCCCCHHHHH		29.14115387403
278PhosphorylationQLQPGRMSPSQFARV
CCCCCCCCHHHHHCC		21.7523401153
280PhosphorylationQPGRMSPSQFARVPG
CCCCCCHHHHHCCCC		30.5322199227
284Asymmetric dimethylarginineMSPSQFARVPGFVGS
CCHHHHHCCCCCCCC		36.13-
284MethylationMSPSQFARVPGFVGS
CCHHHHHCCCCCCCC		36.1352717369
291PhosphorylationRVPGFVGSPLAAMNP
CCCCCCCCCHHHHCH		16.0725159151
292UbiquitinationVPGFVGSPLAAMNPK
CCCCCCCCHHHHCHH		21.7924816145
296SulfoxidationVGSPLAAMNPKLLQG
CCCCHHHHCHHHHCC		7.9921406390
299UbiquitinationPLAAMNPKLLQGRVG
CHHHHCHHHHCCCCC		57.75-
316DimethylationLPPAPGFRAFFSAPP
CCCCCCCCHHCCCCC		36.08-
316MethylationLPPAPGFRAFFSAPP
CCCCCCCCHHCCCCC		36.0830762841
320PhosphorylationPGFRAFFSAPPSATP
CCCCHHCCCCCCCCC		33.15-
324PhosphorylationAFFSAPPSATPPPQQ
HHCCCCCCCCCCCCC		43.6528348404
326PhosphorylationFSAPPSATPPPQQHP
CCCCCCCCCCCCCCC		40.4424719451
344MethylationGPHLQNLRSQAPMFR
CHHHHHHHHCCCCCC		33.98115486509
351MethylationRSQAPMFRPDTTHLH
HHCCCCCCCCCCCCC		23.18115486533
374PhosphorylationQRQQQNRSQHRNLNG
HHHHHHHHHCCCCCC		37.58-
385MethylationNLNGAGDRGSHRSSH
CCCCCCCCCCCCCCC		47.8215315067
387PhosphorylationNGAGDRGSHRSSHQD
CCCCCCCCCCCCCCH		19.3428348404
401PhosphorylationDHLRKDPYANLMLQR
HHHHHCCCHHHHHHH		20.46-
424PhosphorylationQMMQLQSTDPYLDDF
HHHHHCCCCCCHHHH		28.2130576142
436PhosphorylationDDFYYQNYFEKLEKL
HHHHHHHHHHHHHHH		9.5130576142
442UbiquitinationNYFEKLEKLSAAEEI
HHHHHHHHHHHHHHH		59.1729967540
444PhosphorylationFEKLEKLSAAEEIQG
HHHHHHHHHHHHHCC		36.1830576142
4552-HydroxyisobutyrylationEIQGDGPKKERTKLI
HHCCCCCCHHHCCCC		73.18-
460UbiquitinationGPKKERTKLITPQVA
CCCHHHCCCCCHHHH		44.0829967540
463PhosphorylationKERTKLITPQVAKLE
HHHCCCCCHHHHHCC		20.3628555341
468UbiquitinationLITPQVAKLEHAYKP
CCCHHHHHCCCCCCC		56.4029967540
473PhosphorylationVAKLEHAYKPVQFEG
HHHCCCCCCCEEEEC		20.1029978859
474AcetylationAKLEHAYKPVQFEGS
HHCCCCCCCEEEECC		39.2225953088
474UbiquitinationAKLEHAYKPVQFEGS
HHCCCCCCCEEEECC		39.2229967540
481PhosphorylationKPVQFEGSLGKLTVS
CCEEEECCCCEEEEC		27.1020873877
481UbiquitinationKPVQFEGSLGKLTVS
CCEEEECCCCEEEEC		27.1024816145
484AcetylationQFEGSLGKLTVSSVN
EEECCCCEEEECCCC		46.4025953088
484UbiquitinationQFEGSLGKLTVSSVN
EEECCCCEEEECCCC		46.4029967540
488PhosphorylationSLGKLTVSSVNNPRK
CCCEEEECCCCCHHH		24.2728857561
489PhosphorylationLGKLTVSSVNNPRKM
CCEEEECCCCCHHHE		25.2428857561
495AcetylationSSVNNPRKMIDAVVT
CCCCCHHHEEEEEEE		41.2726051181
495UbiquitinationSSVNNPRKMIDAVVT
CCCCCHHHEEEEEEE		41.27-
502PhosphorylationKMIDAVVTSRSEDDE
