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Q62261

- SPTB2_MOUSE

UniProt

Q62261 - SPTB2_MOUSE

Protein

Spectrin beta chain, non-erythrocytic 1

Gene

Sptbn1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 2 (16 May 2006)
      Previous versions | rss
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    Functioni

    Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane.

    GO - Molecular functioni

    1. phospholipid binding Source: InterPro
    2. protein binding Source: MGI
    3. structural constituent of cytoskeleton Source: Ensembl

    GO - Biological processi

    1. actin filament capping Source: UniProtKB-KW
    2. common-partner SMAD protein phosphorylation Source: MGI
    3. Golgi to plasma membrane protein transport Source: Ensembl
    4. membrane assembly Source: Ensembl
    5. mitotic cytokinesis Source: Ensembl
    6. protein targeting to plasma membrane Source: BHF-UCL
    7. SMAD protein import into nucleus Source: MGI

    Keywords - Molecular functioni

    Actin capping

    Keywords - Ligandi

    Actin-binding, Calmodulin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Spectrin beta chain, non-erythrocytic 1
    Alternative name(s):
    Beta-II spectrin
    Embryonic liver fodrin
    Fodrin beta chain
    Gene namesi
    Name:Sptbn1
    Synonyms:Elf, Spnb-2, Spnb2, Sptb2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:98388. Sptbn1.

    Subcellular locationi

    Cytoplasmcytoskeleton 1 Publication. CytoplasmmyofibrilsarcomereM line 1 Publication
    Note: Colocalizes with ANK2 in a distinct intracellular compartment of neonatal cardiomyocytes.

    GO - Cellular componenti

    1. axolemma Source: BHF-UCL
    2. cortical cytoskeleton Source: MGI
    3. cuticular plate Source: MGI
    4. M band Source: BHF-UCL
    5. membrane Source: MGI
    6. nucleolus Source: Ensembl
    7. nucleus Source: MGI
    8. plasma membrane Source: MGI
    9. protein complex Source: Ensembl
    10. spectrin Source: InterPro

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 23632362Spectrin beta chain, non-erythrocytic 1PRO_0000073462Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonineBy similarity
    Modified residuei90 – 901N6-acetyllysineBy similarity
    Modified residuei817 – 8171PhosphoserineBy similarity
    Modified residuei1057 – 10571PhosphoserineBy similarity
    Modified residuei1447 – 14471PhosphoserineBy similarity
    Modified residuei1805 – 18051Phosphotyrosine1 Publication
    Modified residuei1815 – 18151N6-acetyllysineBy similarity
    Modified residuei1913 – 19131N6-acetyllysineBy similarity
    Modified residuei1989 – 19891N6-acetyllysineBy similarity
    Modified residuei2102 – 21021Phosphoserine2 Publications
    Modified residuei2127 – 21271Phosphoserine1 Publication
    Modified residuei2137 – 21371Phosphoserine2 Publications
    Modified residuei2159 – 21591PhosphoserineBy similarity
    Modified residuei2160 – 21601PhosphoserineBy similarity
    Modified residuei2163 – 21631PhosphoserineBy similarity
    Modified residuei2164 – 21641Phosphoserine1 Publication
    Modified residuei2168 – 21681Phosphoserine1 Publication
    Modified residuei2186 – 21861PhosphothreonineBy similarity
    Modified residuei2194 – 21941Phosphothreonine1 Publication
    Modified residuei2318 – 23181PhosphoserineBy similarity
    Modified residuei2319 – 23191PhosphothreonineBy similarity
    Glycosylationi2323 – 23231O-linked (GlcNAc)1 Publication
    Modified residuei2327 – 23271PhosphothreonineBy similarity
    Modified residuei2339 – 23391PhosphoserineBy similarity
    Modified residuei2340 – 23401PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ62261.
    PaxDbiQ62261.
    PRIDEiQ62261.

    PTM databases

    PhosphoSiteiQ62261.

    Expressioni

    Tissue specificityi

    Isoform 2 is present in brain, heart, kidney and liver (at protein level).2 Publications

    Developmental stagei

    Isoform 2 is expressed in brain, heart and liver throughout embryonic development. Isoform 1 is mainly expressed in neonatal developing ventricular cardiomyocytes.1 Publication

    Gene expression databases

    ArrayExpressiQ62261.
    BgeeiQ62261.
    CleanExiMM_SPNB2.
    GenevestigatoriQ62261.

