Hmox1

Functionⁱ

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.

Catalytic activityⁱ

heme b
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+ 3
O₂
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+ 3
reduced [NADPH—hemoprotein reductase]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
=
biliverdin IXα
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
CO
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
Fe²⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
H⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+ 3
H₂O
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+ 3
oxidized [NADPH—hemoprotein reductase]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:O48782 (HMOX1_ARATH)
EC:1.14.14.18
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:O48782 (HMOX1_ARATH)
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
heme b
zoom
+
3
O₂
zoom
+
3
reduced [NADPH—hemoprotein reductase]
FMNH₂
zoom
=
biliverdin IXα
zoom
+
CO
zoom
+
Fe²⁺
zoom
+
H⁺
zoom
+
3
H₂O
zoom
+
3
oxidized [NADPH—hemoprotein reductase]
FMN
zoom

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	18	HemeBy similarity	1
Metal bindingⁱ	25	Iron (heme axial ligand)	1
Binding siteⁱ	134	HemeBy similarity	1
Binding siteⁱ	183	HemeBy similarity	1

GO - Molecular functionⁱ

enzyme binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 15516695
heme binding
Source: RGD
Inferred from direct assayⁱ
- 12044160
heme oxygenase (decyclizing) activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 3865203
metal ion binding Source: UniProtKB-KW
phospholipase D activity
Source: RGD
Inferred from direct assayⁱ
- 12511545
protein homodimerization activity Source: Ensembl

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

angiogenesis
Source: RGD
Inferred from direct assayⁱ
- 12593860
cell death
Source: BHF-UCL
Inferred from direct assayⁱ
- 17430897
cellular iron ion homeostasis Source: Ensembl
cellular response to arsenic-containing substance Source: Ensembl
cellular response to cadmium ion Source: Ensembl
cellular response to cisplatin Source: Ensembl
cellular response to heat Source: Ensembl
cellular response to hypoxia Source: Ensembl
cellular response to nutrient
Source: RGD
Inferred from expression patternⁱ
- 15531134
erythrocyte homeostasis Source: Ensembl
heme catabolic process
Source: RGD
Inferred from direct assayⁱ
- 15226268
heme oxidation
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
intracellular signal transduction
Source: RGD
Inferred from direct assayⁱ
- 12225959
intrinsic apoptotic signaling pathway in response to DNA damage
Source: RGD
Inferred from direct assayⁱ
- 11854317
iron ion homeostasis
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
liver regeneration
Source: RGD
Inferred from mutant phenotypeⁱ
- 24815159
negative regulation of cell proliferation
Source: RGD
Inferred from direct assayⁱ
- 16319139
negative regulation of DNA binding
Source: RGD
Inferred from direct assayⁱ
- 17234154
negative regulation of DNA-binding transcription factor activity
Source: RGD
Inferred from direct assayⁱ
- 17234154
negative regulation of epithelial cell apoptotic process
Source: RGD
Inferred from mutant phenotypeⁱ
- 22093310
negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
negative regulation of macroautophagy Source: Ensembl
negative regulation of mast cell cytokine production
Source: RGD
Inferred from direct assayⁱ
- 17234154
negative regulation of mast cell degranulation
Source: RGD
Inferred from direct assayⁱ
- 17234154
negative regulation of muscle cell apoptotic process
Source: RGD
Inferred from direct assayⁱ
- 12396617
negative regulation of neuron apoptotic process
Source: RGD
Inferred from mutant phenotypeⁱ
- 19177228
negative regulation of smooth muscle cell proliferation
Source: RGD
Inferred from mutant phenotypeⁱ
- 19885007
negative regulation of vascular smooth muscle cell proliferation
Source: RGD
Inferred from mutant phenotypeⁱ
- 22709785
phospholipid metabolic process
Source: RGD
Traceable author statementⁱ
- 12511545
positive regulation of angiogenesis
Source: RGD
Inferred from mutant phenotypeⁱ
- 20925964
positive regulation of apoptotic process Source: Ensembl
positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis Source: Ensembl
positive regulation of cell migration involved in sprouting angiogenesis Source: Ensembl
positive regulation of macroautophagy Source: Ensembl
positive regulation of smooth muscle cell proliferation Source: Ensembl
protein homooligomerization Source: Ensembl
regulation of blood pressure
Source: RGD
Inferred from direct assayⁱ
- 12215473
regulation of DNA-binding transcription factor activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 17430897
regulation of transcription from RNA polymerase II promoter in response to iron Source: Ensembl
regulation of transcription from RNA polymerase II promoter in response to oxidative stress
Source: BHF-UCL
Inferred from direct assayⁱ
- 17430897
response to estrogen
Source: RGD
Inferred from direct assayⁱ
- 15734876
response to hydrogen peroxide
Source: BHF-UCL
Inferred from direct assayⁱ
- 17430897
response to hypoxia
Source: RGD
Inferred from mutant phenotypeⁱ
- 12114196
response to nicotine Source: Ensembl
response to oxidative stress
Source: RGD
Inferred from direct assayⁱ
- 17020887
small GTPase mediated signal transduction
Source: RGD
Inferred from direct assayⁱ
- 12511545
wound healing involved in inflammatory response Source: Ensembl