HEEEEEEECCCCCHH		16.3026261332
503PhosphorylationMIDAVVTSRSEDDET
EEEEEEECCCCCHHH		23.3824719451
505PhosphorylationDAVVTSRSEDDETKE
EEEEECCCCCHHHHH		45.1828348404
510PhosphorylationSRSEDDETKEKQVRD
CCCCCHHHHHHHHHH		52.0428102081
511UbiquitinationRSEDDETKEKQVRDK
CCCCHHHHHHHHHHH		61.9524816145
522PhosphorylationVRDKRRKTLVIIEKT
HHHHHHCEEEEEEEE		25.1723312004
546PhosphorylationYERRYLLSLEEERPA
HHHHHHHCHHHHCCC		31.0119664994
566PhosphorylationKHKICSMYDNLRGKL
HHHHHHHHHHHCCCC		5.8427642862
625AcetylationRNLPFLIKKDAQDEV
HCCCEEEECCCCCCH		46.9123749302
625MalonylationRNLPFLIKKDAQDEV
HCCCEEEECCCCCCH		46.9132601280
634 (in isoform 4)Phosphorylation-16.3424043423
635 (in isoform 4)Phosphorylation-5.3724043423
638PhosphorylationEVLPCLLSPFSLLLY
CHHHHHHCHHHHHHH		15.7928842319
639 (in isoform 4)Phosphorylation-23.8624043423
641PhosphorylationPCLLSPFSLLLYHLP
HHHHCHHHHHHHHCC		22.8428842319
641 (in isoform 4)Phosphorylation-22.8424043423
642 (in isoform 4)Phosphorylation-3.8024043423
648 (in isoform 4)Phosphorylation-21.2624043423
651PhosphorylationLYHLPSVSITSLLRQ
HHHCCCCCHHHHHHH		25.2028842319
654PhosphorylationLPSVSITSLLRQLMN
CCCCCHHHHHHHHHC		24.6024719451
655 (in isoform 4)Phosphorylation-3.2424043423
735UbiquitinationIPQAALAKPISIPTN
CCHHHHCCCCCCCHH		43.67-
738PhosphorylationAALAKPISIPTNLVS
HHHCCCCCCCHHHHH		30.9227067055
762UbiquitinationKLNLLETKLQLVQGI
HHHHHHHHHHHHHCC		25.5129967540
770MethylationLQLVQGIR-------
HHHHHCCC-------		47.51115486525
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
179SPhosphorylationKinaseMTORP42345
PSP
184SPhosphorylationKinaseMTORP42345
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PATL1_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 PATL1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
PRPF3_HUMANPRPF3physical
22939629
PRP4_HUMANPRPF4physical
22939629
SNUT1_HUMANSART1physical
22939629
SF3A1_HUMANSF3A1physical
22939629
PHF20_HUMANPHF20physical
22939629
DDX6_HUMANDDX6physical
23851565
PRPF3_HUMANPRPF3physical
26344197
LRFN4_HUMANLRFN4physical
28514442
MY18A_HUMANMYO18Aphysical
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 PATL1_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-177; SER-179; SER-184AND SER-278, AND MASS 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 THR-178; SER-179 ANDSER-184, AND MASS SPECTROMETRY.
"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-177; SER-179 ANDSER-184, AND MASS SPECTROMETRY.

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