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

Sites

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.</p><p><a href='../manual/site' target='_top'>More...</a></p>Sitei	4302 – 4303	2	Cleavage

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

1. extracellular matrix structural constituent Source: UniProtKB

   <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementⁱ

   • 7513696

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processⁱ

1. cellular protein metabolic process Source: Reactome
2. extracellular fibril organization Source: MGI

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 10611155

3. O-glycan processing Source: Reactome
4. post-translational protein modification Source: Reactome

Enzyme and pathway databases

Protein family/group databases

<p>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><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

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

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componentⁱ

1. extracellular vesicular exosome Source: UniProtKB

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 19199708

2. fibril Source: MGI

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 14749330

3. Golgi lumen Source: Reactome

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - Cellular componentⁱ

<p>Provides information on the disease(s) and phenotype(s) associated with the deficiency of a protein.</p><p><a href='../manual/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	2122 – 2122	1	W → A: No binding to mannose-specific lectin. Loss of secretion from the endoplasmic reticulum. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.13 "C-Mannosylation of MUC5AC and MUC5B Cys subdomains." Perez-Vilar J., Randell S.H., Boucher R.C. Glycobiology 14:325-337(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT TRP-2122, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-2122.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	4302 – 4302	1	D → A or E: Abolishes cleavage. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.8 "Cleavage in the GDPH sequence of the C-terminal cysteine-rich part of the human MUC5AC mucin." Lidell M.E., Hansson G.C. Biochem. J. 399:121-129(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 4303-4312, PROTEOLYTIC PROCESSING, MUTAGENESIS OF ASP-4302.

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

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Denotes the presence of an N-terminal signal peptide.</p><p><a href='../manual/signal' target='_top'>More...</a></p>Signal peptidei	1 – 27	27	Sequence Analysis			Add BLAST
<p>Describes the extent of a polypeptide chain in the mature protein following processing.</p><p><a href='../manual/chain' target='_top'>More...</a></p>Chaini	28 – 5030	5003	Mucin-5AC		PRO_0000158957	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the positions of cysteine residues participating in disulfide bonds.</p><p><a href='../manual/disulfid' target='_top'>More...</a></p>Disulfide bondi	? ↔ 4995		By similarity
<p>Describes the positions of cysteine residues participating in disulfide bonds.</p><p><a href='../manual/disulfid' target='_top'>More...</a></p>Disulfide bondi	103 ↔ 111		By similarity
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	205 – 205	1	N-linked (GlcNAc...)Sequence Analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	258 – 258	1	N-linked (GlcNAc...)Sequence Analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	415 – 415	1	N-linked (GlcNAc...)Sequence Analysis
<p>Describes the positions of cysteine residues participating in disulfide bonds.</p><p><a href='../manual/disulfid' target='_top'>More...</a></p>Disulfide bondi	456 ↔ 464		By similarity
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	524 – 524	1	N-linked (GlcNAc...)Sequence Analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	1308 – 1308	1	N-linked (GlcNAc...)Sequence Analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	1389 – 1389	1	C-linked (Man)Curated
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	1584 – 1584	1	C-linked (Man)Curated
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	1749 – 1749	1	C-linked (Man)Curated
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	1957 – 1957	1	C-linked (Man)Curated
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	2122 – 2122	1	C-linked (Man)
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	2652 – 2652	1	C-linked (Man)Curated
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	2950 – 2950	1	C-linked (Man)Curated
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	3198 – 3198	1	N-linked (GlcNAc...)Sequence Analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	3383 – 3383	1	C-linked (Man)Curated
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	4009 – 4009	1	C-linked (Man)Curated
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	4245 – 4245	1	N-linked (GlcNAc...)Sequence Analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	4318 – 4318	1	N-linked (GlcNAc...)Sequence Analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	4433 – 4433	1	N-linked (GlcNAc...)Sequence Analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	4469 – 4469	1	N-linked (GlcNAc...)Sequence Analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	4612 – 4612	1	N-linked (GlcNAc...)Sequence Analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	4723 – 4723	1	N-linked (GlcNAc...)Sequence Analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	4753 – 4753	1	N-linked (GlcNAc...)Sequence Analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	4762 – 4762	1	N-linked (GlcNAc...)Sequence Analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	4831 – 4831	1	N-linked (GlcNAc...)Sequence Analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	4904 – 4904	1	N-linked (GlcNAc...)Sequence Analysis
<p>Describes the positions of cysteine residues participating in disulfide bonds.</p><p><a href='../manual/disulfid' target='_top'>More...</a></p>Disulfide bondi	4908 ↔ 4958		By similarity
<p>Describes the positions of cysteine residues participating in disulfide bonds.</p><p><a href='../manual/disulfid' target='_top'>More...</a></p>Disulfide bondi	4922 ↔ 4972		By similarity
<p>Describes the positions of cysteine residues participating in disulfide bonds.</p><p><a href='../manual/disulfid' target='_top'>More...</a></p>Disulfide bondi	4933 ↔ 4988		By similarity
<p>Describes the positions of cysteine residues participating in disulfide bonds.</p><p><a href='../manual/disulfid' target='_top'>More...</a></p>Disulfide bondi	4937 ↔ 4990		By similarity
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	4967 – 4967	1	N-linked (GlcNAc...)Sequence Analysis

<p>Describes post-translational modifications (PTMs). This subsection complements the information provided at the sequence level or describes modifications for which position-specific data is not yet available.</p><p><a href='../manual/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - PTMⁱ

Proteomic databases

PTM databases

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

<p>Provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.</p><p><a href='../manual/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

Gene expression databases

Organism-specific databases

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

<p>Provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the ‘Function’ section).</p><p><a href='../manual/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

Protein-protein interaction databases

<p>Provides information on the tertiary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structureⁱ

3D structure databases

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

Domains and Repeats

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.</p><p><a href='../manual/domain' target='_top'>More...</a></p>Domaini	80 – 281	202	VWFD 1PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi PROSITE-ProRule:PRU00580			Add BLAST
<p>Describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.</p><p><a href='../manual/domain' target='_top'>More...</a></p>Domaini	433 – 647	215	VWFD 2PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi PROSITE-ProRule:PRU00580			Add BLAST
<p>Describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.</p><p><a href='../manual/domain' target='_top'>More...</a></p>Domaini	902 – 1109	208	VWFD 3PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi PROSITE-ProRule:PRU00580			Add BLAST
<p>Indicates the positions and types of repeated sequence motifs or repeated domains within the protein.</p><p><a href='../manual/repeat' target='_top'>More...</a></p>Repeati	1383 – 1481	99	Cys-rich subdomain 1			Add BLAST
<p>Indicates the positions and types of repeated sequence motifs or repeated domains within the protein.</p><p><a href='../manual/repeat' target='_top'>More...</a></p>Repeati	1577 – 1677	101	Cys-rich subdomain 2			Add BLAST
<p>Indicates the positions and types of repeated sequence motifs or repeated domains within the protein.</p><p><a href='../manual/repeat' target='_top'>More...</a></p>Repeati	1743 – 1847	105	Cys-rich subdomain 3			Add BLAST
<p>Indicates the positions and types of repeated sequence motifs or repeated domains within the protein.</p><p><a href='../manual/repeat' target='_top'>More...</a></p>Repeati	1950 – 2050	101	Cys-rich subdomain 4			Add BLAST
<p>Indicates the positions and types of repeated sequence motifs or repeated domains within the protein.</p><p><a href='../manual/repeat' target='_top'>More...</a></p>Repeati	2116 – 2220	105	Cys-rich subdomain 5			Add BLAST
<p>Indicates the positions and types of repeated sequence motifs or repeated domains within the protein.</p><p><a href='../manual/repeat' target='_top'>More...</a></p>Repeati	2646 – 2750	105	Cys-rich subdomain 6			Add BLAST
<p>Indicates the positions and types of repeated sequence motifs or repeated domains within the protein.</p><p><a href='../manual/repeat' target='_top'>More...</a></p>Repeati	2944 – 3084	141	Cys-rich subdomain 7			Add BLAST
<p>Indicates the positions and types of repeated sequence motifs or repeated domains within the protein.</p><p><a href='../manual/repeat' target='_top'>More...</a></p>Repeati	3377 – 3481	105	Cys-rich subdomain 8			Add BLAST
<p>Indicates the positions and types of repeated sequence motifs or repeated domains within the protein.</p><p><a href='../manual/repeat' target='_top'>More...</a></p>Repeati	4003 – 4107	105	Cys-rich subdomain 9			Add BLAST
<p>Describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.</p><p><a href='../manual/domain' target='_top'>More...</a></p>Domaini	4296 – 4507	212	VWFD 4PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi PROSITE-ProRule:PRU00580			Add BLAST
<p>Describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.</p><p><a href='../manual/domain' target='_top'>More...</a></p>Domaini	4652 – 4721	70	VWFC 1PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi PROSITE-ProRule:PRU00220			Add BLAST
<p>Describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.</p><p><a href='../manual/domain' target='_top'>More...</a></p>Domaini	4757 – 4824	68	VWFC 2PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi PROSITE-ProRule:PRU00220			Add BLAST
<p>Describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.</p><p><a href='../manual/domain' target='_top'>More...</a></p>Domaini	4908 – 4996	89	CTCKPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi PROSITE-ProRule:PRU00039			Add BLAST

Region

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes a region of interest that cannot be described in other subsections.</p><p><a href='../manual/region' target='_top'>More...</a></p>Regioni	1383 – 4107	2725	9 X Cys-rich subdomain repeats			Add BLAST
<p>Describes a region of interest that cannot be described in other subsections.</p><p><a href='../manual/region' target='_top'>More...</a></p>Regioni	2257 – 2624	368	46 X 8 AA approximate tandem repeats of T-T-S-T-T-S-A-P			Add BLAST
<p>Describes a region of interest that cannot be described in other subsections.</p><p><a href='../manual/region' target='_top'>More...</a></p>Regioni	2787 – 2922	136	17 X 8 AA approximate tandem repeats of T-T-S-T-T-S-A-P			Add BLAST
<p>Describes a region of interest that cannot be described in other subsections.</p><p><a href='../manual/region' target='_top'>More...</a></p>Regioni	3085 – 3355	271	34 X 8 AA approximate tandem repeats of T-T-S-T-T-S-A-P			Add BLAST
<p>Describes a region of interest that cannot be described in other subsections.</p><p><a href='../manual/region' target='_top'>More...</a></p>Regioni	3517 – 3971	455	58 X 8 AA approximate tandem repeats of T-T-S-T-T-S-A-P			Add BLAST

Motif

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.</p><p><a href='../manual/motif' target='_top'>More...</a></p>Motifi	1193 – 1195	3	Cell attachment siteSequence Analysis

Compositional bias

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.</p><p><a href='../manual/compbias' target='_top'>More...</a></p>Compositional biasi	4896 – 4901	6	Poly-Pro

<p>Provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.</p><p><a href='../manual/domain_cc' target='_top'>More...</a></p>Domainⁱ

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>Displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>Indicates if the canonical sequence displayed by default in the entry is complete or not.</p><p><a href='../manual/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Fragments.

<p>Indicates if the canonical sequence displayed by default in the entry is in its mature form or if it represents the precursor.</p><p><a href='../manual/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

        10         20         30         40         50
MSVGRRKLAL LWALALALAC TRHTGHAQDG SSESSYKHHP ALSPIARGPS 
        60         70         80         90        100
GVPLRGATVF PSLRTIPVVR ASNPAHNGRV CSTWGSFHYK TFDGDVFRFP 
       110        120        130        140        150
GLCNYVFSEH CGAAYEDFNI QLRRSQESAA PTLSRVLMKV DGVVIQLTKG 
       160        170        180        190        200
SVLVNGHPVL LPFSQSGVLI QQSSSYTKVE ARLGLVLMWN HDDSLLLELD 
       210        220        230        240        250
TKYANKTCGL CGDFNGMPVV SELLSHNTKL TPMEFGNLQK MDDPTEQCQD 
       260        270        280        290        300
PVPEPPRNCS TGFGICEELL HGQLFSGCVA LVDVGSYLEA CRQDLCFCED 
       310        320        330        340        350
TDLLSCVCHT LAEYSRQCTH AGGLPQDWRG PDFCPQKCPN NMQYHECRSP 
       360        370        380        390        400
CADTCSNQEH SRACEDHCVA GCFCPEGTVL DDIGQTGCVP VSKCACVYNG 
       410        420        430        440        450
AAYAPGATYS TDCTNCTCSG GRWSCQEVPC PDTCSVLGGA HFSTFDGKQY 
       460        470        480        490        500
TVHGDCSYVL TKPCDSSAFT VLAELRRCGL TDSETCLKSV TLSLDGAQTV 
       510        520        530        540        550
VVIKASGEVF LNQIYTQLPI SAANVTIFRP STFFIIAQTS LGLQLNLQPV 
       560        570        580        590        600
PTMQLFMQLA PKLRGQTCGL CGNFNSIQAD DFRTLSGVVE ATAAAFFNTF 
       610        620        630        640        650
KTQAACPNIR NSFEDPCSLS VENEKYAQHW CSQLTDADGP FGRCHAAVKP 
       660        670        680        690        700
GTYYSNCVFD TCNCERSEDC LCAALSSYVH ACAAKGVQLG GWRDGVCTKP 
       710        720        730        740        750
MTTCPKSMTY HYHVSTCQPT CRSLSEGDIT CSVGFIPVDG CICPKGTFLD 
       760        770        780        790        800
DTGKCVQASN CPCYHRGSMI PNGESVHDSG AICTCTHGKL SCIGGQAPAP 
       810        820        830        840        850
VCAAPMVFFD CRNATPGDTG AGCQKSCHTL DMTCYSPQCV PGCVCPDGLV 
       860        870        880        890        900
ADGEGGCITA EDCPCVHNEA SYRAGQTIRV GCNTCTCDSR MWRCTDDPCL 
       910        920        930        940        950
ATCAVYGDGH YLTFDGQSYS FNGDCEYTLV QNHCGGKDST QDSFRVVTEN 
       960        970        980        990       1000
VPCGTTGTTC SKAIKIFLGG FELKLSHGKV EVIGTDESQE VPYTIQQMGI 
      1010       1020       1030       1040       1050
YLVVDTDIGL VLLWDKKTSI FINLSPEFKG RVCGLCGNFD DIAVNDFATR 
      1060       1070       1080       1090       1100
SRSVVGDVLE FGNSWKLSPS CPDALAPKDP CTANPFRKSW AQKQCSILHG 
      1110       1120       1130       1140       1150
PTFAACHAHV EPARYYEACV NDACACDSGG DCECFCTAVA AYAQACHEVG 
      1160       1170       1180       1190       1200
LCVCLRTPSI CPLFCDYYNP EGQCEWHYQP CGVPCLRTCR NPRGDCLRDV 
      1210       1220       1230       1240       1250
RGLEGCYPKC PPEAPIFDED KMQCVATCPT PPLPPRCHVH GKSYRPGAVV 
      1260       1270       1280       1290       1300
PSDKNCQSCL CTERGVECTY KAEACVCTYN GQRFHPGDVI YHTTDGTGGC 
      1310       1320       1330       1340       1350
ISARCGANGT IERRVYPCSP TTPVPPTTFS FSTPPLVVSS THTPSNGPSS 
      1360       1370       1380       1390       1400
AHTGPPSSAW PTTAGTSPRT RLPTASASLP PVCGEKCLWS PWMDVSRPGR 
      1410       1420       1430       1440       1450
GTDSGDFDTL ENLRAHGYRV CESPRSVECR AEDAPGVPLR ALGQRVQCSP 
      1460       1470       1480       1490       1500
DVGLTCRNRE QASGLCYNYQ IRVQCCTPLP CSTSSSPAQT TPPTTSKTTE 
      1510       1520       1530       1540       1550
TRASGSSAPS STPGTVSLST ARTTPAPGTA TSVKKTFSTP SPPPVPATST 
      1560       1570       1580       1590       1600
SSMSTTAPGT SVVSSKPTPT EPSTSSCLQE LCTWTEWIDG SYPAPGINGG 
      1610       1620       1630       1640       1650
DFDTFQNLRD EGYTFCESPR SVQCRAESFP NTPLADLGQD VICSHTEGLI 
      1660       1670       1680       1690       1700
CLNKNQLPPI CYNYEIRIQC CETVNVCRDI TRLPKTVATT RPTPHPTGAQ 
      1710       1720       1730       1740       1750
TQTTFTTHMP SASTEQPTAT SRGGPTATSV TQGTHTTLVT RNCHPRCTWT 
      1760       1770       1780       1790       1800
KWFDVDFPSP GPHGGDKETY NNIIRSGEKI CRRPEEITRV QCRAKSHPEV 
      1810       1820       1830       1840       1850
SIEHLGQVVQ CSREEGLVCR NQDQQGPFKM CLNYEVRVLC CETPRGCHMT 
      1860       1870       1880       1890       1900
STPGSTSSSP AQTTPSTTSK TTEIQASGSS APSSTPGTVS LSTARTTPAP 
      1910       1920       1930       1940       1950
GTATSVKKTF STPSPPPVPA TSTSSMSTTA PGTSVVSSKP TPTEPSTSSC 
      1960       1970       1980       1990       2000
LQELCTWTEW IDGSYPAPGI NGGDFDTFQN LRDEGYTFCE SPRSVQCRAE 
      2010       2020       2030       2040       2050
SFPNTPLGRL GQDVICSHTE GLICLNKNQL PPICYNYEIR IQCCETVNVC 
      2060       2070       2080       2090       2100
RDITRPPKTV ATTRPTPHPT GAQTQTTFTT HMPSASTEQP TATSRGGPTA 
      2110       2120       2130       2140       2150
TSVTQGTHTT PVTRNCHPRC TWTTWFDVDF PSPGPHGGDK ETYNNIIRSG 
      2160       2170       2180       2190       2200
EKICRRPEEI TRLQCRAKSH PEVSIEHLGQ VVQCSREEGL VCRNQDQQGP 
      2210       2220       2230       2240       2250
FKMCLNIEVR VLCCETPKGC PVTSTPVTAP STPSGRAISP TQSTSSWQKS 
      2260       2270       2280       2290       2300
RTTTLVTTST TSTPQTSTTY AHTTSTTSAP TARTTSAPTT STTSVPTTST 
      2310       2320       2330       2340       2350
ISGPKTTPSP VPTTSTTSAA TTSTISAPTT STTSVPGTTP SPVLTTSTTS 
      2360       2370       2380       2390       2400
APTTRTTSAS PAGTTSGPGN TPSPVPTTST ISAPTTSITS APTTSTTSAP 
      2410       2420       2430       2440       2450
TSSTTSGPGT TPSPVPTTSI TSAPTTSTTS APTTSTTSAP TTSTTSAPTT 
      2460       2470       2480       2490       2500
STTSAPTTST TSTPTSSTTS TPQTSTTSAS TTSITSGPGT TPSPVPTTST 
      2510       2520       2530       2540       2550
TSAPTTSTTS AATTSTISAP TTSTTSAPTT STTSASTASK TSGLGTTPSP 
      2560       2570       2580       2590       2600
IPTTSTTSPP TTSTTSASTA SKTSGPGTTP SPVPTTSTIF APRTSTTSAS 
      2610       2620       2630       2640       2650
TTSTTPGPGT TPSPVPTTST ASVSKTSTSH VSISKTTHSQ PVTRDCHLRC 
      2660       2670       2680       2690       2700
TWTKWFDVDF PSPGPHGGDK ETYNNIIRSG EKICRRPEEI TRLQCRAESH 
      2710       2720       2730       2740       2750
PEVSIEHLGQ VVQCSREEGL VCRNQDQQGP FKMCLNYEVR VLCCETPKGC 
      2760       2770       2780       2790       2800
PVTSTPVTAP STPSGRATSP TQSTSSWQKS RTTTLVTTST TSTPQTSTTS 
      2810       2820       2830       2840       2850
APTTSTTSAP TTSTTSAPTT STTSTPQTSI SSAPTSSTTS APTSSTISAR 
      2860       2870       2880       2890       2900
TTSIISAPTT STTSSPTTST TSATTTSTTS APTSSTTSTP QTSKTSAATS 
      2910       2920       2930       2940       2950
STTSSSGTTP SPVTTTSTAS VSKTSTSHVS VSKTTHSQPV TRDCHPRCTW 
      2960       2970       2980       2990       3000
TKWFDVDFPS PGPHGGDKET YNNIIRSGEK ICRRPQEITR LQCRAKSHPE 
      3010       3020       3030       3040       3050
VSIEHLGQVV QCSREEGLVC RNQDQQGPFK MCLNYEVRVL CCETPKGCPV 
      3060       3070       3080       3090       3100
TSTSVTAPSP LVGEPPAQTQ STSSWQKSRT TTLVTSSITS TTQTSTTSAP 
      3110       3120       3130       3140       3150
TTSTTPASIP STTSAPTTST TSAPTTSTTS APTTSTTSTP QTTTSSAPTS 
      3160       3170       3180       3190       3200
STTSAPTTST ISAPTTSTIS APTTSTTSAP TASTTSAPTS TSSAPTTNTT 
      3210       3220       3230       3240       3250
SAPTTSTTSA PITSTISAPT TSTTSTPQTS TISSPTTSTT PTPQTSTTSS 
      3260       3270       3280       3290       3300
PTTSTTSAPT TSTTSAPTTS TTSTPQTSIS SAPTSSTTSA PTASTISAPT 
      3310       3320       3330       3340       3350
TSTTSFHTTS TTSPPTSSTS STPQTSKTSA ATSSTTSGSG TTPSPVPTTS 
      3360       3370       3380       3390       3400
TASVSKTSTS HVSVSKTTHS QPVTRDCHPR CTWTKWFDVD FPSPGPHGGD 
      3410       3420       3430       3440       3450
KETYNNIIRS GEKICRRPEE ITRLQCRAES HPEVSIEHLG QVVQCSREEG 
      3460       3470       3480       3490       3500
LVCRNQDQQG PFKMCLNYEV RVLCCETPKG CPVTSTPVTA PSTPSGRATS 
      3510       3520       3530       3540       3550
PTQSTSSWQK SRTTTLVTTS TTSTPQTSTT SAPTTSTIPA STPSTTSAPT 
      3560       3570       3580       3590       3600
TSTTSAPTTS TTSAPTHRTT SGPTTSTTLA PTTSTTSAPT TSTNSAPTTS 
      3610       3620       3630       3640       3650
TISASTTSTI SAPTTSTISS PTSSTTSTPQ TSKTSAATSS TTSGSGTTPS 
      3660       3670       3680       3690       3700
PVPTTSTTSA STTSTTSAPT TSTTSGPGTT PSPVPSTSIT SAATTSTTSA 
      3710       3720       3730       3740       3750
PTTRTTSAPT SSMTSGPGTT PSPVPTTSTT SAPTTSTTSG PGTTPSPVPT 
      3760       3770       3780       3790       3800
TSTTSAPITS TTSGPGSTPS PVPTTSTTSA PTTSTTSAST ASTTSGPTTS 
      3810       3820       3830       3840       3850
TTSASTTSTI SPLTTSTTSA PITSMPSGPG TTPSPVPTTS TTSAPTTSTT 
      3860       3870       3880       3890       3900
SGPGTTPSPV PTTSTTSAPT TSTTSASTAS TTSGPGTTPS PVPTTSTTSA 
      3910       3920       3930       3940       3950
PTTSTTSAST ASTTSGPGTS LSPVPTTSTT SAPTTSTTSG PGTTPSPVPT 
      3960       3970       3980       3990       4000
TSTTSAPTTS TTSGPGTTPS PVPTTSTTPV SKTSTSHLSV SKTTHSQPVT 
      4010       4020       4030       4040       4050
SDCHPLCAWT KWFDVDFPSP GPHGGDKETY NNIIRSGEKI CRRPEEITRL 
      4060       4070       4080       4090       4100
QCRAESHPEV NIEHLGQVVQ CSREEGLVCR NQDQQGPFKM CLNYEVRVLC 
      4110       4120       4130       4140       4150
CETPRGCPVT SVTPYGTSPT NALYPSLSTS MVSASVASTS VASSSVASSS 
      4160       4170       4180       4190       4200
VAYSTQTCFC NVADRLYPAG STIYRHRDLA GHCYYALCSQ DCQVVRGVDS 
      4210       4220       4230       4240       4250
DCPSTTLPPA PATSPSISTS EPVTELGCPN AVPPRKKGET WATPNCSEAT 
      4260       4270       4280       4290       4300
CEGNNVISLS PRTCPRVEKP TCANGYPAVK VADQDGCCHH YQCQCVCSGW 
      4310       4320       4330       4340       4350
GDPHYITFDG TYYTFLDNCT YVLVQQIVPV YGHFRVLVDN YFCGAEDGLS 
      4360       4370       4380       4390       4400
CPRSIILEYH QDRVVLTRKP VHGVMTNEII FNNKVVSPGF RKNGIVVSRI 
      4410       4420       4430       4440       4450
GVKMYATIPE LGVQVMFSGL IFSVEVPFSK FANNTEGQCG TCTNDRKDEC 
      4460       4470       4480       4490       4500
RTPRGTVVAS CSEMSGLWNV SIPDQPACHR PHPTPTTVGP TTVGSTTVGP 
      4510       4520       4530       4540       4550
TTVGSTTVGP TTPPAPCLPS PICHLILSKV FEPCHTVIPP LLFYEGCVFD 
      4560       4570       4580       4590       4600
RCHMTDLDVV CSSLELYAAL CASHDICIDW RGRTGHMCPF TCPADKVYQP 
      4610       4620       4630       4640       4650
CGPSNPSYCY GNDSASLGAL REAGPITEGC FCPEGMTLFS TSAQVCVPTG 
      4660       4670       4680       4690       4700
CPRCLGPHGE PVKVGHTVGM DCQECTCEAA TWTLTCRPKL CPLPPACPLP 
      4710       4720       4730       4740       4750
GFVPVPAAPQ AGQCCPQYSC ACNTSRCPAP VGCPEGARAI PTYQEGACCP 
      4760       4770       4780       4790       4800
VQNCSWTVCS INGTLYQPGA VVSSSLCETC RCELPGGPPS DAFVVSCETQ 
      4810       4820       4830       4840       4850
ICNTHCPVGF EYQEQSGQCC GTCVQVACVT NTSKSPAHLF YPGETWSDAG 
      4860       4870       4880       4890       4900
NHCVTHQCEK HQDGLVVVTT KKACPPLSCS LDEARMSKDG CCRFCPLPPP 
      4910       4920       4930       4940       4950
PYQNQSTCAV YHRSLIIQQQ GCSSSEPVRL AYCRGNCGDS SSMYSLEGNT 
      4960       4970       4980       4990       5000
VEHRCQCCQE LRTSLRNVTL HCTDGSSRAF SYTEVEECGC MGRRCPAPGD 
      5010       5020       5030
TQHSEEAEPE PSQEAESGSW ERGVPVSPMH                       

<p>Reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.</p><p><a href='../manual/sequence_caution' target='_top'>More...</a></p>Sequence cautionⁱ

Experimental Info

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	221 – 221	1	S → R in AAC15950. (PubMed:9506983)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	432 – 432	1	D → G in AAC15950. (PubMed:9506983)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	549 – 549	1	P → L in AAC15950. (PubMed:9506983)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	658 – 658	1	V → M in AAC15950. (PubMed:9506983)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	702 – 702	1	T → I in AAC15950. (PubMed:9506983)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	716 – 716	1	T → A in AAC15950. (PubMed:9506983)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	817 – 818	2	GD → RG in AAC15950. (PubMed:9506983)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	869 – 869	1	E → K in AAC15950. (PubMed:9506983)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	978 – 978	1	G → R in AAC15950. (PubMed:9506983)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	996 – 996	1	Q → R in AAC15950. (PubMed:9506983)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	1803 – 1803	1	E → N AA sequence (PubMed:2656675)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	2176 – 2176	1	E → N AA sequence (PubMed:2656675)Curated
<p>Is used to indicate that two residues in a sequence are not consecutive and that there is an undetermined number of unsequenced residues between them.</p><p><a href='../manual/non_cons' target='_top'>More...</a></p>Non-adjacent residuesi	2448 – 2449	2	Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	3004 – 3004	1	E → N AA sequence (PubMed:2656675)Curated
<p>Is used to indicate that two residues in a sequence are not consecutive and that there is an undetermined number of unsequenced residues between them.</p><p><a href='../manual/non_cons' target='_top'>More...</a></p>Non-adjacent residuesi	3797 – 3798	2	Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	3990 – 3991	2	VS → HE in AAA18431. (PubMed:7513696)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	4203 – 4203	1	P → R in CAA88307. (PubMed:7775418)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	4260 – 4262	3	SPR → RPP in AAA18431. (PubMed:7513696)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	4275 – 4275	1	G → A in AAA18431. (PubMed:7513696)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	4389 – 4389	1	G → A in CAA88307. (PubMed:7775418)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	4457 – 4460	4	VVAS → HASA in AAH33831. (PubMed:15489334)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	4524 – 4524	1	H → Q in CAA04737. (PubMed:9620876)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	4524 – 4524	1	H → Q in CAA04738. (PubMed:9620876)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	4569 – 4569	1	A → R in AAA18431. (PubMed:7513696)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	4621 – 4621	1	R → P in CAA88307. (PubMed:7775418)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	4640 – 4640	1	S → T in CAA04737. (PubMed:9620876)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	4640 – 4640	1	S → T in CAA04738. (PubMed:9620876)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	4732 – 4732	1	G → R in AAA18431. (PubMed:7513696)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	4739 – 4739	1	A → R in AAA18431. (PubMed:7513696)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	4809 – 4809	1	G → R in AAA18431. (PubMed:7513696)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	4922 – 4922	1	C → S in AAA18431. (PubMed:7513696)Curated

Natural variant

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes natural variant(s) of the protein sequence.</p><p><a href='../manual/variant' target='_top'>More...</a></p>Natural varianti	4897 – 4897	1	L → P.2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.5 "Genomic organization of the 3'-region of the human MUC5AC mucin gene: additional evidence for a common ancestral gene for the 11p15.5 mucin gene family." Buisine M.P., Desseyn J.-L., Porchet N., Degand P., Laine A., Aubert J.-P. Biochem. J. 332:729-738(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 3950-5030, VARIANT PRO-4897. Ref.9 "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4457-5030, VARIANT PRO-4897. Corresponds to variant rs1132436 [ dbSNP | Ensembl ].		VAR_036832

Sequence databases

Polymorphism databases

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityⁱ

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

<p>Provides links to various web resources that are relevant for a specific protein.</p><p><a href='../manual/web_resource' target='_top'>More...</a></p>Web resourcesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>Contains the literature citations that are the sources of data used to annotate the entry. Each reference is numbered and contains several subsections allowing a precise description of a given citation.</p><p><a href='../manual/publications_section' target='_top'>More...</a></p>Publicationsⁱ

1. "Human mucin gene MUC5AC: organization of its 5'-region and central repetitive region."
   Escande F., Aubert J.-P., Porchet N., Buisine M.P.
   Biochem. J. 358:763-772(2001) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-2448, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2449-3797, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3798-4169.
2. "Cloning of the amino-terminal and 5'-flanking region of the human MUC5AC mucin gene and transcriptional up-regulation by bacterial exoproducts."
   Li D., Gallup M., Fan N., Szymkowski D.E., Basbaum C.B.
   J. Biol. Chem. 273:6812-6820(1998) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1104.
   Tissue: Trachea.
   
3. "Cloning and analysis of human gastric mucin cDNA reveals two types of conserved cysteine-rich domains."
   Klomp L.W., Van Rens L., Strous G.J.
   Biochem. J. 308:831-838(1995) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1005-1854.
4. "Proteolytic fragmentation and peptide mapping of human carboxyamidomethylated tracheobronchial mucin."
   Rose M.C., Kaufman B., Martin B.M.
   J. Biol. Chem. 264:8193-8199(1989) [PubMed] [Europe PMC] [Abstract]
   Cited for: PROTEIN SEQUENCE OF 1752-1773; 1796-1805; 2125-2146; 2169-2178; 2655-2676; 2697-2708; 2953-2974; 2997-3006; 3386-3407; 3428-3439 AND 4012-4033.
   Tissue: Tracheobronchial mucosa.
   
5. "Genomic organization of the 3'-region of the human MUC5AC mucin gene: additional evidence for a common ancestral gene for the 11p15.5 mucin gene family."
   Buisine M.P., Desseyn J.-L., Porchet N., Degand P., Laine A., Aubert J.-P.
   Biochem. J. 332:729-738(1998) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 3950-5030, VARIANT PRO-4897.
   Tissue: Placenta and Trachea.
   
6. "Cloning and analysis of cDNA encoding a major airway glycoprotein, human tracheobronchial mucin (MUC5)."
   Meerzaman D., Charles P., Daskal E., Polymeropoulos M.H., Martin B.M., Rose M.C.
   J. Biol. Chem. 269:12932-12939(1994) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3990-5030, PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY.
   Tissue: Nasal polyp.
   
7. "Characterization of a mucin cDNA clone isolated from HT-29 mucus secreting cells: the 3' end of MUC5AC?"
   Lesuffleur T., Roche F., Hill A.S., Lacasa M., Fox M., Swallow D.M., Zweibaum A., Real F.X.
   J. Biol. Chem. 270:13665-13673(1995) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4081-5030.
8. "Cleavage in the GDPH sequence of the C-terminal cysteine-rich part of the human MUC5AC mucin."
   Lidell M.E., Hansson G.C.
   Biochem. J. 399:121-129(2006) [PubMed] [Europe PMC] [Abstract]
   Cited for: PROTEIN SEQUENCE OF 4303-4312, PROTEOLYTIC PROCESSING, MUTAGENESIS OF ASP-4302.
9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
   The MGC Project Team
   Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4457-5030, VARIANT PRO-4897.
   Tissue: Colon.
   
10. "The full-ORF clone resource of the German cDNA consortium."
    Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
    BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4569-5030.
    Tissue: Stomach.
    
11. "In vivo glycosylation of mucin tandem repeats."
    Silverman H.S., Parry S., Sutton-Smith M., Burdick M.D., McDermott K., Reid C.J., Batra S.K., Morris H.R., Hollingsworth M.A., Dell A., Harris A.
    Glycobiology 11:459-471(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE OF O-LINKED CARBOHYDRATES.
12. "The MUC5AC glycoprotein is the primary receptor for Helicobacter pylori in the human stomach."
    Van de Bovenkamp J.H., Mahdavi J., Korteland-Van Male A.M., Bueller H.A., Einerhand A.W., Boren T., Dekker J.
    Helicobacter 8:521-532(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS LEWIS B BLOOD GROUP ANTIGEN, TISSUE SPECIFICITY, INTERACTION WITH HELICOBACTER PYLORI.
13. "C-Mannosylation of MUC5AC and MUC5B Cys subdomains."
    Perez-Vilar J., Randell S.H., Boucher R.C.
    Glycobiology 14:325-337(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT TRP-2122, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-2122.

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

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

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - Technical termⁱ

Documents

1. Human chromosome 11
   Human chromosome 11: entries, gene names and cross-references to MIM
2. Human entries with polymorphisms or disease mutations
   List of human entries with polymorphisms or disease mutations
3. Human polymorphisms and disease mutations
   Index of human polymorphisms and disease mutations
4. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
5. SIMILARITY comments
   Index of protein domains and families

External Data

<p>Provides links to the UniProt Reference Clusters (<a href="/help/uniref">UniRef</a>). UniRef consists of clusters for UniProtKB sequences (including isoforms) and selected UniParc sequences, in order to obtain complete coverage of the sequence space at resolutions of 100%, 90% and 50% identity.</p><p><a href='../manual/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