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O15020 (SPTN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 2
Alternative name(s):
Beta-III spectrin
Spinocerebellar ataxia 5 protein
Gene names
Name:SPTBN2
Synonyms:KIAA0302, SCA5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2390 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probably plays an important role in neuronal membrane skeleton.

Subcellular location

Cytoplasmcytoskeleton. Cytoplasmcell cortex.

Tissue specificity

Highly expressed in brain, kidney, pancreas, and liver, and at lower levels in lung and placenta.

Involvement in disease

Spinocerebellar ataxia 5 (SCA5) [MIM:600224]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA5 is an autosomal dominant cerebellar ataxia (ADCA). It is a slowly progressive disorder with variable age at onset, ranging between 10 and 50 years.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14 Ref.16

Spinocerebellar ataxia, autosomal recessive, 14 (SCAR14) [MIM:615386]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAR14 is characterized by delayed psychomotor development, severe early onset gait ataxia, eye movement abnormalities, cerebellar atrophy on brain imaging, and intellectual disability.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.11

Sequence similarities

Belongs to the spectrin family.

Contains 2 CH (calponin-homology) domains.

Contains 1 PH domain.

Contains 17 spectrin repeats.

Sequence caution

The sequence BAA32700.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Neurodegeneration
Spinocerebellar ataxia
   DomainRepeat
   LigandActin-binding
   Molecular functionActin capping
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament capping

Inferred from electronic annotation. Source: UniProtKB-KW

adult behavior

Inferred from electronic annotation. Source: Ensembl

antigen processing and presentation of exogenous peptide antigen via MHC class II

Traceable author statement. Source: Reactome

axon guidance

Traceable author statement. Source: Reactome

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

cerebellar Purkinje cell layer morphogenesis

Inferred from electronic annotation. Source: Ensembl

multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

synapse assembly

Inferred from electronic annotation. Source: Ensembl

vesicle-mediated transport

Inferred from direct assay Ref.3. Source: UniProtKB

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 22664934. Source: UniProt

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

spectrin

Inferred from direct assay Ref.3. Source: UniProtKB

   Molecular_functionactin binding

Traceable author statement Ref.3. Source: ProtInc

phospholipid binding

Inferred from electronic annotation. Source: InterPro

structural constituent of cytoskeleton

Traceable author statement Ref.3. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O15020-1)

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: O15020-2)

The sequence of this isoform differs from the canonical sequence as follows:
     2314-2390: AEMSSWLRVV...KRFSFFKKNK → VSCPSCSSLS...RRPHQAALPV

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 23902389Spectrin beta chain, non-erythrocytic 2
PRO_0000073463

Regions

Domain2 – 278277Actin-binding
Domain57 – 161105CH 1
Domain176 – 278103CH 2
Repeat305 – 415111Spectrin 1
Repeat425 – 529105Spectrin 2
Repeat531 – 639109Spectrin 3
Repeat641 – 745105Spectrin 4
Repeat747 – 850104Spectrin 5
Repeat852 – 956105Spectrin 6
Repeat958 – 1063106Spectrin 7
Repeat1065 – 1170106Spectrin 8
Repeat1172 – 1276105Spectrin 9
Repeat1278 – 1381104Spectrin 10
Repeat1383 – 1486104Spectrin 11
Repeat1488 – 158699Spectrin 12
Repeat1588 – 1692105Spectrin 13
Repeat1694 – 1799106Spectrin 14
Repeat1801 – 1905105Spectrin 15
Repeat1907 – 2011105Spectrin 16
Repeat2013 – 207563Spectrin 17
Domain2218 – 2328111PH

Amino acid modifications

Modified residue21N-acetylserine Ref.7
Modified residue21711Phosphoserine Ref.5 Ref.6 Ref.7 Ref.9
Modified residue23591Phosphoserine Ref.6 Ref.7

Natural variations

Alternative sequence2314 – 239077AEMSS…FKKNK → VSCPSCSSLSVPFQKLPAAD SPSFPVLPLFPGLVLCGKTG CVRRPHQAALPV in isoform 2.
VSP_000722
Natural variant2531L → P in SCA5. Ref.14
VAR_026767
Natural variant4801R → W in SCA5. Ref.16
VAR_070232
Natural variant532 – 54413Missing in SCA5.
VAR_026768
Natural variant629 – 6346LAAARR → W in SCA5.
VAR_026769
Natural variant7741E → K in a colorectal cancer sample; somatic mutation. Ref.15
VAR_035458
Natural variant8251S → G. Ref.1
Corresponds to variant rs4930388 [ dbSNP | Ensembl ].
VAR_026770
Natural variant8351E → K.
Corresponds to variant rs36054877 [ dbSNP | Ensembl ].
VAR_048631
Natural variant10341V → A.
Corresponds to variant rs506028 [ dbSNP | Ensembl ].
VAR_026771

Secondary structure

......................................... 2390
Helix Strand Turn

Details...

Sequences

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

Last modified October 5, 2010. Version 3.
Checksum: 1CC523CC6493DBFE

FASTA2,390271,325
        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 PEVQSRVPTL 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 

« Hide

Isoform 2 [UniParc].

Checksum: 3C60F49E525BEC79
Show »

FASTA2,365268,309

References

« Hide 'large scale' references
[1]"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."
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLY-825.
Tissue: Brain.
[2]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"A widely expressed betaIII spectrin associated with Golgi and cytoplasmic vesicles."
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.
Proc. Natl. Acad. Sci. U.S.A. 95:14158-14163(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-34.
Tissue: Brain.
[4]"SPTBN2, a new, widely expressed beta III spectrin gene located on human chromosome 11q13 and mouse chromosome 19."
Tse W.T., Peters L.L., John K.M., Lux S.E.
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1900-2390 (ISOFORMS 1 AND 2).
Tissue: Brain.
[5]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2171, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2171 AND SER-2359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2171 AND SER-2359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2171, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Recessive mutations in SPTBN2 implicate beta-III spectrin in both cognitive and motor development."
Lise S., Clarkson Y., Perkins E., Kwasniewska A., Sadighi Akha E., Schnekenberg R.P., Suminaite D., Hope J., Baker I., Gregory L., Green A., Allan C., Lamble S., Jayawant S., Quaghebeur G., Cader M.Z., Hughes S., Armstrong R.J. expand/collapse author list , Kanapin A., Rimmer A., Lunter G., Mathieson I., Cazier J.B., Buck D., Taylor J.C., Bentley D., McVean G., Donnelly P., Knight S.J., Jackson M., Ragoussis J., Nemeth A.H.
PLoS Genet. 8:E1003074-E1003074(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SCAR14.
[11]"Autosomal dominant SCA5 and autosomal recessive infantile SCA are allelic conditions resulting from SPTBN2 mutations."
Elsayed S.M., Heller R., Thoenes M., Zaki M.S., Swan D., Elsobky E., Zuehlke C., Ebermann I., Nuernberg G., Nuernberg P., Bolz H.J.
Eur. J. Hum. Genet. 22:286-288(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SCAR14.
[12]"Solution structure of pleckstrin homology domain of human beta III spectrin."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2004) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 2219-2328.
[13]"Solution structure of the second CH domain of human spectrin beta chain, brain 2."
RIKEN structural genomics initiative (RSGI)
Submitted (AUG-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 178-291.
[14]"Spectrin mutations cause spinocerebellar ataxia type 5."
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.
Nat. Genet. 38:184-190(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SCA5 PRO-253; 532-GLU--MET-544 DEL AND 629-LEU--ARG-634 DELINS TRP.
[15]"The consensus coding sequences of human breast and colorectal cancers."
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. expand/collapse author list , 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.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-774.
[16]"Case of infantile onset spinocerebellar ataxia type 5."
Jacob F.D., Ho E.S., Martinez-Ojeda M., Darras B.T., Khwaja O.S.
J. Child Neurol. 28:1292-1295(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SCA5 TRP-480.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB008567 mRNA. Translation: BAA32700.2. Different initiation.
AP001157 Genomic DNA. No translation available.
AF079569 mRNA. Translation: AAC80006.1.
AF026487 mRNA. Translation: AAC79502.1.
AF026488 mRNA. Translation: AAC79503.1.
AF026488 mRNA. Translation: AAC79504.1.
CCDSCCDS8150.1. [O15020-1]
RefSeqNP_008877.1. NM_006946.2.
XP_005274249.1. XM_005274192.2. [O15020-1]
XP_005274250.1. XM_005274193.2. [O15020-1]
XP_006718733.1. XM_006718670.1. [O15020-1]
XP_006718734.1. XM_006718671.1. [O15020-1]
UniGeneHs.26915.
Hs.586709.
Hs.679104.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WJMNMR-A2219-2328[»]
1WYQNMR-A178-291[»]
ProteinModelPortalO15020.
SMRO15020. Positions 51-291, 302-2084, 2212-2333.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112590. 10 interactions.
DIPDIP-47270N.
IntActO15020. 6 interactions.
STRING9606.ENSP00000311489.

PTM databases

PhosphoSiteO15020.

Proteomic databases

MaxQBO15020.
PaxDbO15020.
PRIDEO15020.

Protocols and materials databases

DNASU6712.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309996; ENSP00000311489; ENSG00000173898. [O15020-1]
ENST00000529997; ENSP00000433593; ENSG00000173898. [O15020-2]
ENST00000533211; ENSP00000432568; ENSG00000173898. [O15020-1]
GeneID6712.
KEGGhsa:6712.
UCSCuc001ojd.3. human. [O15020-1]

Organism-specific databases

CTD6712.
GeneCardsGC11M066453.
HGNCHGNC:11276. SPTBN2.
HPACAB009844.
MIM600224. phenotype.
604985. gene.
615386. phenotype.
neXtProtNX_O15020.
Orphanet352403. Spectrin-associated autosomal recessive cerebellar ataxia.
98766. Spinocerebellar ataxia type 5.
PharmGKBPA36105.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5069.
HOGENOMHOG000007281.
HOVERGENHBG057912.
InParanoidO15020.
KOK06115.
OMAIQGQYSD.
OrthoDBEOG73RB9J.
PhylomeDBO15020.
TreeFamTF313446.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_188576. Developmental Biology.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressO15020.
BgeeO15020.
CleanExHS_SPTBN2.
GenevestigatorO15020.

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]
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

ChiTaRSSPTBN2. human.
EvolutionaryTraceO15020.
GeneWikiSPTBN2.
GenomeRNAi6712.
NextBio26178.
PROO15020.
SOURCESearch...

Entry information

Entry nameSPTN2_HUMAN
AccessionPrimary (citable) accession number: O15020
Secondary accession number(s): O14872, O14873
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: October 5, 2010
Last modified: July 9, 2014
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM