<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	412 – 413	2	Cleavage; by caspase-3

<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. anterior/posterior axon guidance Source: Ensembl
2. apoptotic process Source: Reactome
3. axon guidance Source: Reactome
4. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand 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

   • 18469807

5. negative regulation of neuron apoptotic process 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

   • 18469807

6. positive regulation of apoptotic process Source: Reactome
7. positive regulation of phosphatidylinositol 3-kinase signaling 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

   • 18469807

8. regulation of apoptotic process Source: Reactome
9. signal transduction Source: InterPro

<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 - Biological processⁱ

Enzyme and pathway 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

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	27 – 377	351	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	378 – 398	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	399 – 945	547	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

<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	412 – 412	1	D → N: Abolishes cleavage by caspase-3 and subsequent induction of apoptosis. 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.2 "p53RDL1 regulates of p53-dependent apoptosis." Tanikawa C., Matsuda K., Fukuda S., Nakamura Y., Arakawa H. Nat. Cell Biol. 5:216-223(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF ASP-412.

Organism-specific databases

<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 – 26	26	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	27 – 945	919	Netrin receptor UNC5B		PRO_0000036071	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	69 ↔ 128		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	174 ↔ 225		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	222 – 222	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	258 ↔ 295		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	262 ↔ 299		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	273 ↔ 285		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	347 – 347	1	N-linked (GlcNAc...)Sequence Analysis
<p>Specifies the position(s) and the type of covalently attached lipid group(s).</p><p><a href='../manual/lipid' target='_top'>More...</a></p>Lipidationi	403 – 403	1	S-palmitoyl cysteine1 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.9 "Lipid raft localization and palmitoylation: identification of two requirements for cell death induction by the tumor suppressors UNC5H." Maisse C., Rossin A., Cahuzac N., Paradisi A., Klein C., Haillot M.L., Herincs Z., Mehlen P., Hueber A.O. Exp. Cell Res. 314:2544-2552(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PALMITOYLATION AT CYS-403, SUBCELLULAR LOCATION, INTERACTION WITH DAPK1.

<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

Miscellaneous 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

<p>Reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).</p><p><a href='../manual/induction' target='_top'>More...</a></p>Inductionⁱ

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

<p>Provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.</p><p><a href='../manual/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

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	48 – 145	98	Ig-like			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	147 – 242	96	Ig-like C2-type			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	246 – 300	55	TSP type-1 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:PRU00210			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	302 – 354	53	TSP type-1 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:PRU00210			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	544 – 688	145	ZU5PROSITE-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:PRU00485			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	865 – 943	79	Death			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	689 – 838	150	UPA domainBy similarity			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	707 – 725	19	Interaction with DCCBy similarity			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>Sequences (2)ⁱ

<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.

This entry describes 2<p>Lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.</p><p><a href='../manual/alternative_products' target='_top'>More...</a></p> isoformsⁱ produced by alternative splicing. Align

