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

<p>Describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the ‘Names and taxonomy’ section.</p><p><a href='../manual/catalytic_activity' target='_top'>More...</a></p>Catalytic activityⁱ

<p>Describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.</p><p><a href='../manual/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationⁱ

Sites

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.</p><p><a href='../manual/binding' target='_top'>More...</a></p>Binding sitei	1973 – 1973	1	ATPPROSITE-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:PRU00159
<p>Is used for enzymes and indicates the residues directly involved in catalysis.</p><p><a href='../manual/act_site' target='_top'>More...</a></p>Active sitei	2072 – 2072	1	Proton acceptorPROSITE-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:PRU00159 PROSITE-ProRule:PRU10028

Regions

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.</p><p><a href='../manual/np_bind' target='_top'>More...</a></p>Nucleotide bindingi	1944 – 1952	9	ATPPROSITE-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:PRU00159

<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. ATP binding Source: UniProtKB-KW
2. protein phosphatase binding Source: UniProtKB

   <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ

   • 11266449

3. protein tyrosine kinase activity Source: UniProtKB
4. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB-EC

<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. cell differentiation 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

   • 11266449

2. cell growth Source: UniProtKB
3. cell proliferation 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

   • 11266449

4. columnar/cuboidal epithelial cell development Source: UniProtKB

   <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ

   • 8675006

5. negative regulation of gene expression Source: MGI

   <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ

   • 12773415

6. peptidyl-tyrosine phosphorylation Source: GOC
7. protein phosphorylation 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

   • 11266449

8. regulation of ERK1 and ERK2 cascade 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

   • 11266449

9. regulation of phosphate transport Source: MGI

   <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ

   • 12773415

10. regulation of TOR signaling Source: UniProtKB
11. spermatogenesis Source: UniProtKB

    <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ

    • 8675006

<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 - Molecular functionⁱ

<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 - Ligandⁱ

<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

Topology

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.</p><p><a href='../manual/topo_dom' target='_top'>More...</a></p>Topological domaini	29 – 1854	1826	ExtracellularSequence Analysis			Add BLAST
<p>Describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.</p><p><a href='../manual/transmem' target='_top'>More...</a></p>Transmembranei	1855 – 1875	21	HelicalSequence Analysis			Add BLAST
<p>Describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.</p><p><a href='../manual/topo_dom' target='_top'>More...</a></p>Topological domaini	1876 – 2340	465	CytoplasmicSequence Analysis			Add BLAST

<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. integral component of membrane Source: UniProtKB-KW
2. plasma membrane Source: UniProtKB-SubCell

<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

<p>Describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.</p><p><a href='../manual/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypeⁱ

Mice are viable and healthy. Females display normal fertility while males are sterile due a non-cell autonomous defect in sperm maturation. It is associated with the absence of tall columnar epithelial cells with long microvilli in the proximal part of the caput epididymidis.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.3

  "The c-ros tyrosine kinase receptor controls regionalization and differentiation of epithelial cells in the epididymis."
  Sonnenberg-Riethmacher E., Walter B., Riethmacher D., Goedecke S., Birchmeier C.
  Genes Dev. 10:1184-1193(1996) [PubMed] [Europe PMC] [Abstract]

  Cited for: DISRUPTION PHENOTYPE, FUNCTION IN EPITHELIUM DIFFERENTIATION, TISSUE SPECIFICITY.

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	2267 – 2267	1	Y → F: Abrogates interaction with PTPN6. 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.6 "Negative regulation of Ros receptor tyrosine kinase signaling. An epithelial function of the SH2 domain protein tyrosine phosphatase SHP-1." Keilhack H., Mueller M., Boehmer S.A., Frank C., Weidner K.M., Birchmeier W., Ligensa T., Berndt A., Kosmehl H., Guenther B., Mueller T., Birchmeier C., Boehmer F.D. J. Cell Biol. 152:325-334(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CELL PROLIFERATION, INTERACTION WITH PTPN6, ENZYME REGULATION, PHOSPHORYLATION AT TYR-2267, MUTAGENESIS OF TYR-2267.

<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 - Diseaseⁱ

<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 – 28	28	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	29 – 2340	2312	Proto-oncogene tyrosine-protein kinase ROS		PRO_0000278115	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<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	53 – 53	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	334 – 334	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	362 – 362	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	935 – 935	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	1011 – 1011	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	1243 – 1243	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	1676 – 1676	1	N-linked (GlcNAc...)Sequence Analysis
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	2267 – 2267	1	Phosphotyrosine; by autocatalysis1 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.6 "Negative regulation of Ros receptor tyrosine kinase signaling. An epithelial function of the SH2 domain protein tyrosine phosphatase SHP-1." Keilhack H., Mueller M., Boehmer S.A., Frank C., Weidner K.M., Birchmeier W., Ligensa T., Berndt A., Kosmehl H., Guenther B., Mueller T., Birchmeier C., Boehmer F.D. J. Cell Biol. 152:325-334(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CELL PROLIFERATION, INTERACTION WITH PTPN6, ENZYME REGULATION, PHOSPHORYLATION AT TYR-2267, MUTAGENESIS OF TYR-2267.
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	2327 – 2327	1	Phosphotyrosine; by autocatalysisBy similarity

<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

<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	111 – 206	96	Fibronectin type-III 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:PRU00316			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	207 – 295	89	Fibronectin type-III 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:PRU00316			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	567 – 667	101	Fibronectin type-III 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:PRU00316			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	943 – 1038	96	Fibronectin type-III 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:PRU00316			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	1039 – 1146	108	Fibronectin type-III 5PROSITE-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:PRU00316			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	1442 – 1549	108	Fibronectin type-III 6PROSITE-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:PRU00316			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	1550 – 1649	100	Fibronectin type-III 7PROSITE-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:PRU00316			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	1651 – 1744	94	Fibronectin type-III 8PROSITE-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:PRU00316			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	1745 – 1846	102	Fibronectin type-III 9PROSITE-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:PRU00316			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	1938 – 2216	279	Protein kinasePROSITE-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:PRU00159			Add BLAST

<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: Complete.

<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
MKNICWLTLK LVKFVVLGCI IWISVAQSTV LSSCLTSCVT NLGRQLDSGT 
        60         70         80         90        100
RYNLSEACIH GCQFWNSVDQ ETCALKCNDT YATICERESC EVGCSNAEGS 
       110        120        130        140        150
YEEEVLESTE LPTAPFASSI GSHGVTLRWN PANISGVKYI IQWKYAQLPG 
       160        170        180        190        200
SWTFTETVSK LSYTVEPLHP FTEYIFRVVW IFTAQLHLYS PPSPSYRTHP 
       210        220        230        240        250
YGVPETAPLI LNMESWSPDT VEVSWAPPHF PGGPILGYNL RLISKNQKLD 
       260        270        280        290        300
SGTQRTSFQF YSTLPNTTYR FSIAAVNEVG EGPEAESTVT TPSPSVQEEE 
       310        320        330        340        350
QWLFLSRKTS LRKRSLKYLV DEAHCLWSDA IHHNITGISV YAQQQVVYFS 
       360        370        380        390        400
EGTVIWMKGA ANMSDVSDLR IFYQGSGLVS SISIDWLYQR MYFIMDKLVY 
       410        420        430        440        450
VCELKNCSNL EEITPFSLIA PQKVVVDSYN GYLFYLLRDG IYRVNLPLPS 
       460        470        480        490        500
GRDTKAVRIV ESGTLKDFAV KPQSKRIIYF NDTMQLFMST FLDGSAFHRV 
       510        520        530        540        550
LPWVPLVTVK SFACENNDFL ITDGKAIFQQ DSLSFNEFIV GCDLSHIEEF 
       560        570        580        590        600
GFGNLVIFGS SVQSYPLPGH PQEVSVLFGS REALIQWTPP ALAIGASPSA 
       610        620        630        640        650
WQNWTYEVKV YSQDILEITQ VFSNISGTML NVPELQSSTK YTVSVRASSP 
       660        670        680        690        700
KGPGPWSAPS VGTTLVPATE PPFIMAVKED GLWSKPLCSF GPGEFLSSDV 
       710        720        730        740        750
GNVSDMDWYN NSLYYSDTKG NVYVRPLNGM DISENYHIPS IVGAGALAFE 
       760        770        780        790        800
WLGHFLYWAG KTYVIQRQSV LTGHTDIVTH VKLLVNDMAV DSVGGYLYWT 
       810        820        830        840        850
TLYSVESTRL NGESSLVLQA QPWLSGKKVI ALTLDLSDGL LYWLVQDNQC 
       860        870        880        890        900
IHLYTAVLRG WSGGDATITE FAAWSTSEIS QNALMYYSGR LFWINGFRII 
       910        920        930        940        950
TAQEIGQRTS VSVSEPAKFN QFTIIQTSLK PLPGNFSSTP KVIPDPVQES 
       960        970        980        990       1000
SFRIEGHTSS FQILWNEPPA VDWGIVFYSV EFSTHSKFLI IEQQSLPIFT 
      1010       1020       1030       1040       1050
VEGLEPYTLF NLSVTPYTYW GKGQKTSLSF RAPESVPSAP ENPRIFILSS 
      1060       1070       1080       1090       1100
GRYTKKNEVV VEFRWNKPKH ENGVLTKFEI FYHISKQSGT NRSTEDWMSA 
      1110       1120       1130       1140       1150
SVIPPVMSFQ LEAVSPEYTV AFQVRVFTSK GPGPFSDIVM SKTSEIKPCP 
      1160       1170       1180       1190       1200
YLISLLGNKI VFLDMDQNQV LWTFSLEGDV STVGYTTDDE MGYFAQGDTL 
      1210       1220       1230       1240       1250
FLLNLRNHSS SKLFQDALVS DIRVIAVDWI ARHLYFALKA SQNGTQIFNV 
      1260       1270       1280       1290       1300
DLEHKVKSPR EVKTCKAHTT IISFSIYPLL SRLYWTEVSD LGHQMFYCNI 
      1310       1320       1330       1340       1350
SNHTSQHVLQ PKASNQHGRS QCSCNVTESE LSGAMTVDTS DPDRPWIYFT 
      1360       1370       1380       1390       1400
KRQEIWAMDL EGCQCWKVIM VPTIPGKRII SLTVDGEFIY WIMKTKDDAQ 
      1410       1420       1430       1440       1450
IYQAKKGSGA ILSQVKASRS KHILAYSSAL QPFPDKAYLS LASDMVEATI 
      1460       1470       1480       1490       1500
LYATNTSLTL KLPPVKTNLT WHGITHPTST YLIYYMEANR ANSSDRRHKM 
      1510       1520       1530       1540       1550
LESQENVARI EGLQPFSMYM IQIAVKNYYS EPLEHLPLGK EIQGQTKSGV 
      1560       1570       1580       1590       1600
PGAVCHINAT VLSDTSLHVF WTESHKPNGP KESVRYQLVM SYLAPIPETP 
      1610       1620       1630       1640       1650
LRQGEFPSAK LSLLITKLSG GQLYVMKVLA CHPEEMWCTE SHPVSVNMFD 
      1660       1670       1680       1690       1700
TPEKPSALVP ENTSLQLDWK ARSNVNLTGF WFELQKWKYN EFYHVKASCS 
      1710       1720       1730       1740       1750
QGPVYVCNIT DLQPYTSYNI RVVVVYTTGE NSSSIPESFK TKAGVPSKPG 
      1760       1770       1780       1790       1800
IPKLLEGSKN SIQWEKAEDN GSRLMYYTLE VRKGISNDSQ NQSSRWKVVF 
      1810       1820       1830       1840       1850
NGSCSSICTW RSKNLKGTFQ FRAVAANEIG LGEYSEISED ITLVEDGVWI 
      1860       1870       1880       1890       1900
TETSFILTII VGIFLVATVP LTFVWHRSLK SHKASKEGLS VLNDNDKELA 
      1910       1920       1930       1940       1950
ELRGLAAGVG LANACYAVHT VPTQEEIENL PAFPREKLSL RLLLGSGAFG 
      1960       1970       1980       1990       2000
EVYEGTAIDI LGVGSGEIKV AVKTLKKGST DQEKIEFLKE AHLMSKFNHP 
      2010       2020       2030       2040       2050
NILKQLGVCL LGEPQYIILE LMEGGDLLSY LRKARGTTFH GPSLTLLDLV 
      2060       2070       2080       2090       2100
ELCVDISKGC VYLEQMHFIH RDLAARNCLV SVKDYTSPRV VKIGDFGLAR 
      2110       2120       2130       2140       2150
EIYKNDYYRK RGEGLLPVRW MAPENLMDGI FTSQSDVWSF GILVWEILTL 
      2160       2170       2180       2190       2200
GHQPYPAHSN LDVLNYVQAG GRLEPPRNCP DDLWNLMSQC WAQEPDQRPT 
      2210       2220       2230       2240       2250
FHNIQNQLQL FRNVFLNNVS HCGEAAPTGG VINKGFEGED DEMVTLNSDD 
      2260       2270       2280       2290       2300
TMPVALMETK NQEGLNYMVL ATKCSQGEGS YEGPLGPKEL GSCDLKKDKK 
      2310       2320       2330       2340
QPQADKDFCQ EPQVAYGSPG LSEGLNYACL AHSEHGDVSE            

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	27 – 27	1	Q → L in AAA50600. (PubMed:8544427)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	109 – 111	3	TEL → QAI in AAA50600. (PubMed:8544427)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	329 – 329	1	D → Y in AAA50600. (PubMed:8544427)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	419 – 419	1	I → V in AAA50600. (PubMed:8544427)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	591 – 591	1	A → P in AAA50600. (PubMed:8544427)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	595 – 595	1	G → P in AAA50600. (PubMed:8544427)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	631 – 632	2	NV → KL in AAA50600. (PubMed:8544427)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	642 – 645	4	TVSV → PFSC in AAA50600. (PubMed:8544427)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	656 – 656	1	W → G in AAA50600. (PubMed:8544427)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	671 – 672	2	PP → LL in AAA50600. (PubMed:8544427)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	830 – 830	1	I → V in AAA50600. (PubMed:8544427)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	1050 – 1050	1	S → R in AAA50600. (PubMed:8544427)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	1066 – 1066	1	N → D in AAA50600. (PubMed:8544427)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	1085 – 1085	1	S → F in AAA50600. (PubMed:8544427)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	1235 – 1235	1	Y → C in AAA50600. (PubMed:8544427)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	1276 – 1276	1	I → T in AAA50600. (PubMed:8544427)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	1371 – 1371	1	V → L in AAA50600. (PubMed:8544427)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	1428 – 1429	2	SA → FR in AAA50600. (PubMed:8544427)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	1486 – 1487	2	ME → IK in AAA50600. (PubMed:8544427)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	1541 – 1545	5	EIQGQ → RFKDK in AAA50600. (PubMed:8544427)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	1585 – 1592	8	RYQLVMSY → AISWLMSD in AAA50600. (PubMed:8544427)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	1669 – 1669	1	W → R in AAA50600. (PubMed:8544427)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	1778 – 1778	1	T → S in AAA50600. (PubMed:8544427)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	1893 – 1893	1	N → S in AAA50600. (PubMed:8544427)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	1917 – 1918	2	AV → GI in AAA50600. (PubMed:8544427)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	2087 – 2087	1	S → N in AAA50600. (PubMed:8544427)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	2118 – 2118	1	V → A in AAA50600. (PubMed:8544427)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	2270 – 2272	3	LAT → VPQ in AAA50600. (PubMed:8544427)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	2333 – 2333	1	S → R in AAA50600. (PubMed:8544427)Curated

Sequence databases

Genome annotation databases

<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

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic 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. "Biochemical and functional characterization of the murine ros protooncogene."
   Riethmacher D., Langholz O., Godecke S., Sachs M., Birchmeier C.
   Oncogene 9:3617-3626(1994) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [MRNA].
   Strain: NMRI.
   Tissue: Intestine.
   
2. "Cloning of mouse c-ros renal cDNA, its role in development and relationship to extracellular matrix glycoproteins."
   Kanwar Y.S., Liu Z.Z., Kumar A., Wada J., Carone F.A.
   Kidney Int. 48:1646-1659(1995) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [MRNA].
   Strain: CD-1.
   Tissue: Kidney.
   
3. "The c-ros tyrosine kinase receptor controls regionalization and differentiation of epithelial cells in the epididymis."
   Sonnenberg-Riethmacher E., Walter B., Riethmacher D., Goedecke S., Birchmeier C.
   Genes Dev. 10:1184-1193(1996) [PubMed] [Europe PMC] [Abstract]
   Cited for: DISRUPTION PHENOTYPE, FUNCTION IN EPITHELIUM DIFFERENTIATION, TISSUE SPECIFICITY.
4. "Two chimeric receptors of epidermal growth factor receptor and c-Ros that differ in their transmembrane domains have opposite effects on cell growth."
   Xiong Q., Chan J.L., Zong C.S., Wang L.H.
   Mol. Cell. Biol. 16:1509-1518(1996) [PubMed] [Europe PMC] [Abstract]
   Cited for: FUNCTION IN CELL PROLIFERATION.
5. "Stat3 plays an important role in oncogenic Ros- and insulin-like growth factor I receptor-induced anchorage-independent growth."
   Zong C.S., Zeng L., Jiang Y., Sadowski H.B., Wang L.H.
   J. Biol. Chem. 273:28065-28072(1998) [PubMed] [Europe PMC] [Abstract]
   Cited for: FUNCTION IN STAT3 ACTIVATION.
6. "Negative regulation of Ros receptor tyrosine kinase signaling. An epithelial function of the SH2 domain protein tyrosine phosphatase SHP-1."
   Keilhack H., Mueller M., Boehmer S.A., Frank C., Weidner K.M., Birchmeier W., Ligensa T., Berndt A., Kosmehl H., Guenther B., Mueller T., Birchmeier C., Boehmer F.D.
   J. Cell Biol. 152:325-334(2001) [PubMed] [Europe PMC] [Abstract]
   Cited for: FUNCTION IN CELL PROLIFERATION, INTERACTION WITH PTPN6, ENZYME REGULATION, PHOSPHORYLATION AT TYR-2267, MUTAGENESIS OF TYR-2267.
7. "The role of phosphatidylinositol 3-kinase, rho family GTPases, and STAT3 in Ros-induced cell transformation."
   Nguyen K.T., Zong C.S., Uttamsingh S., Sachdev P., Bhanot M., Le M.T., Chan J.L., Wang L.H.
   J. Biol. Chem. 277:11107-11115(2002) [PubMed] [Europe PMC] [Abstract]
   Cited for: FUNCTION IN PI3 KINASE AND STAT3 ACTIVATION.

<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. MGD cross-references
   Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
2. Human and mouse protein kinases
   Human and mouse protein kinases: classification and index
3. 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