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Q13424

- SNTA1_HUMAN

UniProt

Q13424 - SNTA1_HUMAN

Protein

Alpha-1-syntrophin

Gene

SNTA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the extracellular matrix via the dystrophin glycoprotein complex. Plays an important role in synapse formation and in the organization of UTRN and acetylcholine receptors at the neuromuscular synapse. Binds to phosphatidylinositol 4,5-bisphosphate By similarity.By similarity

    GO - Molecular functioni

    1. ATPase binding Source: BHF-UCL
    2. ion channel binding Source: BHF-UCL
    3. nitric-oxide synthase binding Source: BHF-UCL
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. muscle contraction Source: ProtInc
    2. negative regulation of peptidyl-cysteine S-nitrosylation Source: BHF-UCL
    3. neuromuscular junction development Source: Ensembl
    4. regulation of heart rate Source: BHF-UCL
    5. regulation of sodium ion transmembrane transport Source: BHF-UCL
    6. regulation of vasoconstriction by circulating norepinephrine Source: Ensembl
    7. regulation of ventricular cardiac muscle cell membrane repolarization Source: BHF-UCL
    8. ventricular cardiac muscle cell action potential Source: BHF-UCL

    Keywords - Ligandi

    Actin-binding, Calcium, Calmodulin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-1-syntrophin
    Alternative name(s):
    59 kDa dystrophin-associated protein A1 acidic component 1
    Pro-TGF-alpha cytoplasmic domain-interacting protein 1
    Short name:
    TACIP1
    Syntrophin-1
    Gene namesi
    Name:SNTA1
    Synonyms:SNT1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:11167. SNTA1.

    Subcellular locationi

    Cell membranesarcolemma By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cell junction By similarity. Cytoplasmcytoskeleton By similarity
    Note: In skeletal muscle, it localizes at the cytoplasmic side of the sarcolemmal membrane and at neuromuscular junctions.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-SubCell
    2. cytoplasm Source: UniProtKB-KW
    3. cytoskeleton Source: UniProtKB-SubCell
    4. intracellular Source: UniProtKB
    5. neuromuscular junction Source: Ensembl
    6. postsynaptic membrane Source: Ensembl
    7. protein complex Source: BHF-UCL
    8. sarcolemma Source: UniProtKB-SubCell
    9. syntrophin complex Source: BHF-UCL

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Long QT syndrome 12 (LQT12) [MIM:612955]: A heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti257 – 2571A → G in LQT12; leads to a gain of function of the voltage dependent sodium channel. 1 Publication
    Corresponds to variant rs56157422 [ dbSNP | Ensembl ].
    VAR_062399
    Natural varianti390 – 3901A → V in LQT12; results in released inhibition of nNOS, S-nitrosylation of SCN5A and increased late sodium current. 1 Publication
    VAR_062400

    Keywords - Diseasei

    Disease mutation, Long QT syndrome

    Organism-specific databases

    MIMi612955. phenotype.
    Orphaneti101016. Romano-Ward syndrome.
    PharmGKBiPA36007.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 505505Alpha-1-syntrophinPRO_0000184006Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei189 – 1891Phosphoserine3 Publications
    Modified residuei193 – 1931Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated by CaM-kinase II. Phosphorylation may inhibit the interaction with DMD By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ13424.
    PaxDbiQ13424.
    PRIDEiQ13424.

    PTM databases

    PhosphoSiteiQ13424.

    Expressioni

    Tissue specificityi

    High expression in skeletal muscle and heart. Low expression in brain, pancreas, liver, kidney and lung. Not detected in placenta.

    Gene expression databases

    ArrayExpressiQ13424.
    BgeeiQ13424.
    CleanExiHS_SNTA1.
    GenevestigatoriQ13424.

    Organism-specific databases

    HPAiCAB037059.

    Interactioni

    Subunit structurei

    Monomer and homodimer. Interacts with the other members of the syntrophin family SNTB1 and SNTB2; SGCG and SGCA of the dystrophin glycoprotein complex; NOS1; GRB2; the sodium channel proteins SCN4A and SCN5A; F-actin and calmodulin By similarity. Interacts with dystrophin protein DMD and related proteins DTNA and UTRN and with MAPK12, TGFA and GA. Interacts with MYOC; regulates muscle hypertrophy By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABCA1O954772EBI-717191,EBI-784112
    Mapk12Q635385EBI-717191,EBI-783937From a different organism.

    Protein-protein interaction databases

    BioGridi112523. 77 interactions.
    DIPiDIP-966N.
    IntActiQ13424. 5 interactions.
    MINTiMINT-90249.
    STRINGi9606.ENSP00000217381.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13424.
    SMRiQ13424. Positions 2-270.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini6 – 269264PH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini87 – 17084PDZPROSITE-ProRule annotationAdd
    BLAST
    Domaini293 – 401109PH 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini449 – 50557SUAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni483 – 50523Calmodulin-bindingBy similarityAdd
    BLAST

    Domaini

    The PH 1 domain mediates the oligomerization in a calcium dependent manner, and the association with the phosphatidylinositol 4,5-bisphosphate.By similarity
    The PDZ domain binds to the last three or four amino acids of ion channels and receptor proteins. The association with dystrophin or related proteins probably leaves the PDZ domain available to recruit proteins to the membrane By similarity.By similarity
    The SU domain binds calmodulin in a calcium-dependent manner.By similarity

    Sequence similaritiesi

    Belongs to the syntrophin family.Curated
    Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation
    Contains 2 PH domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG318350.
    HOGENOMiHOG000231596.
    HOVERGENiHBG054204.
    InParanoidiQ13424.
    OMAiTGTRHGV.
    OrthoDBiEOG7R56VZ.
    PhylomeDBiQ13424.
    TreeFamiTF317932.

