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Protein

Spectrin beta chain, non-erythrocytic 2

Gene

SPTBN2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probably plays an important role in neuronal membrane skeleton.

GO - Molecular functioni

  • actin binding Source: ProtInc
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • phospholipid binding Source: InterPro
  • Ras guanyl-nucleotide exchange factor activity Source: Reactome
  • structural constituent of cytoskeleton Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000173898-MONOMER.
ReactomeiR-HSA-2132295. MHC class II antigen presentation.
R-HSA-375165. NCAM signaling for neurite out-growth.
R-HSA-445095. Interaction between L1 and Ankyrins.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-6807878. COPI-mediated anterograde transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Spectrin beta chain, non-erythrocytic 2
Alternative name(s):
Beta-III spectrin
Spinocerebellar ataxia 5 protein
Gene namesi
Name:SPTBN2
Synonyms:KIAA0302, SCA5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:11276. SPTBN2.

Subcellular locationi

GO - Cellular componenti

  • apical plasma membrane Source: Ensembl
  • cell-cell adherens junction Source: BHF-UCL
  • cell junction Source: HPA
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • extracellular space Source: UniProtKB
  • neuronal cell body Source: Ensembl
  • spectrin Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Spinocerebellar ataxia 5 (SCA5)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionSpinocerebellar 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.
See also OMIM:600224
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_026767253L → P in SCA5. 1 PublicationCorresponds to variant rs121918306dbSNPEnsembl.1
Natural variantiVAR_070232480R → W in SCA5. 1 PublicationCorresponds to variant rs397514749dbSNPEnsembl.1
Natural variantiVAR_026768532 – 544Missing in SCA5. 1 PublicationAdd BLAST13
Natural variantiVAR_026769629 – 634LAAARR → W in SCA5. 1 Publication6
Spinocerebellar ataxia, autosomal recessive, 14 (SCAR14)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionSpinocerebellar 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.
See also OMIM:615386

Keywords - Diseasei

Disease mutation, Neurodegeneration, Spinocerebellar ataxia

Organism-specific databases

DisGeNETi6712.
MalaCardsiSPTBN2.
MIMi600224. phenotype.
615386. phenotype.
OpenTargetsiENSG00000173898.
Orphaneti352403. Spectrin-associated autosomal recessive cerebellar ataxia.
98766. Spinocerebellar ataxia type 5.
PharmGKBiPA36105.

Polymorphism and mutation databases

BioMutaiSPTBN2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000734632 – 2390Spectrin beta chain, non-erythrocytic 2Add BLAST2389

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei6PhosphoserineBy similarity1
Modified residuei31PhosphoserineCombined sources1
Modified residuei959PhosphoserineCombined sources1
Modified residuei1073PhosphoserineCombined sources1
Modified residuei2171PhosphoserineCombined sources1
Modified residuei2199PhosphoserineBy similarity1
Modified residuei2354PhosphothreonineCombined sources1
Modified residuei2359PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO15020.
MaxQBiO15020.
PaxDbiO15020.
PeptideAtlasiO15020.
PRIDEiO15020.

PTM databases

iPTMnetiO15020.
PhosphoSitePlusiO15020.
SwissPalmiO15020.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000173898.
CleanExiHS_SPTBN2.
ExpressionAtlasiO15020. baseline and differential.
GenevisibleiO15020. HS.

Organism-specific databases

HPAiCAB009844.
HPA039293.
HPA043529.

Interactioni

GO - Molecular functioni

  • actin binding Source: ProtInc
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL

Protein-protein interaction databases

BioGridi112590. 32 interactors.
DIPiDIP-47270N.
IntActiO15020. 27 interactors.
STRINGi9606.ENSP00000311489.

Structurei

Secondary structure

12390
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi180 – 191Combined sources12
Beta strandi193 – 195Combined sources3
Beta strandi205 – 208Combined sources4
Helixi209 – 218Combined sources10
Turni220 – 222Combined sources3
Turni225 – 227Combined sources3
Helixi234 – 246Combined sources13
Turni256 – 258Combined sources3
Beta strandi261 – 263Combined sources3
Helixi266 – 282Combined sources17
Beta strandi283 – 285Combined sources3
Beta strandi2221 – 2233Combined sources13
Beta strandi2244 – 2251Combined sources8
Beta strandi2254 – 2260Combined sources7
Helixi2261 – 2264Combined sources4
Turni2265 – 2267Combined sources3
Beta strandi2269 – 2272Combined sources4
Beta strandi2282 – 2285Combined sources4
Beta strandi2293 – 2299Combined sources7
Beta strandi2301 – 2303Combined sources3
Beta strandi2305 – 2309Combined sources5
Helixi2313 – 2328Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WJMNMR-A2219-2328[»]
1WYQNMR-A178-291[»]
ProteinModelPortaliO15020.
SMRiO15020.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15020.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 278Actin-bindingAdd BLAST277
Domaini57 – 161CH 1PROSITE-ProRule annotationAdd BLAST105
Domaini176 – 278CH 2PROSITE-ProRule annotationAdd BLAST103
Repeati305 – 415Spectrin 1Add BLAST111
Repeati425 – 529Spectrin 2Add BLAST105
Repeati531 – 639Spectrin 3Add BLAST109
Repeati641 – 745Spectrin 4Add BLAST105
Repeati747 – 850Spectrin 5Add BLAST104
Repeati852 – 956Spectrin 6Add BLAST105
Repeati958 – 1063Spectrin 7Add BLAST106
Repeati1065 – 1170Spectrin 8Add BLAST106
Repeati1172 – 1276Spectrin 9Add BLAST105
Repeati1278 – 1381Spectrin 10Add BLAST104
Repeati1383 – 1486Spectrin 11Add BLAST104
Repeati1488 – 1586Spectrin 12Add BLAST99
Repeati1588 – 1692Spectrin 13Add BLAST105
Repeati1694 – 1799Spectrin 14Add BLAST106
Repeati1801 – 1905Spectrin 15Add BLAST105
Repeati1907 – 2011Spectrin 16Add BLAST105
Repeati2013 – 2075Spectrin 17Add BLAST63
Domaini2218 – 2328PHPROSITE-ProRule annotationAdd BLAST111

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

eggNOGiKOG0035. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118813.
HOGENOMiHOG000007281.
HOVERGENiHBG057912.
InParanoidiO15020.
KOiK06115.
OMAiHLRLCQL.
OrthoDBiEOG091G003V.
PhylomeDBiO15020.
TreeFamiTF313446.

Family and domain databases

CDDicd00014. CH. 2 hits.
Gene3Di1.10.418.10. 2 hits.
2.30.29.30. 1 hit.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR011993. PH_dom-like.
IPR001605. PH_dom-spectrin-type.
IPR001849. PH_domain.
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.
SSF50729. SSF50729. 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. AlignAdd to basket

Isoform 1 (identifier: O15020-1) [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
MSSTLSPTDF DSLEIQGQYS DINNRWDLPD SDWDNDSSSA RLFERSRIKA
60 70 80 90 100
LADEREAVQK KTFTKWVNSH LARVTCRVGD LYSDLRDGRN LLRLLEVLSG
110 120 130 140 150
EILPKPTKGR MRIHCLENVD KALQFLKEQK VHLENMGSHD IVDGNHRLTL
160 170 180 190 200
GLVWTIILRF QIQDISVETE DNKEKKSAKD ALLLWCQMKT AGYPNVNVHN
210 220 230 240 250
FTTSWRDGLA FNAIVHKHRP DLLDFESLKK CNAHYNLQNA FNLAEKELGL
260 270 280 290 300
TKLLDPEDVN VDQPDEKSII TYVATYYHYF SKMKALAVEG KRIGKVLDHA
310 320 330 340 350
MEAERLVEKY ESLASELLQW IEQTIVTLND RQLANSLSGV QNQLQSFNSY
360 370 380 390 400
RTVEKPPKFT EKGNLEVLLF TIQSKLRANN QKVYTPREGR LISDINKAWE
410 420 430 440 450
RLEKAEHERE LALRTELIRQ EKLEQLAARF DRKAAMRETW LSENQRLVSQ
460 470 480 490 500
DNFGLELAAV EAAVRKHEAI ETDIVAYSGR VQAVDAVAAE LAAERYHDIK
510 520 530 540 550
RIAARQHNVA RLWDFLRQMV AARRERLLLN LELQKVFQDL LYLMDWMEEM
560 570 580 590 600
KGRLQSQDLG RHLAGVEDLL QLHELVEADI AVQAERVRAV SASALRFCNP
610 620 630 640 650
GKEYRPCDPQ LVSERVAKLE QSYEALCELA AARRARLEES RRLWRFLWEV
660 670 680 690 700
GEAEAWVREQ QHLLASADTG RDLTGALRLL NKHTALRGEM SGRLGPLKLT
710 720 730 740 750
LEQGQQLVAE GHPGASQASA RAAELQAQWE RLEALAEERA QRLAQAASLY
760 770 780 790 800
QFQADANDME AWLVDALRLV SSPELGHDEF STQALARQHR ALEEEIRSHR
810 820 830 840 850
PTLDALREQA AALPPTLSRT PEVQSRVPTL ERHYEELQAR AGERARALEA
860 870 880 890 900
ALALYTMLSE AGACGLWVEE KEQWLNGLAL PERLEDLEVV QQRFETLEPE
910 920 930 940 950
MNTLAAQITA VNDIAEQLLK ANPPGKDRIV NTQEQLNHRW QQFRRLADGK
960 970 980 990 1000
KAALTSALSI QNYHLECTET QAWMREKTKV IESTQGLGND LAGVLALQRK
1010 1020 1030 1040 1050
LAGTERDLEA IAARVGELTR EANALAAGHP AQAVAINARL REVQTGWEDL
1060 1070 1080 1090 1100
RATMRRREES LGEARRLQDF LRSLDDFQAW LGRTQTAVAS EEGPATLPEA
1110 1120 1130 1140 1150
EALLAQHAAL RGEVERAQSE YSRLRALGEE VTRDQADPQC LFLRQRLEAL
1160 1170 1180 1190 1200
GTGWEELGRM WESRQGRLAQ AHGFQGFLRD ARQAEGVLSS QEYVLSHTEM
1210 1220 1230 1240 1250
PGTLQAADAA IKKLEDFMST MDANGERIHG LLEAGRQLVS EGNIHADKIR
1260 1270 1280 1290 1300
EKADSIERRH KKNQDAAQQF LGRLRDNREQ QHFLQDCHEL KLWIDEKMLT
1310 1320 1330 1340 1350
AQDVSYDEAR NLHTKWQKHQ AFMAELAANK DWLDKVDKEG RELTLEKPEL
1360 1370 1380 1390 1400
KALVSEKLRD LHRRWDELET TTQAKARSLF DANRAELFAQ SCCALESWLE
1410 1420 1430 1440 1450
SLQAQLHSDD YGKDLTSVNI LLKKQQMLEW EMAVREKEVE AIQAQAKALA
1460 1470 1480 1490 1500
QEDQGAGEVE RTSRAVEEKF RALCQPMRER CRRLQASREQ HQFHRDVEDE
1510 1520 1530 1540 1550
ILWVTERLPM ASSMEHGKDL PSVQLLMKKN QTLQKEIQGH EPRIADLRER
1560 1570 1580 1590 1600
QRALGAAAAG PELAELQEMW KRLGHELELR GKRLEDALRA QQFYRDAAEA
1610 1620 1630 1640 1650
EAWMGEQELH MMGQEKAKDE LSAQAEVKKH QVLEQALADY AQTIHQLAAS
1660 1670 1680 1690 1700
SQDMIDHEHP ESTRISIRQA QVDKLYAGLK ELAGERRERL QEHLRLCQLR
1710 1720 1730 1740 1750
RELDDLEQWI QEREVVAASH ELGQDYEHVT MLRDKFREFS RDTSTIGQER
1760 1770 1780 1790 1800
VDSANALANG LIAGGHAARA TVAEWKDSLN EAWADLLELL DTRGQVLAAA
1810 1820 1830 1840 1850
YELQRFLHGA RQALARVQHK QQQLPDGTGR DLNAAEALQR RHCAYEHDIQ
1860 1870 1880 1890 1900
ALSPQVQQVQ DDGHRLQKAY AGDKAEEIGR HMQAVAEAWA QLQGSSAARR
1910 1920 1930 1940 1950
QLLLDTTDKF RFFKAVRELM LWMDEVNLQM DAQERPRDVS SADLVIKNQQ
1960 1970 1980 1990 2000
GIKAEIEARA DRFSSCIDMG KELLARSHYA AEEISEKLSQ LQARRQETAE
2010 2020 2030 2040 2050
KWQEKMDWLQ LVLEVLVFGR DAGMAEAWLC SQEPLVRSAE LGCTVDEVES
2060 2070 2080 2090 2100
LIKRHEAFQK SAVAWEERFC ALEKLTALEE REKERKRKRE EEERRKQPPA
2110 2120 2130 2140 2150
PEPTASVPPG DLVGGQTASD TTWDGTQPRP PPSTQAPSVN GVCTDGEPSQ
2160 2170 2180 2190 2200
PLLGQQRLEH SSFPEGPGPG SGDEANGPRG ERQTRTRGPA PSAMPQSRST
2210 2220 2230 2240 2250
ESAHAATLPP RGPEPSAQEQ MEGMLCRKQE MEAFGKKAAN RSWQNVYCVL
2260 2270 2280 2290 2300
RRGSLGFYKD AKAASAGVPY HGEVPVSLAR AQGSVAFDYR KRKHVFKLGL
2310 2320 2330 2340 2350
QDGKEYLFQA KDEAEMSSWL RVVNAAIATA SSASGEPEEP VVPSTTRGMT
2360 2370 2380 2390
RAMTMPPVSP VGAEGPVVLR SKDGRERERE KRFSFFKKNK
Length:2,390
Mass (Da):271,325
Last modified:October 5, 2010 - v3
Checksum:i1CC523CC6493DBFE
GO
Isoform 2 (identifier: O15020-2) [UniParc]FASTAAdd to basket

