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Protein

Spectrin beta chain, erythrocytic

Gene

Sptb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane.

GO - Molecular functioni

  • actin binding Source: MGI
  • actin filament binding Source: MGI
  • ankyrin binding Source: MGI
  • protein heterodimerization activity Source: MGI
  • structural constituent of cytoskeleton Source: InterPro

GO - Biological processi

  • actin filament capping Source: UniProtKB-KW
  • hemopoiesis Source: MGI
  • plasma membrane organization Source: MGI
  • porphyrin-containing compound biosynthetic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Spectrin beta chain, erythrocytic
Alternative name(s):
Beta-I spectrin
Gene namesi
Name:Sptb
Synonyms:Spnb-1, Spnb1, Sptb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:98387. Sptb.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: MGI
  • cortical cytoskeleton Source: MGI
  • cytoplasm Source: MGI
  • membrane Source: MGI
  • plasma membrane Source: MGI
  • protein complex Source: MGI
  • spectrin Source: InterPro
  • spectrin-associated cytoskeleton Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 21282127Spectrin beta chain, erythrocyticPRO_0000073460Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei36 – 361PhosphoserineCombined sources
Modified residuei104 – 1041PhosphothreonineBy similarity
Modified residuei1289 – 12891PhosphoserineCombined sources
Modified residuei2034 – 20341PhosphoserineBy similarity
Modified residuei2064 – 20641PhosphothreonineBy similarity
Modified residuei2072 – 20721PhosphothreonineCombined sources
Modified residuei2101 – 21011PhosphothreonineBy similarity
Modified residuei2105 – 21051PhosphoserineBy similarity
Modified residuei2108 – 21081PhosphoserineBy similarity
Modified residuei2114 – 21141PhosphoserineBy similarity
Modified residuei2116 – 21161PhosphoserineBy similarity
Modified residuei2119 – 21191PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP15508.
MaxQBiP15508.
PaxDbiP15508.
PeptideAtlasiP15508.
PRIDEiP15508.

PTM databases

iPTMnetiP15508.
PhosphoSiteiP15508.

Expressioni

Gene expression databases

CleanExiMM_SPNB1.

Interactioni

Subunit structurei

Composed of nonhomologous chains, alpha and beta, which aggregate to form dimers, tetramers, and higher polymers.

GO - Molecular functioni

  • actin binding Source: MGI
  • actin filament binding Source: MGI
  • ankyrin binding Source: MGI
  • protein heterodimerization activity Source: MGI

Protein-protein interaction databases

IntActiP15508. 3 interactions.
MINTiMINT-4996478.
STRINGi10090.ENSMUSP00000021458.

Structurei

3D structure databases

ProteinModelPortaliP15508.
SMRiP15508. Positions 173-280, 1056-1265, 1579-2074.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 275274Actin-bindingAdd
BLAST
Domaini54 – 158105CH 1PROSITE-ProRule annotationAdd
BLAST
Domaini173 – 275103CH 2PROSITE-ProRule annotationAdd
BLAST
Repeati276 – 384109Spectrin 1Add
BLAST
Repeati385 – 490106Spectrin 2Add
BLAST
Repeati491 – 599109Spectrin 3Add
BLAST
Repeati600 – 705106Spectrin 4Add
BLAST
Repeati706 – 810105Spectrin 5Add
BLAST
Repeati811 – 916106Spectrin 6Add
BLAST
Repeati917 – 1023107Spectrin 7Add
BLAST
Repeati1024 – 1130107Spectrin 8Add
BLAST
Repeati1131 – 1236106Spectrin 9Add
BLAST
Repeati1237 – 1341105Spectrin 10Add
BLAST
Repeati1342 – 1447106Spectrin 11Add
BLAST
Repeati1448 – 154699Spectrin 12Add
BLAST
Repeati1547 – 1652106Spectrin 13Add
BLAST
Repeati1653 – 1759107Spectrin 14Add
BLAST
Repeati1760 – 1864105Spectrin 15Add
BLAST
Repeati1865 – 1970106Spectrin 16Add
BLAST
Repeati1971 – 2073103Spectrin 17Add
BLAST

Sequence similaritiesi

Belongs to the spectrin family.Curated
Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
Contains 17 spectrin repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0517. Eukaryota.
COG5069. LUCA.
HOVERGENiHBG057912.
InParanoidiP15508.

