Q13884 (SNTB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	SNTB1
Synonyms:	SNT2B1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	538 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 membrane › sarcolemma; Peripheral membrane protein; Cytoplasmic side By similarity. Cell junction By similarity. Cytoplasm › cytoskeleton 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.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	Actin-binding Calcium Calmodulin-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	muscle contraction Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell dystrophin-associated glycoprotein complex Traceable author statement PubMed 8119949. Source: ProtInc sarcolemma Inferred from electronic annotation. Source: UniProtKB-SubCell synapse Inferred from electronic annotation. Source: Compara
Molecular_function	phospholipid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ABCA1	O95477	3	EBI-295843,EBI-784112
DMD	P11532	3	EBI-295843,EBI-295827

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.4 Ref.5
	Chain	2 – 538	537	Beta-1-syntrophin		PRO_0000184009
Regions
	Domain	19 – 298	280	PH 1
	Domain	112 – 195	84	PDZ
	Domain	322 – 433	112	PH 2
	Domain	482 – 538	57	SU
	Region	518 – 538	21	Calmodulin-binding By similarity
	Compositional bias	2 – 10	9	Poly-Ala
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.4 Ref.5
	Modified residue	87	1	Phosphoserine Ref.8 Ref.10
	Modified residue	214	1	Phosphothreonine By similarity
	Modified residue	219	1	Phosphoserine Ref.8 Ref.9
	Modified residue	236	1	Phosphoserine By similarity
	Modified residue	389	1	Phosphoserine Ref.8 Ref.10 Ref.12
Natural variations
	Alternative sequence	379 – 382	4	RLVH → SPHP in isoform 2.		VSP_006354
	Alternative sequence	383 – 538	156	Missing in isoform 2.		VSP_006355

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: BF8E7B416D5CF289	FASTA	538	58,061
	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
	Isoform 2 [UniParc]. Checksum: 5857392A7FCE200D	FASTA	382	40,805
	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 RRKEAWFSPV HTYPLLATSP HP

References

	« Hide 'large scale' referencesShow '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. , 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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
+	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.
IPI	IPI00026059. IPI00216858.
PIR	I59291.
RefSeq	NP_066301.1. NM_021021.3.
UniGene	Hs.46701.
3D structure databases
ProteinModelPortal	Q13884.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-466N.
IntAct	Q13884. 4 interactions.
STRING	9606.ENSP00000378965.
PTM databases
PhosphoSite	Q13884.
Polymorphism databases
DMDM	23822159.
Proteomic databases
PaxDb	Q13884.
PRIDE	Q13884.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000395601; ENSP00000378965; ENSG00000172164. ENST00000517992; ENSP00000431124; ENSG00000172164.
GeneID	6641.
KEGG	hsa:6641.
UCSC	uc003ype.3. human. uc010mdg.3. human.
Organism-specific databases
CTD	6641.
GeneCards	GC08M121619.
H-InvDB	HIX0168940.
HGNC	HGNC:11168. SNTB1.
HPA	HPA024659.
MIM	600026. gene.
neXtProt	NX_Q13884.
PharmGKB	PA36008.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG318350.
HOGENOM	HOG000231596.
HOVERGEN	HBG054204.
InParanoid	Q13884.
OMA	YESMPRI.
OrthoDB	EOG4BRWKJ.
PhylomeDB	Q13884.
Gene expression databases
ArrayExpress	Q13884.
Bgee	Q13884.
CleanEx	HS_SNTB1.
Genevestigator	Q13884.
GermOnline	ENSG00000172164. Homo sapiens.
Family and domain databases
Gene3D	2.30.29.30. 1 hit.
InterPro	IPR001478. PDZ. IPR011993. PH_like_dom. IPR001849. Pleckstrin_homology. IPR015482. Syntrophin. [Graphical view]
PANTHER	PTHR10554. PTHR10554. 1 hit.
Pfam	PF00595. PDZ. 1 hit. PF00169. PH. 1 hit. [Graphical view]
SMART	SM00228. PDZ. 1 hit. SM00233. PH. 2 hits. [Graphical view]
SUPFAM	SSF50156. PDZ. 1 hit.
PROSITE	PS50106. PDZ. 1 hit. PS50003. PH_DOMAIN. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SNTB1. human.
GenomeRNAi	6641.
NextBio	25877.
SOURCE	Search...

Entry information

Entry name

SNTB1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 118 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.