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Q01082

- SPTB2_HUMAN

UniProt

Q01082 - SPTB2_HUMAN

Protein

Spectrin beta chain, non-erythrocytic 1

Gene

SPTBN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 2 (17 Oct 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. actin binding Source: ProtInc
    2. ankyrin binding Source: BHF-UCL
    3. phospholipid binding Source: InterPro
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. structural constituent of cytoskeleton Source: BHF-UCL

    GO - Biological processi

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

    Keywords - Molecular functioni

    Actin capping

    Keywords - Ligandi

    Actin-binding, Calmodulin-binding

    Enzyme and pathway databases

    ReactomeiREACT_18334. NCAM signaling for neurite out-growth.
    REACT_22266. Interaction between L1 and Ankyrins.
    REACT_23832. Nephrin interactions.
    SignaLinkiQ01082.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Spectrin beta chain, non-erythrocytic 1
    Alternative name(s):
    Beta-II spectrin
    Fodrin beta chain
    Spectrin, non-erythroid beta chain 1
    Gene namesi
    Name:SPTBN1
    Synonyms:SPTB2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:11275. SPTBN1.

    Subcellular locationi

    Cytoplasmcytoskeleton By similarity. CytoplasmmyofibrilsarcomereM line By similarity
    Note: Colocalizes with ANK2 in a distinct intracellular compartment of neonatal cardiomyocytes.By similarity
    Isoform 2 : Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity

    GO - Cellular componenti

    1. axolemma Source: BHF-UCL
    2. cuticular plate Source: Ensembl
    3. cytoplasm Source: HGNC
    4. cytosol Source: Reactome
    5. extracellular vesicular exosome Source: UniProt
    6. M band Source: UniProtKB-SubCell
    7. nucleolus Source: HGNC
    8. protein complex Source: Ensembl
    9. spectrin Source: ProtInc
    10. spectrin-associated cytoskeleton Source: BHF-UCL

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36104.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 23642363Spectrin beta chain, non-erythrocytic 1PRO_0000073461Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine3 Publications
    Modified residuei90 – 901N6-acetyllysine1 Publication
    Modified residuei817 – 8171Phosphoserine1 Publication
    Modified residuei825 – 8251Phosphoserine1 Publication
    Modified residuei1057 – 10571Phosphoserine1 Publication
    Modified residuei1447 – 14471Phosphoserine1 Publication
    Modified residuei1805 – 18051PhosphotyrosineBy similarity
    Modified residuei1815 – 18151N6-acetyllysine1 Publication
    Modified residuei1913 – 19131N6-acetyllysine1 Publication
    Modified residuei1989 – 19891N6-acetyllysine1 Publication
    Modified residuei2102 – 21021Phosphoserine7 Publications
    Modified residuei2128 – 21281Phosphoserine1 Publication
    Modified residuei2138 – 21381Phosphoserine6 Publications
    Modified residuei2160 – 21601Phosphoserine1 Publication
    Modified residuei2161 – 21611Phosphoserine1 Publication
    Modified residuei2164 – 21641Phosphoserine1 Publication
    Modified residuei2165 – 21651Phosphoserine1 Publication
    Modified residuei2169 – 21691Phosphoserine4 Publications
    Modified residuei2187 – 21871Phosphothreonine1 Publication
    Modified residuei2195 – 21951PhosphothreonineBy similarity
    Modified residuei2319 – 23191Phosphoserine1 Publication
    Modified residuei2320 – 23201Phosphothreonine3 Publications
    Glycosylationi2324 – 23241O-linked (GlcNAc)By similarity
    Modified residuei2328 – 23281Phosphothreonine1 Publication
    Modified residuei2340 – 23401Phosphoserine1 Publication
    Modified residuei2341 – 23411Phosphoserine3 Publications

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ01082.
    PaxDbiQ01082.
    PRIDEiQ01082.

    PTM databases

    PhosphoSiteiQ01082.

    Expressioni

    Tissue specificityi

    Isoform 2 is present in brain, lung and kidney (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ01082.
    BgeeiQ01082.
    CleanExiHS_SPTBN1.
    GenevestigatoriQ01082.