Family and domain databases

Gene3Di1.10.418.10. 2 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-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.
SMARTiSM00033. CH. 2 hits.
SM00150. SPEC. 17 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P15508-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSATEFENV GNQPPFSRIN ARWDAPDDEL DNDNSSARLF ERSRIKALAD
60 70 80 90 100
EREVVQKKTF TKWVNSHLAR VSCRISDLYK DLRDGRMLIK LLEVLSGEML
110 120 130 140 150
PRPTKGKMRI HCLENVDKAL QFLKEQRVHL ENMGSHDIVD GNHRLVLGLI
160 170 180 190 200
WTIILRFQIQ DIVVQTQEGR EQRSAKDALL LWCQMKTAGY PHVNVTNFTS
210 220 230 240 250
SWKDGLAFNA LIHKHRPDLI DFDKLKDSNA RHNLEHAFDV AERQLGIIPL
260 270 280 290 300
LDPEDVFTEN PDEKSIITYV VAFYHYFSKM KVLAVEGKRV GKVIDHAIET
310 320 330 340 350
EKMIEKYSGL ASDLLTWIEQ TISVLNSRKF ANSLSGVQQQ LQAFSTYRTV
360 370 380 390 400
EKPPKFQEKG NLEVLLFTIQ SRMRANNQKV YTPHDGKLVS DINRAWESLE
410 420 430 440 450
EAEYQRELAL RSELIRQEFD RKAAMRETWL NENQRLVTQD NFGYDLAAVE
460 470 480 490 500
AAKKKHEAIE TDTAAYEERV KALEDLAQEL EKENYHDQKR IIARKDNILR
510 520 530 540 550
LWSYLQELLR SRRQRLEATL ALQKLFQDML HSIDWMDEIK AHILSAEFGK
560 570 580 590 600
HLLEVEDLLQ KHKLMEADIA IQGDKVKAIT AATLQFAEGK GYQPCDPQVI
610 620 630 640 650
QDRVSHLEQC FSELSNMAAG RKAQLEQSKR LWKFFWEMDE AESWIKEKEQ
660 670 680 690 700
IYSSLDYGKD LTSVLILQRK HKAFEDELRG LDAHLKQIFQ EADDMVAQKQ
710 720 730 740 750
FGHPQIETRV KEVSAQWDHL KELAAFRKKD LQDAENFFQF QGDADDLKAW
760 770 780 790 800
LQDAHRLLSG EDVGQDEGAT RALGKKHKEF LEELEESRGV MEHLEHQAQG
810 820 830 840 850
FPEEFRDSPD VTNRLQALRK LYQQVLTQAE LRGHKLQEAL DLYTVFGESD
860 870 880 890 900
ACELWMTEKG KWLDQMDIPN TLEDLEVVQH RFDILDQEMK TLMAQIDGVN
910 920 930 940 950
LAANNLVESG HPRSGEVKQY QDRLNKRWQA FQAVVSEQRE AVDSALRVNN
960 970 980 990 1000
YCVDCEETSK WIMDKTKVVE STKDLGQDLA GVIAIQRKLS GLERDVLAIR
1010 1020 1030 1040 1050
DRVSALERES QYLMESHPEQ KEDIGQRQAD VEKLWKGLQD ALQGQELSLG
1060 1070 1080 1090 1100
EASKLQAFLQ DLDDFKAWLS MAQKAVASED MPESLPEAEQ LLQQHAAIKE
1110 1120 1130 1140 1150
EIDAHRDDYH RVKASGEKVI EGQTDPDYQL LGQRLEGLDT DWDALRRMWE
1160 1170 1180 1190 1200
SRGNTLTQCL GFQEFQKDAK QAEAILSNQE YTLAHLEPPD SLAAAEAGIR
1210 1220 1230 1240 1250
KFEDFLVSME NNRDKILSPV DSGNKLVAEG NLYSNKIMEK VQLIEDRHKK
1260 1270 1280 1290 1300
NNEKAQEATV LLKDNLELQN FLQNCKELTL WINDKLLTSP DVSYDEARNL
1310 1320 1330 1340 1350
HNKWMKHQAF MAELASHQGW LENIDAEGRQ LMAEKPQFKD VVSERLEALH
1360 1370 1380 1390 1400
KLWEELQSTA KAKAEQLSAA RSSDLRLQTH ADLNKWIGAM EDQLRSDDLG
1410 1420 1430 1440 1450
KDLTTVNRML AKLKRVEEQV NLRKEELEEL FADAPSLGAE AGDTDMSIEK
1460 1470 1480 1490 1500
RFLDLLEPLG RRKKQLELSK AKLQISRDLE DETLWVEERL PLAQSADYGT
1510 1520 1530 1540 1550
NLQTVQLFMK KNQTLQNEIL GHAPRVEDVL RRGQELVKAA EIDCQDIEER
1560 1570 1580 1590 1600
LGHLQSSWDT LREAAAGRLQ RLRDAHEAQQ YYLDAGEAEA WISEQELYVF
1610 1620 1630 1640 1650
SDEPPKDEEG AIVMLKRHLR QQRTVEEYGR NIKQLAGRAQ SLLSAGHPEG
1660 1670 1680 1690 1700
EQIIRLQGQV DKQYAGLKDM AEERRRRLEN MYHLFQLKRE ADDLEQWITE
1710 1720 1730 1740 1750
KEMVASSQEM GQDFDHVTML RDKFRDFARE TGAIGQERVD NVTIIERLID
1760 1770 1780 1790 1800
AGHSEAATIA EWKDGLNDMW ADLLELIDTR MQLLAASYDL HRYFYTGTEI
1810 1820 1830 1840 1850
LGLIDEKHRE LPEDVGLDAS TAESFHRVHT AFERELHLLG VQVQQFQDVA
1860 1870 1880 1890 1900
TRLQTAYAGE KADAIQSKEQ EVSAAWQALL DACAGRRAQL VDTADKFRFF
1910 1920 1930 1940 1950
SMVRDLLSWM ESIIRQIETQ ERPRDVSSVE LLLKYHQGIK AEINTRAKNF
1960 1970 1980 1990 2000
STCLELGESL LQRQHQASDE IREKLQQVIS RRQEMNDKWE ARSDRLHMLL
2010 2020 2030 2040 2050
EVCQFSRDAS VAEAWLIAQE PYLASRDFGH TVDSVEKLIK RHEAFEKSTA
2060 2070 2080 2090 2100
SWAERFAALE KPTTLELKER QTPERPTEEP GPQEEEGETA GEAPQVHHAA
2110 2120
TERTSPVSFM SRLSSSWESL LPEPAHPF
Length:2,128
Mass (Da):245,250
Last modified:January 23, 2007 - v4
Checksum:i10E576111106DFE1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S66283 mRNA. Translation: AAB28600.1.
M18641 mRNA. Translation: AAA40126.1.
PIRiA45929.
UniGeneiMm.32881.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S66283 mRNA. Translation: AAB28600.1.
M18641 mRNA. Translation: AAA40126.1.
PIRiA45929.
UniGeneiMm.32881.

