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Q13884 (SNTB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SNTB1
Synonyms:SNT2B1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length538 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.6 Ref.7

Subcellular location

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.

Tissue specificity

Ubiquitous. Ref.1

Domain

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.

The SU domain binds calmodulin in a calcium-dependent manner By similarity.

Post-translational modification

Phosphorylated by CaM-kinase II By similarity.

Sequence similarities

Belongs to the syntrophin family.

Contains 1 PDZ (DHR) domain.

Contains 2 PH domains.

Contains 1 SU (syntrophin unique) domain.

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13884-1)

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.
Isoform 2 (identifier: Q13884-2)

The sequence of this isoform differs from the canonical sequence as follows:
     379-382: RLVH → SPHP
     383-538: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4 Ref.5
Chain2 – 538537Beta-1-syntrophin
PRO_0000184009

Regions

Domain19 – 298280PH 1
Domain112 – 19584PDZ
Domain322 – 433112PH 2
Domain482 – 53857SU
Region518 – 53821Calmodulin-binding By similarity
Compositional bias2 – 109Poly-Ala

Amino acid modifications

Modified residue21N-acetylalanine Ref.4 Ref.5 Ref.13
Modified residue871Phosphoserine Ref.8 Ref.10
Modified residue2141Phosphothreonine By similarity
Modified residue2191Phosphoserine Ref.8 Ref.9
Modified residue3891Phosphoserine Ref.8 Ref.10 Ref.12

Natural variations

Alternative sequence379 – 3824RLVH → SPHP in isoform 2.
VSP_006354
Alternative sequence383 – 538156Missing in isoform 2.
VSP_006355

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: BF8E7B416D5CF289

FASTA53858,061
        10         20         30         40         50         60 
MAVAAAAAAA GPAGAGGGRA QRSGLLEVLV RDRWHKVLVN LSEDALVLSS EEGAAAYNGI 

        70         80         90        100        110        120 
GTATNGSFCR GAGAGHPGAG GAQPPDSPAG VRTAFTDLPE QVPESISNQK RGVKVLKQEL 

       130        140        150        160        170        180 
GGLGISIKGG KENKMPILIS KIFKGLAADQ TQALYVGDAI LSVNGADLRD ATHDEAVQAL 

       190        200        210        220        230        240 
KRAGKEVLLE VKYMREATPY VKKGSPVSEI GWETPPPESP RLGGSTSDPP SSQSFSFHRD 

       250        260        270        280        290        300 
RKSIPLKMCY VTRSMALADP ENRQLEIHSP DAKHTVILRS KDSATAQAWF SAIHSNVNDL 

       310        320        330        340        350        360 
LTRVIAEVRE QLGKTGIAGS REIRHLGWLA EKVPGESKKQ WKPALVVLTE KDLLIYDSMP 

       370        380        390        400        410        420 
RRKEAWFSPV HTYPLLATRL VHSGPGKGSP QAGVDLSFAT RTGTRQGIET HLFRAETSRD 

       430        440        450        460        470        480 
LSHWTRSIVQ GCHNSAELIA EISTACTYKN QECRLTIHYE NGFSITTEPQ EGAFPKTIIQ 

       490        500        510        520        530 
SPYEKLKMSS DDGIRMLYLD FGGKDGEIQL DLHSCPKPIV FIIHSFLSAK ITRLGLVA 

« Hide

Isoform 2 [UniParc].

Checksum: 5857392A7FCE200D
Show »

FASTA38240,805

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L31529 Genomic DNA. Translation: AAA81523.1.
AK292655 mRNA. Translation: BAF85344.1.
BC098573 mRNA. Translation: AAH98573.1.
AF028828 mRNA. Translation: AAB84253.1.
PIRI59291.
RefSeqNP_066301.1. NM_021021.3.
UniGeneHs.46701.

3D structure databases

ProteinModelPortalQ13884.
SMRQ13884. Positions 15-297, 323-435.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112524. 8 interactions.
DIPDIP-466N.
IntActQ13884. 5 interactions.
STRING9606.ENSP00000378965.

PTM databases

PhosphoSiteQ13884.

Polymorphism databases

DMDM23822159.

Proteomic databases

PaxDbQ13884.
PRIDEQ13884.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000395601; ENSP00000378965; ENSG00000172164. [Q13884-1]
ENST00000517992; ENSP00000431124; ENSG00000172164. [Q13884-1]
GeneID6641.
KEGGhsa:6641.
UCSCuc003ype.3. human. [Q13884-2]
uc010mdg.3. human. [Q13884-1]

Organism-specific databases

CTD6641.
GeneCardsGC08M121619.
H-InvDBHIX0168940.
HGNCHGNC:11168. SNTB1.
HPAHPA024659.
MIM600026. gene.
neXtProtNX_Q13884.
PharmGKBPA36008.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG318350.
HOGENOMHOG000231596.
HOVERGENHBG054204.
InParanoidQ13884.
OMADAKHTVV.
OrthoDBEOG7R56VZ.
PhylomeDBQ13884.
TreeFamTF317932.

Gene expression databases

ArrayExpressQ13884.
BgeeQ13884.
CleanExHS_SNTB1.
GenevestigatorQ13884.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
2.30.42.10. 1 hit.
InterProIPR001478. PDZ.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR015482. Syntrophin.
[Graphical view]
PANTHERPTHR10554. PTHR10554. 1 hit.
PfamPF00595. PDZ. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
SMARTSM00228. PDZ. 1 hit.
SM00233. PH. 2 hits.
[Graphical view]
SUPFAMSSF50156. SSF50156. 1 hit.
PROSITEPS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSNTB1. human.
GeneWikiSNTB1.
GenomeRNAi6641.
NextBio25877.
PROQ13884.
SOURCESearch...

Entry information

Entry nameSNTB1_HUMAN
AccessionPrimary (citable) accession number: Q13884
Secondary accession number(s): A8K9E0, O14912, Q4KMG8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 126 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM