MOCOS

Functionⁱ

Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form. In vitro, the C-terminal domain is able to reduce N-hydroxylated prodrugs, such as benzamidoxime.UniRule annotation1 Publication

Catalytic activityⁱ

Molybdenum cofactor + L-cysteine + reduced acceptor + 2 H⁺ = thio-molybdenum cofactor + L-alanine + H₂O + oxidized acceptor.UniRule annotation

Cofactorⁱ

pyridoxal 5'-phosphateUniRule annotation

Kineticsⁱ

K_M=
15 µM for benzamidoxime
1 Publication
Manual assertion based on experiment inⁱ
- Ref.6
  "Identification of the missing component in the mitochondrial benzamidoxime prodrug converting system as a novel molybdenum enzyme."
  Havemeyer A., Bittner F., Wollers S., Mendel R., Kunze T., Clement B.
  J. Biol. Chem. 281:34796-34802(2006) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.

V_max=
0.24 nmol/min/mg enzyme
1 Publication
Manual assertion based on experiment inⁱ
- Ref.6
  "Identification of the missing component in the mitochondrial benzamidoxime prodrug converting system as a novel molybdenum enzyme."
  Havemeyer A., Bittner F., Wollers S., Mendel R., Kunze T., Clement B.
  J. Biol. Chem. 281:34796-34802(2006) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Active siteⁱ	424	UniRule annotation		1

GO - Molecular functionⁱ

molybdenum cofactor sulfurtransferase activity Source: UniProtKB-EC
molybdenum ion binding Source: InterPro
Mo-molybdopterin cofactor sulfurase activity
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 11302742
pyridoxal phosphate binding Source: InterPro

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

molybdopterin cofactor biosynthetic process Source: Reactome
molybdopterin cofactor metabolic process
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 11302742
Mo-molybdopterin cofactor biosynthetic process Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Transferase
Biological process	Molybdenum cofactor biosynthesis
Ligand	Pyridoxal phosphate

Enzyme and pathway databases

Reactomeⁱ	R-HSA-947581 Molybdenum cofactor biosynthesis

Reactomeⁱ

R-HSA-947581 Molybdenum cofactor biosynthesis

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Molybdenum cofactor sulfuraseUniRule annotation (EC:2.8.1.9UniRule annotation) Short name: MCSUniRule annotation Short name: MOSUniRule annotation Short name: MoCo sulfuraseUniRule annotation Short name: hMCS Alternative name(s): Molybdenum cofactor sulfurtransferaseUniRule annotation
Gene namesⁱ	Name:MOCOSUniRule annotation
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [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 › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 18

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000075643.5
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:18234 MOCOS
MIMⁱ	613274 gene
neXtProtⁱ	NX_Q96EN8

Subcellular locationⁱ

GO - Cellular component

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Xanthinuria 2 (XAN2)4 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder characterized by excretion of very large amounts of xanthine in the urine and a tendency to form xanthine stones. Uric acid is strikingly diminished in serum and urine. In addition, XAN2 patients cannot metabolize allopurinol into oxypurinol due to dual deficiency of xanthine dehydrogenase and aldehyde oxidase.

Keywords - Diseaseⁱ

Disease mutation

Organism-specific databases

DisGeNET More...DisGeNETⁱ	55034
MalaCards human disease database More...MalaCardsⁱ	MOCOS
MIMⁱ	603592 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000075643
Orphanetⁱ	93602 Xanthinuria type II
PharmGKBⁱ	PA134964534

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB00114 Pyridoxal Phosphate

DrugBankⁱ

DB00114 Pyridoxal Phosphate

Polymorphism and mutation databases

BioMutaⁱ	MOCOS
DMDMⁱ	296438294

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000249952	1 – 888	Molybdenum cofactor sulfuraseAdd BLAST		888

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	34	PhosphoserineCombined sources	1
Modified residueⁱ	264	N6-(pyridoxal phosphate)lysineUniRule annotation	1
Modified residueⁱ	528	PhosphoserineCombined sources	1
Modified residueⁱ	530	PhosphoserineCombined sources	1

Keywords - PTMⁱ

Phosphoprotein

Proteomic databases

EPDⁱ	Q96EN8
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q96EN8
PaxDbⁱ	Q96EN8
PeptideAtlas More...PeptideAtlasⁱ	Q96EN8
PRIDEⁱ	Q96EN8
ProteomicsDBⁱ	76426

PTM databases

iPTMnetⁱ	Q96EN8
PhosphoSitePlusⁱ	Q96EN8

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000075643
CleanExⁱ	HS_MOCOS
Genevisibleⁱ	Q96EN8 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA039412 HPA047958

HPAⁱ

HPA039412
HPA047958

Interactionⁱ

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
PARVA	Q9NVD7	4	EBI-1220583,EBI-747655

With

Entry

#Exp.

IntAct

Notes

PARVA

Q9NVD7

4

EBI-1220583,EBI-747655

Protein-protein interaction databases

BioGridⁱ	120363, 27 interactors
IntActⁱ	Q96EN8, 6 interactors
Molecular INTeraction database More...MINTⁱ	Q96EN8
STRINGⁱ	9606.ENSP00000261326

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q96EN8
SMRⁱ	Q96EN8
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	706 – 867	MOSCUniRule annotationAdd BLAST		162

Sequence similaritiesⁱ

Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. MOCOS subfamily.UniRule annotation

Phylogenomic databases

eggNOGⁱ	KOG2142 Eukaryota COG0520 LUCA COG3217 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00530000063150
HOGENOMⁱ	HOG000029698
HOVERGENⁱ	HBG081980
InParanoidⁱ	Q96EN8
KEGG Orthology (KO) More...KOⁱ	K15631
OMAⁱ	RVNTYDC
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G03KL
PhylomeDBⁱ	Q96EN8
TreeFamⁱ	TF105761

Family and domain databases

Gene3Dⁱ	3.40.640.10, 1 hit 3.90.1150.10, 1 hit
HAMAPⁱ	MF_03050 MOCOS, 1 hit
InterProⁱ	View protein in InterPro IPR000192 Aminotrans_V_dom IPR005302 MoCF_Sase_C IPR028886 MoCo_sulfurase IPR005303 MOSC_N IPR015424 PyrdxlP-dep_Trfase IPR015422 PyrdxlP-dep_Trfase_dom1 IPR015421 PyrdxlP-dep_Trfase_major IPR011037 Pyrv_Knase-like_insert_dom_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00266 Aminotran_5, 1 hit PF03473 MOSC, 1 hit PF03476 MOSC_N, 1 hit
SUPFAMⁱ	SSF50800 SSF50800, 1 hit SSF53383 SSF53383, 2 hits
PROSITEⁱ	View protein in PROSITE PS51340 MOSC, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Q96EN8-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MAGAAAESGR ELWTFAGSRD PSAPRLAYGY GPGSLRELRA REFSRLAGTV 
        60         70         80         90        100
YLDHAGATLF SQSQLESFTS DLMENTYGNP HSQNISSKLT HDTVEQVRYR 
       110        120        130        140        150
ILAHFHTTAE DYTVIFTAGS TAALKLVAEA FPWVSQGPES SGSRFCYLTD 
       160        170        180        190        200
SHTSVVGMRN VTMAINVIST PVRPEDLWSA EERSASASNP DCQLPHLFCY 
       210        220        230        240        250
PAQSNFSGVR YPLSWIEEVK SGRLHPVSTP GKWFVLLDAA SYVSTSPLDL 
       260        270        280        290        300
SAHQADFVPI SFYKIFGFPT GLGALLVHNR AAPLLRKTYF GGGTASAYLA 
       310        320        330        340        350
GEDFYIPRQS VAQRFEDGTI SFLDVIALKH GFDTLERLTG GMENIKQHTF 
       360        370        380        390        400
TLAQYTYVAL SSLQYPNGAP VVRIYSDSEF SSPEVQGPII NFNVLDDKGN 
       410        420        430        440        450
IIGYSQVDKM ASLYNIHLRT GCFCNTGACQ RHLGISNEMV RKHFQAGHVC 
       460        470        480        490        500
GDNMDLIDGQ PTGSVRISFG YMSTLDDVQA FLRFIIDTRL HSSGDWPVPQ 
       510        520        530        540        550
AHADTGETGA PSADSQADVI PAVMGRRSLS PQEDALTGSR VWNNSSTVNA 
       560        570        580        590        600
VPVAPPVCDV ARTQPTPSEK AAGVLEGALG PHVVTNLYLY PIKSCAAFEV 
       610        620        630        640        650
TRWPVGNQGL LYDRSWMVVN HNGVCLSQKQ EPRLCLIQPF IDLRQRIMVI 
       660        670        680        690        700
KAKGMEPIEV PLEENSERTQ IRQSRVCADR VSTYDCGEKI SSWLSTFFGR 
       710        720        730        740        750
PCHLIKQSSN SQRNAKKKHG KDQLPGTMAT LSLVNEAQYL LINTSSILEL 
       760        770        780        790        800
HRQLNTSDEN GKEELFSLKD LSLRFRANII INGKRAFEEE KWDEISIGSL 
       810        820        830        840        850
RFQVLGPCHR CQMICIDQQT GQRNQHVFQK LSESRETKVN FGMYLMHASL 
       860        870        880 
DLSSPCFLSV GSQVLPVLKE NVEGHDLPAS EKHQDVTS

