ANM9_HUMAN - dbPTM
ANM9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANM9_HUMAN
UniProt AC Q6P2P2
Protein Name Protein arginine N-methyltransferase 9
Gene Name PRMT9 {ECO:0000312|HGNC:HGNC:25099}
Organism Homo sapiens (Human).
Sequence Length 845
Subcellular Localization Cytoplasm .
Protein Description Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA). Specifically mediates the symmetrical dimethylation of SF3B2. Involved in the regulation of alternative splicing of pre-mRNA. [PubMed: 25737013]
Protein Sequence MSNSRPRSRRDAGGGAGAAGRDELVSRSLQSAEHCLGVQDFGTAYAHYLLVLSLAPELKHDVKETFQYTLFRWAEELDALSRIQDLLGCYEQALELFPDDEVICNSMGEHLFRMGFRDEAAGYFHKAVKLNPDFSDAKENFYRVANWLVERWHFIMLNDTKRNTIYNAAIQKAVCLGSKSVLDIGAGTGILSMFAKKAGAHSVYACELSKTMYELACDVVAANKMEAGIKLLHTKSLDIEIPKHIPERVSLVVTETVDAGLFGEGIVESLIHAWEHLLLQPKTKGESANCEKYGKVIPASAVIFGMAVECAEIRRHHRVGIKDIAGIHLPTNVKFQSPAYSSVDTEETIEPYTTEKMSRVPGGYLALTECFEIMTVDFNNLQELKSLATKKPDKIGIPVIKEGILDAIMVWFVLQLDDEHSLSTSPSEETCWEQAVYPVQDLADYWIKPGDHVMMEVSCQDCYLRIQSISVLGLECEMDVAKSFTQNKDLLSLGNEAELCSALANLQTSKPDAVEQTCILESTEIALLNNIPYHEGFKMAMSKVLSSLTPEKLYQTMDTHCQNEMSSGTGQSNTVQNILEPFYVLDVSEGFSVLPVIAGTLGQVKPYSSVEKDQHRIALDLISEANHFPKETLEFWLRHVEDESAMLQRPKSDKLWSIIILDVIEPSGLIQQEIMEKAAISRCLLQSGGKIFPQYVLMFGLLVESQTLLEENAVQGTERTLGLNIAPFINQFQVPIRVFLDLSSLPCIPLSKPVELLRLDLMTPYLNTSNREVKVYVCKSGRLTAIPFWYHMYLDEEIRLDTSSEASHWKQAAVVLDNPIQVEMGEELVLSIQHHKSNVSITVKQ
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------MSNSRPRSR
------CCCCCCCCC
24719451
8PhosphorylationMSNSRPRSRRDAGGG
CCCCCCCCCCCCCCC
24719451
13UbiquitinationPRSRRDAGGGAGAAG
CCCCCCCCCCCCCCC
-
16UbiquitinationRRDAGGGAGAAGRDE
CCCCCCCCCCCCHHH
27667366
16UbiquitinationRRDAGGGAGAAGRDE
CCCCCCCCCCCCHHH
-
25UbiquitinationAAGRDELVSRSLQSA
CCCHHHHHHHHHHHH
-
25UbiquitinationAAGRDELVSRSLQSA
CCCHHHHHHHHHHHH
29967540
48UbiquitinationFGTAYAHYLLVLSLA
HHHHHHHHHHHHHHC
-
51UbiquitinationAYAHYLLVLSLAPEL
HHHHHHHHHHHCHHH
21963094
59UbiquitinationLSLAPELKHDVKETF
HHHCHHHCCCHHHHH
-
84UbiquitinationLDALSRIQDLLGCYE
HHHHHHHHHHHHHHH
-
84UbiquitinationLDALSRIQDLLGCYE
HHHHHHHHHHHHHHH
29967540
111UbiquitinationCNSMGEHLFRMGFRD
ECCCHHHHHHCCCCH
-
117UbiquitinationHLFRMGFRDEAAGYF
HHHHCCCCHHHHHHH
-
117UbiquitinationHLFRMGFRDEAAGYF
HHHHCCCCHHHHHHH
22817900
122UbiquitinationGFRDEAAGYFHKAVK
CCCHHHHHHHHHEEC
-
122UbiquitinationGFRDEAAGYFHKAVK
CCCHHHHHHHHHEEC
21963094
126UbiquitinationEAAGYFHKAVKLNPD
HHHHHHHHEECCCCC
-
129UbiquitinationGYFHKAVKLNPDFSD
HHHHHEECCCCCCHH
27667366
135PhosphorylationVKLNPDFSDAKENFY
ECCCCCCHHHHHHHH
