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Protein mini spindles

 MSPS_DROME              Reviewed;        2042 AA.
Q9VEZ3; Q4QQC0;
02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 3.
16-JAN-2019, entry version 151.
RecName: Full=Protein mini spindles;
Name=msps; ORFNames=CG5000 {ECO:0000312|FlyBase:FBgn0027948};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[4]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10477755; DOI=10.1083/jcb.146.5.1005;
Cullen C.F., Deak P., Glover D.M., Ohkura H.;
"mini spindles: A gene encoding a conserved microtubule-associated
protein required for the integrity of the mitotic spindle in
Drosophila.";
J. Cell Biol. 146:1005-1018(1999).
[5]
FUNCTION, INTERACTION WITH TACC, AND SUBCELLULAR LOCATION.
PubMed=11433295; DOI=10.1038/35083025;
Cullen C.F., Ohkura H.;
"Msps protein is localized to acentrosomal poles to ensure bipolarity
of Drosophila meiotic spindles.";
Nat. Cell Biol. 3:637-642(2001).
[6]
FUNCTION.
PubMed=15530399; DOI=10.1016/j.cub.2004.10.023;
Moon W., Hazelrigg T.;
"The Drosophila microtubule-associated protein mini spindles is
required for cytoplasmic microtubules in oogenesis.";
Curr. Biol. 14:1957-1961(2004).
[7]
FUNCTION.
PubMed=16303556; DOI=10.1016/j.cub.2005.09.054;
Goshima G., Wollman R., Stuurman N., Scholey J.M., Vale R.D.;
"Length control of the metaphase spindle.";
Curr. Biol. 15:1979-1988(2005).
[8]
FUNCTION.
PubMed=15775959; DOI=10.1038/sj.emboj.7600629;
Brittle A.L., Ohkura H.;
"Mini spindles, the XMAP215 homologue, suppresses pausing of
interphase microtubules in Drosophila.";
EMBO J. 24:1387-1396(2005).
[9]
FUNCTION, AND INTERACTION WITH DGT6.
PubMed=19836241; DOI=10.1016/j.cub.2009.09.043;
Bucciarelli E., Pellacani C., Naim V., Palena A., Gatti M.,
Somma M.P.;
"Drosophila Dgt6 interacts with Ndc80, Msps/XMAP215, and gamma-tubulin
to promote kinetochore-driven MT formation.";
Curr. Biol. 19:1839-1845(2009).
[10]
FUNCTION, TOG DOMAIN, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
546-LYS--LYS-549 AND 1102-LYS--ARG-1107.
PubMed=21965297; DOI=10.1091/mbc.E11-06-0520;
Currie J.D., Stewman S., Schimizzi G., Slep K.C., Ma A., Rogers S.L.;
"The microtubule lattice and plus-end association of Drosophila Mini
spindles is spatially regulated to fine-tune microtubule dynamics.";
Mol. Biol. Cell 22:4343-4361(2011).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=26953351; DOI=10.1083/jcb.201503047;
Chen K., Koe C.T., Xing Z.B., Tian X., Rossi F., Wang C., Tang Q.,
Zong W., Hong W.J., Taneja R., Yu F., Gonzalez C., Wu C., Endow S.,
Wang H.;
"Arl2- and Msps-dependent microtubule growth governs asymmetric
division.";
J. Cell Biol. 212:661-676(2016).
[12]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 267-505, TOG DOMAIN,
FUNCTION, AND MUTAGENESIS OF TRP-21 AND TRP-292.
PubMed=17889670; DOI=10.1016/j.molcel.2007.07.023;
Slep K.C., Vale R.D.;
"Structural basis of microtubule plus end tracking by XMAP215, CLIP-
170, and EB1.";
Mol. Cell 27:976-991(2007).
[13]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 848-1084, AND TOG DOMAIN.
PubMed=24966168; DOI=10.1091/mbc.E13-08-0501;
Fox J.C., Howard A.E., Currie J.D., Rogers S.L., Slep K.C.;
"The XMAP215 family drives microtubule polymerization using a
structurally diverse TOG array.";
Mol. Biol. Cell 25:2375-2392(2014).
[14]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 582-825, AND TOG DOMAIN.
PubMed=25720490; DOI=10.1074/jbc.M114.633826;
Howard A.E., Fox J.C., Slep K.C.;
"Drosophila melanogaster mini spindles TOG3 utilizes unique structural
elements to promote domain stability and maintain a TOG1- and TOG2-
like tubulin-binding surface.";
J. Biol. Chem. 290:10149-10162(2015).
-!- FUNCTION: Binds to the plus end of microtubules and regulates
microtubule dynamics and microtubule organization. Promotes
cytoplasmic microtubule nucleation and elongation. May act as a
microtubule antipause factor that rapidly catalyzes the transition
from pause to either growth or shrinkage. Involved in mitotic
spindle elongation. Involved in the establishment of cell polarity
and mitotic spindle orientation in neuroblasts. Required for
maintaining the bipolarity of acentrosomal meiotic spindles; the
function is dependent on tacc and involves ncd. Involved in oocyte
microtubule cytoskeleton organization and bicoid mRNA
localization. Seems to be involved in elongation of kinetochore-
derived microtubule fibers. {ECO:0000269|PubMed:10477755,
ECO:0000269|PubMed:11433295, ECO:0000269|PubMed:15530399,
ECO:0000269|PubMed:15775959, ECO:0000269|PubMed:16303556,
ECO:0000269|PubMed:17889670, ECO:0000269|PubMed:26953351,
ECO:0000305|PubMed:21965297}.
-!- SUBUNIT: Interacts with tacc, dgt6. {ECO:0000269|PubMed:11433295,
ECO:0000269|PubMed:19836241}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:10477755,
ECO:0000269|PubMed:26953351}. Cytoplasm, cytoskeleton, spindle
{ECO:0000269|PubMed:10477755, ECO:0000269|PubMed:11433295}.
Note=Localizes to the plus ends of growing microtubules in the
cell interior in a Eb1-depenedent manner. Localizes to the lattice
of growing and shrinking microtubule in a discontinuous pattern in
the peripheral regions of interphase cells. Localized at
acentrosomal poles of female meiotic spindle.
{ECO:0000269|PubMed:11433295, ECO:0000269|PubMed:21965297}.
-!- DOMAIN: The TOG (tumor overexpressed gene) domains are arranged in
a N-terminal pentameric array with each domain composed of six
(for the most part non-canonical) HEAT repeats forming a oblong
paddle-like structure. Intra-HEAT loops are positioned along a
face of the TOG domain and bind to a single alpha/beta-tubulin
heterodimer. The TOG domains in the array seem to be structurally
and functionally polarized. Differential functions may range from
microtubule (MT) lattice binding and/or free tubulin heterodimer
binding to potentiating stable incorporation of tubulin into the
MT lattice. TOG 1-2 show strong and TOG 3-4 weak tubulin binding;
TOG 1-5 are required for full ability to promote MT
polymerization. {ECO:0000305|PubMed:21965297,
ECO:0000305|PubMed:24966168, ECO:0000305|PubMed:25720490}.
-!- SIMILARITY: Belongs to the TOG/XMAP215 family. {ECO:0000305}.
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EMBL; AE014297; AAF55269.3; -; Genomic_DNA.
EMBL; BT023496; AAY84896.1; -; mRNA.
RefSeq; NP_732105.2; NM_169698.3.
UniGene; Dm.4280; -.
PDB; 2QK2; X-ray; 2.10 A; A=267-505.
PDB; 4QMH; X-ray; 1.65 A; A=848-1084.
PDB; 4Y5J; X-ray; 2.30 A; A=582-825.
PDB; 5VJC; X-ray; 2.00 A; A/B=1141-1411.
PDBsum; 2QK2; -.
PDBsum; 4QMH; -.
PDBsum; 4Y5J; -.
PDBsum; 5VJC; -.
ProteinModelPortal; Q9VEZ3; -.
SMR; Q9VEZ3; -.
IntAct; Q9VEZ3; 6.
PRIDE; Q9VEZ3; -.
