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Q62261 (SPTB2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Spectrin beta chain, non-erythrocytic 1
Alternative name(s):
Beta-II spectrin
Embryonic liver fodrin
Fodrin beta chain
Gene names
Name:Sptbn1
Synonyms:Elf, Spnb-2, Spnb2, Sptb2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2363 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.5

Subcellular location

Cytoplasmcytoskeleton. CytoplasmmyofibrilsarcomereM line. Note: Colocalizes with ANK2 in a distinct intracellular compartment of neonatal cardiomyocytes. Ref.2

Isoform 2: Cell membrane; Peripheral membrane protein; Cytoplasmic side Ref.2.

Tissue specificity

Isoform 2 is present in brain, heart, kidney and liver (at protein level). Ref.2 Ref.5

Developmental stage

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

Post-translational modification

Isoform 2 is phosphorylated on Ser-8 and Ser-10.

Sequence similarities

Belongs to the spectrin family.

Contains 2 CH (calponin-homology) domains.

Contains 1 PH domain.

Contains 17 spectrin repeats.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandActin-binding
Calmodulin-binding
   Molecular functionActin capping
   PTMAcetylation
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi to plasma membrane protein transport

Inferred from electronic annotation. Source: Ensembl

SMAD protein import into nucleus

Inferred from direct assay PubMed 12543979. Source: MGI

actin filament capping

Inferred from electronic annotation. Source: UniProtKB-KW

common-partner SMAD protein phosphorylation

Inferred from direct assay PubMed 12543979. Source: MGI

membrane assembly

Inferred from electronic annotation. Source: Ensembl

mitotic cytokinesis

Inferred from electronic annotation. Source: Ensembl

protein targeting to plasma membrane

Inferred from mutant phenotype PubMed 17620337. Source: BHF-UCL

   Cellular_componentM band

Inferred from direct assay Ref.5. Source: BHF-UCL

axolemma

Inferred from direct assay PubMed 21966409. Source: BHF-UCL

cortical cytoskeleton

Inferred from direct assay PubMed 18723693. Source: MGI

cuticular plate

Inferred from direct assay PubMed 18796539. Source: MGI

membrane

Inferred from direct assay PubMed 18723693. Source: MGI

nucleolus

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 12543979. Source: MGI

plasma membrane

Inferred from direct assay PubMed 12543979. Source: MGI

protein complex

Inferred from electronic annotation. Source: Ensembl

spectrin

Inferred from electronic annotation. Source: InterPro

   Molecular_functionphospholipid binding

Inferred from electronic annotation. Source: InterPro

structural constituent of cytoskeleton

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q62261-1)

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.
Isoform 2 (identifier: Q62261-2)

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).

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 23632362Spectrin beta chain, non-erythrocytic 1
PRO_0000073462

Regions

Domain2 – 275274Actin-binding
Domain54 – 158105CH 1
Domain173 – 275103CH 2
Repeat303 – 411109Spectrin 1
Repeat423 – 525103Spectrin 2
Repeat530 – 636107Spectrin 3
Repeat639 – 742104Spectrin 4
Repeat745 – 847103Spectrin 5
Repeat851 – 952102Spectrin 6
Repeat957 – 1060104Spectrin 7
Repeat1063 – 1166104Spectrin 8
Repeat1169 – 125789Spectrin 9
Repeat1276 – 1376101Spectrin 10
Repeat1381 – 1482102Spectrin 11
Repeat1486 – 1590105Spectrin 12
Repeat1592 – 1696105Spectrin 13
Repeat1698 – 1801104Spectrin 14
Repeat1805 – 1907103Spectrin 15
Repeat1914 – 2014101Spectrin 16
Repeat2018 – 209780Spectrin 17
Domain2196 – 2306111PH
Region1563 – 2093531Interaction with ANK2 By similarity
Region2148 – 217629Mediates interaction with CAMSAP1 By similarity

Amino acid modifications

Modified residue21N-acetylthreonine By similarity
Modified residue901N6-acetyllysine By similarity
Modified residue8171Phosphoserine By similarity
Modified residue10571Phosphoserine By similarity
Modified residue14471Phosphoserine By similarity
Modified residue18051Phosphotyrosine Ref.11
Modified residue18151N6-acetyllysine By similarity
Modified residue19131N6-acetyllysine By similarity
Modified residue19891N6-acetyllysine By similarity
Modified residue21021Phosphoserine Ref.7 Ref.12
Modified residue21271Phosphoserine Ref.6
Modified residue21371Phosphoserine Ref.6 Ref.10
Modified residue21591Phosphoserine By similarity
Modified residue21601Phosphoserine By similarity
Modified residue21631Phosphoserine By similarity
Modified residue21641Phosphoserine Ref.13
Modified residue21681Phosphoserine Ref.13
Modified residue21861Phosphothreonine By similarity
Modified residue21941Phosphothreonine Ref.7
Modified residue23181Phosphoserine By similarity
Modified residue23191Phosphothreonine By similarity
Modified residue23271Phosphothreonine By similarity
Modified residue23391Phosphoserine By similarity
Modified residue23401Phosphoserine By similarity
Glycosylation23231O-linked (GlcNAc) Ref.8

Natural variations

Alternative sequence2 – 4948TTTVA…IKALA → MELQRTSSISGPLSPAYTGQ VPYNYNQLEGRFKQLQ in isoform 2.
VSP_026057
Alternative sequence2140 – 2246107MAGTM…AASGI → VSYRSQTYQNYKNFNSRRTA SDHSWSGM in isoform 2.
VSP_026058
Alternative sequence2247 – 2363117Missing in isoform 2.
VSP_026059

Experimental info

Sequence conflict2521D → A in BAE41221. Ref.4
Sequence conflict3091S → T in AAD01616. Ref.2
Sequence conflict3681T → A in AAD01616. Ref.2
Sequence conflict7371K → I in AAC42040. Ref.1
Sequence conflict7961Y → C in AAD01616. Ref.2
Sequence conflict8461Q → R in AAC42040. Ref.1
Sequence conflict9701W → C in AAD01616. Ref.2
Sequence conflict9961R → C in AAD01616. Ref.2
Sequence conflict1401 – 14033SQI → KPGF in AAC42040. Ref.1
Sequence conflict1414 – 145542SVNIL…KSTDE → QSQYSSEKGNRRRRIRWKFG RKRSRNCRPSPGSSRGRAQM R in AAC42040. Ref.1
Sequence conflict15081A → R in AAC42040. Ref.1
Sequence conflict1619 – 16246EKAKDE → KRPRMK in AAC42040. Ref.1
Sequence conflict18981D → G in AAC42040. Ref.1
Sequence conflict21711L → S in AAC42040. Ref.1
Sequence conflict2345 – 23462EK → AE in AAC42040. Ref.1
Sequence conflict2356 – 23583FSL → STV in AAC42040. Ref.1

Secondary structure

...................... 2363
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 16, 2006. Version 2.
Checksum: 221362054E64BB8C

FASTA2,363274,223
        10         20         30         40         50         60 
MTTTVATDYD NIEIQQQYSD VNNRWDVDDW DNENSSARLF ERSRIKALAD EREAVQKKTF 

        70         80         90        100        110        120 
TKWVNSHLAR VSCRITDLYT DLRDGRMLIK LLEVLSGERL PKPTKGRMRI HCLENVDKAL 

       130        140        150        160        170        180 
QFLKEQRVHL ENMGSHDIVD GNHRLTLGLI WTIILRFQIQ DISVETEDNK EKKSAKDALL 

       190        200        210        220        230        240 
LWCQMKTAGY PNVNIHNFTT SWRDGMAFNA LIHKHRPDLI DFDKLKKSNA HYNLQNAFNL 

       250        260        270        280        290        300 
AEQHLGLTKL LDPEDISVDH PDEKSIITYV VTYYHYFSKM KALAVEGKRI GKVLDNAIET 

       310        320        330        340        350        360 
EKMIEKYESL ASDLLEWIEQ TIIILNNRKF ANSLVGVQQQ LQAFNTYRTV EKPPKFTEKG 

       370        380        390        400        410        420 
NLEVLLFTIQ SKMRANNQKV YMPREGKLIS DINKAWERLE KAEHERELAL RNELIRQEKL 

       430        440        450        460        470        480 
EQLARRFDRK AAMRETWLSE NQRLVSQDNF GFDLPAVEAA TKKHEAIETD IAAYEERVQA 

       490        500        510        520        530        540 
VVAVARELEA ENYHDIKRIT ARKDNVIRLW EYLLELLRAR RQRLEMNLGL QKIFQEMLYI 

       550        560        570        580        590        600 
MDWMDEMKVL LLSQDYGKHL LGVEDLLQKH ALVEADIAIQ AERVRGVNAS AQKFATDGEG 

