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Protein

Spectrin beta chain

Gene

beta-Spec

Organism
Drosophila melanogaster (Fruit fly)
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. Interacts with calmodulin in a calcium-dependent manner.1 Publication

GO - Molecular functioni

  • actin binding Source: FlyBase
  • ankyrin binding Source: FlyBase
  • calmodulin binding Source: FlyBase
  • cytoskeletal protein binding Source: FlyBase
  • microtubule binding Source: FlyBase
  • phosphatidylinositol-4,5-bisphosphate binding Source: FlyBase
  • structural constituent of cytoskeleton Source: InterPro

GO - Biological processi

  • actin filament capping Source: UniProtKB-KW
  • axon guidance Source: FlyBase
  • axon midline choice point recognition Source: FlyBase
  • axonogenesis Source: FlyBase
  • fusome organization Source: FlyBase
  • long-term strengthening of neuromuscular junction Source: FlyBase
  • maintenance of presynaptic active zone structure Source: FlyBase
  • negative regulation of microtubule depolymerization Source: FlyBase
  • nervous system development Source: FlyBase
  • neuromuscular synaptic transmission Source: FlyBase
  • photoreceptor cell axon guidance Source: FlyBase
  • plasma membrane organization Source: FlyBase
  • regulation of synapse organization Source: FlyBase
  • spectrosome organization Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding, Calmodulin-binding

Enzyme and pathway databases

ReactomeiR-DME-375165. NCAM signaling for neurite out-growth.
R-DME-445095. Interaction between L1 and Ankyrins.
R-DME-5673001. RAF/MAP kinase cascade.
R-DME-6807878. COPI-mediated anterograde transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Spectrin beta chain
Gene namesi
Name:beta-Spec
Synonyms:Spec-b
ORF Names:CG5870
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0250788. beta-Spec.

Subcellular locationi

GO - Cellular componenti

  • apicolateral plasma membrane Source: FlyBase
  • axon Source: FlyBase
  • fusome Source: FlyBase
  • lateral plasma membrane Source: FlyBase
  • lipid particle Source: FlyBase
  • neuromuscular junction Source: FlyBase
  • plasma membrane Source: FlyBase
  • spectrin Source: FlyBase
  • spectrosome Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 22912291Spectrin beta chainPRO_0000073468Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2195 – 21951Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ00963.
PRIDEiQ00963.

PTM databases

iPTMnetiQ00963.

Expressioni

Gene expression databases

BgeeiQ00963.
ExpressionAtlasiQ00963. differential.
GenevisibleiQ00963. DM.

Interactioni

Subunit structurei

Native spectrin molecule is a tetramer composed of two antiparallel heterodimers joined head to head so that each end of the native molecule includes the C-terminus of the alpha subunit and the N-terminus of the beta subunit.

GO - Molecular functioni

  • actin binding Source: FlyBase
  • ankyrin binding Source: FlyBase
  • calmodulin binding Source: FlyBase
  • cytoskeletal protein binding Source: FlyBase
  • microtubule binding Source: FlyBase

Protein-protein interaction databases

BioGridi59071. 9 interactions.
DIPiDIP-18565N.
IntActiQ00963. 3 interactions.
MINTiMINT-922069.
STRINGi7227.FBpp0074228.