EnsemblMetazoa; FBtr0301480; FBpp0290695; FBgn0027948.
GeneID; 41952; -.
KEGG; dme:Dmel_CG5000; -.
UCSC; CG5000-RA; d. melanogaster.
CTD; 41952; -.
FlyBase; FBgn0027948; msps.
eggNOG; KOG1820; Eukaryota.
eggNOG; ENOG410XPTW; LUCA.
GeneTree; ENSGT00390000014757; -.
KO; K16803; -.
OMA; NFQVSAK; -.
EvolutionaryTrace; Q9VEZ3; -.
GenomeRNAi; 41952; -.
PRO; PR:Q9VEZ3; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0027948; Expressed in 33 organ(s), highest expression level in head.
ExpressionAtlas; Q9VEZ3; baseline and differential.
GO; GO:0005813; C:centrosome; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0000776; C:kinetochore; IBA:GO_Central.
GO; GO:0005875; C:microtubule associated complex; ISS:FlyBase.
GO; GO:0035371; C:microtubule plus-end; IDA:FlyBase.
GO; GO:0000922; C:spindle pole; IBA:GO_Central.
GO; GO:0008017; F:microtubule binding; ISS:FlyBase.
GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
GO; GO:0015631; F:tubulin binding; IDA:FlyBase.
GO; GO:0007411; P:axon guidance; IMP:FlyBase.
GO; GO:0045450; P:bicoid mRNA localization; IMP:FlyBase.
GO; GO:0051298; P:centrosome duplication; IBA:GO_Central.
GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:FlyBase.
GO; GO:0007029; P:endoplasmic reticulum organization; IMP:FlyBase.
GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:FlyBase.
GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IBA:GO_Central.
GO; GO:0045196; P:establishment or maintenance of neuroblast polarity; IMP:FlyBase.
GO; GO:0007143; P:female meiotic nuclear division; IMP:FlyBase.
GO; GO:0046785; P:microtubule polymerization; IBA:GO_Central.
GO; GO:0007017; P:microtubule-based process; ISS:FlyBase.
GO; GO:0000278; P:mitotic cell cycle; HMP:FlyBase.
GO; GO:0000022; P:mitotic spindle elongation; IMP:FlyBase.
GO; GO:0016325; P:oocyte microtubule cytoskeleton organization; IMP:FlyBase.
GO; GO:0048477; P:oogenesis; IMP:FlyBase.
GO; GO:0090063; P:positive regulation of microtubule nucleation; IDA:FlyBase.
GO; GO:0007344; P:pronuclear fusion; IMP:FlyBase.
GO; GO:0007051; P:spindle organization; IBA:GO_Central.
Gene3D; 1.25.10.10; -; 5.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR024395; CLASP_N_dom.
InterPro; IPR021133; HEAT_type_2.
InterPro; IPR034085; TOG.
Pfam; PF12348; CLASP_N; 2.
SMART; SM01349; TOG; 5.
SUPFAM; SSF48371; SSF48371; 3.
PROSITE; PS50077; HEAT_REPEAT; 1.
1: Evidence at protein level;
3D-structure; Cell cycle; Cell division; Complete proteome; Cytoplasm;
Cytoskeleton; Meiosis; Mitosis; Reference proteome; Repeat.
CHAIN 1 2042 Protein mini spindles.
/FTId=PRO_0000437574.
REPEAT 120 157 HEAT 1. {ECO:0000255}.
REPEAT 160 197 HEAT 2. {ECO:0000255}.
REPEAT 270 311 HEAT 3. {ECO:0000255}.
REPEAT 315 353 HEAT 4. {ECO:0000255}.
REPEAT 357 394 HEAT 5. {ECO:0000255}.
REPEAT 396 433 HEAT 6. {ECO:0000255}.
REPEAT 440 478 HEAT 7. {ECO:0000255|PROSITE-
ProRule:PRU00103}.
REPEAT 587 624 HEAT 8. {ECO:0000255}.
REPEAT 625 662 HEAT 9. {ECO:0000255}.
REPEAT 672 710 HEAT 10. {ECO:0000255}.
