HMOX1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HMOX1_HUMAN
• UniProt AC: P09601
• Protein Name: Heme oxygenase 1
• Gene Name: HMOX1
• Organism: Homo sapiens (Human).
• Sequence Length: 288
• 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: MERPQPDSMPQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYVALEEEIERNKESPVFAPVYFPEELHRKAALEQDLAFWYGPRWQEVIPYTPAMQRYVKRLHEVGRTEPELLVAHAYTRYLGDLSGGQVLKKIAQKALDLPSSGEGLAFFTFPNIASATKFKQLYRSRMNSLEMTPAVRQRVIEEAKTAFLLNIQLFEELQELLTHDTKDQSPSRAPGLRQRASNKVQDSAPVETPRGKPPLNTRSQAPLLRWVLTLSFLVATVAVGLYAM

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
1	Acetylation	-------MERPQPDS -------CCCCCCCC	9.95	-
8	Phosphorylation	MERPQPDSMPQDLSE CCCCCCCCCCHHHHH	38.76	24706070
18	Acetylation	QDLSEALKEATKEVH HHHHHHHHHHHHHHH	52.96	20167786
18	Ubiquitination	QDLSEALKEATKEVH HHHHHHHHHHHHHHH	52.96	21906983
18	Malonylation	QDLSEALKEATKEVH HHHHHHHHHHHHHHH	52.96	26320211
22	Malonylation	EALKEATKEVHTQAE HHHHHHHHHHHHHHH	65.86	26320211
22	Ubiquitination	EALKEATKEVHTQAE HHHHHHHHHHHHHHH	65.86	-
39	Malonylation	EFMRNFQKGQVTRDG HHHHHHCCCCCCHHH	47.36	26320211
39	Acetylation	EFMRNFQKGQVTRDG HHHHHHCCCCCCHHH	47.36	19608861
39	Ubiquitination	EFMRNFQKGQVTRDG HHHHHHCCCCCCHHH	47.36	21906983
53	Phosphorylation	GFKLVMASLYHIYVA HHHHHHHHHHHHHHH	16.03	22210691
55	Phosphorylation	KLVMASLYHIYVALE HHHHHHHHHHHHHHH	5.44	22210691
58	Phosphorylation	MASLYHIYVALEEEI HHHHHHHHHHHHHHH	2.65	-
69	Ubiquitination	EEEIERNKESPVFAP HHHHHHCCCCCCCCC	66.83	6983
86	Ubiquitination	FPEELHRKAALEQDL CCHHHHHHHHHHHCH	27.54	21906983
108	Phosphorylation	WQEVIPYTPAMQRYV HHHHCCCCHHHHHHH	10.14	-
114	Phosphorylation	YTPAMQRYVKRLHEV CCHHHHHHHHHHHHC	8.07	-
137	Phosphorylation	VAHAYTRYLGDLSGG HHHHHHHHHCCCCHH	13.77	20068231
142	Phosphorylation	TRYLGDLSGGQVLKK HHHHCCCCHHHHHHH	45.69	20068231
148	Ubiquitination	LSGGQVLKKIAQKAL CCHHHHHHHHHHHHC	43.19	21906983
149	Ubiquitination	SGGQVLKKIAQKALD CHHHHHHHHHHHHCC	38.83	-
153	Ubiquitination	VLKKIAQKALDLPSS HHHHHHHHHCCCCCC	41.73	21906983
160	Phosphorylation	KALDLPSSGEGLAFF HHCCCCCCCCCEECE	38.63	-
177	Ubiquitination	PNIASATKFKQLYRS CCHHHHHHHHHHHHH	50.73	21906983
179	Ubiquitination	IASATKFKQLYRSRM HHHHHHHHHHHHHHC	40.73	21906983
188	Phosphorylation	LYRSRMNSLEMTPAV HHHHHCHHHCCCHHH	19.16	21406692
192	Phosphorylation	RMNSLEMTPAVRQRV HCHHHCCCHHHHHHH	9.94	21406692
229	Phosphorylation	THDTKDQSPSRAPGL HCCCCCCCCCCCCCH	34.67	22167270
231	Phosphorylation	DTKDQSPSRAPGLRQ CCCCCCCCCCCCHHH	46.45	28287266
241	Phosphorylation	PGLRQRASNKVQDSA CCHHHHHCCCCCCCC	39.10	28857561
243	Ubiquitination	LRQRASNKVQDSAPV HHHHHCCCCCCCCCC	38.48	21906983
243	Acetylation	LRQRASNKVQDSAPV HHHHHCCCCCCCCCC	38.48	412439205
243	Malonylation	LRQRASNKVQDSAPV HHHHHCCCCCCCCCC	38.48	26320211
247	Phosphorylation	ASNKVQDSAPVETPR HCCCCCCCCCCCCCC	19.85	27134283
252	Phosphorylation	QDSAPVETPRGKPPL CCCCCCCCCCCCCCC	20.65	26055452
256	Ubiquitination	PVETPRGKPPLNTRS CCCCCCCCCCCCCCC	44.75	21906983
256	Acetylation	PVETPRGKPPLNTRS CCCCCCCCCCCCCCC	44.75	412439207
286	Phosphorylation	ATVAVGLYAM----- HHHHHHHHCC-----	8.49	-

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
188	S	Phosphorylation	Kinase	AKT1	P31749	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HMOX1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of HMOX1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HMOX1_HUMAN	HMOX1	physical	12500973
UFD1_HUMAN	UFD1L	physical	18544348
PSMD2_HUMAN	PSMD2	physical	18544348
KASH5_HUMAN	CCDC155	physical	25416956
CGT_HUMAN	UGT8	physical	26186194
TX264_HUMAN	TEX264	physical	26186194
1C07_HUMAN	HLA-C	physical	26186194
CGT_HUMAN	UGT8	physical	28514442
TX264_HUMAN	TEX264	physical	28514442
1C07_HUMAN	HLA-C	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 614034: Heme oxygenase 1 deficiency (HMOX1D)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• DB00163: Vitamin E

Related Literatures of Post-Translational Modification

Acetylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
PubMed: 19413330

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-39, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND MASSSPECTROMETRY.
PubMed: 17081983