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Q62261

- SPTB2_MOUSE

UniProt

Q62261 - SPTB2_MOUSE

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Protein

Spectrin beta chain, non-erythrocytic 1

Gene
Sptbn1, Elf, Spnb-2, Spnb2, Sptb2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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. CytoplasmmyofibrilsarcomereM line
Note: Colocalizes with ANK2 in a distinct intracellular compartment of neonatal cardiomyocytes.1 Publication
Isoform 2 : Cell membrane; Peripheral membrane protein; Cytoplasmic side 1 Publication

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
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine By similarity
Modified residuei90 – 901N6-acetyllysine By similarity
Modified residuei817 – 8171Phosphoserine By similarity
Modified residuei1057 – 10571Phosphoserine By similarity
Modified residuei1447 – 14471Phosphoserine By similarity
Modified residuei1805 – 18051Phosphotyrosine1 Publication
Modified residuei1815 – 18151N6-acetyllysine By similarity
Modified residuei1913 – 19131N6-acetyllysine By similarity
Modified residuei1989 – 19891N6-acetyllysine By similarity
Modified residuei2102 – 21021Phosphoserine2 Publications
Modified residuei2127 – 21271Phosphoserine1 Publication
Modified residuei2137 – 21371Phosphoserine2 Publications
Modified residuei2159 – 21591Phosphoserine By similarity
Modified residuei2160 – 21601Phosphoserine By similarity
Modified residuei2163 – 21631Phosphoserine By similarity
Modified residuei2164 – 21641Phosphoserine1 Publication
Modified residuei2168 – 21681Phosphoserine1 Publication
Modified residuei2186 – 21861Phosphothreonine By similarity
Modified residuei2194 – 21941Phosphothreonine1 Publication
Modified residuei2318 – 23181Phosphoserine By similarity
Modified residuei2319 – 23191Phosphothreonine By similarity
Glycosylationi2323 – 23231O-linked (GlcNAc)1 Publication
Modified residuei2327 – 23271Phosphothreonine By similarity
Modified residuei2339 – 23391Phosphoserine By similarity
Modified residuei2340 – 23401Phosphoserine By 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 ANK2.1 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.

Miscellaneous databases

EvolutionaryTraceiQ62261.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 275274Actin-bindingAdd
BLAST
Domaini54 – 158105CH 1Add
BLAST
Domaini173 – 275103CH 2Add
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 – 2306111PHAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1563 – 2093531Interaction with ANK2 By similarityAdd
BLAST
Regioni2148 – 217629Mediates interaction with CAMSAP1 By similarityAdd
BLAST

Sequence similaritiesi

Belongs to the spectrin family.
Contains 1 PH domain.
Contains 17 spectrin repeats.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2 – 4948TTTVA…IKALA → MELQRTSSISGPLSPAYTGQ VPYNYNQLEGRFKQLQ in isoform 2. VSP_026057Add
BLAST
Alternative sequencei2140 – 2246107MAGTM…AASGI → VSYRSQTYQNYKNFNSRRTA SDHSWSGM in isoform 2. VSP_026058Add
BLAST
Alternative sequencei2247 – 2363117Missing in isoform 2. VSP_026059Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti252 – 2521D → A in BAE41221. 1 Publication
Sequence conflicti309 – 3091S → T in AAD01616. 1 Publication
Sequence conflicti368 – 3681T → A in AAD01616. 1 Publication
Sequence conflicti737 – 7371K → I in AAC42040. 1 Publication
Sequence conflicti796 – 7961Y → C in AAD01616. 1 Publication
Sequence conflicti846 – 8461Q → R in AAC42040. 1 Publication
Sequence conflicti970 – 9701W → C in AAD01616. 1 Publication
Sequence conflicti996 – 9961R → C in AAD01616. 1 Publication
Sequence conflicti1401 – 14033SQI → KPGF in AAC42040. 1 Publication
Sequence conflicti1414 – 145542SVNIL…KSTDE → QSQYSSEKGNRRRRIRWKFG RKRSRNCRPSPGSSRGRAQM R in AAC42040. 1 PublicationAdd
BLAST
Sequence conflicti1508 – 15081A → R in AAC42040. 1 Publication
Sequence conflicti1619 – 16246EKAKDE → KRPRMK in AAC42040. 1 Publication
Sequence conflicti1898 – 18981D → G in AAC42040. 1 Publication
Sequence conflicti2171 – 21711L → S in AAC42040. 1 Publication
Sequence conflicti2345 – 23462EK → AE in AAC42040. 1 Publication
Sequence conflicti2356 – 23583FSL → STV in AAC42040. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 145 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

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