Length:888

Mass (Da):98,120

Last modified:May 18, 2010 - v2

Checksum:ⁱ07DB9457516E8C06

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	119	G → E in BAD96606 (PubMed:14702039).Curated		1
Sequence conflictⁱ	689	K → E in BAD96606 (PubMed:14702039).Curated		1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_027528	57	A → P in XAN2. 1 PublicationCorresponds to variant dbSNP:rs886037854EnsemblClinVar.	1
Natural variantⁱVAR_027529	120	S → N. Corresponds to variant dbSNP:rs3744900Ensembl.	1
Natural variantⁱVAR_027530	170	T → I2 PublicationsCorresponds to variant dbSNP:rs623053Ensembl.	1
Natural variantⁱVAR_027531	184	S → G3 PublicationsCorresponds to variant dbSNP:rs540967Ensembl.	1
Natural variantⁱVAR_027532	225	H → R4 PublicationsCorresponds to variant dbSNP:rs623558Ensembl.	1
Natural variantⁱVAR_027533	294	T → I in XAN2. 1 PublicationCorresponds to variant dbSNP:rs577279030Ensembl.	1
Natural variantⁱVAR_027534	358	V → M3 PublicationsCorresponds to variant dbSNP:rs678560Ensembl.	1
Natural variantⁱVAR_027535	495	D → N. Corresponds to variant dbSNP:rs8088347Ensembl.	1
Natural variantⁱVAR_027536	541	V → L. Corresponds to variant dbSNP:rs672924Ensembl.	1
Natural variantⁱVAR_027537	703	H → N2 PublicationsCorresponds to variant dbSNP:rs594445Ensembl.	1
Natural variantⁱVAR_045899	776	R → C in XAN2. 1 PublicationCorresponds to variant dbSNP:rs750896617EnsemblClinVar.	1
Natural variantⁱVAR_027538	867	V → A. Corresponds to variant dbSNP:rs1057251Ensembl.	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AK000740 mRNA Translation: BAA91353.1 AK222886 mRNA Translation: BAD96606.1 AC023043 Genomic DNA No translation available. BC012079 mRNA Translation: AAH12079.1 AL834481 mRNA Translation: CAD39140.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS11919.1
PIRⁱ	JC7680
NCBI Reference Sequences More...RefSeqⁱ	NP_060417.2, NM_017947.2
UniGeneⁱ	Hs.405028

Genome annotation databases

Ensemblⁱ	ENST00000261326; ENSP00000261326; ENSG00000075643
GeneIDⁱ	55034
KEGGⁱ	hsa:55034
UCSC genome browser More...UCSCⁱ	uc002kzq.5 human

Keywords - Coding sequence diversityⁱ

Polymorphism

Protein	Similar proteins		Species	Score	Length
Q96EN8	UPI00083F7919		CALJA		985
Molybdenum cofactor sulfurase		PONAB		898
Molybdenum cofactor sulfurase		CERAT		893
Molybdenum cofactor sulfurase		MACNE		893
Molybdenum cofactor sulfurase		MACFA		891
+24

Protein	Similar proteins		Species	Score	Length
Q96EN8	UPI00083F7919		CALJA		985
Molybdenum cofactor sulfurase		PONAB		898
Molybdenum cofactor sulfurase		MACNE		893
Molybdenum cofactor sulfurase		CERAT		893
Molybdenum cofactor sulfurase		PAPAN		891
+128

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AK000740 mRNA Translation: BAA91353.1 AK222886 mRNA Translation: BAD96606.1 AC023043 Genomic DNA No translation available. BC012079 mRNA Translation: AAH12079.1 AL834481 mRNA Translation: CAD39140.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS11919.1
PIRⁱ	JC7680
NCBI Reference Sequences More...RefSeqⁱ	NP_060417.2, NM_017947.2
UniGeneⁱ	Hs.405028

