SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P13395

- SPTCA_DROME

UniProt

P13395 - SPTCA_DROME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Spectrin alpha chain
Gene
alpha-Spec, SPEC-A, CG1977
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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. Essential for larval survival and development. Stabilizes cell to cell interactions that are critical for the maintenance of cell shape and subcellular organization within embryonic tissues. Lva and spectrin may form a Golgi-based scaffold that mediates interaction of Golgi bodies with microtubules and facilitates Golgi-derived membrane secretion required for the formation of furrows during cellularization.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi2278 – 2289121 Reviewed prediction
Add
BLAST
Calcium bindingi2321 – 2332122 Reviewed prediction
Add
BLAST

GO - Molecular functioni

  1. actin binding Source: FlyBase
  2. calcium ion binding Source: InterPro
  3. cytoskeletal protein binding Source: FlyBase
  4. microtubule binding Source: FlyBase

GO - Biological processi

  1. actin filament capping Source: UniProtKB-KW
  2. axon midline choice point recognition Source: FlyBase
  3. central nervous system development Source: FlyBase
  4. fusome organization Source: FlyBase
  5. germ-line cyst formation Source: FlyBase
  6. germarium-derived female germ-line cyst formation Source: FlyBase
  7. germarium-derived oocyte fate determination Source: FlyBase
  8. long-term strengthening of neuromuscular junction Source: FlyBase
  9. maintenance of presynaptic active zone structure Source: FlyBase
  10. negative regulation of microtubule depolymerization Source: FlyBase
  11. neuromuscular synaptic transmission Source: FlyBase
  12. oocyte construction Source: FlyBase
  13. ovarian follicle cell development Source: FlyBase
  14. plasma membrane organization Source: FlyBase
  15. regulation of cell shape Source: UniProtKB-KW
  16. regulation of synapse organization Source: FlyBase
  17. spectrosome organization Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Biological processi

Cell shape

Keywords - Ligandi

Actin-binding, Calcium, Calmodulin-binding, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_79920. Interaction between L1 and Ankyrins.
SignaLinkiP13395.

Names & Taxonomyi

Protein namesi
Recommended name:
Spectrin alpha chain
Gene namesi
Name:alpha-Spec
Synonyms:SPEC-A
ORF Names:CG1977
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0250789. alpha-Spec.

Subcellular locationi

Cytoplasmcytoskeleton. Golgi apparatus
Note: Near the inner surface of the plasma membrane of nearly all cells. Lva-alpha-spectrin complexes are found at the Golgi.1 Publication

GO - Cellular componenti

  1. Golgi apparatus Source: FlyBase
  2. basolateral plasma membrane Source: FlyBase
  3. cell cortex Source: FlyBase
  4. fusome Source: FlyBase
  5. lipid particle Source: FlyBase
  6. neuromuscular junction Source: FlyBase
  7. plasma membrane Source: FlyBase
  8. spectrin Source: FlyBase
  9. spectrosome Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Golgi apparatus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24152415Spectrin alpha chain
PRO_0000073467Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1032 – 10321Phosphoserine1 Publication
Modified residuei1034 – 10341Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP13395.
PRIDEiP13395.

Expressioni

Tissue specificityi

A substantial pool of maternal protein in the egg undergoes dynamic changes in distribution early in embryogenesis. In gastrulated embryo, the highest level of protein is found in the respiratory tract cells and the lowest in parts of the forming gut.1 Publication

Developmental stagei

Expressed both maternally and zygotically.

Gene expression databases

BgeeiP13395.

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. Interacts with calmodulin in a calcium-dependent manner, interacts with F-actin and also interacts with Lva. Interacts with Ten-m.2 Publications

Protein-protein interaction databases

BioGridi63763. 17 interactions.
DIPiDIP-17516N.
IntActiP13395. 2 interactions.
MINTiMINT-950099.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1393 – 142230
Helixi1428 – 149467

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2SPCX-ray1.80A/B1391-1497[»]
ProteinModelPortaliP13395.
SMRiP13395. Positions 11-2258, 2260-2413.

