ANM3_HUMAN - dbPTM
ANM3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANM3_HUMAN
UniProt AC O60678
Protein Name Protein arginine N-methyltransferase 3
Gene Name PRMT3
Organism Homo sapiens (Human).
Sequence Length 531
Subcellular Localization Cytoplasm.
Protein Description Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in some proteins..
Protein Sequence MCSLASGATGGRGAVENEEDLPELSDSGDEAAWEDEDDADLPHGKQQTPCLFCNRLFTSAEETFSHCKSEHQFNIDSMVHKHGLEFYGYIKLINFIRLKNPTVEYMNSIYNPVPWEKEEYLKPVLEDDLLLQFDVEDLYEPVSVPFSYPNGLSENTSVVEKLKHMEARALSAEAALARAREDLQKMKQFAQDFVMHTDVRTCSSSTSVIADLQEDEDGVYFSSYGHYGIHEEMLKDKIRTESYRDFIYQNPHIFKDKVVLDVGCGTGILSMFAAKAGAKKVLGVDQSEILYQAMDIIRLNKLEDTITLIKGKIEEVHLPVEKVDVIISEWMGYFLLFESMLDSVLYAKNKYLAKGGSVYPDICTISLVAVSDVNKHADRIAFWDDVYGFKMSCMKKAVIPEAVVEVLDPKTLISEPCGIKHIDCHTTSISDLEFSSDFTLKITRTSMCTAIAGYFDIYFEKNCHNRVVFSTGPQSTKTHWKQTVFLLEKPFSVKAGEALKGKVTVHKNKKDPRSLTVTLTLNNSTQTYGLQ
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
2Acetylation------MCSLASGAT
------CCCCCCCCC		4.6119413330
3Phosphorylation-----MCSLASGATG
-----CCCCCCCCCC		26.1825159151
6 (in isoform 2)Phosphorylation-33.9625627689
6Phosphorylation--MCSLASGATGGRG
--CCCCCCCCCCCCC		33.9625627689
9 (in isoform 2)Phosphorylation-43.6325627689
9PhosphorylationCSLASGATGGRGAVE
CCCCCCCCCCCCCCC		43.6325627689
12 (in isoform 2)Phosphorylation-31.1025627689
12PhosphorylationASGATGGRGAVENEE
CCCCCCCCCCCCCCC		31.1025627689
25PhosphorylationEEDLPELSDSGDEAA
CCCCCCCCCCCCHHH		28.2420201521
27PhosphorylationDLPELSDSGDEAAWE
CCCCCCCCCCHHHCC		44.7820201521
69PhosphorylationETFSHCKSEHQFNID
HHHHHHCHHHCCCHH		45.7820873877
81MethylationNIDSMVHKHGLEFYG
CHHHHHHHCCHHHHH		28.1423644510
81"N6,N6-dimethyllysine"NIDSMVHKHGLEFYG
CHHHHHHHCCHHHHH		28.14-
87PhosphorylationHKHGLEFYGYIKLIN
HHCCHHHHHEEEHHE		10.3121059412
125UbiquitinationEEYLKPVLEDDLLLQ
HHHCHHHCCCCEEEE		8.9521890473
171PhosphorylationHMEARALSAEAALAR
HHHHHHHHHHHHHHH		24.0729978859
178MethylationSAEAALARAREDLQK
HHHHHHHHHHHHHHH		34.72115488831
187UbiquitinationREDLQKMKQFAQDFV
HHHHHHHHHHHHHHH		49.6621890473
200MethylationFVMHTDVRTCSSSTS
HHHCCCCCCCCCCCC		32.59115488839
240PhosphorylationMLKDKIRTESYRDFI
HHHHHHCCHHHHHHH		32.5328152594
242PhosphorylationKDKIRTESYRDFIYQ
HHHHCCHHHHHHHHC		25.5128152594
243PhosphorylationDKIRTESYRDFIYQN
HHHCCHHHHHHHHCC		14.1528152594
248PhosphorylationESYRDFIYQNPHIFK
HHHHHHHHCCCCCCC		11.3928152594
270PhosphorylationGCGTGILSMFAAKAG
CCCHHHHHHHHHHCC		15.2122817900
301UbiquitinationMDIIRLNKLEDTITL
HHHHHHHCCHHHEEE		58.82-
305PhosphorylationRLNKLEDTITLIKGK
HHHCCHHHEEEEECC		13.3924702127
307PhosphorylationNKLEDTITLIKGKIE
HCCHHHEEEEECCEE		25.2324702127
387PhosphorylationIAFWDDVYGFKMSCM
EEEHHHHHCCCCHHH		24.6827642862
396UbiquitinationFKMSCMKKAVIPEAV
CCCHHHHCCCCCHHH		22.47-
410UbiquitinationVVEVLDPKTLISEPC
HHHHCCHHHHCCCCC		56.48-
445PhosphorylationFTLKITRTSMCTAIA
CEEEEEEHHHHHHHC		16.5026552605
446PhosphorylationTLKITRTSMCTAIAG
EEEEEEHHHHHHHCE		14.4726552605
449PhosphorylationITRTSMCTAIAGYFD
EEEHHHHHHHCEEEE		16.6826552605
454PhosphorylationMCTAIAGYFDIYFEK
HHHHHCEEEEEEEEC		6.7726552605
458PhosphorylationIAGYFDIYFEKNCHN
HCEEEEEEEECCCCC		13.9226552605
477AcetylationSTGPQSTKTHWKQTV
ECCCCCCCCCCEEEE		43.5719828219
477UbiquitinationSTGPQSTKTHWKQTV
ECCCCCCCCCCEEEE		43.57-
492PhosphorylationFLLEKPFSVKAGEAL
EEEECCCCCCCCHHH		31.1023186163
525PhosphorylationTLTLNNSTQTYGLQ-
EEEECCCCCEECCC-		27.36-
527PhosphorylationTLNNSTQTYGLQ---
EECCCCCEECCC---		21.46-
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 ANM3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANM3_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 ANM3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RS2_HUMANRPS2physical
18573314
FBRL_HUMANFBLphysical
16157300
P53_HUMANTP53physical
21942715
ORF73_HHV8PHHV8GK18_gp81physical
22179613
STAT1_HUMANSTAT1physical
11257227
TERA_HUMANVCPphysical
22939629
ROA1_HUMANHNRNPA1physical
19101556
HIRP3_HUMANHIRIP3physical
22863883
IDE_HUMANIDEphysical
22863883
DNLI1_HUMANLIG1physical
22863883
RO60_HUMANTROVE2physical
22863883
XPO7_HUMANXPO7physical
22863883
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ANM3_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-25 AND SER-27, 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 SER-25 AND SER-27, AND MASSSPECTROMETRY.
"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-25 AND SER-27, 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-25 AND SER-27, AND MASSSPECTROMETRY.

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