Structurei

Secondary structure

1
2291
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2146 – 215712Combined sources
Beta strandi2173 – 218210Combined sources
Beta strandi2185 – 21917Combined sources
Helixi2192 – 21954Combined sources
Beta strandi2219 – 22235Combined sources
Beta strandi2226 – 22305Combined sources
Beta strandi2232 – 22343Combined sources
Beta strandi2236 – 22405Combined sources
Beta strandi2242 – 22443Combined sources
Helixi2245 – 225814Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DRONMR-A2142-2262[»]
ProteinModelPortaliQ00963.
SMRiQ00963. Positions 169-276, 1700-2016, 2141-2262.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00963.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 271271Actin-bindingAdd
BLAST
Domaini50 – 154105CH 1PROSITE-ProRule annotationAdd
BLAST
Domaini169 – 271103CH 2PROSITE-ProRule annotationAdd
BLAST
Repeati298 – 408111Spectrin 1Add
BLAST
Repeati418 – 522105Spectrin 2Add
BLAST
Repeati524 – 633110Spectrin 3Add
BLAST
Repeati635 – 739105Spectrin 4Add
BLAST
Repeati741 – 844104Spectrin 5Add
BLAST
Repeati846 – 950105Spectrin 6Add
BLAST
Repeati952 – 1057106Spectrin 7Add
BLAST
Repeati1059 – 1167109Spectrin 8Add
BLAST
Repeati1169 – 1273105Spectrin 9Add
BLAST
Repeati1275 – 1378104Spectrin 10Add
BLAST
Repeati1380 – 1485106Spectrin 11Add
BLAST
Repeati1487 – 1591105Spectrin 12Add
BLAST
Repeati1593 – 1697105Spectrin 13Add
BLAST
Repeati1699 – 1804106Spectrin 14Add
BLAST
Repeati1806 – 1910105Spectrin 15Add
BLAST
Repeati1912 – 2016105Spectrin 16Add
BLAST
Repeati2018 – 207861Spectrin 17Add
BLAST
Domaini2147 – 2259113PHPROSITE-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.
GeneTreeiENSGT00760000118813.
InParanoidiQ00963.
OMAiRWSQFRE.
OrthoDBiEOG73RB9J.
PhylomeDBiQ00963.

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.

