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O75052

- CAPON_HUMAN

UniProt

O75052 - CAPON_HUMAN

Protein

Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein

Gene

NOS1AP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 3 (04 Jan 2005)
      Previous versions | rss
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    Functioni

    Adapter protein involved in neuronal nitric-oxide (NO) synthesis regulation via its association with nNOS/NOS1. The complex formed with NOS1 and synapsins is necessary for specific NO and synapsin functions at a presynaptic level. Mediates an indirect interaction between NOS1 and RASD1 leading to enhance the ability of NOS1 to activate RASD1. Competes with DLG4 for interaction with NOS1, possibly affecting NOS1 activity by regulating the interaction between NOS1 and DLG4 By similarity.By similarity

    GO - Molecular functioni

    1. nitric-oxide synthase binding Source: UniProtKB

    GO - Biological processi

    1. regulation of apoptotic process Source: DFLAT
    2. regulation of nitric oxide biosynthetic process Source: DFLAT
    3. regulation of nitric-oxide synthase activity Source: DFLAT

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein
    Alternative name(s):
    C-terminal PDZ ligand of neuronal nitric oxide synthase protein
    Nitric oxide synthase 1 adaptor protein
    Gene namesi
    Name:NOS1AP
    Synonyms:CAPON, KIAA0464
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:16859. NOS1AP.

    Pathology & Biotechi

    Organism-specific databases

    MIMi610141. phenotype.
    Orphaneti101016. Romano-Ward syndrome.
    PharmGKBiPA142671259.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 506506Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase proteinPRO_0000089316Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei188 – 1881PhosphoserineBy similarity
    Modified residuei192 – 1921PhosphoserineBy similarity
    Modified residuei195 – 1951PhosphoserineBy similarity
    Modified residuei266 – 2661Phosphoserine1 Publication
    Modified residuei374 – 3741PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO75052.
    PaxDbiO75052.
    PeptideAtlasiO75052.
    PRIDEiO75052.

    PTM databases

    PhosphoSiteiO75052.

    Expressioni

    Gene expression databases

    ArrayExpressiO75052.
    BgeeiO75052.
    CleanExiHS_NOS1AP.
    GenevestigatoriO75052.

    Organism-specific databases

    HPAiCAB018582.

    Interactioni

    Subunit structurei

    Interacts with the PDZ domain of NOS1 or the second PDZ domain of DLG4 through its C-terminus. Interacts with RASD1 and SYN1, SYN2 and SYN3 via its PID domain. Forms a ternary complex with NOS1 and RASD1. Forms a ternary complex with NOS1 and SYN1 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi115071. 9 interactions.
    IntActiO75052. 1 interaction.
    STRINGi9606.ENSP00000355133.

    Structurei

    3D structure databases

    ProteinModelPortaliO75052.
    SMRiO75052. Positions 29-167.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 196171PIDPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni494 – 50613Interaction with NOS1By similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili322 – 36342Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi504 – 5063PDZ-bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi301 – 3088Poly-Gln

    Sequence similaritiesi

    Contains 1 PID domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG244289.
    HOGENOMiHOG000111298.
    HOVERGENiHBG050788.
    InParanoidiO75052.
    KOiK16513.
    OMAiQNTMGSQ.
    OrthoDBiEOG7JDQXM.
    PhylomeDBiO75052.
    TreeFamiTF317226.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR011993. PH_like_dom.
    IPR006020. PTB/PI_dom.
    [Graphical view]
    PfamiPF00640. PID. 1 hit.
    [Graphical view]
    SMARTiSM00462. PTB. 1 hit.
    [Graphical view]
    PROSITEiPS01179. PID. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O75052-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPSKTKYNLV DDGHDLRIPL HNEDAFQHGI CFEAKYVGSL DVPRPNSRVE    50
    IVAAMRRIRY EFKAKNIKKK KVSIMVSVDG VKVILKKKKK LLLLQKKEWT 100
    WDESKMLVMQ DPIYRIFYVS HDSQDLKIFS YIARDGASNI FRCNVFKSKK 150
    KSQAMRIVRT VGQAFEVCHK LSLQHTQQNA DGQEDGESER NSNSSGDPGR 200
    QLTGAERAST ATAEETDIDA VEVPLPGNDV LEFSRGVTDL DAVGKEGGSH 250
    TGSKVSHPQE PMLTASPRML LPSSSSKPPG LGTETPLSTH HQMQLLQQLL 300
    QQQQQQTQVA VAQVHLLKDQ LAAEAAARLE AQARVHQLLL QNKDMLQHIS 350
    LLVKQVQELE LKLSGQNAMG SQDSLLEITF RSGALPVLCD PTTPKPEDLH 400
    SPPLGAGLAD FAHPAGSPLG RRDCLVKLEC FRFLPPEDTP PPAQGEALLG 450
    GLELIKFRES GIASEYESNT DESEERDSWS QEELPRLLNV LQRQELGDGL 500
    DDEIAV 506
    Length:506
    Mass (Da):56,150
    Last modified:January 4, 2005 - v3
    Checksum:iD969C65E87684A7C
    GO
    Isoform 2 (identifier: O75052-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-17: MPSKTKYNLVDDGHDLR → MSLSSLCPVFSAAASSL
         18-312: Missing.

