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Q13424

- SNTA1_HUMAN

UniProt

Q13424 - SNTA1_HUMAN

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Protein
Alpha-1-syntrophin
Gene
SNTA1, SNT1
Organism
Homo sapiens (Human)
Status
Reviewed - 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.

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
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: Chromosome 20

Organism-specific databases

HGNCiHGNC:11167. SNTA1.

Subcellular locationi

Cell membranesarcolemma; Peripheral membrane protein; 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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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-syntrophin
PRO_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.

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.5 Publications

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 269264PH 1
Add
BLAST
Domaini87 – 17084PDZ
Add
BLAST
Domaini293 – 401109PH 2
Add
BLAST
Domaini449 – 50557SU
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni483 – 50523Calmodulin-binding By similarity
Add
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.
The SU domain binds calmodulin in a calcium-dependent manner By similarity.

Sequence similaritiesi

Belongs to the syntrophin family.
Contains 1 PDZ (DHR) domain.
Contains 2 PH domains.

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61R → P in AAB36398. 1 Publication
Sequence conflicti25 – 251G → A in AAB36398. 1 Publication
Sequence conflicti32 – 332LL → PV in AAB36398. 1 Publication
Sequence conflicti66 – 661G → D in AAB36398. 1 Publication

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

« 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], 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: September 3, 2014
This is version 136 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