Q00963-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTDISIVRW DPSQGPGNEY IDEYEYDGGN SSSRLFERSR IKALAEERES
60 70 80 90 100
VQKKTFTKWV NSHLCRVNCR IADLYVDMRD GKHLIKLLEV LSGERLPKPT
110 120 130 140 150
KGKMRIHCLE NVDKALQFLR EQRVHLENIG SHDIVDGNAS LNLGLIWTII
160 170 180 190 200
LRFQIQDITI EEVDNKETKS AKDALLLWCQ MKTAGYHNVN VRNFTTSWRD
210 220 230 240 250
GLAFNAIIHK HRPDLVQFEK LSKTNAIHNL NNAFDVAEDK LGLAKLLDAE
260 270 280 290 300
DVFVEHPDEK SIITYVVTYY HYFSKLKQET VQGKRIGKVV GIAMENDKMV
310 320 330 340 350
HDYENFTSDL LKWIETTIQS LGEREFENSL AGVQGQLAQF SNYRTIEKPP
360 370 380 390 400
KFVEKGNLEV LLFTLQSKMR ANNQKPYTPK EGKMISDINK AWERLEKAEH
410 420 430 440 450
ERELALREEL IRQEKLEQLA ARFDRKASMR ETWLSENQRL VSQDNFGFDL
460 470 480 490 500
AAVEAAAKKH EAIETDIFAY EERVQAVVAV CDELESERYH DVKRILLRKD
510 520 530 540 550
NVMRLWTYLL ELLRARRMRL EISLQLQQNF QEMLYILDNM EEIKQLLMTD
560 570 580 590 600
DYGKHLMGVE DLLQKHSLVE ADINILGERV KVVVQNSQKF LSDDPESYKP
610 620 630 640 650
CDPEIIVSRV QQLEDAYAEL VRLAVERRSR LEESRKLWQF YWDTADEENW
660 670 680 690 700
IKEKEQIVST DEVGHDLTTV NLMLSKHKAL ESEITSHDPQ LQNVAKVGSE
710 720 730 740 750
LITEGHFGAD RIKDRLKEIL NKWDHLLDLT KYRRQRLENA VEYFQLFADA
760 770 780 790 800
DDVDNWMLDT LRIVSSEDVG RDEANVQSLL KKHKDVADEL KNYAEVIDAL
810 820 830 840 850
HKQAESLKLN EAEKANVDKR LEAIDNRYKE LTELAKLRKQ RLLDALSLYK
860 870 880 890 900
LMSEADGVEQ WIKEKTKMLD TMTPGKDIED VEIMKHRFEG FDKEMNANAS
910 920 930 940 950
RVAVVNQLAR QLLHVEHPNS DEILERQNHL NQEWSTLREK AEAKMDDLKS
960 970 980 990 1000
AHGVQTFYIE CRETISWIED KKRILTETDS LEMDLTGVMT LQRRLSGMDR
1010 1020 1030 1040 1050
DLAAIQAKLS SLEREANSIE DEHPEEAKII RERIAQIELI WEQLTQMLKE
1060 1070 1080 1090 1100
RDSKLEEAGD LHRFLRDLDH FQTWLTKTQT DVASEDTPTS LPEAEKLLNQ
1110 1120 1130 1140 1150
HQSIREEIDN YTEDYKNMME YGERLTSEGS TSDDPQYMFL RERLNALKDG
1160 1170 1180 1190 1200
WEELHQMWEN RQVLLSQSLD QQLFNRDARQ TEVLLSQQEH FLSKDDTPVN
1210 1220 1230 1240 1250
LEQAENQLKR HEAFLTTMEA NDDKINTLLQ VADTLVEKDH FDADKIGKRA
1260 1270 1280 1290 1300
ENITGRRDDN RQRALDQHEK LKNQVKLHEF LQDLEELAEW VQEKYATSQD
1310 1320 1330 1340 1350
ESYRSAKTIH SKWTRHQAFE AEIAANKERL FEAEKSAQEL SKEKPEFKDV
1360 1370 1380 1390 1400
IEPKLKELAK QFDDLEVHTK EKGAMLFDAN REVLVQQTCD DIDSYITDLE
1410 1420 1430 1440 1450
KQIVSGDTAN DLTSVNILMQ KQQVIQTQMA VKARQVEEID KQTEYLQKTV
1460 1470 1480 1490 1500
PEEKIEPIVV KKTAVLERFE KIKAPLLERQ KALEKKKEAF QFCRDVEDEK
1510 1520 1530 1540 1550
LWIDEKLPVA NSPDYGNSLF NVHVLKKKNQ SLATEIDNHE PRINAICNNG
1560 1570 1580 1590 1600
RKLIDEGHED AKKFEALISD LTQKWQELKD AIENRRKHLL ESEKVQQYFF
1610 1620 1630 1640 1650
DAQEAESWMS EQELYMMVED RGKDEISAQN LMKKHENLEQ SVEDYANTIR
1660 1670 1680 1690 1700
QLGEVARQFS GDDISSGDAV AVKQSQLDKL YAGLKDLAGE RRARLNEALQ
1710 1720 1730 1740 1750
LFMLSREVDD LEQWITDREV VAGSQELGQD FDHVTLLSER FNEFARDTEA
1760 1770 1780 1790 1800
VGGERVAKVN GIADNLIQAG HSDSATIAEW KDNLNESWQD LLELIETRTQ
1810 1820 1830 1840 1850
MLAASRELHK FFHDCKDVLG RILEKQHGVS DELGRDAGSV STLQRKHYNF
1860 1870 1880 1890 1900
LQDLITLYSQ VQQIQEESAK LQDAYAGDKA KEITNREQEV LHAWDNLQAM
1910 1920 1930 1940 1950
CDARKQKLAD TGDLFRFFNM VRILMIWMED LVRQMNTSEK PRDVSGVELL
1960 1970 1980 1990 2000
MNNHQSLKAE IDTREDNFGA CISLGKELLT RNHYASADIK DRLMTLSNSR
2010 2020 2030 2040 2050
NALLRRWEER WENLQLILEV YQFARDAAVA EAWLIAQEPY LLSSELGHTI
2060 2070 2080 2090 2100
DEVENLIKKH EAFEKSAAAQ EERFSALERL TTFELKEMKR RQELAEEAER
2110 2120 2130 2140 2150
QRIKEEQEAK AASEAAEQAK REAERRDDVD VGASHDDSER GGTPGAGEGH
2160 2170 2180 2190 2200
EGYVTRKHEW DSTTKKASNR SWDKVYMAAK AGRISFYKDQ KGYKSNPELT
2210 2220 2230 2240 2250
FRGEPSYDLQ NAAIEIASDY TKKKHVLRVK LANGALFLLQ AHDDTEMSQW
2260 2270 2280 2290
VTSLKAQSDS TAVAASRSQT LPATSQKDEP KRRSFFTLKK K
Length:2,291
Mass (Da):265,739
Last modified:June 1, 2001 - v2
Checksum:i5CDFB0C548BBC39B
GO

