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Q62261

- SPTB2_MOUSE

UniProt

Q62261 - SPTB2_MOUSE

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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

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. structural constituent of cytoskeleton Source: InterPro

GO - Biological processi

  1. actin filament capping Source: UniProtKB-KW
  2. common-partner SMAD protein phosphorylation Source: MGI
  3. protein targeting to plasma membrane Source: BHF-UCL
  4. SMAD protein import into nucleus Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding, Calmodulin-binding

Enzyme and pathway databases

ReactomeiREACT_237796. NCAM signaling for neurite out-growth.
REACT_244931. Interaction between L1 and Ankyrins.
REACT_257032. Nephrin interactions.

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. nucleus Source: MGI
  7. plasma membrane Source: MGI
  8. 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 – 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

BgeeiQ62261.
CleanExiMM_SPNB2.
ExpressionAtlasiQ62261. baseline and differential.
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 – 220910Combined sources
Beta strandi2211 – 22133Combined sources
Beta strandi2222 – 22298Combined sources
Beta strandi2232 – 22387Combined sources
Helixi2239 – 22446Combined sources
Beta strandi2248 – 22503Combined sources
Beta strandi2253 – 22553Combined sources
Beta strandi2260 – 22634Combined sources
Beta strandi2269 – 22779Combined sources
Beta strandi2283 – 22875Combined sources
Helixi2291 – 230313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118813.
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

