ANM7_HUMAN - dbPTM
ANM7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANM7_HUMAN
UniProt AC Q9NVM4
Protein Name Protein arginine N-methyltransferase 7
Gene Name PRMT7
Organism Homo sapiens (Human).
Sequence Length 692
Subcellular Localization Cytoplasm, cytosol . Nucleus .
Protein Description Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo..
Protein Sequence MKIFCSRANPTTGSVEWLEEDEHYDYHQEIARSSYADMLHDKDRNVKYYQGIRAAVSRVKDRGQKALVLDIGTGTGLLSMMAVTAGADFCYAIEVFKPMADAAVKIVEKNGFSDKIKVINKHSTEVTVGPEGDMPCRANILVTELFDTELIGEGALPSYEHAHRHLVEENCEAVPHRATVYAQLVESGRMWSWNKLFPIHVQTSLGEQVIVPPVDVESCPGAPSVCDIQLNQVSPADFTVLSDVLPMFSIDFSKQVSSSAACHSRRFEPLTSGRAQVVLSWWDIEMDPEGKIKCTMAPFWAHSDPEEMQWRDHWMQCVYFLPQEEPVVQGSALYLVAHHDDYCVWYSLQRTSPEKNERVRQMRPVCDCQAHLLWNRPRFGEINDQDRTDRYVQALRTVLKPDSVCLCVSDGSLLSVLAHHLGVEQVFTVESSAASHKLLRKIFKANHLEDKINIIEKRPELLTNEDLQGRKVSLLLGEPFFTTSLLPWHNLYFWYVRTAVDQHLGPGAMVMPQAASLHAVVVEFRDLWRIRSPCGDCEGFDVHIMDDMIKRALDFRESREAEPHPLWEYPCRSLSEPWQILTFDFQQPVPLQPLCAEGTVELRRPGQSHAAVLWMEYHLTPECTLSTGLLEPADPEGGCCWNPHCKQAVYFFSPAPDPRALLGGPRTVSYAVEFHPDTGDIIMEFRHADTPD
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
2Ubiquitination------MKIFCSRAN
------CCEECCCCC
44.48-
7Methylation-MKIFCSRANPTTGS
-CCEECCCCCCCCCC
39.29115488887
11PhosphorylationFCSRANPTTGSVEWL
ECCCCCCCCCCEEEC
43.5328348404
12PhosphorylationCSRANPTTGSVEWLE
CCCCCCCCCCEEECC
28.8128348404
14PhosphorylationRANPTTGSVEWLEED
CCCCCCCCEEECCCC
18.1228348404
24PhosphorylationWLEEDEHYDYHQEIA
ECCCCCCCCHHHHHH
19.0228796482
26PhosphorylationEEDEHYDYHQEIARS
CCCCCCCHHHHHHHH
9.7628796482
32MethylationDYHQEIARSSYADML
CHHHHHHHHHHHHHH
31.6258859143
42UbiquitinationYADMLHDKDRNVKYY
HHHHHCCCCCCCHHH
48.08-
47UbiquitinationHDKDRNVKYYQGIRA
CCCCCCCHHHHHHHH
41.61-
73PhosphorylationALVLDIGTGTGLLSM
EEEEEECCCCCHHHH
31.72-
109AcetylationAAVKIVEKNGFSDKI
HHHHHHHHCCCCCCE
52.0225953088
109UbiquitinationAAVKIVEKNGFSDKI
HHHHHHHHCCCCCCE
52.02-
115UbiquitinationEKNGFSDKIKVINKH
HHCCCCCCEEEEECC
43.14-
121UbiquitinationDKIKVINKHSTEVTV
CCEEEEECCCCEEEE
28.01-
179PhosphorylationEAVPHRATVYAQLVE
CCCCCCHHHHHHHHH
17.6321406692
181PhosphorylationVPHRATVYAQLVESG
CCCCHHHHHHHHHCC
5.5821406692
187PhosphorylationVYAQLVESGRMWSWN
HHHHHHHCCCCCCCC
24.9921406692
262S-nitrosylationQVSSSAACHSRRFEP
HCCCCHHHCCCCCCC
2.7519483679
262S-nitrosocysteineQVSSSAACHSRRFEP
HCCCCHHHCCCCCCC
2.75-
397PhosphorylationRYVQALRTVLKPDSV
HHHHHHHHHHCCCCE
30.9220068231
444UbiquitinationKLLRKIFKANHLEDK
HHHHHHHHHCCHHHH
52.32-
444MethylationKLLRKIFKANHLEDK
HHHHHHHHHCCHHHH
52.32115975693
451UbiquitinationKANHLEDKINIIEKR
HHCCHHHHHCHHHHC
28.42-
457UbiquitinationDKINIIEKRPELLTN
HHHCHHHHCHHHCCC
63.95-
531MethylationFRDLWRIRSPCGDCE
EHHHEEECCCCCCCC
26.44126257599
550UbiquitinationHIMDDMIKRALDFRE
EEHHHHHHHHHHHHH
25.61-

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 ANM7_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANM7_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 ANM7_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRDM1_HUMANPRDM1physical
18992153
CTCFL_HUMANCTCFLphysical
17048991
H2A2C_HUMANHIST2H2ACphysical
17048991
RSMB_HUMANSNRPBphysical
17709427
H31_HUMANHIST1H3Aphysical
22231400
ORF73_HHV8PHHV8GK18_gp81physical
22179613
SSRG_HUMANSSR3physical
26496610
REPS2_HUMANREPS2physical
26496610
GANAB_HUMANGANABphysical
26496610
ICE1_HUMANICE1physical
26496610

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 ANM7_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP