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O15020

- SPTN2_HUMAN

UniProt

O15020 - SPTN2_HUMAN

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Protein

Spectrin beta chain, non-erythrocytic 2

Gene

SPTBN2

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

Functioni

Probably plays an important role in neuronal membrane skeleton.

GO - Molecular functioni

  1. actin binding Source: ProtInc
  2. phospholipid binding Source: InterPro
  3. structural constituent of cytoskeleton Source: UniProtKB

GO - Biological processi

  1. actin filament capping Source: UniProtKB-KW
  2. adult behavior Source: Ensembl
  3. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  4. axon guidance Source: Reactome
  5. cell death Source: UniProtKB-KW
  6. cerebellar Purkinje cell layer morphogenesis Source: Ensembl
  7. multicellular organism growth Source: Ensembl
  8. synapse assembly Source: Ensembl
  9. vesicle-mediated transport Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_121399. MHC class II antigen presentation.
REACT_18334. NCAM signaling for neurite out-growth.
REACT_22266. Interaction between L1 and Ankyrins.

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
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:11276. SPTBN2.

Subcellular locationi

GO - Cellular componenti

  1. apical plasma membrane Source: Ensembl
  2. cytosol Source: Reactome
  3. extracellular space Source: UniProt
  4. neuronal cell body Source: Ensembl
  5. spectrin Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti253 – 2531L → P in SCA5. 1 Publication
VAR_026767
Natural varianti480 – 4801R → W in SCA5. 1 Publication
VAR_070232
Natural varianti532 – 54413Missing in SCA5. 1 Publication
VAR_026768Add
BLAST
Natural varianti629 – 6346LAAARR → W in SCA5. 1 Publication
VAR_026769
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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Disease mutation, Neurodegeneration, Spinocerebellar ataxia

Organism-specific databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 23902389Spectrin beta chain, non-erythrocytic 2PRO_0000073463Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei2171 – 21711Phosphoserine4 Publications
Modified residuei2359 – 23591Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO15020.
PaxDbiO15020.
PRIDEiO15020.

PTM databases

PhosphoSiteiO15020.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiO15020.
CleanExiHS_SPTBN2.
ExpressionAtlasiO15020. baseline and differential.
GenevestigatoriO15020.

Organism-specific databases

HPAiCAB009844.

Interactioni

Protein-protein interaction databases

BioGridi112590. 8 interactions.
DIPiDIP-47270N.
IntActiO15020. 7 interactions.
STRINGi9606.ENSP00000311489.

Structurei

Secondary structure

1
2390
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi180 – 19112Combined sources
Beta strandi193 – 1953Combined sources
Beta strandi205 – 2084Combined sources
Helixi209 – 21810Combined sources
Turni220 – 2223Combined sources
Turni225 – 2273Combined sources
Helixi234 – 24613Combined sources
Turni256 – 2583Combined sources
Beta strandi261 – 2633Combined sources
Helixi266 – 28217Combined sources
Beta strandi283 – 2853Combined sources
Beta strandi2221 – 223313Combined sources
Beta strandi2244 – 22518Combined sources
Beta strandi2254 – 22607Combined sources
Helixi2261 – 22644Combined sources
Turni2265 – 22673Combined sources
Beta strandi2269 – 22724Combined sources
Beta strandi2282 – 22854Combined sources
Beta strandi2293 – 22997Combined sources
Beta strandi2301 – 23033Combined sources
Beta strandi2305 – 23095Combined sources
Helixi2313 – 232816Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WJMNMR-A2219-2328[»]
1WYQNMR-A178-291[»]
ProteinModelPortaliO15020.
SMRiO15020. Positions 53-291, 302-2084, 2212-2333.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15020.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 278277Actin-bindingAdd
BLAST
Domaini57 – 161105CH 1PROSITE-ProRule annotationAdd
BLAST
Domaini176 – 278103CH 2PROSITE-ProRule annotationAdd
BLAST
Repeati305 – 415111Spectrin 1Add
BLAST
Repeati425 – 529105Spectrin 2Add
BLAST
Repeati531 – 639109Spectrin 3Add
BLAST
Repeati641 – 745105Spectrin 4Add
BLAST
Repeati747 – 850104Spectrin 5Add
BLAST
Repeati852 – 956105Spectrin 6Add
BLAST
Repeati958 – 1063106Spectrin 7Add
BLAST
Repeati1065 – 1170106Spectrin 8Add
BLAST
Repeati1172 – 1276105Spectrin 9Add
BLAST
Repeati1278 – 1381104Spectrin 10Add
BLAST
Repeati1383 – 1486104Spectrin 11Add
BLAST
Repeati1488 – 158699Spectrin 12Add
BLAST
Repeati1588 – 1692105Spectrin 13Add
BLAST
Repeati1694 – 1799106Spectrin 14Add
BLAST
Repeati1801 – 1905105Spectrin 15Add
BLAST
Repeati1907 – 2011105Spectrin 16Add
BLAST
Repeati2013 – 207563Spectrin 17Add
BLAST
Domaini2218 – 2328111PHPROSITE-ProRule annotationAdd
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.
InParanoidiO15020.
KOiK06115.
OMAiIQGQYSD.
OrthoDBiEOG73RB9J.
PhylomeDBiO15020.
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: 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 BAA32700.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti253 – 2531L → P in SCA5. 1 Publication
VAR_026767
Natural varianti480 – 4801R → W in SCA5. 1 Publication
VAR_070232
Natural varianti532 – 54413Missing in SCA5. 1 Publication
VAR_026768Add
BLAST
Natural varianti629 – 6346LAAARR → W in SCA5. 1 Publication
VAR_026769
Natural varianti774 – 7741E → K in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035458
Natural varianti825 – 8251S → G.1 Publication
Corresponds to variant rs4930388 [ dbSNP | Ensembl ].
VAR_026770
Natural varianti835 – 8351E → K.
Corresponds to variant rs36054877 [ dbSNP | Ensembl ].
VAR_048631
Natural varianti1034 – 10341V → A.
Corresponds to variant rs506028 [ dbSNP | Ensembl ].
VAR_026771