    Show »
    Length:211
    Mass (Da):22,955
    Checksum:iE92ED7BE06D43943
    GO
    Isoform 3 (identifier: O75052-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         91-95: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:501
    Mass (Da):55,569
    Checksum:i365A1A9B987EE0F3
    GO

    Sequence cautioni

    The sequence BAA32309.2 differs from that shown. Reason: Erroneous initiation.

    Polymorphismi

    Genetic variation in NOS1AP influences the electrocardiographic QT interval [MIMi:610141]. The QT interval is defined as the time from the beginning of the Q wave to the end of the T wave, representing the duration of ventricular electrical activity. The QT interval, a measure of cardiac repolarization, is a genetically influenced quantitative trait with considerable medical relevance: both high and low values are associated with increased risk of cardiovascular morbidity and mortality.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1717MPSKT…GHDLR → MSLSSLCPVFSAAASSL in isoform 2. 1 PublicationVSP_042751Add
    BLAST
    Alternative sequencei18 – 312295Missing in isoform 2. 1 PublicationVSP_042752Add
    BLAST
    Alternative sequencei91 – 955Missing in isoform 3. 1 PublicationVSP_043350

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB007933 mRNA. Translation: BAA32309.2. Different initiation.
    AY841899 mRNA. Translation: AAW57298.1.
    AL590408, AL450163, AL512785 Genomic DNA. Translation: CAH71497.1.
    AL450163, AL590408, AL512785 Genomic DNA. Translation: CAH73230.1.
    AL512785, AL590408, AL450163 Genomic DNA. Translation: CAI15779.1.
    BC112295 mRNA. Translation: AAI12296.1.
    BC143771 mRNA. Translation: AAI43772.1.
    AF037070 mRNA. Translation: AAC39656.1.
    CCDSiCCDS1237.1. [O75052-1]
    CCDS44267.1. [O75052-2]
    CCDS53421.1. [O75052-3]
    RefSeqiNP_001119532.2. NM_001126060.1. [O75052-2]
    NP_001158229.1. NM_001164757.1. [O75052-3]
    NP_055512.1. NM_014697.2. [O75052-1]
    UniGeneiHs.731942.

    Genome annotation databases

    EnsembliENST00000361897; ENSP00000355133; ENSG00000198929. [O75052-1]
    ENST00000493151; ENSP00000434988; ENSG00000198929. [O75052-2]
    ENST00000530878; ENSP00000431586; ENSG00000198929. [O75052-3]
    GeneIDi9722.
    KEGGihsa:9722.
    UCSCiuc001gbv.2. human. [O75052-1]
    uc001gbw.2. human. [O75052-3]
    uc009wut.1. human. [O75052-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB007933 mRNA. Translation: BAA32309.2 . Different initiation.
    AY841899 mRNA. Translation: AAW57298.1 .
    AL590408 , AL450163 , AL512785 Genomic DNA. Translation: CAH71497.1 .
    AL450163 , AL590408 , AL512785 Genomic DNA. Translation: CAH73230.1 .
    AL512785 , AL590408 , AL450163 Genomic DNA. Translation: CAI15779.1 .
    BC112295 mRNA. Translation: AAI12296.1 .
    BC143771 mRNA. Translation: AAI43772.1 .
    AF037070 mRNA. Translation: AAC39656.1 .
    CCDSi CCDS1237.1. [O75052-1 ]
    CCDS44267.1. [O75052-2 ]
    CCDS53421.1. [O75052-3 ]
    RefSeqi NP_001119532.2. NM_001126060.1. [O75052-2 ]
    NP_001158229.1. NM_001164757.1. [O75052-3 ]
    NP_055512.1. NM_014697.2. [O75052-1 ]
    UniGenei Hs.731942.

    3D structure databases

    ProteinModelPortali O75052.
    SMRi O75052. Positions 29-167.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115071. 9 interactions.
    IntActi O75052. 1 interaction.
    STRINGi 9606.ENSP00000355133.

    PTM databases

    PhosphoSitei O75052.

    Proteomic databases

    MaxQBi O75052.
    PaxDbi O75052.
    PeptideAtlasi O75052.
    PRIDEi O75052.

    Protocols and materials databases

    DNASUi 9722.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361897 ; ENSP00000355133 ; ENSG00000198929 . [O75052-1 ]
    ENST00000493151 ; ENSP00000434988 ; ENSG00000198929 . [O75052-2 ]
    ENST00000530878 ; ENSP00000431586 ; ENSG00000198929 . [O75052-3 ]
    GeneIDi 9722.
    KEGGi hsa:9722.
    UCSCi uc001gbv.2. human. [O75052-1 ]
    uc001gbw.2. human. [O75052-3 ]
    uc009wut.1. human. [O75052-2 ]

    Organism-specific databases

    CTDi 9722.
    GeneCardsi GC01P162039.
    HGNCi HGNC:16859. NOS1AP.
    HPAi CAB018582.
    MIMi 605551. gene.
    610141. phenotype.
    neXtProti NX_O75052.
    Orphaneti 101016. Romano-Ward syndrome.
    PharmGKBi PA142671259.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG244289.
    HOGENOMi HOG000111298.
    HOVERGENi HBG050788.
    InParanoidi O75052.
    KOi K16513.
    OMAi QNTMGSQ.
    OrthoDBi EOG7JDQXM.
    PhylomeDBi O75052.
    TreeFami TF317226.

    Miscellaneous databases

    GeneWikii NOS1AP.
    GenomeRNAii 9722.
    NextBioi 36573.
    PROi O75052.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75052.
    Bgeei O75052.
    CleanExi HS_NOS1AP.
    Genevestigatori O75052.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR011993. PH_like_dom.
    IPR006020. PTB/PI_dom.
    [Graphical view ]
    Pfami PF00640. PID. 1 hit.
    [Graphical view ]
    SMARTi SM00462. PTB. 1 hit.
    [Graphical view ]
    PROSITEi PS01179. PID. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of cDNA clones in size-fractionated cDNA libraries from human brain."
      Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., Nomura N., Ohara O.
      DNA Res. 4:345-349(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "Increased expression in dorsolateral prefrontal cortex of CAPON in schizophrenia and bipolar disorder."
      Xu B., Wratten N., Charych E.I., Buyske S., Firestein B.L., Brzustowicz L.M.
      PLoS Med. 2:E263-E263(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORMS 1 AND 3).
      Tissue: Brain.
    5. "CAPON: a protein associated with neuronal nitric oxide synthase that regulates its interactions with PSD95."
      Jaffrey S.R., Snowman A.M., Eliasson M.J.L., Cohen N.A., Snyder S.H.
      Neuron 20:115-124(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 354-506 (ISOFORM 1), INTERACTION WITH NOS1.
    6. Cited for: INVOLVEMENT IN THE REGULATION OF QT INTERVALS.
    7. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.

    Entry informationi

    Entry nameiCAPON_HUMAN
    AccessioniPrimary (citable) accession number: O75052
    Secondary accession number(s): B7ZLF5
    , O43564, Q3T551, Q5VU95
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 4, 2005
    Last sequence update: January 4, 2005
    Last modified: October 1, 2014
    This is version 104 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3