3D structure databases

ProteinModelPortaliP15508.
SMRiP15508. Positions 173-280, 1056-1265, 1579-2074.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP15508. 3 interactions.
MINTiMINT-4996478.
STRINGi10090.ENSMUSP00000021458.

PTM databases

iPTMnetiP15508.
PhosphoSiteiP15508.

Proteomic databases

EPDiP15508.
MaxQBiP15508.
PaxDbiP15508.
PeptideAtlasiP15508.
PRIDEiP15508.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:98387. Sptb.

Phylogenomic databases

eggNOGiKOG0517. Eukaryota.
COG5069. LUCA.
HOVERGENiHBG057912.
InParanoidiP15508.

Miscellaneous databases

PROiP15508.
SOURCEiSearch...

Gene expression databases

CleanExiMM_SPNB1.

Family and domain databases

Gene3Di1.10.418.10. 2 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-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.
SMARTiSM00033. CH. 2 hits.
SM00150. SPEC. 17 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete nucleotide sequence of the murine erythroid beta-spectrin cDNA and tissue-specific expression in normal and jaundiced mice."
    Bloom M.L., Birkenmeier C.S., Barker J.E.
    Blood 82:2906-2914(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning and nucleotide sequence of a mouse erythrocyte beta-spectrin cDNA."
    Cioe L., Laurila P., Meo P., Krebs K., Goodman S., Curtis P.J.
    Blood 70:915-920(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1055-1290.
  3. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-1289 AND THR-2072, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen and Testis.

Entry informationi

Entry nameiSPTB1_MOUSE
AccessioniPrimary (citable) accession number: P15508
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 128 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

This complex is anchored to the cytoplasmic face of the plasma membrane via another protein, ankyrin, which binds to beta-spectrin and mediates the binding of the whole complex to a transmembrane protein band 3. The interaction of erythrocyte spectrin with other proteins through specific binding domains lead to the formation of an extensive subplasmalemmal meshwork which is thought to be responsible for the maintenance of the biconcave shape of human erythrocytes, for the regulation of plasma membrane components and for the maintenance of the lipid asymmetry of the plasma membrane.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.