        10         20         30         40         50
MTTTVATDYD NIEIQQQYSD VNNRWDVDDW DNENSSARLF ERSRIKALAD
60 70 80 90 100
EREAVQKKTF TKWVNSHLAR VSCRITDLYT DLRDGRMLIK LLEVLSGERL
110 120 130 140 150
PKPTKGRMRI HCLENVDKAL QFLKEQRVHL ENMGSHDIVD GNHRLTLGLI
160 170 180 190 200
WTIILRFQIQ DISVETEDNK EKKSAKDALL LWCQMKTAGY PNVNIHNFTT
210 220 230 240 250
SWRDGMAFNA LIHKHRPDLI DFDKLKKSNA HYNLQNAFNL AEQHLGLTKL
260 270 280 290 300
LDPEDISVDH PDEKSIITYV VTYYHYFSKM KALAVEGKRI GKVLDNAIET
310 320 330 340 350
EKMIEKYESL ASDLLEWIEQ TIIILNNRKF ANSLVGVQQQ LQAFNTYRTV
360 370 380 390 400
EKPPKFTEKG NLEVLLFTIQ SKMRANNQKV YMPREGKLIS DINKAWERLE
410 420 430 440 450
KAEHERELAL RNELIRQEKL EQLARRFDRK AAMRETWLSE NQRLVSQDNF
460 470 480 490 500
GFDLPAVEAA TKKHEAIETD IAAYEERVQA VVAVARELEA ENYHDIKRIT
510 520 530 540 550
ARKDNVIRLW EYLLELLRAR RQRLEMNLGL QKIFQEMLYI MDWMDEMKVL
560 570 580 590 600
LLSQDYGKHL LGVEDLLQKH ALVEADIAIQ AERVRGVNAS AQKFATDGEG
610 620 630 640 650
YKPCDPQVIR DRVAHMEFCY QELCQLAAER RARLEESRRL WKFFWEMAEE
660 670 680 690 700
EGWIREKEKI LSSDDYGKDL TSVMRLLSKH RAFEDEMSGR SGHFEQAIKE
710 720 730 740 750
GEDMIAEEHF GSEKIRERII YIREQWANLE QLSAIRKKRL EEASLLHQFQ
760 770 780 790 800
ADADDIDAWM LDILKIVSSN DVGHDEYSTQ SLVKKHKDVA EEITNYRPTI
810 820 830 840 850
DTLHEQASAL PQAHAESPDV KGRLAGIEER CKEMAELTRL RKQALQDTLA
860 870 880 890 900
LYKMFSEADA CELWIDEKEQ WLNNMQIPEK LEDLEVIQHR FESLEPEMNN
910 920 930 940 950
QASRVAVVNQ IARQLMHNGH PSEKEIRAQQ DKLNTRWSQF RELVDRKKDA
960 970 980 990 1000
LLSALSIQNY HLECNETKSW IREKTKVIES TQDLGNDLAG VMALQRKLTG
1010 1020 1030 1040 1050
MERDLVAIEA KLSDLQKEAE KLESEHPDQA QAILSRLAEI SDVWEEMKTT
1060 1070 1080 1090 1100
LKNREASLGE ASKLQQFLRD LDDFQSWLSR TQTAIASEDM PNTLTEAEKL
1110 1120 1130 1140 1150
LTQHENIKNE IDNYEEDYQK MRDMGEMVTQ GQTDAQYMFL RQRLQALDTG
1160 1170 1180 1190 1200
WNELHKMWEN RQNLLSQSHA YQQFLRDTKQ AEAFLNNQEY VLAHTEMPTT
1210 1220 1230 1240 1250
LEGAEAAIKK QEDFMTTMDA NEEKINAVVE TGRRLVSDGN INSDRIQEKV
1260 1270 1280 1290 1300
DSIDDRHRKN REAASELLMR LKDNRDLQKF LQDCQELSLW INEKMLTAQD
1310 1320 1330 1340 1350
MSYDEARNLH SKWLKHQAFM AELASNKEWL DKIEKEGMQL ISEKPETEAV
1360 1370 1380 1390 1400
VKEKLTGLHK MWEVLESTTQ TKAQRLFDAN KAELFTQSCA DLDKWLHGLE
1410 1420 1430 1440 1450
SQIQSDDYGK DLTSVNILLK KQQMLENQME VRKKEIEELQ SQAQALSQEG
1460 1470 1480 1490 1500
KSTDEVDSKR LTVQTKFMEL LEPLSERKHN LLASKEIHQF NRDVEDEILW
1510 1520 1530 1540 1550
VGERMPLATS TDHGHNLQTV QLLIKKNQTL QKEIQGHQPR IDDIFERSQN
1560 1570 1580 1590 1600
IITDSSSLNA EAIRQRLADL KQLWGLLIEE TEKRHRRLEE AHKAQQYYFD
1610 1620 1630 1640 1650
AAEAEAWMSE QELYMMSEEK AKDEQSAVSM LKKHQILEQA VEDYAETVHQ
1660 1670 1680 1690 1700
LSKTSRALVA DSHPESERIS MRQSKVDKLY AGLKDLAEER RGKLDERHRL
1710 1720 1730 1740 1750
FQLNREVDDL EQWIAEREVV AGSHELGQDY EHVTMLQERF REFARDTGNI
1760 1770 1780 1790 1800
GQERVDTVNN MADELINSGH SDAATIAEWK DGLNEAWADL LELIDTRTQI
1810 1820 1830 1840 1850
LAASYELHKF YHDAKEIFGR IQDKHKKLPE ELGRDQNTVE TLQRMHTTFE
1860 1870 1880 1890 1900
HDIQALGTQV RQLQEDAARL QAAYAGDKAD DIQKRENEVL EAWKSLLDAC
1910 1920 1930 1940 1950
EGRRVRLVDT GDKFRFFSMV RDLMLWMEDV IRQIEAQEKP RDVSSVELLM
1960 1970 1980 1990 2000
NNHQGIKAEI DARNDSFTAC IELGKSLLAR KHYASEEIKE KLLQLTEKRK
2010 2020 2030 2040 2050
EMIDKWEDRW EWLRLILEVH QFSRDASVAE AWLLGQEPYL SSREIGQSVD
2060 2070 2080 2090 2100
EVEKLIKRHE AFEKSAATWD ERFSALERLT TLELLEVRRQ QEEEERKRRP
2110 2120 2130 2140 2150
PSPDPNTKVS EEAESQQWDT SKGDQVSQNG LPAEQGSPRM AGTMETSEMV
2160 2170 2180 2190 2200
NGAAEQRTSS KESSPVPSPT LDRKAKSALP AQSAATLPAR TLETPAAQME
2210 2220 2230 2240 2250
GFLNRKHEWE AHNKKASSRS WHNVYCVINN QEMGFYKDAK SAASGIPYHS
2260 2270 2280 2290 2300
EVPVSLKEAI CEVALDYKKK KHVFKLRLSD GNEYLFQAKD DEEMNTWIQA
2310 2320 2330 2340 2350
ISSAISSDKH DTSASTQSTP ASSRAQTLPT SVVTITSESS PGKREKDKEK
2360
DKEKRFSLFG KKK
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:
     1-49: MTTTVATDYD...FERSRIKALA → MELQRTSSIS...QLEGRFKQLQ
     2140-2246: MAGTMETSEM...KDAKSAASGI → VSYRSQTYQNYKNFNSRRTASDHSWSGM
     2247-2363: Missing.

Note: Contains a phosphoserine at position 14.By similarity

Show »
Length:2,154
Mass (Da):251,156
Checksum:i5128A840C3FD28AC
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 sequencei1 – 4949MTTTV…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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 ENSGT00760000118813.
HOGENOMi HOG000007281.
HOVERGENi HBG057912.
InParanoidi Q62261.
KOi K06115.
OMAi LWQFYWD.
OrthoDBi EOG73RB9J.
PhylomeDBi Q62261.
TreeFami TF313446.

Enzyme and pathway databases

Reactomei REACT_237796. NCAM signaling for neurite out-growth.
REACT_244931. Interaction between L1 and Ankyrins.
REACT_257032. Nephrin interactions.

Miscellaneous databases

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

Gene expression databases

Bgeei Q62261.
CleanExi MM_SPNB2.
ExpressionAtlasi Q62261. baseline and differential.
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: November 26, 2014
This is version 148 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