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Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (C-terminal PDZ ligand of neuronal nitric oxide synthase protein) (Nitric oxide synthase 1 adaptor protein)

 CAPON_HUMAN             Reviewed;         506 AA.
O75052; B7ZLF5; O43564; Q3T551; Q5VU95;
04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
04-JAN-2005, sequence version 3.
22-NOV-2017, entry version 132.
RecName: Full=Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein;
AltName: Full=C-terminal PDZ ligand of neuronal nitric oxide synthase protein;
AltName: Full=Nitric oxide synthase 1 adaptor protein;
Name=NOS1AP; Synonyms=CAPON, KIAA0464;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9455484; DOI=10.1093/dnares/4.5.345;
Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
Nomura N., Ohara O.;
"Characterization of cDNA clones in size-fractionated cDNA libraries
from human brain.";
DNA Res. 4:345-349(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
PubMed=16146415; DOI=10.1371/journal.pmed.0020263;
Xu B., Wratten N., Charych E.I., Buyske S., Firestein B.L.,
Brzustowicz L.M.;
"Increased expression in dorsolateral prefrontal cortex of CAPON in
schizophrenia and bipolar disorder.";
PLoS Med. 2:E263-E263(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 354-506 (ISOFORM 1), AND INTERACTION
WITH NOS1.
PubMed=9459447; DOI=10.1016/S0896-6273(00)80439-0;
Jaffrey S.R., Snowman A.M., Eliasson M.J.L., Cohen N.A., Snyder S.H.;
"CAPON: a protein associated with neuronal nitric oxide synthase that
regulates its interactions with PSD95.";
Neuron 20:115-124(1998).
[6]
INVOLVEMENT IN THE REGULATION OF QT INTERVALS, AND POLYMORPHISM.
PubMed=16648850; DOI=10.1038/ng1790;
Arking D.E., Pfeufer A., Post W., Kao W.H.L., Newton-Cheh C.,
Ikeda M., West K., Kashuk C., Akyol M., Perz S., Jalilzadeh S.,
Illig T., Gieger C., Guo C.-Y., Larson M.G., Wichmann H.E., Marban E.,
O'Donnell C.J., Hirschhorn J.N., Kaeaeb S., Spooner P.M.,
Meitinger T., Chakravarti A.;
"A common genetic variant in the NOS1 regulator NOS1AP modulates
cardiac repolarization.";
Nat. Genet. 38:644-651(2006).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: 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).
{ECO:0000250}.
-!- SUBUNIT: 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). {ECO:0000250}.
-!- INTERACTION:
Q8N9E0:FAM133A; NbExp=3; IntAct=EBI-780467, EBI-10268158;
Q9BUZ4:TRAF4; NbExp=3; IntAct=EBI-780467, EBI-3650647;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O75052-1; Sequence=Displayed;
Name=2;
IsoId=O75052-2; Sequence=VSP_042751, VSP_042752;
Name=3;
IsoId=O75052-3; Sequence=VSP_043350;
Note=No experimental confirmation available.;
-!- POLYMORPHISM: Genetic variation in NOS1AP influences the
electrocardiographic QT interval [MIM: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.
{ECO:0000269|PubMed:16648850}.
-!- SEQUENCE CAUTION:
Sequence=BAA32309.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB007933; BAA32309.2; ALT_INIT; mRNA.
EMBL; AY841899; AAW57298.1; -; mRNA.
EMBL; AL590408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL450163; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL512785; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC112295; AAI12296.1; -; mRNA.
EMBL; BC143771; AAI43772.1; -; mRNA.
EMBL; AF037070; AAC39656.1; -; mRNA.
CCDS; CCDS1237.1; -. [O75052-1]
CCDS; CCDS44267.1; -. [O75052-2]
CCDS; CCDS53421.1; -. [O75052-3]
RefSeq; NP_001119532.2; NM_001126060.1. [O75052-2]
RefSeq; NP_001158229.1; NM_001164757.1. [O75052-3]
RefSeq; NP_055512.1; NM_014697.2. [O75052-1]
UniGene; Hs.731942; -.