Miscellaneous databases

EvolutionaryTraceiP13395.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati18 – 122105Spectrin 1
Add
BLAST
Repeati123 – 228106Spectrin 2
Add
BLAST
Repeati229 – 334106Spectrin 3
Add
BLAST
Repeati335 – 440106Spectrin 4
Add
BLAST
Repeati441 – 546106Spectrin 5
Add
BLAST
Repeati547 – 651105Spectrin 6
Add
BLAST
Repeati652 – 757106Spectrin 7
Add
BLAST
Repeati758 – 863106Spectrin 8
Add
BLAST
Repeati864 – 969106Spectrin 9
Add
BLAST
Repeati970 – 104374Spectrin 10
Add
BLAST
Domaini970 – 102960SH3
Add
BLAST
Repeati1044 – 1151108Spectrin 11
Add
BLAST
Repeati1152 – 1257106Spectrin 12
Add
BLAST
Repeati1258 – 1363106Spectrin 13
Add
BLAST
Repeati1364 – 1469106Spectrin 14
Add
BLAST
Repeati1470 – 1576107Spectrin 15
Add
BLAST
Repeati1577 – 1682106Spectrin 16
Add
BLAST
Repeati1683 – 1788106Spectrin 17
Add
BLAST
Repeati1789 – 1894106Spectrin 18
Add
BLAST
Repeati1895 – 2001107Spectrin 19
Add
BLAST
Repeati2002 – 2115114Spectrin 20
Add
BLAST
Repeati2116 – 2229114Spectrin 21
Add
BLAST
Repeati2230 – 2335106Spectrin 22
Add
BLAST
Domaini2265 – 230036EF-hand 1
Add
BLAST
Domaini2308 – 234336EF-hand 2
Add
BLAST

Sequence similaritiesi

Belongs to the spectrin family.
Contains 2 EF-hand domains.
Contains 1 SH3 domain.
Contains 22 spectrin repeats.

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiNOG237318.
GeneTreeiENSGT00750000117361.
InParanoidiP13395.
KOiK06114.
OrthoDBiEOG7GXP9K.
PhylomeDBiP13395.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR014837. EF-hand_Ca_insen.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001452. SH3_domain.
IPR018159. Spectrin/alpha-actinin.
IPR013315. Spectrin_alpha_SH3.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamiPF13499. EF-hand_7. 1 hit.
PF08726. EFhand_Ca_insen. 1 hit.
PF00018. SH3_1. 1 hit.
PF00435. Spectrin. 20 hits.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
PR01887. SPECTRNALPHA.
SMARTiSM00054. EFh. 2 hits.
SM00326. SH3. 1 hit.
SM00150. SPEC. 20 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P13395-1 [UniParc]FASTAAdd to Basket

