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Protein

Alpha-1-syntrophin

Gene

SNTA1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • ATPase binding Source: BHF-UCL
  • ion channel binding Source: BHF-UCL
  • nitric-oxide synthase binding Source: BHF-UCL

GO - Biological processi

  • muscle contraction Source: ProtInc
  • negative regulation of peptidyl-cysteine S-nitrosylation Source: BHF-UCL
  • neuromuscular junction development Source: Ensembl
  • regulation of heart rate Source: BHF-UCL
  • regulation of sodium ion transmembrane transport Source: BHF-UCL
  • regulation of vasoconstriction by circulating norepinephrine Source: Ensembl
  • regulation of ventricular cardiac muscle cell membrane repolarization Source: BHF-UCL
  • ventricular cardiac muscle cell action potential Source: BHF-UCL
Complete GO annotation...

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 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:11167. SNTA1.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB-KW
  • cytoskeleton Source: UniProtKB-SubCell
  • intracellular Source: UniProtKB
  • neuromuscular junction Source: Ensembl
  • postsynaptic membrane Source: Ensembl
  • protein complex Source: BHF-UCL
  • sarcolemma Source: UniProtKB-SubCell
  • syntrophin complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Involvement in diseasei

Long QT syndrome 12 (LQT12)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:612955
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.

Polymorphism and mutation databases

BioMutaiSNTA1.
DMDMi23822157.

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 residuei184 – 1841Phosphoserine1 Publication
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

BgeeiQ13424.
CleanExiHS_SNTA1.
GenevisibleiQ13424. HS.

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. 78 interactions.
DIPiDIP-966N.
IntActiQ13424. 6 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.
GeneTreeiENSGT00550000074581.
HOGENOMiHOG000231596.
HOVERGENiHBG054204.
InParanoidiQ13424.
OMAiKNSASGT.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q13424-1) [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
MASGRRAPRT GLLELRAGAG SGAGGERWQR VLLSLAEDVL TVSPADGDPG
60 70 80 90 100
PEPGAPREQE PAQLNGAAEP GAGPPQLPEA LLLQRRRVTV RKADAGGLGI
110 120 130 140 150
SIKGGRENKM PILISKIFKG LAADQTEALF VGDAILSVNG EDLSSATHDE
160 170 180 190 200
AVQVLKKTGK EVVLEVKYMK DVSPYFKNST GGTSVGWDSP PASPLQRQPS
210 220 230 240 250
SPGPTPRNFS EAKHMSLKMA YVSKRCTPND PEPRYLEICS ADGQDTLFLR
260 270 280 290 300
AKDEASARSW ATAIQAQVNT LTPRVKDELQ ALLAATSTAG SQDIKQIGWL
310 320 330 340 350
TEQLPSGGTA PTLALLTEKE LLLYLSLPET REALSRPART APLIATRLVH
360 370 380 390 400
SGPSKGSVPY DAELSFALRT GTRHGVDTHL FSVESPQELA AWTRQLVDGC
410 420 430 440 450
HRAAEGVQEV STACTWNGRP CSLSVHIDKG FTLWAAEPGA ARAVLLRQPF
460 470 480 490 500
EKLQMSSDDG ASLLFLDFGG AEGEIQLDLH SCPKTIVFII HSFLSAKVTR

LGLLA
Length:505
Mass (Da):53,895
Last modified:November 1, 1996 - v1
Checksum:iC07DA5F21C775CF8
GO
Isoform 2 (identifier: Q13424-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     254-328: Missing.

Note: No experimental confirmation available.
Show »
Length:430
Mass (Da):45,951
Checksum:iCC6ACFC81506F650
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei254 – 32875Missing in isoform 2. 1 PublicationVSP_056827Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40571 mRNA. Translation: AAC50448.1.
S81737 mRNA. Translation: AAB36398.1.
AL355392 Genomic DNA. Translation: CAC15884.1.
AK291994 mRNA. Translation: BAF84683.1.
AK301800 mRNA. Translation: BAG63252.1.
CH471077 Genomic DNA. Translation: EAW76316.1.
CH471077 Genomic DNA. Translation: EAW76317.1.
BC026215 mRNA. Translation: AAH26215.1.
CCDSiCCDS13220.1. [Q13424-1]
PIRiS62894.
RefSeqiNP_003089.1. NM_003098.2. [Q13424-1]
UniGeneiHs.31121.

Genome annotation databases

EnsembliENST00000217381; ENSP00000217381; ENSG00000101400.
GeneIDi6640.
KEGGihsa:6640.
UCSCiuc002wzd.1. human. [Q13424-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40571 mRNA. Translation: AAC50448.1.
S81737 mRNA. Translation: AAB36398.1.
AL355392 Genomic DNA. Translation: CAC15884.1.
AK291994 mRNA. Translation: BAF84683.1.
AK301800 mRNA. Translation: BAG63252.1.
CH471077 Genomic DNA. Translation: EAW76316.1.
CH471077 Genomic DNA. Translation: EAW76317.1.
BC026215 mRNA. Translation: AAH26215.1.
CCDSiCCDS13220.1. [Q13424-1]
PIRiS62894.
RefSeqiNP_003089.1. NM_003098.2. [Q13424-1]
UniGeneiHs.31121.

3D structure databases

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

Protein-protein interaction databases

BioGridi112523. 78 interactions.
DIPiDIP-966N.
IntActiQ13424. 6 interactions.
MINTiMINT-90249.
STRINGi9606.ENSP00000217381.

PTM databases

PhosphoSiteiQ13424.

Polymorphism and mutation databases

BioMutaiSNTA1.
DMDMi23822157.

Proteomic databases

MaxQBiQ13424.
PaxDbiQ13424.
PRIDEiQ13424.

Protocols and materials databases

DNASUi6640.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000217381; ENSP00000217381; ENSG00000101400.
GeneIDi6640.
KEGGihsa:6640.
UCSCiuc002wzd.1. human. [Q13424-1]

Organism-specific databases

CTDi6640.
GeneCardsiGC20M031995.
GeneReviewsiSNTA1.
HGNCiHGNC:11167. SNTA1.
HPAiCAB037059.
MIMi601017. gene.
612955. phenotype.
neXtProtiNX_Q13424.
Orphaneti101016. Romano-Ward syndrome.
PharmGKBiPA36007.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG318350.
GeneTreeiENSGT00550000074581.
HOGENOMiHOG000231596.
HOVERGENiHBG054204.
InParanoidiQ13424.
OMAiKNSASGT.
OrthoDBiEOG7R56VZ.
PhylomeDBiQ13424.
TreeFamiTF317932.

Miscellaneous databases

ChiTaRSiSNTA1. human.
GeneWikiiSyntrophin,_alpha_1.
GenomeRNAii6640.
NextBioi25873.
PROiQ13424.
SOURCEiSearch...

Gene expression databases

BgeeiQ13424.
CleanExiHS_SNTA1.
GenevisibleiQ13424. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1), 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] (ISOFORM 1), 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] (ISOFORM 1), 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] (ISOFORMS 1 AND 2).
    Tissue: Small intestine and Testis.
  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] (ISOFORM 1).
    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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. Cited for: VARIANT LQT12 GLY-257, CHARACTERIZATION OF VARIANT LQT12 GLY-257.
  16. "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
, B4DX40, E1P5N1, Q16438
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 146 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.