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Protein

Beta-1-syntrophin

Gene

SNTB1

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 dystrophin glycoprotein complex.

GO - Biological processi

  1. muscle contraction Source: ProtInc
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calcium, Calmodulin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-1-syntrophin
Alternative name(s):
59 kDa dystrophin-associated protein A1 basic component 1
Short name:
DAPA1B
BSYN2
Syntrophin-2
Tax interaction protein 43
Short name:
TIP-43
Gene namesi
Name:SNTB1
Synonyms:SNT2B1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:11168. SNTB1.

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. cytoplasm Source: UniProtKB-KW
  2. cytoskeleton Source: UniProtKB-SubCell
  3. dystrophin-associated glycoprotein complex Source: ProtInc
  4. focal adhesion Source: UniProtKB
  5. protein complex Source: MGI
  6. sarcolemma Source: UniProtKB-SubCell
  7. synapse Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36008.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 538537Beta-1-syntrophinPRO_0000184009Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei87 – 871Phosphoserine3 Publications
Modified residuei126 – 1261Phosphoserine1 Publication
Modified residuei214 – 2141Phosphothreonine1 Publication
Modified residuei219 – 2191Phosphoserine3 Publications
Modified residuei232 – 2321Phosphoserine1 Publication
Modified residuei389 – 3891Phosphoserine4 Publications

Post-translational modificationi

Phosphorylated by CaM-kinase II.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ13884.
PaxDbiQ13884.
PRIDEiQ13884.

PTM databases

PhosphoSiteiQ13884.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ13884.
CleanExiHS_SNTB1.
ExpressionAtlasiQ13884. baseline and differential.
GenevestigatoriQ13884.

Organism-specific databases

HPAiHPA024659.

Interactioni

Subunit structurei

Monomer and homodimer (Probable). Interacts with the other members of the syntrophin family SNTA1 and SNTB2; with the sodium channel proteins SCN4A and SCN5A (By similarity). Interacts with the viral HTLV-1 TAX protein and with dystrophin protein DMD and related proteins DTNA and UTRN.By similarityCurated2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABCA1O954773EBI-295843,EBI-784112
DMDP115323EBI-295843,EBI-295827

Protein-protein interaction databases

BioGridi112524. 9 interactions.
DIPiDIP-466N.
IntActiQ13884. 5 interactions.
STRINGi9606.ENSP00000378965.

Structurei

3D structure databases

ProteinModelPortaliQ13884.
SMRiQ13884. Positions 15-297.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 298280PH 1PROSITE-ProRule annotationAdd
BLAST
Domaini112 – 19584PDZPROSITE-ProRule annotationAdd
BLAST
Domaini322 – 433112PH 2PROSITE-ProRule annotationAdd
BLAST
Domaini482 – 53857SUAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni518 – 53821Calmodulin-bindingBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 109Poly-Ala

Domaini

The PH 1 domain mediates the oligomerization in a calcium dependent manner.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.
InParanoidiQ13884.
OMAiDAKHTVV.
OrthoDBiEOG7R56VZ.
PhylomeDBiQ13884.
TreeFamiTF317932.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR015482. Syntrophin.
[Graphical view]
PANTHERiPTHR10554. PTHR10554. 1 hit.
PfamiPF00595. PDZ. 1 hit.
PF00169. PH. 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.

Sequence processingi: The displayed sequence is further processed into a mature form.

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

Isoform 1 (identifier: Q13884-1) [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
MAVAAAAAAA GPAGAGGGRA QRSGLLEVLV RDRWHKVLVN LSEDALVLSS
60 70 80 90 100
EEGAAAYNGI GTATNGSFCR GAGAGHPGAG GAQPPDSPAG VRTAFTDLPE
110 120 130 140 150
QVPESISNQK RGVKVLKQEL GGLGISIKGG KENKMPILIS KIFKGLAADQ
160 170 180 190 200
TQALYVGDAI LSVNGADLRD ATHDEAVQAL KRAGKEVLLE VKYMREATPY
210 220 230 240 250
VKKGSPVSEI GWETPPPESP RLGGSTSDPP SSQSFSFHRD RKSIPLKMCY
260 270 280 290 300
VTRSMALADP ENRQLEIHSP DAKHTVILRS KDSATAQAWF SAIHSNVNDL
310 320 330 340 350
LTRVIAEVRE QLGKTGIAGS REIRHLGWLA EKVPGESKKQ WKPALVVLTE
360 370 380 390 400
KDLLIYDSMP RRKEAWFSPV HTYPLLATRL VHSGPGKGSP QAGVDLSFAT
410 420 430 440 450
RTGTRQGIET HLFRAETSRD LSHWTRSIVQ GCHNSAELIA EISTACTYKN
460 470 480 490 500
QECRLTIHYE NGFSITTEPQ EGAFPKTIIQ SPYEKLKMSS DDGIRMLYLD
510 520 530
FGGKDGEIQL DLHSCPKPIV FIIHSFLSAK ITRLGLVA
Length:538
Mass (Da):58,061
Last modified:January 23, 2007 - v3
Checksum:iBF8E7B416D5CF289
GO
Isoform 2 (identifier: Q13884-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     379-382: RLVH → SPHP
     383-538: Missing.

Note: No experimental confirmation available.