    Organism-specific databases

    HPAiHPA012685.
    HPA013149.

    Interactioni

    Subunit structurei

    Like erythrocyte spectrin, the spectrin-like proteins are capable to form dimers which can further associate to tetramers. Interacts with CAMSAP1. Interacts with ANK2. Isoform Short cannot bind to the axonal protein fodaxin.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DISC1Q9NRI53EBI-351561,EBI-529989
    SPTA1P025493EBI-351561,EBI-375617
    SPTAN1Q138137EBI-351561,EBI-351450

    Protein-protein interaction databases

    BioGridi112589. 83 interactions.
    DIPiDIP-33182N.
    IntActiQ01082. 46 interactions.
    MINTiMINT-1136298.
    STRINGi9606.ENSP00000349259.

    Structurei

    Secondary structure

    1
    2364
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi174 – 18613
    Turni187 – 1893
    Beta strandi196 – 1994
    Helixi200 – 2023
    Helixi206 – 21510
    Helixi217 – 2193
    Helixi222 – 2243
    Helixi230 – 24516
    Helixi253 – 2564
    Beta strandi257 – 2604
    Helixi263 – 27715
    Helixi1697 – 172125
    Helixi1730 – 176738
    Helixi1773 – 182654
    Helixi1836 – 185217
    Helixi1854 – 187320
    Helixi1877 – 193559
    Helixi1943 – 196220
    Helixi1964 – 197916
    Helixi1985 – 201430

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AA2X-ray2.00A173-280[»]
    1BKRX-ray1.10A172-280[»]
    3EDVX-ray1.95A/B1697-2015[»]
    ProteinModelPortaliQ01082.
    SMRiQ01082. Positions 48-280, 299-2086, 2200-2305.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ01082.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 275275Actin-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
    Domaini2197 – 2307111PHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1563 – 2093531Interaction with ANK2Add
    BLAST
    Regioni2149 – 217729Mediates interaction with CAMSAP1Add
    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.
    HOVERGENiHBG057912.
    InParanoidiQ01082.
    KOiK06115.
    OMAiLWQFYWD.
    OrthoDBiEOG73RB9J.
    PhylomeDBiQ01082.
    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.
    PF00169. PH. 1 hit.
    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 (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: Q01082-1) [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