    Interactioni

    Subunit structurei

    Like erythrocyte spectrin, the spectrin-like proteins are capable to form dimers which can further associate to tetramers. Interacts with CAMSAP1 By similarity. Interacts with ANK2.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi203461. 9 interactions.
    DIPiDIP-31558N.
    IntActiQ62261. 13 interactions.
    MINTiMINT-4135469.

    Structurei

    Secondary structure

    1
    2363
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2200 – 220910
    Beta strandi2211 – 22133
    Beta strandi2222 – 22298
    Beta strandi2232 – 22387
    Helixi2239 – 22446
    Beta strandi2248 – 22503
    Beta strandi2253 – 22553
    Beta strandi2260 – 22634
    Beta strandi2269 – 22779
    Beta strandi2283 – 22875
    Helixi2291 – 230313

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BTNX-ray2.00A2199-2304[»]
    1MPHNMR-A2199-2304[»]
    ProteinModelPortaliQ62261.
    SMRiQ62261. Positions 173-280, 1697-2086, 2199-2304.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ62261.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 275274Actin-bindingAdd
    BLAST
    Domaini54 – 158105CH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini173 – 275103CH 2PROSITE-ProRule annotationAdd
    BLAST
    Repeati303 – 411109Spectrin 1Add
    BLAST
    Repeati423 – 525103Spectrin 2Add
    BLAST
    Repeati530 – 636107Spectrin 3Add
    BLAST
    Repeati639 – 742104Spectrin 4Add
    BLAST
    Repeati745 – 847103Spectrin 5Add
    BLAST
    Repeati851 – 952102Spectrin 6Add
    BLAST
    Repeati957 – 1060104Spectrin 7Add
    BLAST
    Repeati1063 – 1166104Spectrin 8Add
    BLAST
    Repeati1169 – 125789Spectrin 9Add
    BLAST
    Repeati1276 – 1376101Spectrin 10Add
    BLAST
    Repeati1381 – 1482102Spectrin 11Add
    BLAST
    Repeati1486 – 1590105Spectrin 12Add
    BLAST
    Repeati1592 – 1696105Spectrin 13Add
    BLAST
    Repeati1698 – 1801104Spectrin 14Add
    BLAST
    Repeati1805 – 1907103Spectrin 15Add
    BLAST
    Repeati1914 – 2014101Spectrin 16Add
    BLAST
    Repeati2018 – 209780Spectrin 17Add
    BLAST
    Domaini2196 – 2306111PHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1563 – 2093531Interaction with ANK2By similarityAdd
    BLAST
    Regioni2148 – 217629Mediates interaction with CAMSAP1By similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the spectrin family.Curated
    Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
    Contains 1 PH domain.PROSITE-ProRule annotation
    Contains 17 spectrin repeats.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5069.
    GeneTreeiENSGT00700000104022.
    HOGENOMiHOG000007281.
    HOVERGENiHBG057912.
    InParanoidiQ62261.
    KOiK06115.
    OMAiLWQFYWD.
    OrthoDBiEOG73RB9J.
    PhylomeDBiQ62261.
    TreeFamiTF313446.

    Family and domain databases

    Gene3Di1.10.418.10. 2 hits.
    2.30.29.30. 1 hit.
    InterProiIPR001589. Actinin_actin-bd_CS.
    IPR001715. CH-domain.
    IPR001605. PH_dom-spectrin-type.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR018159. Spectrin/alpha-actinin.
    IPR016343. Spectrin_bsu.
    IPR002017. Spectrin_repeat.
    [Graphical view]
    PfamiPF00307. CH. 2 hits.
    PF00435. Spectrin. 17 hits.
    [Graphical view]
    PIRSFiPIRSF002297. Spectrin_beta_subunit. 1 hit.
    PRINTSiPR00683. SPECTRINPH.
    SMARTiSM00033. CH. 2 hits.
    SM00233. PH. 1 hit.
    SM00150. SPEC. 17 hits.
    [Graphical view]
    SUPFAMiSSF47576. SSF47576. 1 hit.
    PROSITEiPS00019. ACTININ_1. 1 hit.
    PS00020. ACTININ_2. 1 hit.
    PS50021. CH. 2 hits.
    PS50003. PH_DOMAIN. 1 hit.
    [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. Align