       610        620        630        640        650        660 
YKPCDPQVIR DRVAHMEFCY QELCQLAAER RARLEESRRL WKFFWEMAEE EGWIREKEKI 

       670        680        690        700        710        720 
LSSDDYGKDL TSVMRLLSKH RAFEDEMSGR SGHFEQAIKE GEDMIAEEHF GSEKIRERII 

       730        740        750        760        770        780 
YIREQWANLE QLSAIRKKRL EEASLLHQFQ ADADDIDAWM LDILKIVSSN DVGHDEYSTQ 

       790        800        810        820        830        840 
SLVKKHKDVA EEITNYRPTI DTLHEQASAL PQAHAESPDV KGRLAGIEER CKEMAELTRL 

       850        860        870        880        890        900 
RKQALQDTLA LYKMFSEADA CELWIDEKEQ WLNNMQIPEK LEDLEVIQHR FESLEPEMNN 

       910        920        930        940        950        960 
QASRVAVVNQ IARQLMHNGH PSEKEIRAQQ DKLNTRWSQF RELVDRKKDA LLSALSIQNY 

       970        980        990       1000       1010       1020 
HLECNETKSW IREKTKVIES TQDLGNDLAG VMALQRKLTG MERDLVAIEA KLSDLQKEAE 

      1030       1040       1050       1060       1070       1080 
KLESEHPDQA QAILSRLAEI SDVWEEMKTT LKNREASLGE ASKLQQFLRD LDDFQSWLSR 

      1090       1100       1110       1120       1130       1140 
TQTAIASEDM PNTLTEAEKL LTQHENIKNE IDNYEEDYQK MRDMGEMVTQ GQTDAQYMFL 

      1150       1160       1170       1180       1190       1200 
RQRLQALDTG WNELHKMWEN RQNLLSQSHA YQQFLRDTKQ AEAFLNNQEY VLAHTEMPTT 

      1210       1220       1230       1240       1250       1260 
LEGAEAAIKK QEDFMTTMDA NEEKINAVVE TGRRLVSDGN INSDRIQEKV DSIDDRHRKN 

      1270       1280       1290       1300       1310       1320 
REAASELLMR LKDNRDLQKF LQDCQELSLW INEKMLTAQD MSYDEARNLH SKWLKHQAFM 

      1330       1340       1350       1360       1370       1380 
AELASNKEWL DKIEKEGMQL ISEKPETEAV VKEKLTGLHK MWEVLESTTQ TKAQRLFDAN 

      1390       1400       1410       1420       1430       1440 
KAELFTQSCA DLDKWLHGLE SQIQSDDYGK DLTSVNILLK KQQMLENQME VRKKEIEELQ 

      1450       1460       1470       1480       1490       1500 
SQAQALSQEG KSTDEVDSKR LTVQTKFMEL LEPLSERKHN LLASKEIHQF NRDVEDEILW 

      1510       1520       1530       1540       1550       1560 
VGERMPLATS TDHGHNLQTV QLLIKKNQTL QKEIQGHQPR IDDIFERSQN IITDSSSLNA 

      1570       1580       1590       1600       1610       1620 
EAIRQRLADL KQLWGLLIEE TEKRHRRLEE AHKAQQYYFD AAEAEAWMSE QELYMMSEEK 

      1630       1640       1650       1660       1670       1680 
AKDEQSAVSM LKKHQILEQA VEDYAETVHQ LSKTSRALVA DSHPESERIS MRQSKVDKLY 

      1690       1700       1710       1720       1730       1740 
AGLKDLAEER RGKLDERHRL FQLNREVDDL EQWIAEREVV AGSHELGQDY EHVTMLQERF 

      1750       1760       1770       1780       1790       1800 
REFARDTGNI GQERVDTVNN MADELINSGH SDAATIAEWK DGLNEAWADL LELIDTRTQI 

      1810       1820       1830       1840       1850       1860 
LAASYELHKF YHDAKEIFGR IQDKHKKLPE ELGRDQNTVE TLQRMHTTFE HDIQALGTQV 

      1870       1880       1890       1900       1910       1920 
RQLQEDAARL QAAYAGDKAD DIQKRENEVL EAWKSLLDAC EGRRVRLVDT GDKFRFFSMV 

      1930       1940       1950       1960       1970       1980 
RDLMLWMEDV IRQIEAQEKP RDVSSVELLM NNHQGIKAEI DARNDSFTAC IELGKSLLAR 

      1990       2000       2010       2020       2030       2040 
KHYASEEIKE KLLQLTEKRK EMIDKWEDRW EWLRLILEVH QFSRDASVAE AWLLGQEPYL 

      2050       2060       2070       2080       2090       2100 
SSREIGQSVD EVEKLIKRHE AFEKSAATWD ERFSALERLT TLELLEVRRQ QEEEERKRRP 

      2110       2120       2130       2140       2150       2160 
PSPDPNTKVS EEAESQQWDT SKGDQVSQNG LPAEQGSPRM AGTMETSEMV NGAAEQRTSS 

      2170       2180       2190       2200       2210       2220 
KESSPVPSPT LDRKAKSALP AQSAATLPAR TLETPAAQME GFLNRKHEWE AHNKKASSRS 

      2230       2240       2250       2260       2270       2280 
WHNVYCVINN QEMGFYKDAK SAASGIPYHS EVPVSLKEAI CEVALDYKKK KHVFKLRLSD 

      2290       2300       2310       2320       2330       2340 
GNEYLFQAKD DEEMNTWIQA ISSAISSDKH DTSASTQSTP ASSRAQTLPT SVVTITSESS 

      2350       2360 
PGKREKDKEK DKEKRFSLFG KKK 

« Hide

Isoform 2 (Elf3) [UniParc].

Checksum: 4C28E2F4B311D9CD
Show »

FASTA2,155251,288

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_033286.2. NM_009260.2.
NP_787030.2. NM_175836.2.
XP_006514662.1. XM_006514599.1.
XP_006514663.1. XM_006514600.1.
UniGeneMm.123110.
Mm.466085.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BTNX-ray2.00A2199-2304[»]
1MPHNMR-A2199-2304[»]
ProteinModelPortalQ62261.
SMRQ62261. Positions 173-280, 1697-2086, 2199-2304.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203461. 8 interactions.
DIPDIP-31558N.
IntActQ62261. 12 interactions.
MINTMINT-4135469.

PTM databases

PhosphoSiteQ62261.

Proteomic databases

PaxDbQ62261.
PRIDEQ62261.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000006629; ENSMUSP00000006629; ENSMUSG00000020315. [Q62261-1]
ENSMUST00000011877; ENSMUSP00000011877; ENSMUSG00000020315. [Q62261-1]
GeneID20742.
KEGGmmu:20742.
UCSCuc007ihs.1. mouse. [Q62261-1]
uc007iht.1. mouse. [Q62261-2]

Organism-specific databases

CTD6711.
MGIMGI:98388. Sptbn1.

Phylogenomic databases

eggNOGCOG5069.
GeneTreeENSGT00700000104022.
HOGENOMHOG000007281.
HOVERGENHBG057912.
InParanoidQ62261.
KOK06115.
OMALWQFYWD.
OrthoDBEOG73RB9J.
PhylomeDBQ62261.
TreeFamTF313446.

Gene expression databases

ArrayExpressQ62261.
BgeeQ62261.
CleanExMM_SPNB2.
GenevestigatorQ62261.

Family and domain databases

Gene3D1.10.418.10. 2 hits.
2.30.29.30. 1 hit.
InterProIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR001605. PH_dom-spectrin-type.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR018159. Spectrin/alpha-actinin.
IPR016343. Spectrin_bsu.
IPR002017. Spectrin_repeat.
[Graphical view]
PANTHERPTHR11915:SF188. PTHR11915:SF188. 1 hit.
PfamPF00307. CH. 2 hits.
PF00435. Spectrin. 17 hits.
[Graphical view]
PIRSFPIRSF002297. Spectrin_beta_subunit. 1 hit.
PRINTSPR00683. SPECTRINPH.
SMARTSM00033. CH. 2 hits.
SM00233. PH. 1 hit.
SM00150. SPEC. 17 hits.
[Graphical view]
SUPFAMSSF47576. SSF47576. 1 hit.
PROSITEPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ62261.
NextBio299385.
PROQ62261.
SOURCESearch...

Entry information

Entry nameSPTB2_MOUSE
AccessionPrimary (citable) accession number: Q62261
Secondary accession number(s): A2AFU1 expand/collapse secondary AC list , Q3TEM7, Q5SQL8, Q5SQL9, Q9QWJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 16, 2006
Last modified: April 16, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot