HMOX2_HUMAN - dbPTM
HMOX2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HMOX2_HUMAN
UniProt AC P30519
Protein Name Heme oxygenase 2
Gene Name HMOX2
Organism Homo sapiens (Human).
Sequence Length 316
Subcellular Localization Microsome. Endoplasmic reticulum.
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. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter..
Protein Sequence MSAEVETSEGVDESEKKNSGALEKENQMRMADLSELLKEGTKEAHDRAENTQFVKDFLKGNIKKELFKLATTALYFTYSALEEEMERNKDHPAFAPLYFPMELHRKEALTKDMEYFFGENWEEQVQCPKAAQKYVERIHYIGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPSTGEGTQFYLFENVDNAQQFKQLYRARMNALDLNMKTKERIVEEANKAFEYNMQIFNELDQAGSTLARETLEDGFPVHDGKGDMRKCPFYAAEQDKGALEGSSCPFRTAMAVLRKPSLQFILAAGVALAAGLLAWYYM
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------MSAEVETSE
------CCCCEECCC
32.8930108239
2Acetylation------MSAEVETSE
------CCCCEECCC
32.8925944712
7Phosphorylation-MSAEVETSEGVDES
-CCCCEECCCCCCHH
36.9430108239
8PhosphorylationMSAEVETSEGVDESE
CCCCEECCCCCCHHH
20.8830108239
14PhosphorylationTSEGVDESEKKNSGA
CCCCCCHHHHHCCCH
50.6930108239
19PhosphorylationDESEKKNSGALEKEN
CHHHHHCCCHHHHHH
34.0328450419
24UbiquitinationKNSGALEKENQMRMA
HCCCHHHHHHHHHHH
63.92-
242-HydroxyisobutyrylationKNSGALEKENQMRMA
HCCCHHHHHHHHHHH
63.92-
30SulfoxidationEKENQMRMADLSELL
HHHHHHHHHHHHHHH
2.6021406390
34PhosphorylationQMRMADLSELLKEGT
HHHHHHHHHHHHHHH
27.0921712546
38UbiquitinationADLSELLKEGTKEAH
HHHHHHHHHHHHHHH
67.72-
38AcetylationADLSELLKEGTKEAH
HHHHHHHHHHHHHHH
67.7226051181
55UbiquitinationAENTQFVKDFLKGNI
HHHHHHHHHHHCCCH
44.0121890473
59UbiquitinationQFVKDFLKGNIKKEL
HHHHHHHCCCHHHHH
50.32-
592-HydroxyisobutyrylationQFVKDFLKGNIKKEL
HHHHHHHCCCHHHHH
50.32-
59MalonylationQFVKDFLKGNIKKEL
HHHHHHHCCCHHHHH
50.3226320211
79PhosphorylationTALYFTYSALEEEME
HHHHHHHHHHHHHHH
24.2614527438
109UbiquitinationELHRKEALTKDMEYF
HHHHHHHHHHHHHHH
6.8421890473
115PhosphorylationALTKDMEYFFGENWE
HHHHHHHHHHCCCHH
9.5126074081
157PhosphorylationVAHAYTRYMGDLSGG
HHHHHHHHHCCCCHH
9.5421406692
158SulfoxidationAHAYTRYMGDLSGGQ
HHHHHHHHCCCCHHH
2.8021406390
162PhosphorylationTRYMGDLSGGQVLKK
HHHHCCCCHHHHHHH
45.6921406692
1682-HydroxyisobutyrylationLSGGQVLKKVAQRAL
CCHHHHHHHHHHHHH
46.47-
169UbiquitinationSGGQVLKKVAQRALK
CHHHHHHHHHHHHHC
38.35-
176UbiquitinationKVAQRALKLPSTGEG
HHHHHHHCCCCCCCC
58.32-
179PhosphorylationQRALKLPSTGEGTQF
HHHHCCCCCCCCCEE
60.5228348404
180PhosphorylationRALKLPSTGEGTQFY
HHHCCCCCCCCCEEE
36.9928348404
184PhosphorylationLPSTGEGTQFYLFEN
CCCCCCCCEEEEEEC
15.9428348404
199UbiquitinationVDNAQQFKQLYRARM
CCCHHHHHHHHHHHH
34.75-
199AcetylationVDNAQQFKQLYRARM
CCCHHHHHHHHHHHH
34.7526051181
202PhosphorylationAQQFKQLYRARMNAL
HHHHHHHHHHHHHHH
10.34-
206SulfoxidationKQLYRARMNALDLNM
HHHHHHHHHHHCCCC
3.1630846556
213SulfoxidationMNALDLNMKTKERIV
HHHHCCCCCHHHHHH
8.3030846556
214AcetylationNALDLNMKTKERIVE
HHHCCCCCHHHHHHH
56.2025953088
214UbiquitinationNALDLNMKTKERIVE
HHHCCCCCHHHHHHH
56.20-
216AcetylationLDLNMKTKERIVEEA
HCCCCCHHHHHHHHH
39.2019813205
225UbiquitinationRIVEEANKAFEYNMQ
HHHHHHHHHHHHHHH
62.59-
229PhosphorylationEANKAFEYNMQIFNE
HHHHHHHHHHHHHHH
14.9629978859
242O-linked_GlycosylationNELDQAGSTLARETL
HHHHHHCCHHHHHHH
24.2229351928
242PhosphorylationNELDQAGSTLARETL
HHHHHHCCHHHHHHH
24.2224173317
243O-linked_GlycosylationELDQAGSTLARETLE
HHHHHCCHHHHHHHH
24.4229351928
259UbiquitinationGFPVHDGKGDMRKCP
CCCCCCCCCCHHCCC
58.77-
262SulfoxidationVHDGKGDMRKCPFYA
CCCCCCCHHCCCCCE
6.3421406390
264UbiquitinationDGKGDMRKCPFYAAE
CCCCCHHCCCCCEEC
39.35-
268PhosphorylationDMRKCPFYAAEQDKG
CHHCCCCCEECCCCC
7.0525159151
280PhosphorylationDKGALEGSSCPFRTA
CCCCCCCCCCHHHHH
21.2823312004
281PhosphorylationKGALEGSSCPFRTAM
CCCCCCCCCHHHHHH
36.3423312004
282S-nitrosylationGALEGSSCPFRTAMA
CCCCCCCCHHHHHHH
3.8522178444
286PhosphorylationGSSCPFRTAMAVLRK
CCCCHHHHHHHHHCC
22.59-
295PhosphorylationMAVLRKPSLQFILAA
HHHHCCCCHHHHHHH
37.5322496350
314PhosphorylationAAGLLAWYYM-----
HHHHHHHHHC-----
5.53-
315PhosphorylationAGLLAWYYM------
HHHHHHHHC------
5.90-

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 HMOX2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HMOX2_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 HMOX2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HAP1_HUMANHAP1physical
16169070
CSN6_HUMANCOPS6physical
16169070
GASP1_HUMANGPRASP1physical
16169070
SETB1_HUMANSETDB1physical
16169070
MED31_HUMANMED31physical
16169070
GIT1_HUMANGIT1physical
16169070
CE126_HUMANKIAA1377physical
16169070
LRIF1_HUMANLRIF1physical
16169070
EF1G_HUMANEEF1Gphysical
16169070
MIC60_HUMANIMMTphysical
21900206
EIF3C_HUMANEIF3Cphysical
21900206
TIP_HUMANITFG1physical
21900206
GCR_HUMANNR3C1physical
21900206
A2MG_HUMANA2Mphysical
21900206
NKRF_HUMANNKRFphysical
21900206
GIT1_HUMANGIT1physical
21900206
HAP1_HUMANHAP1physical
21900206
CE126_HUMANKIAA1377physical
21900206
ATPB_HUMANATP5Bphysical
21900206
PLXB2_HUMANPLXNB2physical
21900206
BL1S2_HUMANBLOC1S2physical
21900206
JADE1_HUMANJADE1physical
21900206
INP5K_HUMANINPP5Kphysical
21900206
ZFP28_HUMANZFP28physical
21900206
SHC1_HUMANSHC1physical
21900206
ZN746_HUMANZNF746physical
21900206
CEBPZ_HUMANCEBPZphysical
21900206
RBBP4_HUMANRBBP4physical
21900206
NDUS2_HUMANNDUFS2physical
21900206
SNX5_HUMANSNX5physical
21900206
SNX7_HUMANSNX7physical
21900206
SKA2_HUMANSKA2physical
21988832
POTEE_HUMANPOTEEphysical
26186194
SNG1_HUMANSYNGR1physical
26186194
TM214_HUMANTMEM214physical
26186194
ALG2_HUMANALG2physical
26186194
CGT_HUMANUGT8physical
26186194
PRAF2_HUMANPRAF2physical
26186194
GBB2_HUMANGNB2physical
26186194
ADPGK_HUMANADPGKphysical
26186194
CISD2_HUMANCISD2physical
26186194
PTN1_HUMANPTPN1physical
26186194
TM205_HUMANTMEM205physical
26186194
LMF2_HUMANLMF2physical
26186194
POTEE_HUMANPOTEEphysical
28514442
ALG2_HUMANALG2physical
28514442
CGT_HUMANUGT8physical
28514442
ADPGK_HUMANADPGKphysical
28514442
TM214_HUMANTMEM214physical
28514442
PRAF2_HUMANPRAF2physical
28514442
GBB2_HUMANGNB2physical
28514442
LMF2_HUMANLMF2physical
28514442
CISD2_HUMANCISD2physical
28514442
PTH2_HUMANPTRH2physical
28514442
TM205_HUMANTMEM205physical
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 HMOX2_HUMAN

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Related Literatures of Post-Translational Modification

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