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

Show »
Length:2,365
Mass (Da):268,309
Checksum:i3C60F49E525BEC79
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_026767253L → P in SCA5. 1 PublicationCorresponds to variant rs121918306dbSNPEnsembl.1
Natural variantiVAR_070232480R → W in SCA5. 1 PublicationCorresponds to variant rs397514749dbSNPEnsembl.1
Natural variantiVAR_026768532 – 544Missing in SCA5. 1 PublicationAdd BLAST13
Natural variantiVAR_026769629 – 634LAAARR → W in SCA5. 1 Publication6
Natural variantiVAR_035458774E → K in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_026770825S → G.1 PublicationCorresponds to variant rs4930388dbSNPEnsembl.1
Natural variantiVAR_048631835E → K.Corresponds to variant rs36054877dbSNPEnsembl.1
Natural variantiVAR_0267711034V → A.Corresponds to variant rs506028dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0007222314 – 2390AEMSS…FKKNK → VSCPSCSSLSVPFQKLPAAD SPSFPVLPLFPGLVLCGKTG CVRRPHQAALPV in isoform 2. 1 PublicationAdd BLAST77

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS8150.1. [O15020-1]
RefSeqiNP_008877.1. NM_006946.2.
XP_005274249.1. XM_005274192.4. [O15020-1]
XP_005274250.1. XM_005274193.3. [O15020-1]
XP_006718734.1. XM_006718671.3. [O15020-1]
XP_016873663.1. XM_017018174.1. [O15020-1]
XP_016873664.1. XM_017018175.1. [O15020-1]
XP_016873665.1. XM_017018176.1. [O15020-1]
XP_016873666.1. XM_017018177.1. [O15020-1]
XP_016873667.1. XM_017018178.1. [O15020-1]
UniGeneiHs.26915.
Hs.586709.
Hs.679104.

