HMOX1_RAT - dbPTM
HMOX1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HMOX1_RAT
UniProt AC P06762
Protein Name Heme oxygenase 1
Gene Name Hmox1
Organism Rattus norvegicus (Rat).
Sequence Length 289
Subcellular Localization Microsome. Endoplasmic reticulum membrane
Peripheral membrane protein
Cytoplasmic side.
Protein Description Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis..
Protein Sequence MERPQLDSMSQDLSEALKEATKEVHIRAENSEFMRNFQKGQVSREGFKLVMASLYHIYTALEEEIERNKQNPVYAPLYFPEELHRRAALEQDMAFWYGPHWQEAIPYTPATQHYVKRLHEVGGTHPELLVAHAYTRYLGDLSGGQVLKKIAQKAMALPSSGEGLAFFTFPSIDNPTKFKQLYRARMNTLEMTPEVKHRVTEEAKTAFLLNIELFEELQALLTEEHKDQSPSQTEFLRQRPASLVQDTTSAETPRGKSQISTSSSQTPLLRWVLTLSFLLATVAVGIYAM
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
18AcetylationQDLSEALKEATKEVH
HHHHHHHHHHHHHHH
52.963937071
22AcetylationEALKEATKEVHIRAE
HHHHHHHHHHHHHHC
65.863937053
39AcetylationEFMRNFQKGQVSREG
HHHHHHHCCCCCHHH
47.363937047
48AcetylationQVSREGFKLVMASLY
CCCHHHHHHHHHHHH
51.533937065
69AcetylationEEEIERNKQNPVYAP
HHHHHHCCCCCCCCC
58.643937059
149AcetylationSGGQVLKKIAQKAMA
CHHHHHHHHHHHHCC
38.8318194664
153AcetylationVLKKIAQKAMALPSS
HHHHHHHHHCCCCCC
30.9818194664
179AcetylationIDNPTKFKQLYRARM
CCCCHHHHHHHHHHH
40.733937083
196AcetylationLEMTPEVKHRVTEEA
CCCCHHHHHHCCHHH
24.833937077
229PhosphorylationTEEHKDQSPSQTEFL
CHHHCCCCHHHHHHH
36.3325532521
231PhosphorylationEHKDQSPSQTEFLRQ
HHCCCCHHHHHHHHH
55.7922673903
233PhosphorylationKDQSPSQTEFLRQRP
CCCCHHHHHHHHHCC
32.8022673903
242PhosphorylationFLRQRPASLVQDTTS
HHHHCCHHHHCCCCC
31.5829779826
247PhosphorylationPASLVQDTTSAETPR
CHHHHCCCCCCCCCC
12.9323984901
248PhosphorylationASLVQDTTSAETPRG
HHHHCCCCCCCCCCC
33.9423984901
249PhosphorylationSLVQDTTSAETPRGK
HHHCCCCCCCCCCCC
26.6323984901
252PhosphorylationQDTTSAETPRGKSQI
CCCCCCCCCCCCCCC
20.2922027198
257PhosphorylationAETPRGKSQISTSSS
CCCCCCCCCCCCCCC
35.2519700791
260PhosphorylationPRGKSQISTSSSQTP
CCCCCCCCCCCCCCH
18.0130181290
261PhosphorylationRGKSQISTSSSQTPL
CCCCCCCCCCCCCHH
33.9730181290
262PhosphorylationGKSQISTSSSQTPLL
CCCCCCCCCCCCHHH
22.6230181290
263PhosphorylationKSQISTSSSQTPLLR
CCCCCCCCCCCHHHH
26.9319700791
264PhosphorylationSQISTSSSQTPLLRW
CCCCCCCCCCHHHHH
37.5330181290
266PhosphorylationISTSSSQTPLLRWVL
CCCCCCCCHHHHHHH
20.1830181290

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 HMOX1_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HMOX1_RAT !!

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 HMOX1_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC_RATUbcphysical
21073519

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HMOX1_RAT

loading...

Related Literatures of Post-Translational Modification

TOP