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O75052

- CAPON_HUMAN

UniProt

O75052 - CAPON_HUMAN

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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

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
Complete GO annotation...

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

BgeeiO75052.
CleanExiHS_NOS1AP.
ExpressionAtlasiO75052. baseline and differential.
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. 11 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.
GeneTreeiENSGT00510000046975.
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

        10         20         30         40         50
MPSKTKYNLV DDGHDLRIPL HNEDAFQHGI CFEAKYVGSL DVPRPNSRVE
60 70 80 90 100
IVAAMRRIRY EFKAKNIKKK KVSIMVSVDG VKVILKKKKK LLLLQKKEWT
110 120 130 140 150
WDESKMLVMQ DPIYRIFYVS HDSQDLKIFS YIARDGASNI FRCNVFKSKK
160 170 180 190 200
KSQAMRIVRT VGQAFEVCHK LSLQHTQQNA DGQEDGESER NSNSSGDPGR
210 220 230 240 250
QLTGAERAST ATAEETDIDA VEVPLPGNDV LEFSRGVTDL DAVGKEGGSH
260 270 280 290 300
TGSKVSHPQE PMLTASPRML LPSSSSKPPG LGTETPLSTH HQMQLLQQLL
310 320 330 340 350
QQQQQQTQVA VAQVHLLKDQ LAAEAAARLE AQARVHQLLL QNKDMLQHIS
360 370 380 390 400
LLVKQVQELE LKLSGQNAMG SQDSLLEITF RSGALPVLCD PTTPKPEDLH
410 420 430 440 450
SPPLGAGLAD FAHPAGSPLG RRDCLVKLEC FRFLPPEDTP PPAQGEALLG
460 470 480 490 500
GLELIKFRES GIASEYESNT DESEERDSWS QEELPRLLNV LQRQELGDGL

DDEIAV
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. 11 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.
GeneTreei ENSGT00510000046975.
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

Bgeei O75052.
CleanExi HS_NOS1AP.
ExpressionAtlasi O75052. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 105 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