    Family and domain databases

    Gene3Di2.30.42.10. 1 hit.
    InterProiIPR001478. PDZ.
    IPR001849. PH_domain.
    IPR028552. SNTA1.
    IPR015482. Syntrophin.
    [Graphical view]
    PANTHERiPTHR10554. PTHR10554. 1 hit.
    PTHR10554:SF6. PTHR10554:SF6. 1 hit.
    PfamiPF00595. PDZ. 1 hit.
    [Graphical view]
    SMARTiSM00228. PDZ. 1 hit.
    SM00233. PH. 2 hits.
    [Graphical view]
    SUPFAMiSSF50156. SSF50156. 1 hit.
    PROSITEiPS50106. PDZ. 1 hit.
    PS50003. PH_DOMAIN. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q13424-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASGRRAPRT GLLELRAGAG SGAGGERWQR VLLSLAEDVL TVSPADGDPG    50
    PEPGAPREQE PAQLNGAAEP GAGPPQLPEA LLLQRRRVTV RKADAGGLGI 100
    SIKGGRENKM PILISKIFKG LAADQTEALF VGDAILSVNG EDLSSATHDE 150
    AVQVLKKTGK EVVLEVKYMK DVSPYFKNST GGTSVGWDSP PASPLQRQPS 200
    SPGPTPRNFS EAKHMSLKMA YVSKRCTPND PEPRYLEICS ADGQDTLFLR 250
    AKDEASARSW ATAIQAQVNT LTPRVKDELQ ALLAATSTAG SQDIKQIGWL 300
    TEQLPSGGTA PTLALLTEKE LLLYLSLPET REALSRPART APLIATRLVH 350
    SGPSKGSVPY DAELSFALRT GTRHGVDTHL FSVESPQELA AWTRQLVDGC 400
    HRAAEGVQEV STACTWNGRP CSLSVHIDKG FTLWAAEPGA ARAVLLRQPF 450
    EKLQMSSDDG ASLLFLDFGG AEGEIQLDLH SCPKTIVFII HSFLSAKVTR 500
    LGLLA 505
    Length:505
    Mass (Da):53,895
    Last modified:November 1, 1996 - v1
    Checksum:iC07DA5F21C775CF8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61R → P in AAB36398. (PubMed:8612778)Curated
    Sequence conflicti25 – 251G → A in AAB36398. (PubMed:8612778)Curated
    Sequence conflicti32 – 332LL → PV in AAB36398. (PubMed:8612778)Curated
    Sequence conflicti66 – 661G → D in AAB36398. (PubMed:8612778)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti257 – 2571A → G in LQT12; leads to a gain of function of the voltage dependent sodium channel. 1 Publication
    Corresponds to variant rs56157422 [ dbSNP | Ensembl ].
    VAR_062399
    Natural varianti364 – 3641L → F.
    Corresponds to variant rs1046815 [ dbSNP | Ensembl ].
    VAR_014075
    Natural varianti390 – 3901A → V in LQT12; results in released inhibition of nNOS, S-nitrosylation of SCN5A and increased late sodium current. 1 Publication
    VAR_062400

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40571 mRNA. Translation: AAC50448.1.
    S81737 mRNA. Translation: AAB36398.1.
    AL355392 Genomic DNA. Translation: CAC15884.1.
    AK291994 mRNA. Translation: BAF84683.1.
    CH471077 Genomic DNA. Translation: EAW76316.1.
    CH471077 Genomic DNA. Translation: EAW76317.1.
    BC026215 mRNA. Translation: AAH26215.1.
    CCDSiCCDS13220.1.
    PIRiS62894.
    RefSeqiNP_003089.1. NM_003098.2.
    UniGeneiHs.31121.

    Genome annotation databases

    EnsembliENST00000217381; ENSP00000217381; ENSG00000101400.
    GeneIDi6640.
    KEGGihsa:6640.
    UCSCiuc002wzd.1. human.

    Polymorphism databases

    DMDMi23822157.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40571 mRNA. Translation: AAC50448.1 .
    S81737 mRNA. Translation: AAB36398.1 .
    AL355392 Genomic DNA. Translation: CAC15884.1 .
    AK291994 mRNA. Translation: BAF84683.1 .
    CH471077 Genomic DNA. Translation: EAW76316.1 .
    CH471077 Genomic DNA. Translation: EAW76317.1 .
    BC026215 mRNA. Translation: AAH26215.1 .
    CCDSi CCDS13220.1.
    PIRi S62894.
    RefSeqi NP_003089.1. NM_003098.2.
    UniGenei Hs.31121.

    3D structure databases

    ProteinModelPortali Q13424.
    SMRi Q13424. Positions 2-270.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112523. 77 interactions.
    DIPi DIP-966N.
    IntActi Q13424. 5 interactions.
    MINTi MINT-90249.
    STRINGi 9606.ENSP00000217381.

    PTM databases

    PhosphoSitei Q13424.

    Polymorphism databases

    DMDMi 23822157.

    Proteomic databases

    MaxQBi Q13424.
    PaxDbi Q13424.
    PRIDEi Q13424.

    Protocols and materials databases

    DNASUi 6640.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000217381 ; ENSP00000217381 ; ENSG00000101400 .
    GeneIDi 6640.
    KEGGi hsa:6640.
    UCSCi uc002wzd.1. human.

    Organism-specific databases

    CTDi 6640.
    GeneCardsi GC20M031995.
    GeneReviewsi SNTA1.
    HGNCi HGNC:11167. SNTA1.
    HPAi CAB037059.
    MIMi 601017. gene.
    612955. phenotype.
    neXtProti NX_Q13424.
    Orphaneti 101016. Romano-Ward syndrome.
    PharmGKBi PA36007.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG318350.
    HOGENOMi HOG000231596.
    HOVERGENi HBG054204.
    InParanoidi Q13424.
    OMAi TGTRHGV.
    OrthoDBi EOG7R56VZ.
    PhylomeDBi Q13424.
    TreeFami TF317932.

    Miscellaneous databases

    ChiTaRSi SNTA1. human.
    GeneWikii Syntrophin,_alpha_1.
    GenomeRNAii 6640.
    NextBioi 25873.
    PROi Q13424.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13424.
    Bgeei Q13424.
    CleanExi HS_SNTA1.
    Genevestigatori Q13424.

    Family and domain databases

    Gene3Di 2.30.42.10. 1 hit.
    InterProi IPR001478. PDZ.
    IPR001849. PH_domain.
    IPR028552. SNTA1.
    IPR015482. Syntrophin.
    [Graphical view ]
    PANTHERi PTHR10554. PTHR10554. 1 hit.
    PTHR10554:SF6. PTHR10554:SF6. 1 hit.
    Pfami PF00595. PDZ. 1 hit.
    [Graphical view ]
    SMARTi SM00228. PDZ. 1 hit.
    SM00233. PH. 2 hits.
    [Graphical view ]
    SUPFAMi SSF50156. SSF50156. 1 hit.
    PROSITEi PS50106. PDZ. 1 hit.
    PS50003. PH_DOMAIN. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The three human syntrophin genes are expressed in diverse tissues, have distinct chromosomal locations, and each bind to dystrophin and its relatives."
      Ahn A.H., Feener C.A., Gussoni E., Yoshida M., Ozawa E., Kunkel L.M.
      J. Biol. Chem. 271:2724-2730(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH DMD; DTNA AND UTRN.
      Tissue: Muscle.
    2. "Characterization of the dystrophin-syntrophin interaction using the two-hybrid system in yeast."
      Castello A., Brocheriou V., Chafey P., Kahn A., Gilgenkrantz H.
      FEBS Lett. 383:124-128(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH DMD.
      Tissue: Heart.
    3. "Stress-activated protein kinase-3 interacts with the PDZ domain of alpha1-syntrophin. A mechanism for specific substrate recognition."
      Hasegawa M., Cuenda A., Spillantini M.G., Thomas G.M., Buee-Scherrer V., Cohen P., Goedert M.
      J. Biol. Chem. 274:12626-12631(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MAPK12.
    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: Small intestine.
    5. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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].
      Tissue: Liver.
    8. "A role for a PDZ protein in the early secretory pathway for the targeting of proTGF-alpha to the cell surface."
      Fernandez-Larrea J., Merlos-Suarez A., Urena J.M., Baselga J., Arribas J.
      Mol. Cell 3:423-433(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TGFA.
    9. "The C-terminus of human glutaminase L mediates association with PDZ domain-containing proteins."
      Olalla L., Aledo J.C., Bannenberg G., Marquez J.
      FEBS Lett. 488:116-122(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GA.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189 AND SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189 AND SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: VARIANT LQT12 GLY-257, CHARACTERIZATION OF VARIANT LQT12 GLY-257.
    15. "Syntrophin mutation associated with long QT syndrome through activation of the nNOS-SCN5A macromolecular complex."
      Ueda K., Valdivia C., Medeiros-Domingo A., Tester D.J., Vatta M., Farrugia G., Ackerman M.J., Makielski J.C.
      Proc. Natl. Acad. Sci. U.S.A. 105:9355-9360(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LQT12 VAL-390, CHARACTERIZATION OF VARIANT LQT12 VAL-390.

    Entry informationi

    Entry nameiSNTA1_HUMAN
    AccessioniPrimary (citable) accession number: Q13424
    Secondary accession number(s): A8K7H9, E1P5N1, Q16438
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 10, 2002
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 137 of the entry and version 1 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 20
      Human chromosome 20: 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

    Dasty 3