Genome annotation databases

EnsembliENST00000309996; ENSP00000311489; ENSG00000173898. [O15020-1]
ENST00000529997; ENSP00000433593; ENSG00000173898. [O15020-2]
ENST00000533211; ENSP00000432568; ENSG00000173898. [O15020-1]
GeneIDi6712.
KEGGihsa:6712.
UCSCiuc001ojc.2. human. [O15020-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS8150.1. [O15020-1]
RefSeqiNP_008877.1. NM_006946.2.
XP_005274249.1. XM_005274192.4. [O15020-1]
XP_005274250.1. XM_005274193.3. [O15020-1]
XP_006718734.1. XM_006718671.3. [O15020-1]
XP_016873663.1. XM_017018174.1. [O15020-1]
XP_016873664.1. XM_017018175.1. [O15020-1]
XP_016873665.1. XM_017018176.1. [O15020-1]
XP_016873666.1. XM_017018177.1. [O15020-1]
XP_016873667.1. XM_017018178.1. [O15020-1]
UniGeneiHs.26915.
Hs.586709.
Hs.679104.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WJMNMR-A2219-2328[»]
1WYQNMR-A178-291[»]
ProteinModelPortaliO15020.
SMRiO15020.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112590. 32 interactors.
DIPiDIP-47270N.
IntActiO15020. 27 interactors.
STRINGi9606.ENSP00000311489.

PTM databases

iPTMnetiO15020.
PhosphoSitePlusiO15020.
SwissPalmiO15020.

Polymorphism and mutation databases

BioMutaiSPTBN2.

Proteomic databases

EPDiO15020.
MaxQBiO15020.
PaxDbiO15020.
PeptideAtlasiO15020.
PRIDEiO15020.

Protocols and materials databases

DNASUi6712.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000309996; ENSP00000311489; ENSG00000173898. [O15020-1]
ENST00000529997; ENSP00000433593; ENSG00000173898. [O15020-2]
ENST00000533211; ENSP00000432568; ENSG00000173898. [O15020-1]
GeneIDi6712.
KEGGihsa:6712.
UCSCiuc001ojc.2. human. [O15020-1]

Organism-specific databases

CTDi6712.
DisGeNETi6712.
GeneCardsiSPTBN2.
HGNCiHGNC:11276. SPTBN2.
HPAiCAB009844.
HPA039293.
HPA043529.
MalaCardsiSPTBN2.
MIMi600224. phenotype.
604985. gene.
615386. phenotype.
neXtProtiNX_O15020.
OpenTargetsiENSG00000173898.
Orphaneti352403. Spectrin-associated autosomal recessive cerebellar ataxia.
98766. Spinocerebellar ataxia type 5.
PharmGKBiPA36105.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0035. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118813.
HOGENOMiHOG000007281.
HOVERGENiHBG057912.
InParanoidiO15020.
KOiK06115.
OMAiHLRLCQL.
OrthoDBiEOG091G003V.
PhylomeDBiO15020.
TreeFamiTF313446.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000173898-MONOMER.
ReactomeiR-HSA-2132295. MHC class II antigen presentation.
R-HSA-375165. NCAM signaling for neurite out-growth.
R-HSA-445095. Interaction between L1 and Ankyrins.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-6807878. COPI-mediated anterograde transport.

Miscellaneous databases

ChiTaRSiSPTBN2. human.
EvolutionaryTraceiO15020.
GeneWikiiSPTBN2.
GenomeRNAii6712.
PROiO15020.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000173898.
CleanExiHS_SPTBN2.
ExpressionAtlasiO15020. baseline and differential.
GenevisibleiO15020. HS.

Family and domain databases

CDDicd00014. CH. 2 hits.
Gene3Di1.10.418.10. 2 hits.
2.30.29.30. 1 hit.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR011993. PH_dom-like.
IPR001605. PH_dom-spectrin-type.
IPR001849. PH_domain.
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.
SSF50729. SSF50729. 1 hit.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSPTN2_HUMAN
AccessioniPrimary (citable) accession number: O15020
Secondary accession number(s): O14872, O14873
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: October 5, 2010
Last modified: November 30, 2016
This is version 166 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.