ProteinModelPortal; O75052; -.
BioGrid; 115071; 58.
CORUM; O75052; -.
IntAct; O75052; 25.
STRING; 9606.ENSP00000355133; -.
iPTMnet; O75052; -.
PhosphoSitePlus; O75052; -.
BioMuta; NOS1AP; -.
MaxQB; O75052; -.
PaxDb; O75052; -.
PeptideAtlas; O75052; -.
PRIDE; O75052; -.
DNASU; 9722; -.
Ensembl; ENST00000361897; ENSP00000355133; ENSG00000198929. [O75052-1]
Ensembl; ENST00000493151; ENSP00000434988; ENSG00000198929. [O75052-2]
Ensembl; ENST00000530878; ENSP00000431586; ENSG00000198929. [O75052-3]
GeneID; 9722; -.
KEGG; hsa:9722; -.
UCSC; uc001gbv.3; human. [O75052-1]
CTD; 9722; -.
DisGeNET; 9722; -.
EuPathDB; HostDB:ENSG00000198929.12; -.
GeneCards; NOS1AP; -.
HGNC; HGNC:16859; NOS1AP.
HPA; CAB018582; -.
HPA; HPA030066; -.
HPA; HPA055561; -.
MalaCards; NOS1AP; -.
MIM; 605551; gene.
MIM; 610141; phenotype.
neXtProt; NX_O75052; -.
OpenTargets; ENSG00000198929; -.
Orphanet; 101016; Romano-Ward syndrome.
PharmGKB; PA142671259; -.
eggNOG; KOG4458; Eukaryota.
eggNOG; KOG4815; Eukaryota.
eggNOG; ENOG410ZTVD; LUCA.
GeneTree; ENSGT00510000046975; -.
HOGENOM; HOG000111298; -.
HOVERGEN; HBG050788; -.
InParanoid; O75052; -.
KO; K16513; -.
OMA; XIFYVSH; -.
OrthoDB; EOG091G183F; -.
PhylomeDB; O75052; -.
TreeFam; TF317226; -.
ChiTaRS; NOS1AP; human.
GeneWiki; NOS1AP; -.
GenomeRNAi; 9722; -.
PRO; PR:O75052; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000198929; -.
CleanEx; HS_NOS1AP; -.
ExpressionAtlas; O75052; baseline and differential.
Genevisible; O75052; HS.
GO; GO:0005901; C:caveola; IEA:Ensembl.
GO; GO:0005829; C:cytosol; ISS:BHF-UCL.
GO; GO:0005739; C:mitochondrion; ISS:BHF-UCL.
GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:BHF-UCL.
GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISS:BHF-UCL.
GO; GO:0030315; C:T-tubule; IEA:Ensembl.
GO; GO:0030018; C:Z disc; ISS:BHF-UCL.
GO; GO:0050998; F:nitric-oxide synthase binding; ISS:UniProtKB.
GO; GO:1902261; P:positive regulation of delayed rectifier potassium channel activity; ISS:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; ISS:BHF-UCL.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:BHF-UCL.
GO; GO:0010750; P:positive regulation of nitric oxide mediated signal transduction; ISS:BHF-UCL.
GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; ISS:BHF-UCL.
GO; GO:2000170; P:positive regulation of peptidyl-cysteine S-nitrosylation; ISS:BHF-UCL.
GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; ISS:BHF-UCL.
GO; GO:1903762; P:positive regulation of voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; ISS:BHF-UCL.
GO; GO:0042981; P:regulation of apoptotic process; NAS:DFLAT.
GO; GO:1902514; P:regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; ISS:BHF-UCL.
GO; GO:0098901; P:regulation of cardiac muscle cell action potential; ISS:BHF-UCL.
GO; GO:0003062; P:regulation of heart rate by chemical signal; IMP:BHF-UCL.
GO; GO:1901841; P:regulation of high voltage-gated calcium channel activity; ISS:BHF-UCL.
GO; GO:0045428; P:regulation of nitric oxide biosynthetic process; NAS:DFLAT.
GO; GO:0050999; P:regulation of nitric-oxide synthase activity; NAS:DFLAT.
GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IMP:BHF-UCL.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR006020; PTB/PI_dom.
Pfam; PF00640; PID; 1.
SMART; SM00462; PTB; 1.
SUPFAM; SSF50729; SSF50729; 1.
PROSITE; PS01179; PID; 1.
1: Evidence at protein level;
Alternative splicing; Coiled coil; Complete proteome; Phosphoprotein;
Reference proteome.
CHAIN 1 506 Carboxyl-terminal PDZ ligand of neuronal
nitric oxide synthase protein.
/FTId=PRO_0000089316.
DOMAIN 26 196 PID. {ECO:0000255|PROSITE-
ProRule:PRU00148}.
REGION 494 506 Interaction with NOS1. {ECO:0000250}.
COILED 322 363 {ECO:0000255}.
MOTIF 504 506 PDZ-binding. {ECO:0000250}.
COMPBIAS 301 308 Poly-Gln.
MOD_RES 188 188 Phosphoserine.
{ECO:0000250|UniProtKB:Q9D3A8}.
MOD_RES 192 192 Phosphoserine.
{ECO:0000250|UniProtKB:Q9D3A8}.
MOD_RES 195 195 Phosphoserine.
{ECO:0000250|UniProtKB:Q9D3A8}.
MOD_RES 266 266 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 371 371 Phosphoserine.
{ECO:0000250|UniProtKB:Q9D3A8}.
MOD_RES 374 374 Phosphoserine.
{ECO:0000250|UniProtKB:Q9D3A8}.
MOD_RES 401 401 Phosphoserine.
{ECO:0000250|UniProtKB:Q9D3A8}.
MOD_RES 417 417 Phosphoserine.
{ECO:0000250|UniProtKB:Q9D3A8}.
VAR_SEQ 1 17 MPSKTKYNLVDDGHDLR -> MSLSSLCPVFSAAASSL
(in isoform 2).
{ECO:0000303|PubMed:16146415}.
/FTId=VSP_042751.
VAR_SEQ 18 312 Missing (in isoform 2).
{ECO:0000303|PubMed:16146415}.
/FTId=VSP_042752.
VAR_SEQ 91 95 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_043350.
SEQUENCE 506 AA; 56150 MW; D969C65E87684A7C CRC64;
MPSKTKYNLV DDGHDLRIPL HNEDAFQHGI CFEAKYVGSL DVPRPNSRVE IVAAMRRIRY
EFKAKNIKKK KVSIMVSVDG VKVILKKKKK LLLLQKKEWT WDESKMLVMQ DPIYRIFYVS
HDSQDLKIFS YIARDGASNI FRCNVFKSKK KSQAMRIVRT VGQAFEVCHK LSLQHTQQNA
DGQEDGESER NSNSSGDPGR QLTGAERAST ATAEETDIDA VEVPLPGNDV LEFSRGVTDL
DAVGKEGGSH TGSKVSHPQE PMLTASPRML LPSSSSKPPG LGTETPLSTH HQMQLLQQLL
QQQQQQTQVA VAQVHLLKDQ LAAEAAARLE AQARVHQLLL QNKDMLQHIS LLVKQVQELE
LKLSGQNAMG SQDSLLEITF RSGALPVLCD PTTPKPEDLH SPPLGAGLAD FAHPAGSPLG
RRDCLVKLEC FRFLPPEDTP PPAQGEALLG GLELIKFRES GIASEYESNT DESEERDSWS
QEELPRLLNV LQRQELGDGL DDEIAV


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