RN145_HUMAN - dbPTM
RN145_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RN145_HUMAN
UniProt AC Q96MT1
Protein Name RING finger protein 145 {ECO:0000305}
Gene Name RNF145 {ECO:0000312|PROSITE:PS50089}
Organism Homo sapiens (Human).
Sequence Length 663
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description E3 ubiquitin ligase that catalyzes the direct transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a specific substrate. In response to bacterial infection, negatively regulates the phagocyte oxidative burst by controlling the turnover of the NADPH oxidase complex subunits. Promotes monoubiquitination of CYBA and 'Lys-48'-linked polyubiquitination and degradation of CYBB NADPH oxidase catalytic subunits, both essential for the generation of antimicrobial reactive oxygen species. Involved in the maintenance of cholesterol homeostasis. In response to high sterol concentrations ubiquitinates HMGCR, a rate-limiting enzyme in cholesterol biosynthesis, and targets it for degradation. The interaction with INSIG1 is required for this function. In addition, triggers ubiquitination of SCAP, likely inhibiting its transport to the Golgi apparatus and the subsequent processing/maturation of SREBPF2, ultimately downregulating cholesterol biosynthesis..
Protein Sequence MAAKEKLEAVLNVALRVPSIMLLDVLYRWDVSSFFQQIQRSSLSNNPLFQYKYLALNMHYVGYILSVVLLTLPRQHLVQLYLYFLTALLLYAGHQISRDYVRSELEFAYEGPMYLEPLSMNRFTTALIGQLVVCTLCSCVMKTKQIWLFSAHMLPLLARLCLVPLETIVIINKFAMIFTGLEVLYFLGSNLLVPYNLAKSAYRELVQVVEVYGLLALGMSLWNQLVVPVLFMVFWLVLFALQIYSYFSTRDQPASRERLLFLFLTSIAECCSTPYSLLGLVFTVSFVALGVLTLCKFYLQGYRAFMNDPAMNRGMTEGVTLLILAVQTGLIELQVVHRAFLLSIILFIVVASILQSMLEIADPIVLALGASRDKSLWKHFRAVSLCLFLLVFPAYMAYMICQFFHMDFWLLIIISSSILTSLQVLGTLFIYVLFMVEEFRKEPVENMDDVIYYVNGTYRLLEFLVALCVVAYGVSETIFGEWTVMGSMIIFIHSYYNVWLRAQLGWKSFLLRRDAVNKIKSLPIATKEQLEKHNDICAICYQDMKSAVITPCSHFFHAGCLKKWLYVQETCPLCHCHLKNSSQLPGLGTEPVLQPHAGAEQNVMFQEGTEPPGQEHTPGTRIQEGSRDNNEYIARRPDNQEGAFDPKEYPHSAKDEAHPVESA
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
9 (in isoform 2)Phosphorylation-22.8722210691
9 (in isoform 5)Phosphorylation-22.8730631047
11 (in isoform 5)Phosphorylation-5.7130631047
13 (in isoform 5)Phosphorylation-4.6730631047
15 (in isoform 5)Phosphorylation-5.0330631047
18PhosphorylationLNVALRVPSIMLLDV
HHHHHHCCHHHHHHH
16.23-
18 (in isoform 2)Phosphorylation-16.23-
19PhosphorylationNVALRVPSIMLLDVL
HHHHHCCHHHHHHHH
20.1327732954
20 (in isoform 5)Phosphorylation-1.5230631047
53PhosphorylationNPLFQYKYLALNMHY
CCCHHHHHHHHHHHH
7.7124043423
60PhosphorylationYLALNMHYVGYILSV
HHHHHHHHHHHHHHH
5.7024043423
63PhosphorylationLNMHYVGYILSVVLL
HHHHHHHHHHHHHHH
6.6624043423
66PhosphorylationHYVGYILSVVLLTLP
HHHHHHHHHHHHHCC
10.7124043423
71PhosphorylationILSVVLLTLPRQHLV
HHHHHHHHCCHHHHH
30.4724719451
298PhosphorylationVLTLCKFYLQGYRAF
HHHHHHHHHHHHHHH
5.43-
352PhosphorylationILFIVVASILQSMLE
HHHHHHHHHHHHHHH
16.54-
507 (in isoform 1)Ubiquitination-29.5421890473
507UbiquitinationLRAQLGWKSFLLRRD
HHHHHCCCHHHHCHH
29.54-
508PhosphorylationRAQLGWKSFLLRRDA
HHHHCCCHHHHCHHH
18.0224719451
520UbiquitinationRDAVNKIKSLPIATK
HHHHHHHHCCCCCCH
47.77-
520 (in isoform 1)Ubiquitination-47.7721890473
521PhosphorylationDAVNKIKSLPIATKE
HHHHHHHCCCCCCHH
42.74-
527 (in isoform 1)Ubiquitination-34.1521890473
527UbiquitinationKSLPIATKEQLEKHN
HCCCCCCHHHHHHCC
34.15-
532UbiquitinationATKEQLEKHNDICAI
CCHHHHHHCCCEEEE
57.19-
535 (in isoform 2)Ubiquitination-36.7421890473
535UbiquitinationEQLEKHNDICAICYQ
HHHHHCCCEEEEHHH
36.7421890473
535UbiquitinationEQLEKHNDICAICYQ
HHHHHCCCEEEEHHH
36.7421890473
535UbiquitinationEQLEKHNDICAICYQ
HHHHHCCCEEEEHHH
36.7421890473
545UbiquitinationAICYQDMKSAVITPC
EEHHHCHHHCEEECC
43.48-
548 (in isoform 2)Ubiquitination-6.9021890473
555 (in isoform 2)Ubiquitination-2.4921890473
562UbiquitinationFFHAGCLKKWLYVQE
HCCCCHHHHHHHHCC
46.08-
563UbiquitinationFHAGCLKKWLYVQET
CCCCHHHHHHHHCCC
29.50-
647UbiquitinationQEGAFDPKEYPHSAK
CCCCCCCCCCCCCCC
72.26-
662 (in isoform 5)Phosphorylation-39.2427642862

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 RN145_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RN145_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 RN145_HUMAN !!

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

Oops, there are no PPI records of RN145_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RN145_HUMAN

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Related Literatures of Post-Translational Modification

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