29743597
138UbiquitinationNPDFSDAKENFYRVA
CCCCHHHHHHHHHHH
29967540
161UbiquitinationFIMLNDTKRNTIYNA
EEECCCCCCCHHHHH
-
164PhosphorylationLNDTKRNTIYNAAIQ
CCCCCCCHHHHHHHH
30622161
166PhosphorylationDTKRNTIYNAAIQKA
CCCCCHHHHHHHHHH
30622161
172UbiquitinationIYNAAIQKAVCLGSK
HHHHHHHHHHHCCCC
-
192PhosphorylationGAGTGILSMFAKKAG
CCCCCHHHHHHHHHC
-
197UbiquitinationILSMFAKKAGAHSVY
HHHHHHHHHCCCEEE
29967540
209UbiquitinationSVYACELSKTMYELA
EEEEHHHCHHHHHHH
-
221UbiquitinationELACDVVAANKMEAG
HHHHHHHHHCHHHHC
29967540
224UbiquitinationCDVVAANKMEAGIKL
HHHHHHCHHHHCEEE
-
230UbiquitinationNKMEAGIKLLHTKSL
CHHHHCEEEEEECCC
22817900
235 (in isoform 1)Ubiquitination-21906983
235UbiquitinationGIKLLHTKSLDIEIP
CEEEEEECCCCEECC
21906983
236PhosphorylationIKLLHTKSLDIEIPK
EEEEEECCCCEECCC
28348404
243UbiquitinationSLDIEIPKHIPERVS
CCCEECCCCCCCCEE
21963094
243UbiquitinationSLDIEIPKHIPERVS
CCCEECCCCCCCCEE
-
277UbiquitinationLIHAWEHLLLQPKTK
HHHHHHHHHCCCCCC
29967540
322UbiquitinationRHHRVGIKDIAGIHL
HHHCCCCCCCCCCCC
-
334UbiquitinationIHLPTNVKFQSPAYS
CCCCCCCCCCCCCCC
29967540
337PhosphorylationPTNVKFQSPAYSSVD
CCCCCCCCCCCCCCC
-
348PhosphorylationSSVDTEETIEPYTTE
CCCCCCCCCCCCCCH
-
356 (in isoform 1)Ubiquitination-21906983
356UbiquitinationIEPYTTEKMSRVPGG
CCCCCCHHHHCCCCC
21963094
390UbiquitinationELKSLATKKPDKIGI
HHHHHHCCCCCCCCC
29967540
447UbiquitinationQDLADYWIKPGDHVM
HHHHHHCCCCCCEEE
21987572
538UbiquitinationIPYHEGFKMAMSKVL
CCCCHHHHHHHHHHH
29967540
547PhosphorylationAMSKVLSSLTPEKLY
HHHHHHHHCCHHHHH
28348404
549PhosphorylationSKVLSSLTPEKLYQT
HHHHHHCCHHHHHHH
23312004
639UbiquitinationTLEFWLRHVEDESAM
HHHHHHHHCCCHHHH
21987572
639UbiquitinationTLEFWLRHVEDESAM
HHHHHHHHCCCHHHH
-
651UbiquitinationSAMLQRPKSDKLWSI
HHHHCCCCCCCCEEE
29967540
652PhosphorylationAMLQRPKSDKLWSII
HHHCCCCCCCCEEEE
29116813
717PhosphorylationEENAVQGTERTLGLN
HHHCCCCCCCCCCCC
-
743PhosphorylationIRVFLDLSSLPCIPL
EEEEECCCCCCCEEC
23663014
744PhosphorylationRVFLDLSSLPCIPLS
EEEECCCCCCCEECC
23663014
751PhosphorylationSLPCIPLSKPVELLR
CCCCEECCCCHHHHH
23663014
752UbiquitinationLPCIPLSKPVELLRL
CCCEECCCCHHHHHH
21987572
779AcetylationEVKVYVCKSGRLTAI
EEEEEEECCCCCCEE
25953088

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 ANM9_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANM9_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 ANM9_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ANM9_HUMAN !!

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 ANM9_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP