RDM1_HUMAN - dbPTM
RDM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RDM1_HUMAN
UniProt AC Q8NG50
Protein Name RAD52 motif-containing protein 1
Gene Name RDM1
Organism Homo sapiens (Human).
Sequence Length 284
Subcellular Localization Nucleus . Cytoplasm . Nucleus, nucleolus . Isoform 3 and isoform 10 are predominantly nuclear and nucleolar. After treatment with proteasomal inhibitors and mild heat-shock stress, isoform 1, isoform 3, isoform 5, isoform 7, isoform 8 and isoform 10
Protein Description May confer resistance to the antitumor agent cisplatin. Binds to DNA and RNA..
Protein Sequence MAELVPFAVPIESDKTLLVWELSSGPTAEALHHSLFTAFSQFGLLYSVRVFPNAAVAHPGFYAVIKFYSARAAHRAQKACDRKQLFQKSPVKVRLGTRHKAVQHQALALNSSKCQELANYYFGFNGCSKRIIKLQELSDLEERENEDSMVPLPKQSLKFFCALEVVLPSCDCRSPGIGLVEEPMDKVEEGPLSFLMKRKTAQKLAIQKALSDAFQKLLIVVLESGKIAVEYRPSEDIVGVRCEEELHGLIQVPCSPWKQYGQEEEGYLSDFSLEEEEFRLPELD
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
16 (in isoform 7)Phosphorylation-30.2522210691
23 (in isoform 7)Phosphorylation-23.0222210691
24 (in isoform 7)Phosphorylation-62.5122210691
65UbiquitinationHPGFYAVIKFYSARA
CCCHHHHHHHHHHHH
1.6229967540
76 (in isoform 7)Phosphorylation-12.83-
77UbiquitinationARAAHRAQKACDRKQ
HHHHHHHHHHCCHHH
33.5629967540
78 (in isoform 7)Phosphorylation-50.42-
88UbiquitinationDRKQLFQKSPVKVRL
CHHHHHHHCCCEEEC
49.7629967540
100UbiquitinationVRLGTRHKAVQHQAL
EECCCCHHHHHHHHH
47.1429967540
106UbiquitinationHKAVQHQALALNSSK
HHHHHHHHHHCCCHH
7.8322817900
110 (in isoform 2)Ubiquitination-38.3321906983
110UbiquitinationQHQALALNSSKCQEL
HHHHHHCCCHHHHHH
38.3322817900
110 (in isoform 6)Ubiquitination-38.3321906983
113 (in isoform 4)Phosphorylation-39.49-
113UbiquitinationALALNSSKCQELANY
HHHCCCHHHHHHHHH
39.49-
115 (in isoform 4)Phosphorylation-53.10-
129UbiquitinationFGFNGCSKRIIKLQE
HCCCCHHHHHHHHHH
52.2522817900
133 (in isoform 5)Ubiquitination-41.5721906983
133UbiquitinationGCSKRIIKLQELSDL
CHHHHHHHHHHHHHH
41.5722817900
133 (in isoform 8)Ubiquitination-41.5721906983
133 (in isoform 1)Ubiquitination-41.5721906983
136 (in isoform 3)Phosphorylation-61.76-
138 (in isoform 3)Phosphorylation-39.12-
224PhosphorylationLLIVVLESGKIAVEY
HHHHHHCCCCEEEEE
41.02-

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 RDM1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RDM1_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 RDM1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RUVB2_HUMANRUVBL2physical
26186194
PI4KB_HUMANPI4KBphysical
26186194
PI4KB_HUMANPI4KBphysical
28514442
RUVB2_HUMANRUVBL2physical
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 RDM1_HUMAN

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Related Literatures of Post-Translational Modification

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