Q9QYB8 (ADDB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-adducin

Alternative name(s):
Add97
Erythrocyte adducin subunit beta

Gene names

Name:

Add2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	725 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	Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Binds to calmodulin. Calmodulin binds preferentially to the beta subunit By similarity.
Subunit structure	Heterodimer of an alpha and a beta subunit.
Subcellular location	Cytoplasm › cytoskeleton By similarity. Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity.
Domain	Each subunit is comprised of three regions: a NH2-terminal protease-resistant globular head region, a short connecting subdomain, and a protease-sensitive tail region.
Sequence similarities	Belongs to the aldolase class II family. Adducin subfamily.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing
Ligand	Actin-binding Calmodulin-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin filament bundle assembly Inferred from electronic annotation. Source: Compara barbed-end actin filament capping Inferred from electronic annotation. Source: Compara hemopoiesis Inferred from mutant phenotype PubMed 10485892. Source: MGI positive regulation of protein binding Inferred from electronic annotation. Source: Compara
Cellular_component	F-actin capping protein complex Inferred from electronic annotation. Source: Compara cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW membrane Inferred from direct assay PubMed 10485892. Source: MGI plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: InterPro structural molecule activity Inferred from direct assay PubMed 10485892. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q9QYB8-1)

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: Q9QYB8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     532-562: STESQLMSKGDADTKDESEETVPNPFSQLTD → VQQRLPPTEGEVYQTPGAGQGTPESSGPLTP
     563-725: Missing.

Note: Contains a phosphothreonine at position 561.

Isoform 3 (identifier: Q9QYB8-3)

Also known as: Delta;

The sequence of this isoform differs from the canonical sequence as follows:
     284-531: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 725	724	Beta-adducin		PRO_0000218534
Regions
	Region	425 – 444	20	Interaction with calmodulin Potential
	Region	703 – 720	18	Interaction with calmodulin Potential
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.6
	Modified residue	55	1	Phosphothreonine By similarity
	Modified residue	530	1	Phosphoserine By similarity
	Modified residue	532	1	Phosphoserine Ref.8
	Modified residue	535	1	Phosphoserine Ref.8
	Modified residue	561	1	Phosphothreonine Ref.5
	Modified residue	594	1	Phosphoserine Ref.6 Ref.9
	Modified residue	598	1	Phosphoserine By similarity
	Modified residue	602	1	Phosphoserine Ref.6 Ref.7
	Modified residue	606	1	Phosphoserine By similarity
	Modified residue	612	1	Phosphothreonine By similarity
	Modified residue	614	1	Phosphoserine By similarity
	Modified residue	618	1	Phosphoserine By similarity
	Modified residue	687	1	Phosphothreonine Ref.7
	Modified residue	692	1	Phosphoserine By similarity
	Modified residue	696	1	Phosphoserine By similarity
	Modified residue	702	1	Phosphoserine By similarity
	Modified residue	712	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	284 – 531	248	Missing in isoform 3.		VSP_022596
	Alternative sequence	532 – 562	31	STESQ…SQLTD → VQQRLPPTEGEVYQTPGAGQ GTPESSGPLTP in isoform 2.		VSP_000184
	Alternative sequence	563 – 725	163	Missing in isoform 2.		VSP_000185
Experimental info
	Sequence conflict	219	1	R → T in AAF29503. Ref.2
	Sequence conflict	469	1	E → Q in AAF24972. Ref.1
	Sequence conflict	469	1	E → Q in AAF24973. Ref.1
	Sequence conflict	518	1	Q → H in BAC25943. Ref.3
	Sequence conflict	634	1	A → R in AAF24972. Ref.1
	Sequence conflict	666	1	G → V in AAF24972. Ref.1
	Sequence conflict	675	1	D → V in AAF29502. Ref.2
	Sequence conflict	675	1	D → V in AAF29503. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 479153AB1BD6C0DA	FASTA	725	80,642
	10 20 30 40 50 60 MSEDTVPEAA SPPPSQGQHY FDRFSEDDPE YLRLRNRAAD LRQDFNLMEQ KKRVTMILQS 70 80 90 100 110 120 PSFREELEGL IQEQMKKGNN SSNIWALRQI ADFMASTSHA VFPASSMNFS MMTPINDLHT 130 140 150 160 170 180 ADSLNLAKGE RLMRCKISSV YRLLDLYGWA QLSDTYVTLR VSKEQDHFLI SPKGVSCSEV 190 200 210 220 230 240 TASSLIKVNI LGEVVEKGSS CFPVDTTGFS LHSAIYAARP DVRCAIHLHT PATAAVSAMK 250 260 270 280 290 300 CGLLPVSHNA LLVGDMAYYD FNGEMEQEAD RINLQKCLGP TCKILVLRNH GMVALGDTVE 310 320 330 340 350 360 EAFYKVFHLQ AACEVQVSAL SSAGGTENLI LLEQEKHRPH EVGSVQWAGS TFGPMQKSRL 370 380 390 400 410 420 GEHEFEALMR MLDNLGYRTG YTYRHPFVQE KTKHKSEVEI PATVTAFVFE EDGVPVPALR 430 440 450 460 470 480 QHAQKQQKEK TRWLNTPNTY LRVNVADEVQ RNMGSPRPKT TWMKADEVEK SSSGMPIRIE 490 500 510 520 530 540 NPNQFVPLYT DPQEVLDMRN KIREQNRQDI KSAGPQSQLL ASVIAEKSRS PSTESQLMSK 550 560 570 580 590 600 GDADTKDESE ETVPNPFSQL TDQELEEYKK EVERKKLEQE QEGEKDIATE KPGSPVKSTP 610 620 630 640 650 660 ASPVQSPSKA GTKSPAVSPS KTSEDTKKTE VSEANTEPEP VKPEGLVVNG KEEEPSVEEA 670 680 690 700 710 720 LSKGLGQMTT NADTDGDSYK DKTESVTSGP LSPEGSPSKS PSKKKKKFRT PSFLKKSKKK EKVES
	Isoform 2 [UniParc]. Checksum: AECF298E23B44CB8	FASTA	562	62,816
	10 20 30 40 50 60 MSEDTVPEAA SPPPSQGQHY FDRFSEDDPE YLRLRNRAAD LRQDFNLMEQ KKRVTMILQS 70 80 90 100 110 120 PSFREELEGL IQEQMKKGNN SSNIWALRQI ADFMASTSHA VFPASSMNFS MMTPINDLHT 130 140 150 160 170 180 ADSLNLAKGE RLMRCKISSV YRLLDLYGWA QLSDTYVTLR VSKEQDHFLI SPKGVSCSEV 190 200 210 220 230 240 TASSLIKVNI LGEVVEKGSS CFPVDTTGFS LHSAIYAARP DVRCAIHLHT PATAAVSAMK 250 260 270 280 290 300 CGLLPVSHNA LLVGDMAYYD FNGEMEQEAD RINLQKCLGP TCKILVLRNH GMVALGDTVE 310 320 330 340 350 360 EAFYKVFHLQ AACEVQVSAL SSAGGTENLI LLEQEKHRPH EVGSVQWAGS TFGPMQKSRL 370 380 390 400 410 420 GEHEFEALMR MLDNLGYRTG YTYRHPFVQE KTKHKSEVEI PATVTAFVFE EDGVPVPALR 430 440 450 460 470 480 QHAQKQQKEK TRWLNTPNTY LRVNVADEVQ RNMGSPRPKT TWMKADEVEK SSSGMPIRIE 490 500 510 520 530 540 NPNQFVPLYT DPQEVLDMRN KIREQNRQDI KSAGPQSQLL ASVIAEKSRS PVQQRLPPTE 550 560 GEVYQTPGAG QGTPESSGPL TP
	Isoform 3 (Delta) [UniParc]. Checksum: A15E5687AFD48EF0	FASTA	477	52,522
	10 20 30 40 50 60 MSEDTVPEAA SPPPSQGQHY FDRFSEDDPE YLRLRNRAAD LRQDFNLMEQ KKRVTMILQS 70 80 90 100 110 120 PSFREELEGL IQEQMKKGNN SSNIWALRQI ADFMASTSHA VFPASSMNFS MMTPINDLHT 130 140 150 160 170 180 ADSLNLAKGE RLMRCKISSV YRLLDLYGWA QLSDTYVTLR VSKEQDHFLI SPKGVSCSEV 190 200 210 220 230 240 TASSLIKVNI LGEVVEKGSS CFPVDTTGFS LHSAIYAARP DVRCAIHLHT PATAAVSAMK 250 260 270 280 290 300 CGLLPVSHNA LLVGDMAYYD FNGEMEQEAD RINLQKCLGP TCKSTESQLM SKGDADTKDE 310 320 330 340 350 360 SEETVPNPFS QLTDQELEEY KKEVERKKLE QEQEGEKDIA TEKPGSPVKS TPASPVQSPS 370 380 390 400 410 420 KAGTKSPAVS PSKTSEDTKK TEVSEANTEP EPVKPEGLVV NGKEEEPSVE EALSKGLGQM 430 440 450 460 470 TTNADTDGDS YKDKTESVTS GPLSPEGSPS KSPSKKKKKF RTPSFLKKSK KKEKVES