« Hide

MENFTPKEVK ILETVEDIQE RREQVLSRYN DFKIETRQKR EKLEDSRRFQ     50
YFKRDADELE SWIHEKLQAA SEESYRDPTN LQAKIQKHQA FEAEVSAHSN 100
AIVSLDNTGQ EMINQQHFAS ESIQVRLDEL HKLWELLLSR LAEKGLKLQQ 150
ALVLVQFLRQ CEEVMFWIKD KETFVTADEF GQDLEHVEVL QRKFDEFQKD 200
MASQEYRVTE VNQLADKLVQ DGHPERDTIT KRKEELNEAW QRLKQLAIVR 250
QEKLFGAHEI QRFNRDADET VAWIAEKDVV LSSDDYGRDL ASVQALQRKH 300
EGVERDLAAL EDKVSTLGAE AQRLCSIHAD HSDQIRDKQA EIANYWQSLT 350
TKARERKQKL DESYYLHRFL ADFRDLVSWI NGMKAIISAD ELAKDVAGAE 400
ALLERHQEHK GEIDAREDSF KLTTESGQKL LEREHYAAAE IQEKLAALEN 450
DKSSLLSLWE DRRILYEQCM DLQLFYRDTE QADTWMAKQE AFLANEDLGD 500
SLDSVEALIK KHEDFEKSLA AQEEKIKALD IFATKLIDGQ HYAADDVAQR 550
RQMLLARRAA LQEKSSKRRQ LLEDSNRYQQ FERDCDETKG WISEKLKFAT 600
DDSYLDPTNL NGKMQKHQNF EHELNANKSR IEDITNVGTE LIEKQHYAAD 650
QINTRMQEIV VLWETLVQAS DKKGTKLNEA CQQQQFNRTI EDIELWLSEI 700
EGQLLSEDHG KDLTSVQNLQ KKHALLEADV MAHQDRIESI KVAANKFIES 750
GHFDADNIRN KEGNLSARYA ALAAPMGERK QHLLDSLQVQ QLFRDLEDEA 800
AWIREKEPIA ASTNRGRDLI GVQNLIKKHQ AVLAEINNHE ARLLNVISSG 850
ENMLKDQPFA SDDIRQRLEA LQEQWNTLKE KSSQRKQDLD DSLQAHQYFA 900
DANEAESWMR EKEPIATGSD YGKDEDSSEA LLKKHEALVS DLEAFGNTIQ 950
ALQEQAKNCR QQETPVVDIT GKECVVALYD YTEKSPREVS MKKGDVLTLL 1000
NSNNKDWWKV EVNDRQGFVP AAYIKKIDAG LSASQQNLVD NHSIAKRQNQ 1050
INSQYDNLLA LARERQNKLN ETVKAYVLVR EAADLAQWIR DKENHAQIAD 1100
VVGEDLEEVE VLQKKFDDFN DDLKANEVRL ANMNEIAVQL TSLGQTEAAL 1150
KIQTQMQDLN EKWNNLQTLT AEKASQLGSA HEVQRFHRDI DETKDWIAEK 1200
ANALNNDDLG KDLRSVQTLQ RKHEGVERDL AALRDKIRQL DETANRLMQS 1250
HPDTAEQTYA KQKEINEMWD QIITKSTARK EKLLDSYDLQ RFLSDYRDLL 1300
AWINSMMSLV TSDELANDVT GAEALIERHQ EHRTEIDARA GTFGAFEQFG 1350
NELLQANHYA SPEIKEKIED LAKAREDLEK AWTERRLQLE QNLDLQLYMR 1400
DCELAESWMS AREAFLNADD DANAGGNVEA LIKKHEDFDK AINGHEQKIA 1450
ALQTVADQLI AQNHYASNLV DEKRKQVLER WRHLKEGLIE KRSRLGDEQT 1500
LQQFSRDADE IENWIAEKLQ LATEESYKDP ANIQSKHQKH QAFEAELAAN 1550
ADRIQSVLAM GGNLIDKKQC SGSEDAVQKR LTQIADQWEY LTHKTTEKSL 1600
KLKEANKQRT YIAAVKDLDF WLGEVESLLT TEDSGKDLAS VQNLMKKHQL 1650
VEADIVAHED RIKDMNNQAD SLVESGQFDT AGIQEKRQSI NERYERICNL 1700
AAHRQARLNE ALTLHQFFRD IADEESWIKE KKLLVGSDDY GRDLTGVQNL 1750
KKKHKRLEAE LGSHEPAIQA VQEAGEKLMD VSNLGVPEIE QRLKALNQAW 1800
AELKNLAATR GQKLDESLTY QQFLAQVEEE EAWITEKQQL LSVEDYGDSM 1850
AAVQGLLKKH DAFETDFTAH KDRCSLICDQ GSELVEAKNH HGESIAQRCQ 1900
QLRLKLDNLS ALAARRKGAL LDNSAYLQFM WKADVVESWI DDKENYVRSD 1950
EFGRDLSTVQ TLLTKQETFD AGLNAFEQEG IHNITALKDQ LINASHAQSP 2000
AILKRHGDVI ARWQKLRDAS NTRKDRLLAM QEQFRQIEEL YLTFAKKASA 2050
FNSWFENAEE DLTDPVRCNS IEEIRALRDA HAQFQASLSS AEADFKALAA 2100
LDQKIKSFNV GPNPYTWFTM EALEETWRNL QKIIEERDGE LAKEAKRQEE 2150
NDKLRKEFAK HANLFHQWLT ETRTSMMEGS GSLEQQLEAL RVKATEVRAR 2200
RVDLKKIEEL GALLEEHLIL DNRYTEHSTV GLAQQWDQLD QLSMRMQHNL 2250
EQQIQARNHS GVSEDSLKEF SMMFKHFDKD KSGKLNHQEF KSCLRALGYD 2300
LPMVEEGQPD PEFEAILDVV DPNRDGYVSL QEYIAFMISK ETENVQSYEE 2350
IENAFRAITA ADRPYVTKEE LYCNLTKDMA DYCVQRMKPF SEPRSGQPIK 2400
DALDYIDFTR TLFQN 2415
Length:2,415
Mass (Da):278,303
Last modified:June 20, 2001 - v2
Checksum:iF1F72FB990EB0A37
GO

Sequence cautioni

The sequence ABA81823.1 differs from that shown. Reason: Frameshift at position 1549.
The sequence AAL39886.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti110 – 1101Q → D in AAB29441. 1 Publication
Sequence conflicti212 – 2121N → I in ABA81823. 1 Publication
Sequence conflicti337 – 3371D → G in ABA81823. 1 Publication
Sequence conflicti651 – 6511Q → L in ABA81823. 1 Publication
Sequence conflicti1555 – 15551Q → H in AAL39886. 1 Publication
Sequence conflicti1562 – 15621G → E in ABA81823. 1 Publication
Sequence conflicti1668 – 16681Q → R in AAA28907. 1 Publication
Sequence conflicti1908 – 19081N → S in ABA81823. 1 Publication
Sequence conflicti2203 – 22031D → G in ABA81823. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M26400 mRNA. Translation: AAA28907.1.
AE014296 Genomic DNA. Translation: AAF47569.1.
BT023889 mRNA. Translation: ABA81823.1. Frameshift.
S67762 Genomic DNA. Translation: AAB29441.2.
S67765 Genomic DNA. Translation: AAB29442.1.
AY069741 mRNA. Translation: AAL39886.1. Different initiation.
PIRiA33733.
RefSeqiNP_476739.1. NM_057391.4.
UniGeneiDm.7397.

Genome annotation databases

EnsemblMetazoaiFBtr0072789; FBpp0072672; FBgn0250789.
GeneIDi38231.
KEGGidme:Dmel_CG1977.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M26400 mRNA. Translation: AAA28907.1 .
AE014296 Genomic DNA. Translation: AAF47569.1 .
BT023889 mRNA. Translation: ABA81823.1 . Frameshift.
S67762 Genomic DNA. Translation: AAB29441.2 .
S67765 Genomic DNA. Translation: AAB29442.1 .
AY069741 mRNA. Translation: AAL39886.1 . Different initiation.
PIRi A33733.
RefSeqi NP_476739.1. NM_057391.4.
UniGenei Dm.7397.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2SPC X-ray 1.80 A/B 1391-1497 [» ]
ProteinModelPortali P13395.
SMRi P13395. Positions 11-2258, 2260-2413.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 63763. 17 interactions.
DIPi DIP-17516N.
IntActi P13395. 2 interactions.
MINTi MINT-950099.

Proteomic databases

PaxDbi P13395.
PRIDEi P13395.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0072789 ; FBpp0072672 ; FBgn0250789 .
GeneIDi 38231.
KEGGi dme:Dmel_CG1977.

Organism-specific databases

CTDi 38231.
FlyBasei FBgn0250789. alpha-Spec.

Phylogenomic databases

eggNOGi NOG237318.
GeneTreei ENSGT00750000117361.
InParanoidi P13395.
KOi K06114.
OrthoDBi EOG7GXP9K.
PhylomeDBi P13395.

Enzyme and pathway databases

Reactomei REACT_79920. Interaction between L1 and Ankyrins.
SignaLinki P13395.

Miscellaneous databases

EvolutionaryTracei P13395.
GenomeRNAii 38231.
NextBioi 807649.
PROi P13395.

Gene expression databases

Bgeei P13395.

Family and domain databases

Gene3Di 1.10.238.10. 2 hits.
InterProi IPR011992. EF-hand-dom_pair.
IPR014837. EF-hand_Ca_insen.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001452. SH3_domain.
IPR018159. Spectrin/alpha-actinin.
IPR013315. Spectrin_alpha_SH3.
IPR002017. Spectrin_repeat.
[Graphical view ]
Pfami PF13499. EF-hand_7. 1 hit.
PF08726. EFhand_Ca_insen. 1 hit.
PF00018. SH3_1. 1 hit.
PF00435. Spectrin. 20 hits.
[Graphical view ]
PRINTSi PR00452. SH3DOMAIN.
PR01887. SPECTRNALPHA.
SMARTi SM00054. EFh. 2 hits.
SM00326. SH3. 1 hit.
SM00150. SPEC. 20 hits.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
PROSITEi PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The complete sequence of Drosophila alpha-spectrin: conservation of structural domains between alpha-spectrins and alpha-actinin."
    Dubreuil R.R., Byers T.J., Sillman A.L., Bar-Zvi D., Goldstein L.S.B., Branton D.
    J. Cell Biol. 109:2197-2205(1989) [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. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. "Cell shape and interaction defects in alpha-spectrin mutants of Drosophila melanogaster."
    Lee J.K., Coyne R.S., Dubreuil R.R., Goldstein L.S.B., Branton D.
    J. Cell Biol. 123:1797-1809(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-150 AND 2192-2415, FUNCTION.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1539-2415.
    Strain: Berkeley.
    Tissue: Larva and Pupae.
  7. "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.
  8. "Lava lamp, a novel peripheral Golgi protein, is required for Drosophila melanogaster cellularization."
    Sisson J.C., Field C., Ventura R., Royou A., Sullivan W.
    J. Cell Biol. 151:905-918(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
  9. "Drosophila spectrin: the membrane skeleton during embryogenesis."
    Pesacreta T.C., Byers T.J., Dubreuil R., Kiehart D.P., Branton D.
    J. Cell Biol. 108:1697-1709(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  10. "The Drosophila cell survival gene discs lost encodes a cytoplasmic Codanin-1-like protein, not a homolog of tight junction PDZ protein Patj."
    Pielage J., Stork T., Bunse I., Klaembt C.
    Dev. Cell 5:841-851(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE STRUCTURE.
  11. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
    Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
    Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1034, IDENTIFICATION BY MASS SPECTROMETRY.
  12. "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-1032 AND SER-1034, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  13. "Trans-synaptic Teneurin signalling in neuromuscular synapse organization and target choice."
    Mosca T.J., Hong W., Dani V.S., Favaloro V., Luo L.
    Nature 484:237-241(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TEN-M.
  14. "Crystal structure of the repetitive segments of spectrin."
    Yan Y., Winograd E., Viel A., Cronin T., Harrison S.C., Branton D.
    Science 262:2027-2030(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1391-1497.

Entry informationi

Entry nameiSPTCA_DROME
AccessioniPrimary (citable) accession number: P13395
Secondary accession number(s): Q26340
, Q3KN50, Q8SZW7, Q9W085
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: June 20, 2001
Last modified: September 3, 2014
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

Its transcript shares the first untranslated exon with the dlt transcript, suggesting a common regulation.

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

External Data

Dasty 3

Similar proteinsi