Sequence cautioni

The sequence AAR82828.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2278 – 22781D → Y in AAA28399 (PubMed:1631106).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M92288 mRNA. Translation: AAA28399.1.
AE014298 Genomic DNA. Translation: AAF48751.1.
BT011160 mRNA. Translation: AAR82828.1. Sequence problems.
PIRiA46147.
RefSeqiNP_523388.1. NM_078664.3.
UniGeneiDm.7022.

Genome annotation databases

EnsemblMetazoaiFBtr0074454; FBpp0074228; FBgn0250788.
GeneIDi32746.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M92288 mRNA. Translation: AAA28399.1.
AE014298 Genomic DNA. Translation: AAF48751.1.
BT011160 mRNA. Translation: AAR82828.1. Sequence problems.
PIRiA46147.
RefSeqiNP_523388.1. NM_078664.3.
UniGeneiDm.7022.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DRONMR-A2142-2262[»]
ProteinModelPortaliQ00963.
SMRiQ00963. Positions 169-276, 1700-2016, 2141-2262.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59071. 9 interactions.
DIPiDIP-18565N.
IntActiQ00963. 3 interactions.
MINTiMINT-922069.
STRINGi7227.FBpp0074228.

PTM databases

iPTMnetiQ00963.

Proteomic databases

PaxDbiQ00963.
PRIDEiQ00963.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0074454; FBpp0074228; FBgn0250788.
GeneIDi32746.

Organism-specific databases

CTDi32746.
FlyBaseiFBgn0250788. beta-Spec.

Phylogenomic databases

eggNOGiKOG0035. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118813.
InParanoidiQ00963.
OMAiRWSQFRE.
OrthoDBiEOG73RB9J.
PhylomeDBiQ00963.

Enzyme and pathway databases

ReactomeiR-DME-375165. NCAM signaling for neurite out-growth.
R-DME-445095. Interaction between L1 and Ankyrins.
R-DME-5673001. RAF/MAP kinase cascade.
R-DME-6807878. COPI-mediated anterograde transport.

Miscellaneous databases

ChiTaRSibeta-Spec. fly.
EvolutionaryTraceiQ00963.
GenomeRNAii32746.
NextBioi780161.
PROiQ00963.

Gene expression databases

BgeeiQ00963.
ExpressionAtlasiQ00963. differential.
GenevisibleiQ00963. DM.

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. "The complete sequence of Drosophila beta-spectrin reveals supra-motifs comprising eight 106-residue segments."
    Byers T.J., Brandin E., Lue R., Winograd E., Branton D.
    Proc. Natl. Acad. Sci. U.S.A. 89:6187-6191(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1404.
    Strain: Berkeley.
    Tissue: Testis.
  5. "Drosophilia spectrin. I. Characterization of the purified protein."
    Dubreuil R., Byers T.J., Branton D., Goldstein L.S.B., Kiehart D.P.
    J. Cell Biol. 105:2095-2102(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2195, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  7. "Solution structure of the pleckstrin homology domain of Drosophila beta-spectrin."
    Zhang P., Talluri S., Deng H., Branton D., Wagner G.
    Structure 3:1185-1195(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 2145-2262.

Entry informationi

Entry nameiSPTCB_DROME
AccessioniPrimary (citable) accession number: Q00963
Secondary accession number(s): Q6NNX2, Q9VX30
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.