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The mouse adducin gene family: alternative splicing and chromosomal localization." Suriyapperuma S.P., Lozovatsky L., Ciciotte S.L., Peters L.L., Gilligan D.M. Mamm. Genome 11:16-23(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
[2]	"Mild spherocytic hereditary elliptocytosis and altered levels of alpha- and gamma-adducins in beta-adducin-deficient mice." Muro A.F., Marro M.L., Gajovic S., Porro F., Luzzatto L., Baralle F.E. Blood 95:3978-3985(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3). Strain: C57BL/6.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Strain: C57BL/6J and NOD. Tissue: Embryonic liver and Spleen.
[4]	"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 2). Strain: C57BL/6. Tissue: Embryonic brain.
[5]	"Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-561 (ISOFORM 2), MASS SPECTROMETRY. Tissue: Embryonic brain.
[6]	"Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION AT SER-594 AND SER-602, MASS SPECTROMETRY. Tissue: Brain.
[7]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-602 AND THR-687, MASS SPECTROMETRY. Tissue: Brain cortex.
[8]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-532 AND SER-535, MASS SPECTROMETRY. Tissue: Liver.
[9]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF100422 mRNA. Translation: AAF24972.1. AF100423 mRNA. Translation: AAF24973.1. AF189769 mRNA. Translation: AAF29502.1. AF189770 mRNA. Translation: AAF29503.1. AK014496 mRNA. Translation: BAB29395.1. AK028425 mRNA. Translation: BAC25943.1. AK156954 mRNA. Translation: BAE33913.1. BC046783 mRNA. Translation: AAH46783.1. BC053032 mRNA. Translation: AAH53032.1.
IPI	IPI00311962. IPI00323122. IPI00400328.
PIR	A60670.
RefSeq	NP_001258786.1. NM_001271857.1. NP_001258787.1. NM_001271858.1. NP_001258788.1. NM_001271859.1. NP_001258789.1. NM_001271860.1. NP_001258790.1. NM_001271861.1. NP_038486.2. NM_013458.5.
UniGene	Mm.104155.
3D structure databases
ProteinModelPortal	Q9QYB8.
SMR	Q9QYB8. Positions 149-327.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9QYB8. 1 interaction.
STRING	10090.ENSMUSP00000032069.
PTM databases
PhosphoSite	Q9QYB8.
2D gel databases
REPRODUCTION-2DPAGE	Q9QYB8.
Proteomic databases
PaxDb	Q9QYB8.
PRIDE	Q9QYB8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000032069; ENSMUSP00000032069; ENSMUSG00000030000.
GeneID	11519.
KEGG	mmu:11519.
UCSC	uc009crd.1. mouse. uc009cre.1. mouse. uc012eoj.1. mouse.
Organism-specific databases
CTD	119.
MGI	MGI:87919. Add2.
Phylogenomic databases
eggNOG	COG0235.
GeneTree	ENSGT00390000016462.
HOVERGEN	HBG004180.
InParanoid	Q9QYB8.
OMA	SGPMSPE.
OrthoDB	EOG4894M8.
Gene expression databases
Bgee	Q9QYB8.
CleanEx	MM_ADD2.
Genevestigator	Q9QYB8.
GermOnline	ENSMUSG00000030000. Mus musculus.
Family and domain databases
Gene3D	3.40.225.10. 1 hit.
InterPro	IPR001303. Aldolase_II/adducin_N. [Graphical view]
Pfam	PF00596. Aldolase_II. 1 hit. [Graphical view]
SMART	SM01007. Aldolase_II. 1 hit. [Graphical view]
SUPFAM	SSF53639. Aldolase_II_N. 1 hit.
ProtoNet	Search...
Other
NextBio	278952.
SOURCE	Search...

Entry information

Entry name

ADDB_MOUSE

Accession

Primary (citable) accession number: Q9QYB8
Secondary accession number(s): Q3U0E1 , Q80VH9, Q8C1C4, Q9CXE3, Q9JLE4, Q9JLE5, Q9QYB7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 107 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program