    Isoform 1 (identifier: Q62261-1) [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

    MTTTVATDYD NIEIQQQYSD VNNRWDVDDW DNENSSARLF ERSRIKALAD     50
    EREAVQKKTF TKWVNSHLAR VSCRITDLYT DLRDGRMLIK LLEVLSGERL 100
    PKPTKGRMRI HCLENVDKAL QFLKEQRVHL ENMGSHDIVD GNHRLTLGLI 150
    WTIILRFQIQ DISVETEDNK EKKSAKDALL LWCQMKTAGY PNVNIHNFTT 200
    SWRDGMAFNA LIHKHRPDLI DFDKLKKSNA HYNLQNAFNL AEQHLGLTKL 250
    LDPEDISVDH PDEKSIITYV VTYYHYFSKM KALAVEGKRI GKVLDNAIET 300
    EKMIEKYESL ASDLLEWIEQ TIIILNNRKF ANSLVGVQQQ LQAFNTYRTV 350
    EKPPKFTEKG NLEVLLFTIQ SKMRANNQKV YMPREGKLIS DINKAWERLE 400
    KAEHERELAL RNELIRQEKL EQLARRFDRK AAMRETWLSE NQRLVSQDNF 450
    GFDLPAVEAA TKKHEAIETD IAAYEERVQA VVAVARELEA ENYHDIKRIT 500
    ARKDNVIRLW EYLLELLRAR RQRLEMNLGL QKIFQEMLYI MDWMDEMKVL 550
    LLSQDYGKHL LGVEDLLQKH ALVEADIAIQ AERVRGVNAS AQKFATDGEG 600
    YKPCDPQVIR DRVAHMEFCY QELCQLAAER RARLEESRRL WKFFWEMAEE 650
    EGWIREKEKI LSSDDYGKDL TSVMRLLSKH RAFEDEMSGR SGHFEQAIKE 700
    GEDMIAEEHF GSEKIRERII YIREQWANLE QLSAIRKKRL EEASLLHQFQ 750
    ADADDIDAWM LDILKIVSSN DVGHDEYSTQ SLVKKHKDVA EEITNYRPTI 800
    DTLHEQASAL PQAHAESPDV KGRLAGIEER CKEMAELTRL RKQALQDTLA 850
    LYKMFSEADA CELWIDEKEQ WLNNMQIPEK LEDLEVIQHR FESLEPEMNN 900
    QASRVAVVNQ IARQLMHNGH PSEKEIRAQQ DKLNTRWSQF RELVDRKKDA 950
    LLSALSIQNY HLECNETKSW IREKTKVIES TQDLGNDLAG VMALQRKLTG 1000
    MERDLVAIEA KLSDLQKEAE KLESEHPDQA QAILSRLAEI SDVWEEMKTT 1050
    LKNREASLGE ASKLQQFLRD LDDFQSWLSR TQTAIASEDM PNTLTEAEKL 1100
    LTQHENIKNE IDNYEEDYQK MRDMGEMVTQ GQTDAQYMFL RQRLQALDTG 1150
    WNELHKMWEN RQNLLSQSHA YQQFLRDTKQ AEAFLNNQEY VLAHTEMPTT 1200
    LEGAEAAIKK QEDFMTTMDA NEEKINAVVE TGRRLVSDGN INSDRIQEKV 1250
    DSIDDRHRKN REAASELLMR LKDNRDLQKF LQDCQELSLW INEKMLTAQD 1300
    MSYDEARNLH SKWLKHQAFM AELASNKEWL DKIEKEGMQL ISEKPETEAV 1350
    VKEKLTGLHK MWEVLESTTQ TKAQRLFDAN KAELFTQSCA DLDKWLHGLE 1400
    SQIQSDDYGK DLTSVNILLK KQQMLENQME VRKKEIEELQ SQAQALSQEG 1450
    KSTDEVDSKR LTVQTKFMEL LEPLSERKHN LLASKEIHQF NRDVEDEILW 1500
    VGERMPLATS TDHGHNLQTV QLLIKKNQTL QKEIQGHQPR IDDIFERSQN 1550
    IITDSSSLNA EAIRQRLADL KQLWGLLIEE TEKRHRRLEE AHKAQQYYFD 1600
    AAEAEAWMSE QELYMMSEEK AKDEQSAVSM LKKHQILEQA VEDYAETVHQ 1650
    LSKTSRALVA DSHPESERIS MRQSKVDKLY AGLKDLAEER RGKLDERHRL 1700
    FQLNREVDDL EQWIAEREVV AGSHELGQDY EHVTMLQERF REFARDTGNI 1750
    GQERVDTVNN MADELINSGH SDAATIAEWK DGLNEAWADL LELIDTRTQI 1800
    LAASYELHKF YHDAKEIFGR IQDKHKKLPE ELGRDQNTVE TLQRMHTTFE 1850
    HDIQALGTQV RQLQEDAARL QAAYAGDKAD DIQKRENEVL EAWKSLLDAC 1900
    EGRRVRLVDT GDKFRFFSMV RDLMLWMEDV IRQIEAQEKP RDVSSVELLM 1950
    NNHQGIKAEI DARNDSFTAC IELGKSLLAR KHYASEEIKE KLLQLTEKRK 2000
    EMIDKWEDRW EWLRLILEVH QFSRDASVAE AWLLGQEPYL SSREIGQSVD 2050
    EVEKLIKRHE AFEKSAATWD ERFSALERLT TLELLEVRRQ QEEEERKRRP 2100
    PSPDPNTKVS EEAESQQWDT SKGDQVSQNG LPAEQGSPRM AGTMETSEMV 2150
    NGAAEQRTSS KESSPVPSPT LDRKAKSALP AQSAATLPAR TLETPAAQME 2200
    GFLNRKHEWE AHNKKASSRS WHNVYCVINN QEMGFYKDAK SAASGIPYHS 2250
    EVPVSLKEAI CEVALDYKKK KHVFKLRLSD GNEYLFQAKD DEEMNTWIQA 2300
    ISSAISSDKH DTSASTQSTP ASSRAQTLPT SVVTITSESS PGKREKDKEK 2350
    DKEKRFSLFG KKK 2363
    Length:2,363
    Mass (Da):274,223
    Last modified:May 16, 2006 - v2
    Checksum:i221362054E64BB8C
    GO
    Isoform 2 (identifier: Q62261-2) [UniParc]FASTAAdd to Basket

