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UniProtKB/Swiss-Prot entry O15020


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SPTN2_HUMAN
Primary accession number O15020
Secondary accession numbers O14872 O14873
Integrated into Swiss-Prot on November 16, 2001
Sequence was last modified on January 1, 1999 (Sequence version 2)
Annotations were last modified on    April 14, 2009 (Entry version 86)
Name and origin of the protein
Protein name Spectrin beta chain, brain 2
Synonyms Spectrin, non-erythroid beta chain 2
Beta-III spectrin
Gene name
Name: SPTBN2
Synonyms: KIAA0302
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
DOI=10.1093/dnares/4.2.141; PubMed=9205841 [NCBI, ExPASy, EBI, Israel, Japan]
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro.";
DNA Res. 4:141-150(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-34.
TISSUE=Brain;
DOI=10.1073/pnas.95.24.14158; PubMed=9826670 [NCBI, ExPASy, EBI, Israel, Japan]
Stankewich M.C., Tse W.T., Peters L.L., Ch'ng Y., John K.M., Stabach P.R., Devarajan P., Morrow J.S., Lux S.E.;
"A widely expressed betaIII spectrin associated with Golgi and cytoplasmic vesicles.";
Proc. Natl. Acad. Sci. U.S.A. 95:14158-14163(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1900-2390 (ISOFORMS 1 AND 2).
TISSUE=Brain;
Tse W.T., Peters L.L., John K.M., Lux S.E.;
"SPTBN2, a new, widely expressed beta III spectrin gene located on human chromosome 11q13 and mouse chromosome 19.";
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2171, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2359, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2171 AND SER-2359, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[7]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[8]
STRUCTURE BY NMR OF 2219-2328.
RIKEN structural genomics initiative (RSGI);
"Solution structure of pleckstrin homology domain of human beta III spectrin.";
Submitted (NOV-2004) to the PDB data bank.
[9]
STRUCTURE BY NMR OF 178-291.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the second CH domain of human spectrin beta chain, brain 2.";
Submitted (AUG-2005) to the PDB data bank.
[10]
VARIANTS SCA5 PRO-253; 532-GLU--MET-544 DEL AND 629-LEU--ARG-634 DELINS TRP.
DOI=10.1038/ng1728; PubMed=16429157 [NCBI, ExPASy, EBI, Israel, Japan]
Ikeda Y., Dick K.A., Weatherspoon M.R., Gincel D., Armbrust K.R., Dalton J.C., Stevanin G., Duerr A., Zuehlke C., Buerk K., Clark H.B., Brice A., Rothstein J.D., Schut L.J., Day J.W., Ranum L.P.W.;
"Spectrin mutations cause spinocerebellar ataxia type 5.";
Nat. Genet. 38:184-190(2006).
[11]
VARIANT [LARGE SCALE ANALYSIS] LYS-774.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB008567; BAA32700.2; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF079569; AAC80006.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF026487; AAC79502.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF026488; AAC79503.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF026488; AAC79504.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00012645; -.
IPI00218207; -.
RefSeq NP_008877.1; -.
UniGene Hs.26915
3D structure databases
PDB
1WJM; NMR; -; A=2219-2328.[ExPASy / RCSB / EBI]
1WYQ; NMR; -; A=178-291.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1WJM; -.
1WYQ; -.
SMR O15020; 2212-2333.
ModBase O15020.
Protein-protein interaction databases
IntAct O15020; 1.
PTM databases
PhosphoSite O15020; -.
Organism-specific databases
GeneCards GC11M066209; -.
H-InvDB HIX0021762; -.
HGNC HGNC:11276; SPTBN2.
GenAtlas SPTBN2.
HPA CAB009844; -.
MIM 600224; phenotype. [NCBI / EBI]
604985; gene. [NCBI / EBI]
Orphanet 98766; Ataxia, spinocerebellar, type 5.
99; Autosomal dominant cerebellar ataxia.
PharmGKB PA36105; -.
HUGE KIAA0302.
Gene expression databases
ArrayExpress O15020; -.
Bgee O15020; -.
CleanEx HS_SPTBN2; -.
GermOnline ENSG00000173898; Homo sapiens.
Ontologies
GO
GO:0008091; Cellular component: spectrin (inferred from direct assay from UniProtKB).
GO:0003779; Molecular function: actin binding (traceable author statement from ProtInc).
GO:0005200; Molecular function: structural constituent of cytoskeleton (traceable author statement from UniProtKB).
GO:0051016; Biological process: barbed-end actin filament capping (inferred from electronic annotation from UniProtKB-KW).