        10         20         30         40         50
MGARSGARGA LLLALLLCWD PRLSQAGTDS GSEVLPDSFP SAPAEPLPYF 
        60         70         80         90        100
LQEPQDAYIV KNKPVELRCR AFPATQIYFK CNGEWVSQND HVTQEGLDEA 
       110        120        130        140        150
TGLRVREVQI EVSRQQVEEL FGLEDYWCQC VAWSSAGTTK SRRAYVRIAY 
       160        170        180        190        200
LRKNFDQEPL GKEVPLDHEV LLQCRPPEGV PVAEVEWLKN EDVIDPTQDT 
       210        220        230        240        250
NFLLTIDHNL IIRQARLSDT ANYTCVAKNI VAKRRSTTAT VIVYVNGGWS 
       260        270        280        290        300
SWAEWSPCSN RCGRGWQKRT RTCTNPAPLN GGAFCEGQAF QKTACTTICP 
       310        320        330        340        350
VDGAWTEWSK WSACSTECAH WRSRECMAPP PQNGGRDCSG TLLDSKNCTD 
       360        370        380        390        400
GLCMQNKKTL SDPNSHLLEA SGDAALYAGL VVAIFVVVAI LMAVGVVVYR 
       410        420        430        440        450
RNCRDFDTDI TDSSAALTGG FHPVNFKTAR PSNPQLLHPS VPPDLTASAG 
       460        470        480        490        500
IYRGPVYALQ DSTDKIPMTN SPLLDPLPSL KVKVYSSSTT GSGPGLADGA 
       510        520        530        540        550
DLLGVLPPGT YPSDFARDTH FLHLRSASLG SQQLLGLPRD PGSSVSGTFG 
       560        570        580        590        600
CLGGRLSIPG TGVSLLVPNG AIPQGKFYEM YLLINKAEST LPLSEGTQTV 
       610        620        630        640        650
LSPSVTCGPT GLLLCRPVIL TMPHCAEVSA RDWIFQLKTQ AHQGHWEEVV 
       660        670        680        690        700
TLDEETLNTP CYCQLEPRAC HILLDQLGTY VFTGESYSRS AVKRLQLAVF 
       710        720        730        740        750
APALCTSLEY SLRVYCLEDT PVALKEVLEL ERTLGGYLVE EPKPLMFKDS 
       760        770        780        790        800
YHNLRLSLHD LPHAHWRSKL LAKYQEIPFY HIWSGSQKAL HCTFTLERHS 
       810        820        830        840        850
LASTELTCKI CVRQVEGEGQ IFQLHTTLAE TPAGSLDTLC SAPGSTVTTQ 
       860        870        880        890        900
LGPYAFKIPL SIRQKICNSL DAPNSRGNDW RMLAQKLSMD RYLNYFATKA 
       910        920        930        940 
SPTGVILDLW EALQQDDGDL NSLASALEEM GKSEMLVAVA TDGDC 

        10         20         30         40         50
MGARSGARGA LLLALLLCWD PRLSQAGTDS GSEVLPDSFP SAPAEPLPYF 
        60         70         80         90        100
LQEPQDAYIV KNKPVELRCR AFPATQIYFK CNGEWVSQND HVTQEGLDEA 
       110        120        130        140        150
TGLRVREVQI EVSRQQVEEL FGLEDYWCQC VAWSSAGTTK SRRAYVRIAY 
       160        170        180        190        200
LRKNFDQEPL GKEVPLDHEV LLQCRPPEGV PVAEVEWLKN EDVIDPTQDT 
       210        220        230        240        250
NFLLTIDHNL IIRQARLSDT ANYTCVAKNI VAKRRSTTAT VIVYVNGGWS 
       260        270        280        290        300
SWAEWSPCSN RCGRGWQKRT RTCTNPAPLN GGAFCEGQAF QKTACTTICP 
       310        320        330        340        350
VDGAWTEWSK WSACSTECAH WRSRECMAPP PQNGGRDCSG TLLDSKNCTD 
       360        370        380        390        400
GLCMQMLEAS GDAALYAGLV VAIFVVVAIL MAVGVVVYRR NCRDFDTDIT 
       410        420        430        440        450
DSSAALTGGF HPVNFKTARP SNPQLLHPSV PPDLTASAGI YRGPVYALQD 
       460        470        480        490        500
STDKIPMTNS PLLDPLPSLK VKVYSSSTTG SGPGLADGAD LLGVLPPGTY 
       510        520        530        540        550
PSDFARDTHF LHLRSASLGS QQLLGLPRDP GSSVSGTFGC LGGRLSIPGT 
       560        570        580        590        600
GVSLLVPNGA IPQGKFYEMY LLINKAESTL PLSEGTQTVL SPSVTCGPTG 
       610        620        630        640        650
LLLCRPVILT MPHCAEVSAR DWIFQLKTQA HQGHWEEVVT LDEETLNTPC 
       660        670        680        690        700
YCQLEPRACH ILLDQLGTYV FTGESYSRSA VKRLQLAVFA PALCTSLEYS 
       710        720        730        740        750
LRVYCLEDTP VALKEVLELE RTLGGYLVEE PKPLMFKDSY HNLRLSLHDL 
       760        770        780        790        800
PHAHWRSKLL AKYQEIPFYH IWSGSQKALH CTFTLERHSL ASTELTCKIC 
       810        820        830        840        850
VRQVEGEGQI FQLHTTLAET PAGSLDTLCS APGSTVTTQL GPYAFKIPLS 
       860        870        880        890        900
IRQKICNSLD APNSRGNDWR MLAQKLSMDR YLNYFATKAS PTGVILDLWE 
       910        920        930 
ALQQDDGDLN SLASALEEMG KSEMLVAVAT DGDC            

<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	483 – 483	1	K → E in BAC04382. (PubMed:12975309)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	851 – 851	1	L → P in BAB14276. (PubMed:12975309)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	242 – 242	1	I → V. Corresponds to variant rs34957097 [ dbSNP | Ensembl ].		VAR_052472
<p>Describes natural variant(s) of the protein sequence.</p><p><a href='../manual/variant' target='_top'>More...</a></p>Natural varianti	516 – 516	1	A → T. Corresponds to variant rs10509332 [ dbSNP | Ensembl ].		VAR_019730

Alternative sequence

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.</p><p><a href='../manual/var_seq' target='_top'>More...</a></p>Alternative sequencei	356 – 367	12	NKKTL…PNSHL → M in isoform 2. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini Ref.1 "Modulation of G(ialpha(2)) signaling by the axonal guidance molecule UNC5H2." Komatsuzaki K., Dalvin S., Kinane T.B. Biochem. Biophys. Res. Commun. 297:898-905(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, INTERACTION WITH GNAI2.		VSP_011698	Add BLAST

Sequence databases

Genome annotation 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

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>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. "Modulation of G(ialpha(2)) signaling by the axonal guidance molecule UNC5H2."
   Komatsuzaki K., Dalvin S., Kinane T.B.
   Biochem. Biophys. Res. Commun. 297:898-905(2002) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, INTERACTION WITH GNAI2.
   Tissue: Lung.
   
2. "p53RDL1 regulates of p53-dependent apoptosis."
   Tanikawa C., Matsuda K., Fukuda S., Nakamura Y., Arakawa H.
   Nat. Cell Biol. 5:216-223(2003) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF ASP-412.
3. "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E.

   , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
   Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.

   , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
   Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
   Tissue: Amygdala, Teratocarcinoma and Testis.
   
5. "The DNA sequence and comparative analysis of human chromosome 10."
   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.

   , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
   Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
6. Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R.

   , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
   Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
7. "The netrin-1 receptors UNC5H are putative tumor suppressors controlling cell death commitment."
   Thiebault K., Mazelin L., Pays L., Llambi F., Joly M.-O., Scoazec J.-Y., Saurin J.-C., Romeo G., Mehlen P.
   Proc. Natl. Acad. Sci. U.S.A. 100:4173-4178(2003) [PubMed] [Europe PMC] [Abstract]
   Cited for: DOWN-REGULATION IN CANCER.
8. "The dependence receptor UNC5H2 mediates apoptosis through DAP-kinase."
   Llambi F., Lourenco F.C., Gozuacik D., Guix C., Pays L., Del Rio G., Kimchi A., Mehlen P.
   EMBO J. 24:1192-1201(2005) [PubMed] [Europe PMC] [Abstract]
   Cited for: FUNCTION, INTERACTION WITH DAPK1.
9. "Lipid raft localization and palmitoylation: identification of two requirements for cell death induction by the tumor suppressors UNC5H."
   Maisse C., Rossin A., Cahuzac N., Paradisi A., Klein C., Haillot M.L., Herincs Z., Mehlen P., Hueber A.O.
   Exp. Cell Res. 314:2544-2552(2008) [PubMed] [Europe PMC] [Abstract]
   Cited for: PALMITOYLATION AT CYS-403, SUBCELLULAR LOCATION, INTERACTION WITH DAPK1.

<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

Miscellaneous

<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 10
   Human chromosome 10: 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