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Q9QYB8

- ADDB_MOUSE

UniProt

Q9QYB8 - ADDB_MOUSE

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Protein

Beta-adducin

Gene

Add2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Binds to the erythrocyte membrane receptor SLC2A1/GLUT1 and may therefore provide a link between the spectrin cytoskeleton to the plasma membrane. Binds to calmodulin. Calmodulin binds preferentially to the beta subunit (By similarity).By similarity

GO - Molecular functioni

  1. structural molecule activity Source: MGI

GO - Biological processi

  1. actin filament bundle assembly Source: Ensembl
  2. barbed-end actin filament capping Source: Ensembl
  3. hemopoiesis Source: MGI
  4. positive regulation of protein binding Source: Ensembl
  5. protein complex assembly Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calmodulin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-adducin
Alternative name(s):
Add97
Erythrocyte adducin subunit beta
Gene namesi
Name:Add2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:87919. Add2.

Subcellular locationi

Cytoplasmcytoskeleton By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity

GO - Cellular componenti

  1. cytoplasmic membrane-bounded vesicle Source: UniProtKB
  2. F-actin capping protein complex Source: Ensembl
  3. membrane Source: MGI
  4. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 725725Beta-adducinPRO_0000218534Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei55 – 551PhosphothreonineBy similarity
Modified residuei530 – 5301PhosphoserineBy similarity
Modified residuei532 – 5321Phosphoserine1 Publication
Modified residuei535 – 5351Phosphoserine1 Publication
Modified residuei561 – 5611Phosphothreonine
Modified residuei594 – 5941PhosphoserineBy similarity
Modified residuei598 – 5981PhosphoserineBy similarity
Modified residuei602 – 6021Phosphoserine1 Publication
Modified residuei606 – 6061PhosphoserineBy similarity
Modified residuei612 – 6121PhosphothreonineBy similarity
Modified residuei614 – 6141PhosphoserineBy similarity
Modified residuei618 – 6181PhosphoserineBy similarity
Modified residuei692 – 6921PhosphoserineBy similarity
Modified residuei696 – 6961PhosphoserineBy similarity
Modified residuei702 – 7021PhosphoserineBy similarity
Modified residuei712 – 7121PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9QYB8.
PaxDbiQ9QYB8.
PRIDEiQ9QYB8.

2D gel databases

REPRODUCTION-2DPAGEQ9QYB8.

PTM databases

PhosphoSiteiQ9QYB8.

Expressioni

Gene expression databases

BgeeiQ9QYB8.
CleanExiMM_ADD2.
GenevestigatoriQ9QYB8.

Interactioni

Subunit structurei

Found in a complex with ADD2, DMTN and SLC2A1. Interacts with SLC2A1 (By similarity). Heterodimer of an alpha and a beta subunit.By similarity

Protein-protein interaction databases

BioGridi197982. 1 interaction.
IntActiQ9QYB8. 3 interactions.
MINTiMINT-4998363.
STRINGi10090.ENSMUSP00000032069.

Structurei

3D structure databases

ProteinModelPortaliQ9QYB8.
SMRiQ9QYB8. Positions 149-327.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni425 – 44420Interaction with calmodulinSequence AnalysisAdd
BLAST
Regioni703 – 72018Interaction with calmodulinSequence AnalysisAdd
BLAST

Domaini

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 similaritiesi

Phylogenomic databases

eggNOGiCOG0235.
GeneTreeiENSGT00390000016462.
HOVERGENiHBG004180.
InParanoidiQ9QYB8.
OMAiSGPMSPE.
OrthoDBiEOG7HF1HR.
PhylomeDBiQ9QYB8.
TreeFamiTF313003.

Family and domain databases

Gene3Di3.40.225.10. 1 hit.
InterProiIPR027773. ADD2.
IPR001303. Aldolase_II/adducin_N.
[Graphical view]
PANTHERiPTHR10672:SF6. PTHR10672:SF6. 1 hit.
PfamiPF00596. Aldolase_II. 1 hit.
[Graphical view]
SMARTiSM01007. Aldolase_II. 1 hit.
[Graphical view]
SUPFAMiSSF53639. SSF53639. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q9QYB8-1) [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
MSEDTVPEAA SPPPSQGQHY FDRFSEDDPE YLRLRNRAAD LRQDFNLMEQ
60 70 80 90 100
KKRVTMILQS PSFREELEGL IQEQMKKGNN SSNIWALRQI ADFMASTSHA
110 120 130 140 150
VFPASSMNFS MMTPINDLHT ADSLNLAKGE RLMRCKISSV YRLLDLYGWA
160 170 180 190 200
QLSDTYVTLR VSKEQDHFLI SPKGVSCSEV TASSLIKVNI LGEVVEKGSS
210 220 230 240 250
CFPVDTTGFS LHSAIYAARP DVRCAIHLHT PATAAVSAMK CGLLPVSHNA
260 270 280 290 300
LLVGDMAYYD FNGEMEQEAD RINLQKCLGP TCKILVLRNH GMVALGDTVE
310 320 330 340 350
EAFYKVFHLQ AACEVQVSAL SSAGGTENLI LLEQEKHRPH EVGSVQWAGS
360 370 380 390 400
TFGPMQKSRL GEHEFEALMR MLDNLGYRTG YTYRHPFVQE KTKHKSEVEI
410 420 430 440 450
PATVTAFVFE EDGVPVPALR QHAQKQQKEK TRWLNTPNTY LRVNVADEVQ
460 470 480 490 500
RNMGSPRPKT TWMKADEVEK SSSGMPIRIE NPNQFVPLYT DPQEVLDMRN
510 520 530 540 550
KIREQNRQDI KSAGPQSQLL ASVIAEKSRS PSTESQLMSK GDADTKDESE
560 570 580 590 600
ETVPNPFSQL TDQELEEYKK EVERKKLEQE QEGEKDIATE KPGSPVKSTP
610 620 630 640 650
ASPVQSPSKA GTKSPAVSPS KTSEDTKKTE VSEANTEPEP VKPEGLVVNG
660 670 680 690 700
KEEEPSVEEA LSKGLGQMTT NADTDGDSYK DKTESVTSGP LSPEGSPSKS
710 720
PSKKKKKFRT PSFLKKSKKK EKVES
Length:725
Mass (Da):80,642
Last modified:January 23, 2007 - v4
Checksum:i479153AB1BD6C0DA
GO
Isoform 2 (identifier: Q9QYB8-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:562
Mass (Da):62,816
Checksum:iAECF298E23B44CB8
GO
Isoform 3 (identifier: Q9QYB8-3) [UniParc]FASTAAdd to Basket

Also known as: Delta

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

Show »
Length:477
Mass (Da):52,522
Checksum:iA15E5687AFD48EF0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti219 – 2191R → T in AAF29503. (PubMed:10845937)Curated
Sequence conflicti469 – 4691E → Q in AAF24972. (PubMed:10602987)Curated
Sequence conflicti469 – 4691E → Q in AAF24973. (PubMed:10602987)Curated
Sequence conflicti518 – 5181Q → H in BAC25943. (PubMed:16141072)Curated
Sequence conflicti634 – 6341A → R in AAF24972. (PubMed:10602987)Curated
Sequence conflicti666 – 6661G → V in AAF24972. (PubMed:10602987)Curated
Sequence conflicti675 – 6751D → V in AAF29502. (PubMed:10845937)Curated
Sequence conflicti675 – 6751D → V in AAF29503. (PubMed:10845937)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei284 – 531248Missing in isoform 3. 1 PublicationVSP_022596Add
BLAST
Alternative sequencei532 – 56231STESQ…SQLTD → VQQRLPPTEGEVYQTPGAGQ GTPESSGPLTP in isoform 2. 2 PublicationsVSP_000184Add
BLAST
Alternative sequencei563 – 725163Missing in isoform 2. 2 PublicationsVSP_000185Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS20308.1. [Q9QYB8-1]
PIRiA60670.
RefSeqiNP_001258786.1. NM_001271857.1. [Q9QYB8-1]
NP_001258787.1. NM_001271858.1. [Q9QYB8-1]
NP_001258788.1. NM_001271859.1. [Q9QYB8-1]
NP_001258789.1. NM_001271860.1. [Q9QYB8-2]
NP_001258790.1. NM_001271861.1. [Q9QYB8-2]
NP_038486.2. NM_013458.5. [Q9QYB8-1]
UniGeneiMm.104155.
Mm.489430.

Genome annotation databases

EnsembliENSMUST00000032069; ENSMUSP00000032069; ENSMUSG00000030000. [Q9QYB8-1]
GeneIDi11519.
KEGGimmu:11519.
UCSCiuc009crd.1. mouse. [Q9QYB8-2]
uc009cre.1. mouse. [Q9QYB8-1]
uc012eoj.1. mouse. [Q9QYB8-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS20308.1. [Q9QYB8-1 ]
PIRi A60670.
RefSeqi NP_001258786.1. NM_001271857.1. [Q9QYB8-1 ]
NP_001258787.1. NM_001271858.1. [Q9QYB8-1 ]
NP_001258788.1. NM_001271859.1. [Q9QYB8-1 ]
NP_001258789.1. NM_001271860.1. [Q9QYB8-2 ]
NP_001258790.1. NM_001271861.1. [Q9QYB8-2 ]
NP_038486.2. NM_013458.5. [Q9QYB8-1 ]
UniGenei Mm.104155.
Mm.489430.

3D structure databases

ProteinModelPortali Q9QYB8.
SMRi Q9QYB8. Positions 149-327.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 197982. 1 interaction.
IntActi Q9QYB8. 3 interactions.
MINTi MINT-4998363.
STRINGi 10090.ENSMUSP00000032069.

PTM databases

PhosphoSitei Q9QYB8.

2D gel databases

REPRODUCTION-2DPAGE Q9QYB8.

Proteomic databases

MaxQBi Q9QYB8.
PaxDbi Q9QYB8.
PRIDEi Q9QYB8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000032069 ; ENSMUSP00000032069 ; ENSMUSG00000030000 . [Q9QYB8-1 ]
GeneIDi 11519.
KEGGi mmu:11519.
UCSCi uc009crd.1. mouse. [Q9QYB8-2 ]
uc009cre.1. mouse. [Q9QYB8-1 ]
uc012eoj.1. mouse. [Q9QYB8-3 ]

Organism-specific databases

CTDi 119.
MGIi MGI:87919. Add2.

Phylogenomic databases

eggNOGi COG0235.
GeneTreei ENSGT00390000016462.
HOVERGENi HBG004180.
InParanoidi Q9QYB8.
OMAi SGPMSPE.
OrthoDBi EOG7HF1HR.
PhylomeDBi Q9QYB8.
TreeFami TF313003.

Miscellaneous databases

NextBioi 278952.
PROi Q9QYB8.
SOURCEi Search...

Gene expression databases

Bgeei Q9QYB8.
CleanExi MM_ADD2.
Genevestigatori Q9QYB8.

Family and domain databases

Gene3Di 3.40.225.10. 1 hit.
InterProi IPR027773. ADD2.
IPR001303. Aldolase_II/adducin_N.
[Graphical view ]
PANTHERi PTHR10672:SF6. PTHR10672:SF6. 1 hit.
Pfami PF00596. Aldolase_II. 1 hit.
[Graphical view ]
SMARTi SM01007. Aldolase_II. 1 hit.
[Graphical view ]
SUPFAMi SSF53639. SSF53639. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-561 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-602, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-532 AND SER-535, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiADDB_MOUSE
AccessioniPrimary (citable) accession number: Q9QYB8
Secondary accession number(s): Q3U0E1
, Q80VH9, Q8C1C4, Q9CXE3, Q9JLE4, Q9JLE5, Q9QYB7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 121 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3