3D structure databases

ProteinModelPortalⁱ	Q96EN8
SMRⁱ	Q96EN8
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	120363, 27 interactors
IntActⁱ	Q96EN8, 6 interactors
Molecular INTeraction database More...MINTⁱ	Q96EN8
STRINGⁱ	9606.ENSP00000261326

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB00114 Pyridoxal Phosphate

DrugBankⁱ

DB00114 Pyridoxal Phosphate

PTM databases

iPTMnetⁱ	Q96EN8
PhosphoSitePlusⁱ	Q96EN8

Polymorphism and mutation databases

BioMutaⁱ	MOCOS
DMDMⁱ	296438294

Proteomic databases

EPDⁱ	Q96EN8
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q96EN8
PaxDbⁱ	Q96EN8
PeptideAtlas More...PeptideAtlasⁱ	Q96EN8
PRIDEⁱ	Q96EN8
ProteomicsDBⁱ	76426

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	55034
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000261326; ENSP00000261326; ENSG00000075643
GeneIDⁱ	55034
KEGGⁱ	hsa:55034
UCSC genome browser More...UCSCⁱ	uc002kzq.5 human

Organism-specific databases

CTDⁱ	55034
DisGeNET More...DisGeNETⁱ	55034
EuPathDBⁱ	HostDB:ENSG00000075643.5
GeneCardsⁱ	MOCOS
H-InvDBⁱ	HIX0202662
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:18234 MOCOS
Human Protein Atlas More...HPAⁱ	HPA039412 HPA047958
MalaCards human disease database More...MalaCardsⁱ	MOCOS
MIMⁱ	603592 phenotype 613274 gene
neXtProtⁱ	NX_Q96EN8
Open Targets More...OpenTargetsⁱ	ENSG00000075643
Orphanetⁱ	93602 Xanthinuria type II
PharmGKBⁱ	PA134964534
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG2142 Eukaryota COG0520 LUCA COG3217 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00530000063150
HOGENOMⁱ	HOG000029698
HOVERGENⁱ	HBG081980
InParanoidⁱ	Q96EN8
KEGG Orthology (KO) More...KOⁱ	K15631
OMAⁱ	RVNTYDC
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G03KL
PhylomeDBⁱ	Q96EN8
TreeFamⁱ	TF105761

Enzyme and pathway databases

Reactomeⁱ	R-HSA-947581 Molybdenum cofactor biosynthesis

Reactomeⁱ

R-HSA-947581 Molybdenum cofactor biosynthesis

Miscellaneous databases

GeneWikiⁱ	MOCOS
GenomeRNAiⁱ	55034
Protein Ontology More...PROⁱ	PR:Q96EN8
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000075643
CleanExⁱ	HS_MOCOS
Genevisibleⁱ	Q96EN8 HS

Family and domain databases

Gene3Dⁱ	3.40.640.10, 1 hit 3.90.1150.10, 1 hit
HAMAPⁱ	MF_03050 MOCOS, 1 hit
InterProⁱ	View protein in InterPro IPR000192 Aminotrans_V_dom IPR005302 MoCF_Sase_C IPR028886 MoCo_sulfurase IPR005303 MOSC_N IPR015424 PyrdxlP-dep_Trfase IPR015422 PyrdxlP-dep_Trfase_dom1 IPR015421 PyrdxlP-dep_Trfase_major IPR011037 Pyrv_Knase-like_insert_dom_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00266 Aminotran_5, 1 hit PF03473 MOSC, 1 hit PF03476 MOSC_N, 1 hit
SUPFAMⁱ	SSF50800 SSF50800, 1 hit SSF53383 SSF53383, 2 hits
PROSITEⁱ	View protein in PROSITE PS51340 MOSC, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	MOCOS_HUMAN
Accessionⁱ	Q96EN8Primary (citable) accession number: Q96EN8 Secondary accession number(s): Q53GP5, Q8N3A4, Q9NWM7
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	September 19, 2006
	Last sequence update:	May 18, 2010
	Last modified:	July 18, 2018
	This is version 139 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

Documents

Human chromosome 18
Human chromosome 18: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
SIMILARITY comments
Index of protein domains and families

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UniProtKB - Q96EN8 (MOCOS_HUMAN)

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Molybdenum cofactor sulfurase

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 ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

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

<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 - 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

Cytosol

<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

Organism-specific databases

Chemistry databases

Polymorphism and mutation 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

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

Organism-specific 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

Protein-protein interaction 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

3D structure 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

Domains and Repeats

<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

Experimental Info

Natural variant

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation 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

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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Functionⁱ

Kineticsⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