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Protein

Spectrin beta chain, non-erythrocytic 2

Gene

Sptbn2

Organism
Rattus norvegicus (Rat)
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

  • phospholipid binding Source: InterPro
  • structural constituent of cytoskeleton Source: UniProtKB

GO - Biological processi

  • actin filament capping Source: UniProtKB-KW
  • cellular response to ethanol Source: RGD
  • regulation of calcium ion-dependent exocytosis Source: UniProtKB
  • synaptic vesicle docking Source: UniProtKB
  • synaptic vesicle exocytosis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Spectrin beta chain, non-erythrocytic 2
Alternative name(s):
Beta SpIII sigma 1
Beta-III spectrin
Glutamate transporter EAAT4-associated protein 41
SPNB-3
Spectrin-like protein GTRAP41
Gene namesi
Name:Sptbn2
Synonyms:Spnb3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3751. Sptbn2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • endosome Source: RGD
  • Golgi membrane Source: RGD
  • nuclear matrix Source: UniProtKB
  • perinuclear region of cytoplasm Source: RGD
  • plasma membrane Source: RGD
  • spectrin Source: UniProtKB
  • synaptic vesicle Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 23882387Spectrin beta chain, non-erythrocytic 2PRO_0000073464Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei6 – 61PhosphoserineCombined sources
Modified residuei31 – 311PhosphoserineCombined sources
Modified residuei959 – 9591PhosphoserineBy similarity
Modified residuei1073 – 10731PhosphoserineCombined sources
Modified residuei1574 – 15741PhosphoserineCombined sources
Modified residuei2169 – 21691PhosphoserineCombined sources
Modified residuei2199 – 21991PhosphoserineCombined sources
Modified residuei2354 – 23541PhosphothreonineBy similarity
Modified residuei2359 – 23591PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ9QWN8.
PRIDEiQ9QWN8.

PTM databases

iPTMnetiQ9QWN8.
PhosphoSiteiQ9QWN8.

Expressioni

Tissue specificityi

Abundantly transcribed in the brain. Neurons are the predominant cell-type to express the gene. Found abundantly in Purkinje cells.

Interactioni

Protein-protein interaction databases

BioGridi247889. 1 interaction.
MINTiMINT-4566756.
STRINGi10116.ENSRNOP00000026573.

Structurei

3D structure databases

ProteinModelPortaliQ9QWN8.
SMRiQ9QWN8. Positions 48-291, 1068-1277, 2212-2333.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiKOG0035. Eukaryota.
COG5069. LUCA.
HOGENOMiHOG000007281.
HOVERGENiHBG057912.
InParanoidiQ9QWN8.
PhylomeDBiQ9QWN8.

Family and domain databases

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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9QWN8-1 [UniParc]FASTAAdd to basket

« 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
ETLPKPTKGR 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
MEAEHLVEKY 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 LAAEHYHDIK
510 520 530 540 550
RIAARQNNVA RLWDFLREMV AARRERLLLN LELQKVFQDL LYLMDWMAEM
560 570 580 590 600
KGRLQSQDLG KHLAGVEDLL QLHELVEADI AVQAERVRAV SASALRFCDP
610 620 630 640 650
GKEYRPCDPQ LVSERVATLE QSYEALCELA ATRRARLEES RRLWRFLWEV
660 670 680 690 700
GEAEAWVREQ QHLLASAETG RDLTGVLRLL NKHTALRGEM SGRLGPLKLT
710 720 730 740 750
LEQGQQLVAE GHPGANQAST RAAELQAQWE RLEALAEERA QRLAQAASLY
760 770 780 790 800
QFQADANDME AWLVDALRLV SSPEVGHDEF STQALARQHR ALEEEIRAHR
810 820 830 840 850
PTLDALREQA AALPPALSHT PEVQGRVPTL EQHYEELQAR AGERARALEA
860 870 880 890 900
ALAFYTMLSE AGACGLWVEE KEQWLNGLAL PERLEDLEVV QQRFETLEPE
910 920 930 940 950
MNALAARVTA VSDIAEQLLK ASPPGKDRII GTQEQLNQRW QQFRSLADGK
960 970 980 990 1000
KAALTSALSI QNYHLECTET QAWMREKTKV IESTQDLGND LAGVLALQRK
1010 1020 1030 1040 1050
LAGTERDLEA ISARVGELTQ EANALAAGHP AQAPAINTRL GEVQTGWEDL
1060 1070 1080 1090 1100
RATMRRREES LGEARRLQDF LRSLDDFQAW LGRTQTAVAS EEGPATLPEA
1110 1120 1130 1140 1150
EALLAQHAAL RGEVERAQSE YSRLRTLGEE VTRDQADPQC LFLRQRLEAL
1160 1170 1180 1190 1200
GTGWEELGRM WESRQGRLAQ AHGFQGFLRD ARQAEGVLSS QEYFLSHTEM
1210 1220 1230 1240 1250
PGTLQAADAA IKKLEDFMST MDANGERIRG LLEAGRQLVS KGNIHAEKIQ
1260 1270 1280 1290 1300
EKADSIEKRH RKNQEAVQQL LGRLRDNREQ QHFLQDCQEL KLWIDEKMLT
1310 1320 1330 1340 1350
AQDVSYDEAR NLHTKWQKHQ AFMAELAANK DWLDKVDKEG RELTLEKPEL
1360 1370 1380 1390 1400
KVLVSEKLED LHRRWDELET TTQAKARSLF DANRAELFAQ SCSALESWLE
1410 1420 1430 1440 1450
SLQAQLHSDD YGKDLTSVNI LLKKQQMLER EMAVREKEVE AIQAQAKALA
1460 1470 1480 1490 1500
QEDQSAGEVE RTSRAVEEKF RALCQPMKDR CRRLQASREQ HQFHRDVEDE
1510 1520 1530 1540 1550
ILWVTERLPM ASSLEHGKDL PSVQLLMKKN QTLQKEIQGH EPRIADLKER
1560 1570 1580 1590 1600
QRTLGTAAAG PELAELQEMW KRLSHELELR GKRLEEALRA QQFYRDAAEA
1610 1620 1630 1640 1650
EAWMGEQELH MMGQEKAKDE LSAQAEVKKH QVLEQALADY AQTIKQLAAS
1660 1670 1680 1690 1700
SQDMIDHEHP ESTRLTIRQA 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
ALSTQVQQVQ DDGLRLQKAY AGDKAEEIGR HMQAVAEAWA QLQGSSAARR
1910 1920 1930 1940 1950
QLLLDTTDKF RFFKAVRELM LWMDGINLQM DAQERPRDVS SADLVIKNQQ
1960 1970 1980 1990 2000
GIKAEIEARA DRFSACIDMG QELLARNHYA AEEISEKLSQ LQSRRQETAE
2010 2020 2030 2040 2050
KWQEKMDWLQ LVLEVLVFGR DAGMAEAWLC SQEPLVRSAE LGCTVDEVES
2060 2070 2080 2090 2100
LIKRHEAFQK SAVAWEERFS ALEKLTALEE RENEQKRKRE EEERRKQPPT
2110 2120 2130 2140 2150
SEPMASQPEG SLVDGQRVLD TAWDGTQSKL PPSTQAPSIN GVCTDTESSQ
2160 2170 2180 2190 2200
PLLEQQRLEQ SNVPEGPGSG TGDESSGPRG ERQTLPRGPA PSPMPQSRSS
2210 2220 2230 2240 2250
ESAHVATLPA RGAELSAQEQ MEGTLCRKQE MEAFNKKAAN RSWQNVYCVL
2260 2270 2280 2290 2300
RRGSLGFYKD ARAASAGVPY HGEVPVSLAR AQGSVAFDYR KRKHVFKLGL
2310 2320 2330 2340 2350
QDGKEYLFQA KDEAEMSSWL RVVNAAIATA SSASGEPEEP VVPSASRGLT
2360 2370 2380
RAMTMPPVSQ PEGSIVLRSK DGREREREKR FSFFKKNK
Length:2,388
Mass (Da):271,064
Last modified:November 16, 2001 - v2
Checksum:i3EC8966AF0665F19
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti326 – 3283VTL → GTF in AAG28596 (PubMed:11242047).Curated
Sequence conflicti543 – 5431L → F in BAA32473 (PubMed:9704016).Curated
Sequence conflicti608 – 6081D → G in AAG28596 (PubMed:11242047).Curated
Sequence conflicti887 – 8871L → P in AAG28596 (PubMed:11242047).Curated
Sequence conflicti908 – 9081V → I in AAG28596 (PubMed:11242047).Curated
Sequence conflicti948 – 9481D → G in AAG28596 (PubMed:11242047).Curated
Sequence conflicti1156 – 11572EL → GA in BAA32473 (PubMed:9704016).Curated
Sequence conflicti1194 – 11941F → V in BAA32473 (PubMed:9704016).Curated
Sequence conflicti1194 – 11941F → V in AAG28596 (PubMed:11242047).Curated
Sequence conflicti1555 – 15551G → R in AAG28596 (PubMed:11242047).Curated
Sequence conflicti1769 – 17691R → W in AAG28596 (PubMed:11242047).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB008551 mRNA. Translation: BAA32699.1.
AB001347 mRNA. Translation: BAA32473.1.
AF225960 mRNA. Translation: AAG28596.1.
PIRiJE0271.
UniGeneiRn.20389.

Genome annotation databases

UCSCiRGD:3751. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB008551 mRNA. Translation: BAA32699.1.
AB001347 mRNA. Translation: BAA32473.1.
AF225960 mRNA. Translation: AAG28596.1.
PIRiJE0271.
UniGeneiRn.20389.

3D structure databases

ProteinModelPortaliQ9QWN8.
SMRiQ9QWN8. Positions 48-291, 1068-1277, 2212-2333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247889. 1 interaction.
MINTiMINT-4566756.
STRINGi10116.ENSRNOP00000026573.

PTM databases

iPTMnetiQ9QWN8.
PhosphoSiteiQ9QWN8.

Proteomic databases

PaxDbiQ9QWN8.
PRIDEiQ9QWN8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:3751. rat.

Organism-specific databases

RGDi3751. Sptbn2.

Phylogenomic databases

eggNOGiKOG0035. Eukaryota.
COG5069. LUCA.
HOGENOMiHOG000007281.
HOVERGENiHBG057912.
InParanoidiQ9QWN8.
PhylomeDBiQ9QWN8.

Miscellaneous databases

NextBioi608384.
PROiQ9QWN8.

Family and domain databases

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...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of a new beta-spectrin gene which is predominantly expressed in brain."
    Ohara O., Ohara R., Yamakawa H., Nakajima D., Nakayama M.
    Brain Res. Mol. Brain Res. 57:181-192(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. "A novel brain-specific isoform of beta spectrin: isolation and its interaction with Munc13."
    Sakaguchi G., Orita S., Naito A., Maeda M., Igarashi H., Sasaki T., Takai Y.
    Biochem. Biophys. Res. Commun. 248:846-851(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brain.
  3. "Modulation of the neuronal glutamate transporter EAAT4 by two interacting proteins."
    Jackson M., Song W., Liu M.-Y., Jin L., Dykes-Hoberg M., Lin C.-L.G., Bowers W.J., Federoff H.J., Sternweis P.C., Rothstein J.D.
    Nature 410:89-93(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1574, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-31; SER-1073; SER-2169 AND SER-2199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSPTN2_RAT
AccessioniPrimary (citable) accession number: Q9QWN8
Secondary accession number(s): O88197, Q9ES68
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: November 16, 2001
Last modified: March 16, 2016
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.