    VLSQDYGKHL LGVEDLLQKH TLVEADIGIQ AERVRGVNAS AQKFATDGEG 600
    YKPCDPQVIR DRVAHMEFCY QELCQLAAER RARLEESRRL WKFFWEMAEE 650
    EGWIREKEKI LSSDDYGKDL TSVMRLLSKH RAFEDEMSGR SGHFEQAIKE 700
    GEDMIAEEHF GSEKIRERII YIREQWANLE QLSAIRKKRL EEASLLHQFQ 750
    ADADDIDAWM LDILKIVSSS DVGHDEYSTQ SLVKKHKDVA EEIANYRPTL 800
    DTLHEQASAL PQEHAESPDV RGRLSGIEER YKEVAELTRL RKQALQDTLA 850
    LYKMFSEADA CELWIDEKEQ WLNNMQIPEK LEDLEVIQHR FESLEPEMNN 900
    QASRVAVVNQ IARQLMHSGH PSEKEIKAQQ 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 RETASELLMR LKDNRDLQKF LQDCQELSLW INEKMLTAQD 1300
    MSYDEARNLH SKWLKHQAFM AELASNKEWL DKIEKEGMQL ISEKPETEAV 1350
    VKEKLTGLHK MWEVLESTTQ TKAQRLFDAN KAELFTQSCA DLDKWLHGLE 1400
    SQIQSDDYGK DLTSVNILLK KQQMLENQME VRKKEIEELQ SQAQALSQEG 1450
    KSTDEVDSKR LTVQTKFMEL LEPLNERKHN LLASKEIHQF NRDVEDEILW 1500
    VGERMPLATS TDHGHNLQTV QLLIKKNQTL QKEIQGHQPR IDDIFERSQN 1550
    IVTDSSSLSA EAIRQRLADL KQLWGLLIEE TEKRHRRLEE AHRAQQYYFD 1600
    AAEAEAWMSE QELYMMSEEK AKDEQSAVSM LKKHQILEQA VEDYAETVHQ 1650
    LSKTSRALVA DSHPESERIS MRQSKVDKLY AGLKDLAEER RGKLDERHRL 1700
    FQLNREVDDL EQWIAEREVV AGSHELGQDY EHVTMLQERF REFARDTGNI 1750
    GQERVDTVNH LADELINSGH SDAATIAEWK DGLNEAWADL LELIDTRTQI 1800
    LAASYELHKF YHDAKEIFGR IQDKHKKLPE ELGRDQNTVE TLQRMHTTFE 1850
    HDIQALGTQV RQLQEDAARL QAAYAGDKAD DIQKRENEVL EAWKSLLDAC 1900
    ESRRVRLVDT GDKFRFFSMV RDLMLWMEDV IRQIEAQEKP RDVSSVELLM 1950
    NNHQGIKAEI DARNDSFTTC IELGKSLLAR KHYASEEIKE KLLQLTEKRK 2000
    EMIDKWEDRW EWLRLILEVH QFSRDASVAE AWLLGQEPYL SSREIGQSVD 2050
    EVEKLIKRHE AFEKSAATWD ERFSALERLT TLELLEVRRQ QEEEERKRRP 2100
    PSPEPSTKVS EEAESQQQWD TSKGEQVSQN GLPAEQGSPR MAETVDTSEM 2150
    VNGATEQRTS SKESSPIPSP TSDRKAKTAL PAQSAATLPA RTQETPSAQM 2200
    EGFLNRKHEW EAHNKKASSR SWHNVYCVIN NQEMGFYKDA KTAASGIPYH 2250
    SEVPVSLKEA VCEVALDYKK KKHVFKLRLN DGNEYLFQAK DDEEMNTWIQ 2300
    AISSAISSDK HEVSASTQST PASSRAQTLP TSVVTITSES SPGKREKDKE 2350
    KDKEKRFSLF GKKK 2364
    Length:2,364
    Mass (Da):274,609
    Last modified:October 17, 2006 - v2
    Checksum:i1770C3B0EB07B892
    GO
    Isoform Short (identifier: Q01082-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2141-2168: MAETVDTSEMVNGATEQRTSSKESSPIP → VSYRSQTYQNYKNFNSRRTASDQPWSGL
         2169-2364: Missing.