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Biological process	Apoptosis
Ligand	Heme, Iron, Metal-binding

Enzyme and pathway databases

BRENDAⁱ	1.14.99.3 5301
Reactomeⁱ	R-RNO-189483 Heme degradation R-RNO-917937 Iron uptake and transport
SABIO-RKⁱ	P06762

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Heme oxygenase 1 (EC:1.14.14.18By similarity) Short name: HO-1 Alternative name(s): HSP32
Gene namesⁱ	Name:Hmox1
Organismⁱ	Rattus norvegicus (Rat)
Taxonomic identifierⁱ	10116 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesⁱ	UP000002494 Componentⁱ: Chromosome 19

Organism-specific databases

Rat genome database More...RGDⁱ	2806 Hmox1

RGDⁱ

2806 Hmox1

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechⁱ

Chemistry databases

ChEMBLⁱ	CHEMBL5035
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	1441

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000209690	1 – 289	Heme oxygenase 1Add BLAST		289

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	229	PhosphoserineBy similarity		1
Modified residueⁱ	242	PhosphoserineCombined sources		1

Keywords - PTMⁱ

Phosphoprotein

Proteomic databases

jPOSTⁱ	P06762
PaxDbⁱ	P06762
PRIDEⁱ	P06762

PTM databases

iPTMnetⁱ	P06762
PhosphoSitePlusⁱ	P06762

Expressionⁱ

Inductionⁱ

Heme oxygenase 1 activity is highly inducible by its substrate heme and by various non-heme substances such as heavy metals, bromobenzene, and endotoxin.

Gene expression databases

Bgeeⁱ	ENSRNOG00000014117 Expressed in 10 organ(s), highest expression level in spleen
Genevisibleⁱ	P06762 RN

Interactionⁱ

GO - Molecular functionⁱ

enzyme binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 15516695
protein homodimerization activity Source: Ensembl

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	246615, 1 interactor
Molecular INTeraction database More...MINTⁱ	P06762
STRINGⁱ	10116.ENSRNOP00000019192

Chemistry databases

BindingDBⁱ

P06762

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	13 – 29	Combined sources	17
Helixⁱ	32 – 39	Combined sources	8
Helixⁱ	44 – 67	Combined sources	24
Turnⁱ	68 – 70	Combined sources	3
Turnⁱ	72 – 74	Combined sources	3
Helixⁱ	75 – 77	Combined sources	3
Helixⁱ	80 – 83	Combined sources	4
Helixⁱ	86 – 97	Combined sources	12
Helixⁱ	101 – 103	Combined sources	3
Helixⁱ	109 – 124	Combined sources	16
Helixⁱ	126 – 128	Combined sources	3
Helixⁱ	129 – 140	Combined sources	12
Helixⁱ	143 – 155	Combined sources	13
Helixⁱ	165 – 167	Combined sources	3
Helixⁱ	175 – 186	Combined sources	12
Helixⁱ	193 – 221	Combined sources	29

Show more details

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1DVE	X-ray	2.40	A	1-267	[»]
	1DVG	X-ray	2.20	A/B	1-267	[»]
	1IRM	X-ray	2.55	A/B/C	1-267	[»]
	1IVJ	X-ray	1.90	A	1-267	[»]
	1IX3	X-ray	2.00	A	1-267	[»]
	1IX4	X-ray	1.80	A	1-267	[»]
	1J02	X-ray	1.70	A	1-267	[»]
	1J2C	X-ray	2.40	A	1-267	[»]
	1UBB	X-ray	2.30	A	1-267	[»]
	1ULX	X-ray	2.00	A	1-267	[»]
	1VGI	X-ray	1.90	A	1-267	[»]
	2DY5	X-ray	2.70	A	1-267	[»]
	2E7E	X-ray	1.85	A	1-267	[»]
	2ZVU	X-ray	2.20	A	1-267	[»]
	3I9T	X-ray	2.15	A	1-261	[»]
	3I9U	X-ray	2.25	A	1-261	[»]
	3WKT	X-ray	4.30	C/D	1-267	[»]
	4G7L	X-ray	1.80	A	1-267	[»]
	4G7P	X-ray	1.90	A	1-267	[»]
	4G7T	X-ray	1.90	A	1-267	[»]
	4G7U	X-ray	1.90	A	1-267	[»]
	4G8P	X-ray	1.90	A	1-267	[»]
	4G8U	X-ray	2.10	A	1-267	[»]
	4G8W	X-ray	2.40	A	1-267	[»]
	4G98	X-ray	2.30	A	1-267	[»]
	4G99	X-ray	2.30	A	1-267	[»]
	4MEC	X-ray	3.20	A/B/C/D/E/F/G	1-232	[»]
ProteinModelPortalⁱ	P06762
SMRⁱ	P06762
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P06762

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the heme oxygenase family.Curated

Phylogenomic databases

eggNOGⁱ	KOG4480 Eukaryota COG5398 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000017673
HOGENOMⁱ	HOG000233221
HOVERGENⁱ	HBG005982
InParanoidⁱ	P06762
KEGG Orthology (KO) More...KOⁱ	K00510
OMAⁱ	KKSHTMA
Database of Orthologous Groups More...OrthoDBⁱ	1424194at2759
PhylomeDBⁱ	P06762
TreeFamⁱ	TF314786

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00232 HemeO, 1 hit
Gene3Dⁱ	1.20.910.10, 1 hit
InterProⁱ	View protein in InterPro IPR002051 Haem_Oase IPR016053 Haem_Oase-like IPR016084 Haem_Oase-like_multi-hlx IPR018207 Haem_oxygenase_CS
PANTHERⁱ	PTHR10720 PTHR10720, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01126 Heme_oxygenase, 1 hit
PIRSFⁱ	PIRSF000343 Haem_Oase, 1 hit
PRINTSⁱ	PR00088 HAEMOXYGNASE
SUPFAMⁱ	SSF48613 SSF48613, 1 hit
PROSITEⁱ	View protein in PROSITE PS00593 HEME_OXYGENASE, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P06762-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MERPQLDSMS QDLSEALKEA TKEVHIRAEN SEFMRNFQKG QVSREGFKLV 
        60         70         80         90        100
MASLYHIYTA LEEEIERNKQ NPVYAPLYFP EELHRRAALE QDMAFWYGPH 
       110        120        130        140        150
WQEAIPYTPA TQHYVKRLHE VGGTHPELLV AHAYTRYLGD LSGGQVLKKI 
       160        170        180        190        200
AQKAMALPSS GEGLAFFTFP SIDNPTKFKQ LYRARMNTLE MTPEVKHRVT 
       210        220        230        240        250
EEAKTAFLLN IELFEELQAL LTEEHKDQSP SQTEFLRQRP ASLVQDTTSA 
       260        270        280 
ETPRGKSQIS TSSSQTPLLR WVLTLSFLLA TVAVGIYAM

Length:289

Mass (Da):33,006

Last modified:January 1, 1988 - v1

Checksum:ⁱEF7D2B98048AF44D

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	J02722 Genomic DNA Translation: AAA41346.1 BC091164 mRNA Translation: AAH91164.1
PIRⁱ	A92645 OHRTD
NCBI Reference Sequences More...RefSeqⁱ	NP_036712.1, NM_012580.2
UniGeneⁱ	Rn.3160

Genome annotation databases

Ensemblⁱ	ENSRNOT00000019192; ENSRNOP00000019192; ENSRNOG00000014117
GeneIDⁱ	24451
KEGGⁱ	rno:24451
UCSC genome browser More...UCSCⁱ	RGD:2806 rat

Protein	Similar proteins		Species	Score	Length	Source
P06762	Heme oxygenase 1		MOUSE		289	UniRef90_P14901
Heme oxygenase 1 (Fragment)		MUSSP		140
Heme oxygenase 1 (Fragment)		HUMAN		121
Heme oxygenase		MESAU		290
Heme oxygenase		CRIGR		290
+9

Protein	Similar proteins		Species	Score	Length	Source
P06762	Heme oxygenase 1		MOUSE		289	UniRef50_P14901
Heme oxygenase 1 (Fragment)		MUSSP		140
Heme oxygenase 1 (Fragment)		HUMAN		121
Heme oxygenase		MESAU		290
Heme oxygenase		CRIGR		290
+89

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	J02722 Genomic DNA Translation: AAA41346.1 BC091164 mRNA Translation: AAH91164.1
PIRⁱ	A92645 OHRTD
RefSeqⁱ	NP_036712.1, NM_012580.2
UniGeneⁱ	Rn.3160