    Also known as: Elf3

    The sequence of this isoform differs from the canonical sequence as follows:
         2-49: TTTVATDYDN...FERSRIKALA → MELQRTSSIS...QLEGRFKQLQ
         2140-2246: MAGTMETSEM...KDAKSAASGI → VSYRSQTYQNYKNFNSRRTASDHSWSGM
         2247-2363: Missing.

    Note: Contains a phosphoserine at position 14.By similarity

    Show »
    Length:2,155
    Mass (Da):251,288
    Checksum:i4C28E2F4B311D9CD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti252 – 2521D → A in BAE41221. (PubMed:16141072)Curated
    Sequence conflicti309 – 3091S → T in AAD01616. (PubMed:9927192)Curated
    Sequence conflicti368 – 3681T → A in AAD01616. (PubMed:9927192)Curated
    Sequence conflicti737 – 7371K → I in AAC42040. (PubMed:8479293)Curated
    Sequence conflicti796 – 7961Y → C in AAD01616. (PubMed:9927192)Curated
    Sequence conflicti846 – 8461Q → R in AAC42040. (PubMed:8479293)Curated
    Sequence conflicti970 – 9701W → C in AAD01616. (PubMed:9927192)Curated
    Sequence conflicti996 – 9961R → C in AAD01616. (PubMed:9927192)Curated
    Sequence conflicti1401 – 14033SQI → KPGF in AAC42040. (PubMed:8479293)Curated
    Sequence conflicti1414 – 145542SVNIL…KSTDE → QSQYSSEKGNRRRRIRWKFG RKRSRNCRPSPGSSRGRAQM R in AAC42040. (PubMed:8479293)CuratedAdd
    BLAST
    Sequence conflicti1508 – 15081A → R in AAC42040. (PubMed:8479293)Curated
    Sequence conflicti1619 – 16246EKAKDE → KRPRMK in AAC42040. (PubMed:8479293)Curated
    Sequence conflicti1898 – 18981D → G in AAC42040. (PubMed:8479293)Curated
    Sequence conflicti2171 – 21711L → S in AAC42040. (PubMed:8479293)Curated
    Sequence conflicti2345 – 23462EK → AE in AAC42040. (PubMed:8479293)Curated
    Sequence conflicti2356 – 23583FSL → STV in AAC42040. (PubMed:8479293)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 4948TTTVA…IKALA → MELQRTSSISGPLSPAYTGQ VPYNYNQLEGRFKQLQ in isoform 2. 2 PublicationsVSP_026057Add
    BLAST
    Alternative sequencei2140 – 2246107MAGTM…AASGI → VSYRSQTYQNYKNFNSRRTA SDHSWSGM in isoform 2. 2 PublicationsVSP_026058Add
    BLAST
    Alternative sequencei2247 – 2363117Missing in isoform 2. 2 PublicationsVSP_026059Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M74773 mRNA. Translation: AAC42040.1.
    AF017112 mRNA. Translation: AAD01616.1.
    AL731792, AL672225 Genomic DNA. Translation: CAI24366.1.
    AL731792, AL672225 Genomic DNA. Translation: CAI24367.1.
    AL672225, AL731792 Genomic DNA. Translation: CAI25429.1.
    AL672225, AL731792 Genomic DNA. Translation: CAI25430.1.
    AL731792, AL672225 Genomic DNA. Translation: CAM16973.1.
    AL672225, AL731792 Genomic DNA. Translation: CAM22716.1.
    AK169544 mRNA. Translation: BAE41221.1.
    CCDSiCCDS36123.1. [Q62261-1]
    RefSeqiNP_033286.2. NM_009260.2.
    NP_787030.2. NM_175836.2. [Q62261-1]
    XP_006514662.1. XM_006514599.1. [Q62261-1]
    XP_006514663.1. XM_006514600.1. [Q62261-1]
    UniGeneiMm.123110.
    Mm.466085.

    Genome annotation databases

    EnsembliENSMUST00000006629; ENSMUSP00000006629; ENSMUSG00000020315. [Q62261-1]
    ENSMUST00000011877; ENSMUSP00000011877; ENSMUSG00000020315. [Q62261-1]
    GeneIDi20742.
    KEGGimmu:20742.
    UCSCiuc007ihs.1. mouse. [Q62261-1]
    uc007iht.1. mouse. [Q62261-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M74773 mRNA. Translation: AAC42040.1 .
    AF017112 mRNA. Translation: AAD01616.1 .
    AL731792 , AL672225 Genomic DNA. Translation: CAI24366.1 .
    AL731792 , AL672225 Genomic DNA. Translation: CAI24367.1 .
    AL672225 , AL731792 Genomic DNA. Translation: CAI25429.1 .
    AL672225 , AL731792 Genomic DNA. Translation: CAI25430.1 .
    AL731792 , AL672225 Genomic DNA. Translation: CAM16973.1 .
    AL672225 , AL731792 Genomic DNA. Translation: CAM22716.1 .
    AK169544 mRNA. Translation: BAE41221.1 .
    CCDSi CCDS36123.1. [Q62261-1 ]
    RefSeqi NP_033286.2. NM_009260.2.
    NP_787030.2. NM_175836.2. [Q62261-1 ]
    XP_006514662.1. XM_006514599.1. [Q62261-1 ]
    XP_006514663.1. XM_006514600.1. [Q62261-1 ]
    UniGenei Mm.123110.
    Mm.466085.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BTN X-ray 2.00 A 2199-2304 [» ]
    1MPH NMR - A 2199-2304 [» ]
    ProteinModelPortali Q62261.
    SMRi Q62261. Positions 173-280, 1697-2086, 2199-2304.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 203461. 9 interactions.
    DIPi DIP-31558N.
    IntActi Q62261. 13 interactions.
    MINTi MINT-4135469.

    PTM databases

    PhosphoSitei Q62261.