GO:0008219; Biological process: cell death (inferred from electronic annotation from UniProtKB-KW).
GO:0016192; Biological process: vesicle-mediated transport (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR001589; Actinin_actin-bd_CS.
IPR001715; Calponin_act_bd.
IPR011993; PH_type.
IPR001849; Pleckstrin_homology.
IPR018159; Spectrin/alpha-actinin.
IPR016343; Spectrin_bsu.
IPR001605; Spectrin_PH.
IPR002017; Spectrin_repeat.
Graphical view of domain structure.
Gene3D G3DSA:1.10.418.10; Calponin-homology; 2.
G3DSA:2.30.29.30; PH_type; 1.
Pfam PF00307; CH; 2.
PF00169; PH; 1.
PF00435; Spectrin; 17.
Pfam graphical view of domain structure.
PIRSF PIRSF002297; Spectrin_beta_subunit; 1.
PRINTS PR00683; SPECTRINPH.
SMART SM00033; CH; 2.
SM00233; PH; 1.
SM00150; SPEC; 17.
SMART graphical view of domain structure.
PROSITE PS00019; ACTININ_1; 1.
PS00020; ACTININ_2; 1.
PS50021; CH; 2.
PS50003; PH_DOMAIN; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE O15020; -.
Genome annotation databases
Ensembl ENSG00000173898; Homo sapiens. [Contig view]
GeneID 6712; -.
KEGG hsa:6712; -.
Phylogenomic databases
HOGENOM O15020; -.
HOVERGEN O15020; -.
Other
NextBio 26178; -.
SOURCE SPTBN2; Homo sapiens.
ProtoNet O15020.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Actin capping; Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton; Disease mutation; Neurodegeneration; Phosphoprotein; Polymorphism; Repeat; Spinocerebellar ataxia.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   2390  2390     Spectrin beta chain, brain 2. PRO_0000073463
DOMAIN   1    278  278     Actin-binding. 
DOMAIN   57    161  105     CH 1. 
DOMAIN   176    278  103     CH 2. 
REPEAT   305    415  111     Spectrin 1. 
REPEAT   425    529  105     Spectrin 2. 
REPEAT   531    639  109     Spectrin 3. 
REPEAT   641    745  105     Spectrin 4. 
REPEAT   747    850  104     Spectrin 5. 
REPEAT   852    956  105     Spectrin 6. 
REPEAT   958   1063  106     Spectrin 7. 
REPEAT   1065   1170  106     Spectrin 8. 
REPEAT   1172   1276  105     Spectrin 9. 
REPEAT   1278   1381  104     Spectrin 10. 
REPEAT   1383   1486  104     Spectrin 11. 
REPEAT   1488   1586  99     Spectrin 12. 
REPEAT   1588   1692  105     Spectrin 13. 
REPEAT   1694   1799  106     Spectrin 14. 
REPEAT   1801   1905  105     Spectrin 15. 
REPEAT   1907   2011  105     Spectrin 16. 
REPEAT   2013   2075  63     Spectrin 17. 
DOMAIN   2218   2328  111     PH. 
MOD_RES   2171   2171        Phosphoserine. 
MOD_RES   2199   2199        Phosphoserine (By similarity). 
MOD_RES   2354   2354        Phosphothreonine (By similarity). 
MOD_RES   2359   2359        Phosphoserine. 
VAR_SEQ   2314   2390        AEMSSWLRVVNAAIATASSASGEPEEPVVPSTTRGMTRAM TMPPVSPVGAEGPVVLRSKDGREREREKRFSFFKKNK -> VSCPSCSSLSVPFQKLPAADSPSFPVLPLFPGLVLCGKTG CVRRPHQAALPV (in isoform 2). VSP_000722
VARIANT   253    253  1     L -> P (in SCA5). VAR_026767 [3D]
VARIANT   532    544  13     Missing (in SCA5). VAR_026768
VARIANT   629    634  6     LAAARR -> W (in SCA5). VAR_026769
VARIANT   774    774  1     E -> K (in a colorectal cancer sample; somatic mutation). VAR_035458 
VARIANT   825    825  1     G -> S (in dbSNP:rs4930388 [NCBI]). VAR_026770 
VARIANT   835    835  1     E -> K (in dbSNP:rs36054877 [NCBI]). VAR_048631 
VARIANT   1034   1034  1     V -> A (in dbSNP:rs506028 [NCBI]). VAR_026771 
HELIX   180    191  12      
STRAND   193    195  3      
STRAND   205    208  4      
HELIX   209    218  10      
TURN   220    222  3      
TURN   225    227  3      
HELIX   234    246  13      
TURN   256    258  3      
STRAND   261    263  3      
HELIX   266    282  17      
STRAND   283    285  3      
STRAND   2221   2233  13      
STRAND   2244   2251  8      
STRAND   2254   2260  7      
HELIX   2261   2264  4      
TURN   2265   2267  3      
STRAND   2269   2272  4      
STRAND   2282   2285  4      
STRAND   2293   2299  7      
STRAND   2301   2303  3      
STRAND   2305   2309  5      
HELIX   2313   2328  16      
Sequence information
Length: 2390 AA [This is the length of the unprocessed precursor] Molecular weight: 271295 Da [This is the MW of the unprocessed precursor] CRC64: E8C3033DD25A674C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSSTLSPTDF DSLEIQGQYS DINNRWDLPD SDWDNDSSSA RLFERSRIKA LADEREAVQK 

        70         80         90        100        110        120 
KTFTKWVNSH LARVTCRVGD LYSDLRDGRN LLRLLEVLSG EILPKPTKGR MRIHCLENVD 

       130        140        150        160        170        180 
KALQFLKEQK VHLENMGSHD IVDGNHRLTL GLVWTIILRF QIQDISVETE DNKEKKSAKD 

       190        200        210        220        230        240 
ALLLWCQMKT AGYPNVNVHN FTTSWRDGLA FNAIVHKHRP DLLDFESLKK CNAHYNLQNA 

       250        260        270        280        290        300 
FNLAEKELGL TKLLDPEDVN VDQPDEKSII TYVATYYHYF SKMKALAVEG KRIGKVLDHA 

       310        320        330        340        350        360 
MEAERLVEKY ESLASELLQW IEQTIVTLND RQLANSLSGV QNQLQSFNSY RTVEKPPKFT 

       370        380        390        400        410        420 
EKGNLEVLLF TIQSKLRANN QKVYTPREGR LISDINKAWE RLEKAEHERE LALRTELIRQ 

       430        440        450        460        470        480 
EKLEQLAARF DRKAAMRETW LSENQRLVSQ DNFGLELAAV EAAVRKHEAI ETDIVAYSGR 

       490        500        510        520        530        540 
VQAVDAVAAE LAAERYHDIK RIAARQHNVA RLWDFLRQMV AARRERLLLN LELQKVFQDL 

       550        560        570        580        590        600 
LYLMDWMEEM KGRLQSQDLG RHLAGVEDLL QLHELVEADI AVQAERVRAV SASALRFCNP 

       610        620        630        640        650        660 
GKEYRPCDPQ LVSERVAKLE QSYEALCELA AARRARLEES RRLWRFLWEV GEAEAWVREQ 

       670        680        690        700        710        720 
QHLLASADTG RDLTGALRLL NKHTALRGEM SGRLGPLKLT LEQGQQLVAE GHPGASQASA 

       730        740        750        760        770        780 
RAAELQAQWE RLEALAEERA QRLAQAASLY QFQADANDME AWLVDALRLV SSPELGHDEF 

       790        800        810        820        830        840 
STQALARQHR ALEEEIRSHR PTLDALREQA AALPPTLSRT PEVQGRVPTL ERHYEELQAR 

       850        860        870        880        890        900 
AGERARALEA ALALYTMLSE AGACGLWVEE KEQWLNGLAL PERLEDLEVV QQRFETLEPE 

       910        920        930        940        950        960 
MNTLAAQITA VNDIAEQLLK ANPPGKDRIV NTQEQLNHRW QQFRRLADGK KAALTSALSI 

       970        980        990       1000       1010       1020 
QNYHLECTET QAWMREKTKV IESTQGLGND LAGVLALQRK LAGTERDLEA IAARVGELTR 

      1030       1040       1050       1060       1070       1080 
EANALAAGHP AQAVAINARL REVQTGWEDL RATMRRREES LGEARRLQDF LRSLDDFQAW 

      1090       1100       1110       1120       1130       1140 
LGRTQTAVAS EEGPATLPEA EALLAQHAAL RGEVERAQSE YSRLRALGEE VTRDQADPQC 

      1150       1160       1170       1180       1190       1200 
LFLRQRLEAL GTGWEELGRM WESRQGRLAQ AHGFQGFLRD ARQAEGVLSS QEYVLSHTEM 

      1210       1220       1230       1240       1250       1260 
PGTLQAADAA IKKLEDFMST MDANGERIHG LLEAGRQLVS EGNIHADKIR EKADSIERRH 

      1270       1280       1290       1300       1310       1320 
KKNQDAAQQF LGRLRDNREQ QHFLQDCHEL KLWIDEKMLT AQDVSYDEAR NLHTKWQKHQ 

      1330       1340       1350       1360       1370       1380 
AFMAELAANK DWLDKVDKEG RELTLEKPEL KALVSEKLRD LHRRWDELET TTQAKARSLF 

      1390       1400       1410       1420       1430       1440 
DANRAELFAQ SCCALESWLE SLQAQLHSDD YGKDLTSVNI LLKKQQMLEW EMAVREKEVE 

      1450       1460       1470       1480       1490       1500 
AIQAQAKALA QEDQGAGEVE RTSRAVEEKF RALCQPMRER CRRLQASREQ HQFHRDVEDE 

      1510       1520       1530       1540       1550       1560 
ILWVTERLPM ASSMEHGKDL PSVQLLMKKN QTLQKEIQGH EPRIADLRER QRALGAAAAG 

      1570       1580       1590       1600       1610       1620 
PELAELQEMW KRLGHELELR GKRLEDALRA QQFYRDAAEA EAWMGEQELH MMGQEKAKDE 

      1630       1640       1650       1660       1670       1680 
LSAQAEVKKH QVLEQALADY AQTIHQLAAS SQDMIDHEHP ESTRISIRQA QVDKLYAGLK 

      1690       1700       1710       1720       1730       1740 
ELAGERRERL QEHLRLCQLR RELDDLEQWI QEREVVAASH ELGQDYEHVT MLRDKFREFS 

      1750       1760       1770       1780       1790       1800 
RDTSTIGQER VDSANALANG LIAGGHAARA TVAEWKDSLN EAWADLLELL DTRGQVLAAA 

      1810       1820       1830       1840       1850       1860 
YELQRFLHGA RQALARVQHK QQQLPDGTGR DLNAAEALQR RHCAYEHDIQ ALSPQVQQVQ 

      1870       1880       1890       1900       1910       1920 
DDGHRLQKAY AGDKAEEIGR HMQAVAEAWA QLQGSSAARR QLLLDTTDKF RFFKAVRELM 

      1930       1940       1950       1960       1970       1980 
LWMDEVNLQM DAQERPRDVS SADLVIKNQQ GIKAEIEARA DRFSSCIDMG KELLARSHYA 

      1990       2000       2010       2020       2030       2040 
AEEISEKLSQ LQARRQETAE KWQEKMDWLQ LVLEVLVFGR DAGMAEAWLC SQEPLVRSAE 

      2050       2060       2070       2080       2090       2100 
LGCTVDEVES LIKRHEAFQK SAVAWEERFC ALEKLTALEE REKERKRKRE EEERRKQPPA 

      2110       2120       2130       2140       2150       2160 
PEPTASVPPG DLVGGQTASD TTWDGTQPRP PPSTQAPSVN GVCTDGEPSQ PLLGQQRLEH 

      2170       2180       2190       2200       2210       2220 
SSFPEGPGPG SGDEANGPRG ERQTRTRGPA PSAMPQSRST ESAHAATLPP RGPEPSAQEQ 

      2230       2240       2250       2260       2270       2280 
MEGMLCRKQE MEAFGKKAAN RSWQNVYCVL RRGSLGFYKD AKAASAGVPY HGEVPVSLAR 

      2290       2300       2310       2320       2330       2340 
AQGSVAFDYR KRKHVFKLGL QDGKEYLFQA KDEAEMSSWL RVVNAAIATA SSASGEPEEP 

      2350       2360       2370       2380       2390 
VVPSTTRGMT RAMTMPPVSP VGAEGPVVLR SKDGRERERE KRFSFFKKNK 

O15020 in FASTA format

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