ANM2_HUMAN - dbPTM
ANM2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANM2_HUMAN
UniProt AC P55345
Protein Name Protein arginine N-methyltransferase 2
Gene Name PRMT2
Organism Homo sapiens (Human).
Sequence Length 433
Subcellular Localization Isoform 1: Cytoplasm. Nucleus. Translocates from the cytoplasm to the nucleus, after hormone exposure. Excluded from nucleolus.
Isoform PRMT2Alpha: Nucleus. Excluded from nucleolus.
Isoform PRMT2Beta: Cytoplasm. Nucleus. Nucleus, nucleolus.
I
Protein Description Arginine methyltransferase that methylates the guanidino nitrogens of arginyl residues in proteins such as STAT3, FBL, histone H4. Acts as a coactivator (with NCOA2) of the androgen receptor (AR)-mediated transactivation. Acts as a coactivator (with estrogen) of estrogen receptor (ER)-mediated transactivation. Enhances PGR, PPARG, RARA-mediated transactivation. May inhibit NF-kappa-B transcription and promote apoptosis. Represses E2F1 transcriptional activity (in a RB1-dependent manner). May be involved in growth regulation..
Protein Sequence MATSGDCPRSESQGEEPAECSEAGLLQEGVQPEEFVAIADYAATDETQLSFLRGEKILILRQTTADWWWGERAGCCGYIPANHVGKHVDEYDPEDTWQDEEYFGSYGTLKLHLEMLADQPRTTKYHSVILQNKESLTDKVILDVGCGTGIISLFCAHYARPRAVYAVEASEMAQHTGQLVLQNGFADIITVYQQKVEDVVLPEKVDVLVSEWMGTCLLFEFMIESILYARDAWLKEDGVIWPTMAALHLVPCSADKDYRSKVLFWDNAYEFNLSALKSLAVKEFFSKPKYNHILKPEDCLSEPCTILQLDMRTVQISDLETLRGELRFDIRKAGTLHGFTAWFSVHFQSLQEGQPPQVLSTGPFHPTTHWKQTLFMMDDPVPVHTGDVVTGSVVLQRNPVWRRHMSVALSWAVTSRQDPTSQKVGEKVFPIWR
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
41PhosphorylationEFVAIADYAATDETQ
HHEEEEEEECCCHHH
6.7922817900
53MethylationETQLSFLRGEKILIL
HHHHHHHCCCEEEEE
49.5758854897
56UbiquitinationLSFLRGEKILILRQT
HHHHCCCEEEEEEEC
45.71-
61Asymmetric dimethylarginineGEKILILRQTTADWW
CCEEEEEEECCCCCC
25.46-
61MethylationGEKILILRQTTADWW
CCEEEEEEECCCCCC
25.4624129315
72Asymmetric dimethylarginineADWWWGERAGCCGYI
CCCCCCCCCCCCCEE
32.13-
72MethylationADWWWGERAGCCGYI
CCCCCCCCCCCCCEE
32.1324129315
86UbiquitinationIPANHVGKHVDEYDP
EEHHHCCCCCCCCCC
39.09-
124UbiquitinationADQPRTTKYHSVILQ
CCCCCCCCEEEEEEC
40.11-
125PhosphorylationDQPRTTKYHSVILQN
CCCCCCCEEEEEECC
9.3817322306
127PhosphorylationPRTTKYHSVILQNKE
CCCCCEEEEEECCCC
14.0428857561
133UbiquitinationHSVILQNKESLTDKV
EEEEECCCCCCCCCE
35.40-
222UbiquitinationTCLLFEFMIESILYA
HHHHHHHHHHHHHHH
2.33-
277UbiquitinationEFNLSALKSLAVKEF
HCCHHHHHHHHHHHH
43.04-
286PhosphorylationLAVKEFFSKPKYNHI
HHHHHHHCCCCCCCC
54.0624719451
406PhosphorylationPVWRRHMSVALSWAV
CCHHHHHHHHHHHHH
9.7124043423
410PhosphorylationRHMSVALSWAVTSRQ
HHHHHHHHHHHHCCC
11.8524043423
414PhosphorylationVALSWAVTSRQDPTS
HHHHHHHHCCCCCCC
15.5024043423
415PhosphorylationALSWAVTSRQDPTSQ
HHHHHHHCCCCCCCC
22.7324043423
427UbiquitinationTSQKVGEKVFPIWR-
CCCCCCCEEECCCC-
43.16-

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 ANM2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANM2_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 ANM2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DMRTB_HUMANDMRTB1physical
16189514
CPSF7_HUMANCPSF7physical
16189514
HNRL1_HUMANHNRNPUL1physical
11513728
ORF73_HHV8PHHV8GK18_gp81physical
22179613
ROA1_HUMANHNRNPA1physical
19101556
RB_HUMANRB1physical
16616919
PSB3_HUMANPSMB3physical
21988832
UBB_HUMANUBBphysical
26186194
SALL2_HUMANSALL2physical
26186194
GET4_HUMANGET4physical
26186194
SHAN3_HUMANSHANK3physical
26186194
HD_HUMANHTTphysical
26186194
TAB1_HUMANTAB1physical
26186194
KANK2_HUMANKANK2physical
26186194
LRFN1_HUMANLRFN1physical
26186194
PKHH3_HUMANPLEKHH3physical
26186194
P121A_HUMANPOM121physical
26186194
SF01_HUMANSF1physical
26186194
LMBL3_HUMANL3MBTL3physical
26186194
TIGD5_HUMANTIGD5physical
26186194
KSR1_HUMANKSR1physical
26186194
KRBA1_HUMANKRBA1physical
26186194
RBPMS_HUMANRBPMSphysical
26186194
PPM1E_HUMANPPM1Ephysical
26186194
ANTR1_HUMANANTXR1physical
26186194
TPC2A_HUMANTRAPPC2physical
26186194
TPC2B_HUMANTRAPPC2physical
26186194
SET1B_HUMANSETD1Bphysical
26186194
SET1A_HUMANSETD1Aphysical
26186194
P85A_HUMANPIK3R1physical
26186194
FHOD1_HUMANFHOD1physical
26186194
CXXC1_HUMANCXXC1physical
26186194
ERF_HUMANERFphysical
26186194
TTC28_HUMANTTC28physical
26186194
SETD5_HUMANSETD5physical
26186194
SAMD1_HUMANSAMD1physical
26186194
VCIP1_HUMANVCPIP1physical
26186194
CO039_HUMANC15orf39physical
26186194
M3K7_HUMANMAP3K7physical
26186194
LMBL3_HUMANL3MBTL3physical
28514442
SHAN3_HUMANSHANK3physical
28514442
HD_HUMANHTTphysical
28514442
SAMD1_HUMANSAMD1physical
28514442
KSR1_HUMANKSR1physical
28514442
UBB_HUMANUBBphysical
28514442
TIGD5_HUMANTIGD5physical
28514442
CXXC1_HUMANCXXC1physical
28514442
KRBA1_HUMANKRBA1physical
28514442
ERF_HUMANERFphysical
28514442
SET1B_HUMANSETD1Bphysical
28514442
FHOD1_HUMANFHOD1physical
28514442
SET1A_HUMANSETD1Aphysical
28514442
ANTR1_HUMANANTXR1physical
28514442
TTC28_HUMANTTC28physical
28514442
SETD5_HUMANSETD5physical
28514442
VCIP1_HUMANVCPIP1physical
28514442
PPM1E_HUMANPPM1Ephysical
28514442
CO039_HUMANC15orf39physical
28514442
P121A_HUMANPOM121physical
28514442
LRFN1_HUMANLRFN1physical
28514442
UBR5_HUMANUBR5physical
28514442
P85B_HUMANPIK3R2physical
28514442
SALL2_HUMANSALL2physical
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 ANM2_HUMAN

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Related Literatures of Post-Translational Modification

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