3D structure databases

Select the link destinations: PDBeⁱ RCSB PDBⁱ PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1DVE	X-ray	2.40	A	1-267	[»]
	1DVG	X-ray	2.20	A/B	1-267	[»]
	1IRM	X-ray	2.55	A/B/C	1-267	[»]
	1IVJ	X-ray	1.90	A	1-267	[»]
	1IX3	X-ray	2.00	A	1-267	[»]
	1IX4	X-ray	1.80	A	1-267	[»]
	1J02	X-ray	1.70	A	1-267	[»]
	1J2C	X-ray	2.40	A	1-267	[»]
	1UBB	X-ray	2.30	A	1-267	[»]
	1ULX	X-ray	2.00	A	1-267	[»]
	1VGI	X-ray	1.90	A	1-267	[»]
	2DY5	X-ray	2.70	A	1-267	[»]
	2E7E	X-ray	1.85	A	1-267	[»]
	2ZVU	X-ray	2.20	A	1-267	[»]
	3I9T	X-ray	2.15	A	1-261	[»]
	3I9U	X-ray	2.25	A	1-261	[»]
	3WKT	X-ray	4.30	C/D	1-267	[»]
	4G7L	X-ray	1.80	A	1-267	[»]
	4G7P	X-ray	1.90	A	1-267	[»]
	4G7T	X-ray	1.90	A	1-267	[»]
	4G7U	X-ray	1.90	A	1-267	[»]
	4G8P	X-ray	1.90	A	1-267	[»]
	4G8U	X-ray	2.10	A	1-267	[»]
	4G8W	X-ray	2.40	A	1-267	[»]
	4G98	X-ray	2.30	A	1-267	[»]
	4G99	X-ray	2.30	A	1-267	[»]
	4MEC	X-ray	3.20	A/B/C/D/E/F/G	1-232	[»]
ProteinModelPortalⁱ	P06762
SMRⁱ	P06762
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	246615, 1 interactor
MINTⁱ	P06762
STRINGⁱ	10116.ENSRNOP00000019192

Chemistry databases

BindingDBⁱ	P06762
ChEMBLⁱ	CHEMBL5035
GuidetoPHARMACOLOGYⁱ	1441

PTM databases

iPTMnetⁱ	P06762
PhosphoSitePlusⁱ	P06762

Proteomic databases

jPOSTⁱ	P06762
PaxDbⁱ	P06762
PRIDEⁱ	P06762

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSRNOT00000019192; ENSRNOP00000019192; ENSRNOG00000014117
GeneIDⁱ	24451
KEGGⁱ	rno:24451
UCSCⁱ	RGD:2806 rat

Organism-specific databases

CTDⁱ	3162
RGDⁱ	2806 Hmox1

Phylogenomic databases

eggNOGⁱ	KOG4480 Eukaryota COG5398 LUCA
GeneTreeⁱ	ENSGT00390000017673
HOGENOMⁱ	HOG000233221
HOVERGENⁱ	HBG005982
InParanoidⁱ	P06762
KOⁱ	K00510
OMAⁱ	KKSHTMA
OrthoDBⁱ	1424194at2759
PhylomeDBⁱ	P06762
TreeFamⁱ	TF314786

Enzyme and pathway databases

BRENDAⁱ	1.14.99.3 5301
Reactomeⁱ	R-RNO-189483 Heme degradation R-RNO-917937 Iron uptake and transport
SABIO-RKⁱ	P06762

Miscellaneous databases

EvolutionaryTraceⁱ	P06762
Protein Ontology More...PROⁱ	PR:P06762

Gene expression databases

Bgeeⁱ	ENSRNOG00000014117 Expressed in 10 organ(s), highest expression level in spleen
Genevisibleⁱ	P06762 RN

Family and domain databases

CDDⁱ	cd00232 HemeO, 1 hit
Gene3Dⁱ	1.20.910.10, 1 hit
InterProⁱ	View protein in InterPro IPR002051 Haem_Oase IPR016053 Haem_Oase-like IPR016084 Haem_Oase-like_multi-hlx IPR018207 Haem_oxygenase_CS
PANTHERⁱ	PTHR10720 PTHR10720, 1 hit
Pfamⁱ	View protein in Pfam PF01126 Heme_oxygenase, 1 hit
PIRSFⁱ	PIRSF000343 Haem_Oase, 1 hit
PRINTSⁱ	PR00088 HAEMOXYGNASE
SUPFAMⁱ	SSF48613 SSF48613, 1 hit
PROSITEⁱ	View protein in PROSITE PS00593 HEME_OXYGENASE, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	HMOX1_RAT
Accessionⁱ	P06762Primary (citable) accession number: P06762 Secondary accession number(s): Q5BK87
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
	Last sequence update:	January 1, 1988
	Last modified:	January 16, 2019
	This is version 164 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P06762 (HMOX1_RAT)

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Heme oxygenase 1

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Endoplasmic reticulum

Cytosol

Endoplasmic reticulum

Nucleus

Plasma Membrane

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

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Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

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Keywords - Technical termi

Documents

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