    Proteomic databases

    MaxQBi Q62261.
    PaxDbi Q62261.
    PRIDEi Q62261.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000006629 ; ENSMUSP00000006629 ; ENSMUSG00000020315 . [Q62261-1 ]
    ENSMUST00000011877 ; ENSMUSP00000011877 ; ENSMUSG00000020315 . [Q62261-1 ]
    GeneIDi 20742.
    KEGGi mmu:20742.
    UCSCi uc007ihs.1. mouse. [Q62261-1 ]
    uc007iht.1. mouse. [Q62261-2 ]

    Organism-specific databases

    CTDi 6711.
    MGIi MGI:98388. Sptbn1.

    Phylogenomic databases

    eggNOGi COG5069.
    GeneTreei ENSGT00700000104022.
    HOGENOMi HOG000007281.
    HOVERGENi HBG057912.
    InParanoidi Q62261.
    KOi K06115.
    OMAi LWQFYWD.
    OrthoDBi EOG73RB9J.
    PhylomeDBi Q62261.
    TreeFami TF313446.

    Miscellaneous databases

    EvolutionaryTracei Q62261.
    NextBioi 299385.
    PROi Q62261.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q62261.
    Bgeei Q62261.
    CleanExi MM_SPNB2.
    Genevestigatori Q62261.

    Family and domain databases

    Gene3Di 1.10.418.10. 2 hits.
    2.30.29.30. 1 hit.
    InterProi IPR001589. Actinin_actin-bd_CS.
    IPR001715. CH-domain.
    IPR001605. PH_dom-spectrin-type.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR018159. Spectrin/alpha-actinin.
    IPR016343. Spectrin_bsu.
    IPR002017. Spectrin_repeat.
    [Graphical view ]
    Pfami PF00307. CH. 2 hits.
    PF00435. Spectrin. 17 hits.
    [Graphical view ]
    PIRSFi PIRSF002297. Spectrin_beta_subunit. 1 hit.
    PRINTSi PR00683. SPECTRINPH.
    SMARTi SM00033. CH. 2 hits.
    SM00233. PH. 1 hit.
    SM00150. SPEC. 17 hits.
    [Graphical view ]
    SUPFAMi SSF47576. SSF47576. 1 hit.
    PROSITEi PS00019. ACTININ_1. 1 hit.
    PS00020. ACTININ_2. 1 hit.
    PS50021. CH. 2 hits.
    PS50003. PH_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete amino acid sequence for brain beta spectrin (beta fodrin): relationship to globin sequences."
      Ma Y., Zimmer W.E., Riederer B.M., Goodman S.R.
      Brain Res. Mol. Brain Res. 18:87-99(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: BALB/c.
    2. "Elf3 encodes a novel 200-kD beta-spectrin: role in liver development."
      Mishra L., Cai T., Yu P., Monga S.P., Mishra B.
      Oncogene 18:353-364(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION.
      Strain: C57BL/6.
      Tissue: Liver.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "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] OF 1-399 (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Thymus.
    5. "Ankyrin-B targets beta2-spectrin to an intracellular compartment in neonatal cardiomyocytes."
      Mohler P.J., Yoon W., Bennett V.
      J. Biol. Chem. 279:40185-40193(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ANK2, TISSUE SPECIFICITY.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2127 AND SER-2137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    7. "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-2102 AND THR-2194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    8. "O-linked N-acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry."
      Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F., Maltby D.A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:923-934(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT SER-2323.
      Tissue: Brain.
    9. "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.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    11. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1805, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    12. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
      Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
      J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    13. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2164 AND SER-2168, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    14. "Structure of the pleckstrin homology domain from beta-spectrin."
      Macias M.J., Musacchio A., Ponstingl H., Nilges M., Saraste M., Oschkinat H.
      Nature 369:675-677(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 2199-2304.
    15. "Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from beta-spectrin."
      Nilges M., Macias M.J., O'Donoghue S.I., Oschkinat H.
      J. Mol. Biol. 269:408-422(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 2199-2304.
    16. "Structure of the binding site for inositol phosphates in a PH domain."
      Hyvoenen M., Macias M.J., Nilges M., Oschkinat H., Saraste M., Wilmanns M.
      EMBO J. 14:4676-4685(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2199-2304.

    Entry informationi

    Entry nameiSPTB2_MOUSE
    AccessioniPrimary (citable) accession number: Q62261
    Secondary accession number(s): A2AFU1
    , Q3TEM7, Q5SQL8, Q5SQL9, Q9QWJ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 16, 2006
    Last modified: October 1, 2014
    This is version 146 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3