    Show »
    Length:2,168
    Mass (Da):253,091
    Checksum:i34F9C77E47199043
    GO
    Isoform 2 (identifier: Q01082-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-49: MTTTVATDYD...FERSRIKALA → MELQRTSSIS...QLEGRFKQLQ
         2141-2225: MAETVDTSEM...KASSRSWHNV → VSYRSQTYQNYKNFNSRRTASDQPWSGL
         2226-2364: Missing.

    Note: Contains a phosphoserine at position 14.

    Show »
    Length:2,155
    Mass (Da):251,397
    Checksum:i2CA864D7AAC0182C
    GO

    Sequence cautioni

    The sequence BAD92985.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti583 – 5831R → W in BAD92985. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1411 – 14111D → H.2 Publications
    Corresponds to variant rs1052790 [ dbSNP | Ensembl ].
    VAR_032641

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4949MTTTV…IKALA → MELQRTSSISGPLSPAYTGQ VPYNYNQLEGRFKQLQ in isoform 2. 2 PublicationsVSP_026054Add
    BLAST
    Alternative sequencei2141 – 222585MAETV…SWHNV → VSYRSQTYQNYKNFNSRRTA SDQPWSGL in isoform 2. 2 PublicationsVSP_026055Add
    BLAST
    Alternative sequencei2141 – 216828MAETV…SSPIP → VSYRSQTYQNYKNFNSRRTA SDQPWSGL in isoform Short. 1 PublicationVSP_000720Add
    BLAST
    Alternative sequencei2169 – 2364196Missing in isoform Short. 1 PublicationVSP_000721Add
    BLAST
    Alternative sequencei2226 – 2364139Missing in isoform 2. 2 PublicationsVSP_026056Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M96803 mRNA. Translation: AAA60580.1.
    AF327441 mRNA. Translation: AAO15362.1.
    AB209748 mRNA. Translation: BAD92985.1. Different initiation.
    AC093110 Genomic DNA. Translation: AAY24229.1.
    AC092839 Genomic DNA. No translation available.
    CH471053 Genomic DNA. Translation: EAX00147.1.
    BC137282 mRNA. Translation: AAI37283.1.
    BC137283 mRNA. Translation: AAI37284.1.
    S65762 mRNA. Translation: AAB28324.1.
    AJ005694 mRNA. Translation: CAA06678.1.
    AJ238723 Genomic DNA. Translation: CAB91088.1.
    CCDSiCCDS33198.1. [Q01082-1]
    CCDS33199.1. [Q01082-3]
    PIRiA44159.
    A47213.
    RefSeqiNP_003119.2. NM_003128.2. [Q01082-1]
    NP_842565.2. NM_178313.2. [Q01082-3]
    XP_005264574.1. XM_005264517.1. [Q01082-1]
    XP_006712150.1. XM_006712087.1. [Q01082-1]
    UniGeneiHs.503178.
    Hs.705692.

    Genome annotation databases

    EnsembliENST00000333896; ENSP00000334156; ENSG00000115306. [Q01082-3]
    ENST00000356805; ENSP00000349259; ENSG00000115306. [Q01082-1]
    GeneIDi6711.
    KEGGihsa:6711.
    UCSCiuc002rxu.3. human. [Q01082-1]
    uc002rxx.3. human. [Q01082-3]

    Polymorphism databases

    DMDMi116242799.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M96803 mRNA. Translation: AAA60580.1 .
    AF327441 mRNA. Translation: AAO15362.1 .
    AB209748 mRNA. Translation: BAD92985.1 . Different initiation.
    AC093110 Genomic DNA. Translation: AAY24229.1 .
    AC092839 Genomic DNA. No translation available.
    CH471053 Genomic DNA. Translation: EAX00147.1 .
    BC137282 mRNA. Translation: AAI37283.1 .
    BC137283 mRNA. Translation: AAI37284.1 .
    S65762 mRNA. Translation: AAB28324.1 .
    AJ005694 mRNA. Translation: CAA06678.1 .
    AJ238723 Genomic DNA. Translation: CAB91088.1 .
    CCDSi CCDS33198.1. [Q01082-1 ]
    CCDS33199.1. [Q01082-3 ]
    PIRi A44159.
    A47213.
    RefSeqi NP_003119.2. NM_003128.2. [Q01082-1 ]
    NP_842565.2. NM_178313.2. [Q01082-3 ]
    XP_005264574.1. XM_005264517.1. [Q01082-1 ]
    XP_006712150.1. XM_006712087.1. [Q01082-1 ]
    UniGenei Hs.503178.
    Hs.705692.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AA2 X-ray 2.00 A 173-280 [» ]
    1BKR X-ray 1.10 A 172-280 [» ]
    3EDV X-ray 1.95 A/B 1697-2015 [» ]
    ProteinModelPortali Q01082.
    SMRi Q01082. Positions 48-280, 299-2086, 2200-2305.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112589. 83 interactions.
    DIPi DIP-33182N.
    IntActi Q01082. 46 interactions.
    MINTi MINT-1136298.
    STRINGi 9606.ENSP00000349259.

    PTM databases

    PhosphoSitei Q01082.

    Polymorphism databases

    DMDMi 116242799.

    Proteomic databases

    MaxQBi Q01082.
    PaxDbi Q01082.
    PRIDEi Q01082.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000333896 ; ENSP00000334156 ; ENSG00000115306 . [Q01082-3 ]
    ENST00000356805 ; ENSP00000349259 ; ENSG00000115306 . [Q01082-1 ]
    GeneIDi 6711.
    KEGGi hsa:6711.
    UCSCi uc002rxu.3. human. [Q01082-1 ]
    uc002rxx.3. human. [Q01082-3 ]

    Organism-specific databases

    CTDi 6711.
    GeneCardsi GC02P054665.
    H-InvDB HIX0002055.
    HGNCi HGNC:11275. SPTBN1.
    HPAi HPA012685.
    HPA013149.
    MIMi 182790. gene.
    neXtProti NX_Q01082.
    PharmGKBi PA36104.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5069.
    HOVERGENi HBG057912.
    InParanoidi Q01082.
    KOi K06115.
    OMAi LWQFYWD.
    OrthoDBi EOG73RB9J.
    PhylomeDBi Q01082.
    TreeFami TF313446.

    Enzyme and pathway databases

    Reactomei REACT_18334. NCAM signaling for neurite out-growth.
    REACT_22266. Interaction between L1 and Ankyrins.
    REACT_23832. Nephrin interactions.
    SignaLinki Q01082.

    Miscellaneous databases

    ChiTaRSi SPTBN1. human.
    EvolutionaryTracei Q01082.
    GeneWikii SPTBN1.
    GenomeRNAii 6711.
    NextBioi 26172.
    PROi Q01082.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q01082.
    Bgeei Q01082.
    CleanExi HS_SPTBN1.
    Genevestigatori Q01082.

    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.
    PF00169. PH. 1 hit.
    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. "Characterization of human brain cDNA encoding the general isoform of beta-spectrin."
      Hu R.J., Watanabe M., Bennett V.
      J. Biol. Chem. 267:18715-18722(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANT HIS-1411.
      Tissue: Brain.
    2. "A novel isoform of beta-spectrin II localizes to cerebellar Purkinje-cell bodies and interacts with neurofibromatosis type 2 gene product schwannomin."
      Chen Y., Yu P., Lu D., Tagle D.A., Cai T.
      J. Mol. Neurosci. 17:59-70(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, VARIANT HIS-1411.
    3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
      Tissue: Brain.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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).
    7. "Cloning of a portion of the chromosomal gene and cDNA for human beta-fodrin, the nonerythroid form of beta-spectrin."
      Chang J.G., Scarpa A., Eddy R.L., Byers M.G., Harris A.S., Morrow J.S., Watkins P., Shows T.B., Forget B.G.
      Genomics 17:287-293(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 293-1544.
    8. "Identification of a novel C-terminal variant of betaII spectrin: two isoforms of betaII spectrin have distinct intracellular locations and activities."
      Hayes N.V.L., Scott C., Heerkens E., Ohanian V., Maggs A.M., Pinder J.C., Kordeli E., Baines A.J.
      J. Cell Sci. 113:2023-2034(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 2087-2168 (ISOFORM SHORT).
      Tissue: Skeletal muscle.
    9. "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.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102 AND SER-2138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    13. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102; SER-2138; SER-2165; SER-2169; THR-2187; THR-2320; THR-2328 AND SER-2341, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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-1447; SER-2138; SER-2169 AND SER-2341, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-90; LYS-1815; LYS-1913 AND LYS-1989, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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-817; SER-825; SER-1057; SER-2102; SER-2138; SER-2169; THR-2320 AND SER-2341, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "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-2102; SER-2128; SER-2138; SER-2160; SER-2161; SER-2164; SER-2169; SER-2319; THR-2320 AND SER-2340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "A conserved sequence in CAMSAP1 (calmodulin regulated spectrin-associated protein 1) links its interaction with spectrin and calmodulin to neurite outgrowth."
      King M.D., Phillips G.W., Bignone P.A., Hayes N.V., Pinder J.C., Baines A.J.
      J. Neurochem. 128:391-402(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CAMSAP1.
    25. "Crystal structure of a calponin homology domain."
      Carugo K.D., Banuelos S., Saraste M.
      Nat. Struct. Biol. 4:175-179(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 173-280.
    26. "Structural comparisons of calponin homology domains: implications for actin binding."
      Banuelos S., Saraste M., Carugo K.D.
      Structure 6:1419-1431(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 173-281.

    Entry informationi

    Entry nameiSPTB2_HUMAN
    AccessioniPrimary (citable) accession number: Q01082
    Secondary accession number(s): B2RP63
    , O60837, Q16057, Q53R99, Q59ER3, Q8IX99
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 157 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3