Show »
Length:382
Mass (Da):40,805
Checksum:i5857392A7FCE200D
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei379 – 3824RLVH → SPHP in isoform 2. 1 PublicationVSP_006354
Alternative sequencei383 – 538156Missing in isoform 2. 1 PublicationVSP_006355Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L31529 Genomic DNA. Translation: AAA81523.1.
AK292655 mRNA. Translation: BAF85344.1.
BC098573 mRNA. Translation: AAH98573.1.
AF028828 mRNA. Translation: AAB84253.1.
CCDSiCCDS6334.1. [Q13884-1]
PIRiI59291.
RefSeqiNP_066301.1. NM_021021.3. [Q13884-1]
UniGeneiHs.46701.

Genome annotation databases

EnsembliENST00000395601; ENSP00000378965; ENSG00000172164. [Q13884-1]
ENST00000517992; ENSP00000431124; ENSG00000172164. [Q13884-1]
GeneIDi6641.
KEGGihsa:6641.
UCSCiuc003ype.3. human. [Q13884-2]
uc010mdg.3. human. [Q13884-1]

Polymorphism databases

DMDMi23822159.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L31529 Genomic DNA. Translation: AAA81523.1.
AK292655 mRNA. Translation: BAF85344.1.
BC098573 mRNA. Translation: AAH98573.1.
AF028828 mRNA. Translation: AAB84253.1.
CCDSiCCDS6334.1. [Q13884-1]
PIRiI59291.
RefSeqiNP_066301.1. NM_021021.3. [Q13884-1]
UniGeneiHs.46701.

3D structure databases

ProteinModelPortaliQ13884.
SMRiQ13884. Positions 15-297.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112524. 9 interactions.
DIPiDIP-466N.
IntActiQ13884. 5 interactions.
STRINGi9606.ENSP00000378965.

PTM databases

PhosphoSiteiQ13884.

Polymorphism databases

DMDMi23822159.

Proteomic databases

MaxQBiQ13884.
PaxDbiQ13884.
PRIDEiQ13884.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000395601; ENSP00000378965; ENSG00000172164. [Q13884-1]
ENST00000517992; ENSP00000431124; ENSG00000172164. [Q13884-1]
GeneIDi6641.
KEGGihsa:6641.
UCSCiuc003ype.3. human. [Q13884-2]
uc010mdg.3. human. [Q13884-1]

Organism-specific databases

CTDi6641.
GeneCardsiGC08M121619.
H-InvDBHIX0168940.
HGNCiHGNC:11168. SNTB1.
HPAiHPA024659.
MIMi600026. gene.
neXtProtiNX_Q13884.
PharmGKBiPA36008.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG318350.
GeneTreeiENSGT00550000074581.
HOGENOMiHOG000231596.
HOVERGENiHBG054204.
InParanoidiQ13884.
OMAiDAKHTVV.
OrthoDBiEOG7R56VZ.
PhylomeDBiQ13884.
TreeFamiTF317932.

Miscellaneous databases

ChiTaRSiSNTB1. human.
GeneWikiiSNTB1.
GenomeRNAii6641.
NextBioi25877.
PROiQ13884.
SOURCEiSearch...

Gene expression databases

BgeeiQ13884.
CleanExiHS_SNTB1.
ExpressionAtlasiQ13884. baseline and differential.
GenevestigatoriQ13884.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR015482. Syntrophin.
[Graphical view]
PANTHERiPTHR10554. PTHR10554. 1 hit.
PfamiPF00595. PDZ. 1 hit.
PF00169. PH. 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. "Cloning of human basic A1, a distinct 59-kDa dystrophin-associated protein encoded on chromosome 8q23-24."
    Ahn A.H., Yoshida M., Anderson M.S., Feener C.A., Selig S., Hagiwara Y., Ozawa E., Kunkel L.M.
    Proc. Natl. Acad. Sci. U.S.A. 91:4446-4450(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), PROTEIN SEQUENCE OF 105-114; 197-208; 339-348 AND 351-355, TISSUE SPECIFICITY.
    Tissue: Skeletal muscle.
  2. "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] (ISOFORM 1).
    Tissue: Thymus.
  3. "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: Lung.
  4. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-19, ACETYLATION AT ALA-2.
    Tissue: Platelet.
  5. Bienvenut W.V., Okada H.
    Submitted (OCT-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-19; 23-31; 145-169; 325-332 AND 364-379, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Histiocytic lymphoma.
  6. "The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction with the PDZ domain of cellular proteins."
    Rousset R., Fabre S., Desbois C., Bantignies F., Jalinot P.
    Oncogene 16:643-654(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 95-538 (ISOFORM 2), INTERACTION WITH HTLV-1 TAX.
    Tissue: Lymphocyte.
  7. "Syntrophin binds to an alternatively spliced exon of dystrophin."
    Ahn A.H., Kunkel L.M.
    J. Cell Biol. 128:363-371(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DMD; DTNA AND UTRN.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-219 AND SER-389, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  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-87 AND SER-389, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  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-87; SER-126; THR-214; SER-219; SER-232 AND SER-389, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSNTB1_HUMAN
AccessioniPrimary (citable) accession number: Q13884
Secondary accession number(s): A8K9E0, O14912, Q4KMG8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 134 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: 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

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.