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2314 – 239077AEMSS…FKKNK → VSCPSCSSLSVPFQKLPAAD SPSFPVLPLFPGLVLCGKTG CVRRPHQAALPV in isoform 2. 1 PublicationVSP_000722Add
BLAST

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_005274192.2. [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]
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.
UCSCiuc001ojd.3. 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 .
CCDSi CCDS8150.1. [O15020-1 ]
RefSeqi NP_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 ]
UniGenei Hs.26915.
Hs.586709.
Hs.679104.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WJM NMR - A 2219-2328 [» ]
1WYQ NMR - A 178-291 [» ]
ProteinModelPortali O15020.
SMRi O15020. Positions 53-291, 302-2084, 2212-2333.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112590. 8 interactions.
DIPi DIP-47270N.
IntActi O15020. 7 interactions.
STRINGi 9606.ENSP00000311489.

PTM databases

PhosphoSitei O15020.

Proteomic databases

MaxQBi O15020.
PaxDbi O15020.
PRIDEi O15020.

Protocols and materials databases

DNASUi 6712.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000309996 ; ENSP00000311489 ; ENSG00000173898 . [O15020-1 ]
ENST00000529997 ; ENSP00000433593 ; ENSG00000173898 . [O15020-2 ]
ENST00000533211 ; ENSP00000432568 ; ENSG00000173898 . [O15020-1 ]
GeneIDi 6712.
KEGGi hsa:6712.
UCSCi uc001ojd.3. human. [O15020-1 ]

Organism-specific databases

CTDi 6712.
GeneCardsi GC11M066453.
HGNCi HGNC:11276. SPTBN2.
HPAi CAB009844.
MIMi 600224. phenotype.
604985. gene.
615386. phenotype.
neXtProti NX_O15020.
Orphaneti 352403. Spectrin-associated autosomal recessive cerebellar ataxia.
98766. Spinocerebellar ataxia type 5.
PharmGKBi PA36105.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5069.
GeneTreei ENSGT00760000118813.
HOGENOMi HOG000007281.
HOVERGENi HBG057912.
InParanoidi O15020.
KOi K06115.
OMAi IQGQYSD.
OrthoDBi EOG73RB9J.
PhylomeDBi O15020.
TreeFami TF313446.

Enzyme and pathway databases

Reactomei REACT_121399. MHC class II antigen presentation.
REACT_18334. NCAM signaling for neurite out-growth.
REACT_22266. Interaction between L1 and Ankyrins.

Miscellaneous databases

ChiTaRSi SPTBN2. human.
EvolutionaryTracei O15020.
GeneWikii SPTBN2.
GenomeRNAii 6712.
NextBioi 26178.
PROi O15020.
SOURCEi Search...

Gene expression databases

Bgeei O15020.
CleanExi HS_SPTBN2.
ExpressionAtlasi O15020. baseline and differential.
Genevestigatori O15020.

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. "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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. 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. 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. 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. 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. Cited for: VARIANTS SCA5 PRO-253; 532-GLU--MET-544 DEL AND 629-LEU--ARG-634 DELINS TRP.
  15. Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-774.
  16. Cited for: VARIANT SCA5 TRP-480.

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 26, 2014
This is version 145 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

External Data

Dasty 3