REPEAT 745 782 HEAT 11. {ECO:0000255}.
REPEAT 856 893 HEAT 12. {ECO:0000255}.
REPEAT 896 933 HEAT 13. {ECO:0000255}.
REPEAT 937 974 HEAT 14. {ECO:0000255}.
REPEAT 1017 1054 HEAT 15. {ECO:0000255}.
REPEAT 1205 1242 HEAT 16. {ECO:0000255}.
REPEAT 1272 1309 HEAT 17. {ECO:0000255}.
REPEAT 1311 1344 HEAT 18. {ECO:0000255}.
REPEAT 1346 1383 HEAT 19. {ECO:0000255}.
REGION 1 516 Promotes microtubule polymerization.
{ECO:0000269|PubMed:24966168}.
REGION 1 505 Binds tubulin.
{ECO:0000269|PubMed:24966168}.
REGION 1 229 TOG 1. {ECO:0000305|PubMed:17889670}.
REGION 267 505 TOG 2. {ECO:0000305|PubMed:17889670}.
REGION 498 821 Association with microtubule lattice.
{ECO:0000269|PubMed:21965297}.
REGION 581 1080 Promotes microtubule polymerization.
{ECO:0000269|PubMed:24966168}.
REGION 581 814 TOG 3. {ECO:0000305|PubMed:17889670}.
REGION 849 1087 TOG 4. {ECO:0000305|PubMed:17889670}.
REGION 1099 1428 Association with microtubule lattice.
{ECO:0000269|PubMed:21965297}.
REGION 1179 1415 TOG 5. {ECO:0000305|PubMed:17889670}.
MUTAGEN 21 21 W->E: Impairs microtubule polymerization.
Disrupts tubulin binding; when associated
with E-292. {ECO:0000269|PubMed:17889670,
ECO:0000269|PubMed:24966168}.
MUTAGEN 292 292 W->E: Impairs microtubule polymerization.
Disrupts tubulin binding; when associated
with E-21. {ECO:0000269|PubMed:17889670,
ECO:0000269|PubMed:24966168}.
MUTAGEN 546 549 KVLK->EAAE: Disrupts microtubule lattice
binding. {ECO:0000269|PubMed:21965297}.
MUTAGEN 606 606 W->E: Impairs microtubule polymerization,
decreases microtubule lattice
localization.
{ECO:0000269|PubMed:24966168}.
MUTAGEN 874 874 W->E: Impairs microtubule polymerization,
decreases microtubule lattice
localization.
{ECO:0000269|PubMed:24966168}.
MUTAGEN 1102 1107 KLKTVR->ELEAAA: Disrupts microtubule
lattice binding.
{ECO:0000269|PubMed:21965297}.
HELIX 276 278 {ECO:0000244|PDB:2QK2}.
HELIX 283 287 {ECO:0000244|PDB:2QK2}.
HELIX 292 308 {ECO:0000244|PDB:2QK2}.
STRAND 310 312 {ECO:0000244|PDB:2QK2}.
HELIX 318 330 {ECO:0000244|PDB:2QK2}.
HELIX 334 351 {ECO:0000244|PDB:2QK2}.
HELIX 352 355 {ECO:0000244|PDB:2QK2}.
HELIX 356 368 {ECO:0000244|PDB:2QK2}.
HELIX 369 371 {ECO:0000244|PDB:2QK2}.
HELIX 375 389 {ECO:0000244|PDB:2QK2}.
HELIX 394 404 {ECO:0000244|PDB:2QK2}.
HELIX 410 424 {ECO:0000244|PDB:2QK2}.
HELIX 429 431 {ECO:0000244|PDB:2QK2}.
HELIX 434 448 {ECO:0000244|PDB:2QK2}.
HELIX 453 470 {ECO:0000244|PDB:2QK2}.
HELIX 472 475 {ECO:0000244|PDB:2QK2}.
HELIX 476 479 {ECO:0000244|PDB:2QK2}.
HELIX 484 496 {ECO:0000244|PDB:2QK2}.
HELIX 595 602 {ECO:0000244|PDB:4Y5J}.
HELIX 606 619 {ECO:0000244|PDB:4Y5J}.
HELIX 620 622 {ECO:0000244|PDB:4Y5J}.
HELIX 630 639 {ECO:0000244|PDB:4Y5J}.
STRAND 640 643 {ECO:0000244|PDB:4Y5J}.
HELIX 644 646 {ECO:0000244|PDB:4Y5J}.
HELIX 650 666 {ECO:0000244|PDB:4Y5J}.
HELIX 671 683 {ECO:0000244|PDB:4Y5J}.
HELIX 684 686 {ECO:0000244|PDB:4Y5J}.
TURN 688 690 {ECO:0000244|PDB:4Y5J}.
HELIX 691 704 {ECO:0000244|PDB:4Y5J}.
HELIX 707 720 {ECO:0000244|PDB:4Y5J}.
HELIX 724 741 {ECO:0000244|PDB:4Y5J}.
HELIX 747 758 {ECO:0000244|PDB:4Y5J}.
HELIX 763 780 {ECO:0000244|PDB:4Y5J}.
HELIX 782 788 {ECO:0000244|PDB:4Y5J}.
HELIX 793 806 {ECO:0000244|PDB:4Y5J}.
HELIX 858 860 {ECO:0000244|PDB:4QMH}.
HELIX 863 869 {ECO:0000244|PDB:4QMH}.
HELIX 874 891 {ECO:0000244|PDB:4QMH}.
HELIX 901 909 {ECO:0000244|PDB:4QMH}.
HELIX 914 931 {ECO:0000244|PDB:4QMH}.
HELIX 932 938 {ECO:0000244|PDB:4QMH}.
HELIX 939 949 {ECO:0000244|PDB:4QMH}.
HELIX 955 972 {ECO:0000244|PDB:4QMH}.
HELIX 975 977 {ECO:0000244|PDB:4QMH}.
HELIX 982 988 {ECO:0000244|PDB:4QMH}.
HELIX 992 1005 {ECO:0000244|PDB:4QMH}.
HELIX 1006 1008 {ECO:0000244|PDB:4QMH}.
HELIX 1011 1013 {ECO:0000244|PDB:4QMH}.
HELIX 1016 1029 {ECO:0000244|PDB:4QMH}.
HELIX 1035 1052 {ECO:0000244|PDB:4QMH}.
HELIX 1054 1064 {ECO:0000244|PDB:4QMH}.
HELIX 1069 1079 {ECO:0000244|PDB:4QMH}.
HELIX 1080 1082 {ECO:0000244|PDB:4QMH}.
HELIX 1153 1162 {ECO:0000244|PDB:5VJC}.
HELIX 1176 1188 {ECO:0000244|PDB:5VJC}.
HELIX 1193 1199 {ECO:0000244|PDB:5VJC}.
HELIX 1204 1217 {ECO:0000244|PDB:5VJC}.
TURN 1218 1220 {ECO:0000244|PDB:5VJC}.
HELIX 1222 1227 {ECO:0000244|PDB:5VJC}.
HELIX 1229 1239 {ECO:0000244|PDB:5VJC}.
HELIX 1245 1264 {ECO:0000244|PDB:5VJC}.
HELIX 1271 1282 {ECO:0000244|PDB:5VJC}.
TURN 1283 1286 {ECO:0000244|PDB:5VJC}.
HELIX 1290 1306 {ECO:0000244|PDB:5VJC}.
HELIX 1309 1318 {ECO:0000244|PDB:5VJC}.
HELIX 1319 1321 {ECO:0000244|PDB:5VJC}.
HELIX 1325 1342 {ECO:0000244|PDB:5VJC}.
HELIX 1344 1346 {ECO:0000244|PDB:5VJC}.
HELIX 1349 1357 {ECO:0000244|PDB:5VJC}.
HELIX 1358 1360 {ECO:0000244|PDB:5VJC}.
HELIX 1364 1381 {ECO:0000244|PDB:5VJC}.
HELIX 1382 1384 {ECO:0000244|PDB:5VJC}.
HELIX 1385 1388 {ECO:0000244|PDB:5VJC}.
HELIX 1394 1404 {ECO:0000244|PDB:5VJC}.
SEQUENCE 2042 AA; 225980 MW; F79B31535CE56D2E CRC64;
MAEDTEYKKL PVEERCVHKL WKARVDGYEE AAKIFRELDD EKSPEWSKFA GLIKKMVVDS
NALAQEKGLE AALIFVENSG LAGRTVGDVM TGIVQKCIAA PKTKTKELSV QVALMYVEIE
KQEAVVEELV KGMEAKNPKI VSACVAATTL ALREFGHKVI GVKPLIKKLA PLMSDRDKTV
RDEGKQLAVE IYRWIGAAMK AQISTLPQVT LKELEDEFDK LKGERVEPSR YLKSQQEKQA
KIADAAATED AYNEDDGEAG VEEIDPMDLL DPVDILSKMP KDFYDKLEEK KWTLRKESLE
VLEKLLTDHP KLENGEYGAL VSALKKVITK DSNVVLVAMA GKCLALLAKG LAKRFSNYAS
ACVPSLLEKF KEKKPNVVTA LREAIDAIYA STSLEAQQES IVESLSNKNP SVKSETALFI
ARALTRTQPT ALNKKLLKLL TTSLVKTLNE PDPTVRDSSA EALGTLIKLM GDKAVTPLLA
DVDPLKMAKI KECQEKAEIK IKVAGPKKET RPASAPTAKA AAPAKTVAGS VDPKPVTRPA
TTGARKVLKK PATVSGGGAT SAPTAALKAG GKPLATEREI TPEELQEKSE EILPAEILNG
LVDSNWKNRL AAVEQLLGEI SGFDAKQAGI SQILIRTISG RKPGLKEMNF QVLKFKLDII
RSVAENYPLT TTTVDLVINE IIEKLADAKN GAAAADVLSA FAEATKLEYV VGKVLSFAFE
QKSPKVQSEA FNWVNRSIIE FGFQLQPKTL IEDVRKGVQS TNPTVRASAI QMVGTMSMYM
GKALMMFFDS EKPALKSQIQ VEFDKNVGEK PPKPVRGVQR SSGGTAGNSP DNEDDDGGAA
GEEEPINMAD LLPRVDIAPQ ITEALLKEMS DKDWKTRNEG LTKLQAIISE ARLIKPSIGD
LAPALAHRLV DSNAKIAQTT LAICEQLATA MGAGCRNHVR NLFPGFLHAL GDNKSFVRAA
ALNCINSFGE KGGYKEFFES EMIADALKGG SPALKTELWA WLADKLPGLP PKSVSKEDIH
SMVPHLYAHI CDRNADVRKN ANEAVLGIMI HLGFDAMNRA LDKQKPASKK DILAALEKAR
PNLPVKPLPK GKHQAPIPEE PKLKTVRGGG AGGAPGIQKS ATARVAGGQD KQVPARKKDE
DIDTSPLLCA NSAKNQRLLD EQKMKVLKWT FVTPREEFTE LLRDQMMTAN VNKALIANMF
HDDFRYHLKV IEQLSEDLAG NSKALVCNLD LILKWLTLRF YDTNPSVLIK GLEYLVQVFQ
VLIDEEYILA ENEGSSFVPH LLLKIGDPKD AVRNGVRRVL RQVILVFPFV KVFGYVMEGL
KSKNARQRTE CLDELTFLIE SYGMNICPQS AVREIARQIS DRDNSVRNAA LNCIVQVFFL
SGEKTYKMIG HLNEKDLSML DERIKRAKKT KKPTPPPSVD VPAPQRHDSI EIEDAEVGNG
CDELPPPDED GTFDQAPSSQ LLLLQQQLQQ LQQQAQQQKP SGPFGLDSQV ISEIEKDWVR
VDQMEQKPLL NVDISSLDEP IKVRPTRAGI HYPQEKFDRL ISRQHYMQQT LTTSPSSTAG
MTSGVSPYRS PMRLQHQQPQ QQLENNIPNL ADVLPKHDPQ LVKVIKGVSS TDTLKARAAI
NELAAIIEAP EKQAVLRDYE EIFIQNVLAQ FKNLSQIPSA QSVVVYQPLL SILYTFFHAN
ILGKTLSVAC IKNLMSALLN LMADPKLAVG DDSQYNKVIN GICLKVLDKV DFTNLNCALI
RLLRETCPEA KLPKFTDLLM KCIWRNVKML PERSNELNYD AVILEVHEFM LALPSTWWQN
RPSDTPMRTI KTILHNMAKV KGNAILQHLN QIPTHSELHT YLIRILKNFQ KDGSASGIGA
SPQRAKEIAS KRISHQTHDT VSQIFKLISD RDTKQQGLQK LYDFKQQNPD IDLSTFLQGS
SAPFHKYIEE GLAEIERNQN AGSTQDNRTD VNYQNNGPDP DFWMDRLQYH MTGGAAKLAS
ARSADDGSHM LDNKVVDENL CLNGMNAQKA SLIKREKRDM SPNRLQHLQA KLAQIKKENH
AQ


Related products :

Catalog number Product name Quantity
NT-010-MEM Mini Pig Tissue Membrane Protein Panel Species: Mini Pig Membrane Protein 10X0.025mg
NT-010-NUC Mini Pig Tissue Nuclear Protein Panel Species: Mini Pig Nuclear Protein 10X0.025mg
NT-010-CYT Mini Pig Tissue Cytoplasmic Protein Panel Species: Mini Pig Cytoplasmic Protein 10X0.05mg
NT-213-NUC Mini Pig Liver Nuclear Protein Species: Mini Pig Nuclear Protein 0.1mg
NT-102-MEM Mini Pig S. Muscles Membrane Protein Species: Mini Pig Membrane Protein 0.1mg
NT-701-NUC Mini Pig Spleen Nuclear Protein Species: Mini Pig Nuclear Protein 0.1mg
NT-801-NUC Mini Pig Heart Nuclear Protein Species: Mini Pig Nuclear Protein 0.1mg
NT-901-MEM Mini Pig Kidney Membrane Protein Species: Mini Pig Membrane Protein 0.1mg
NT-801-MEM Mini Pig Heart Membrane Protein Species: Mini Pig Membrane Protein 0.1mg
NT-901-NUC Mini Pig Kidney Nuclear Protein Species: Mini Pig Nuclear Protein 0.1mg
NT-701-MEM Mini Pig Spleen Membrane Protein Species: Mini Pig Membrane Protein 0.1mg
NT-601-MEM Mini Pig Lung Membrane Protein Species: Mini Pig Membrane Protein 0.1mg
NT-411-MEM Mini Pig Uterus Membrane Protein Species: Mini Pig Membrane Protein 0.1mg
NT-101-MEM Mini Pig Skin Membrane Protein Species: Mini Pig Membrane Protein 0.1mg
NT-901-CYT Mini Pig Kidney Cytoplasmic Protein Species: Mini Pig Cytoplasmic Protein 0.5mg
NT-302-NUC Mini Pig Stomach Nuclear Protein Species: Mini Pig Nuclear Protein 0.1mg
NT-306-NUC Mini Pig Intestine Nuclear Protein Species: Mini Pig Nuclear Protein 0.1mg
NT-311-NUC Mini Pig Colon Nuclear Protein Species: Mini Pig Nuclear Protein 0.1mg
NT-313-NUC Mini Pig Pancreas Nuclear Protein Species: Mini Pig Nuclear Protein 0.1mg
NT-401-NUC Mini Pig Testis Nuclear Protein Species: Mini Pig Nuclear Protein 0.1mg
NT-102-NUC Mini Pig S. Muscles Nuclear Protein Species: Mini Pig Nuclear Protein 0.1mg
NT-406-NUC Mini Pig Ovary Nuclear Protein Species: Mini Pig Nuclear Protein 0.1mg
NT-411-NUC Mini Pig Uterus Nuclear Protein Species: Mini Pig Nuclear Protein 0.1mg
NT-201-NUC Mini Pig Brain Nuclear Protein Species: Mini Pig Nuclear Protein 0.1mg
NT-601-NUC Mini Pig Lung Nuclear Protein Species: Mini Pig Nuclear Protein 0.1mg

Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism
WP1676: Non-homologous end-joining
WP1678: Nucleotide excision repair

Related Genes :
[msps CG5000] Protein mini spindles
[mrnC yazC BSU00950] Mini-ribonuclease 3 (Mini-3) (Mini-RNase 3) (EC 3.1.26.-) (Mini-RNase III) (Mini-III)
[CTSH] Pro-cathepsin H [Cleaved into: Cathepsin H mini chain; Cathepsin H (EC 3.4.22.16); Cathepsin H heavy chain; Cathepsin H light chain]
[MIF1 At1g74660 F1M20.34] Mini zinc finger protein 1 (AtMIF1)
[CTSH CPSB] Pro-cathepsin H [Cleaved into: Cathepsin H mini chain; Cathepsin H (EC 3.4.22.16); Cathepsin H heavy chain; Cathepsin H light chain]
[Ctsh] Pro-cathepsin H [Cleaved into: Cathepsin H mini chain; Cathepsin H (EC 3.4.22.16); Cathepsin H heavy chain; Cathepsin H light chain]
[Ctsh] Pro-cathepsin H (Cathepsin B3) (Cathepsin BA) [Cleaved into: Cathepsin H mini chain; Cathepsin H (EC 3.4.22.16); Cathepsin H heavy chain; Cathepsin H light chain]
[CTSH] Pro-cathepsin H [Cleaved into: Cathepsin H mini chain; Cathepsin H (EC 3.4.22.16); Cathepsin H heavy chain; Cathepsin H light chain]
[TMPRSS15 ENTK PRSS7] Enteropeptidase (EC 3.4.21.9) (Enterokinase) (Serine protease 7) (Transmembrane protease serine 15) [Cleaved into: Enteropeptidase non-catalytic mini chain; Enteropeptidase non-catalytic heavy chain; Enteropeptidase catalytic light chain]
[ask1 mug181 SPBC27.02c] DASH complex subunit ask1 (Associated with spindles and kinetochores protein 1) (Meiotically up-regulated gene 181 protein) (Outer kinetochore protein ask1)
[ASK1 YKL052C YKL306] DASH complex subunit ASK1 (Associated with spindles and kinetochores protein 1) (Outer kinetochore protein ASK1)
[MCMBP C10orf119] Mini-chromosome maintenance complex-binding protein (MCM-BP) (MCM-binding protein)
[tll1 mfn tld tolloid] Dorsal-ventral patterning tolloid-like protein 1 (EC 3.4.24.-) (Mini fin protein)
[cysS mrnC HMPREF1250_1653] Multifunctional fusion protein [Includes: Mini-ribonuclease 3 (Mini-3) (Mini-RNase 3) (EC 3.1.26.-) (Mini-RNase III) (Mini-III); Cysteine--tRNA ligase (EC 6.1.1.16) (Cysteinyl-tRNA synthetase) (CysRS)]
[ETG1 At2g40550 T2P4.10] Mini-chromosome maintenance complex-binding protein (MCM-BP) (MCM-binding protein) (Protein E2F TARGET GENE 1)
[WRKY10 MINI3 At1g55600 F20N2.3] Probable WRKY transcription factor 10 (Protein MINISEED 3) (WRKY DNA-binding protein 10)
[RANGAP1 KIAA1835 SD] Ran GTPase-activating protein 1 (RanGAP1)
[DUO1 YGL061C] DASH complex subunit DUO1 (Death upon overproduction protein 1) (Outer kinetochore protein DUO1)
[Klp61F KLP2 CG9191] Kinesin-like protein Klp61F (Bipolar kinesin KRP-130)
[KIF2A KIF2 KNS2] Kinesin-like protein KIF2A (Kinesin-2) (hK2)
[mgr CG6719] Prefoldin subunit 3 (Protein merry-go-round) (von Hippel-Lindau-binding protein 1)
[kif11-b eg5] Kinesin-like protein KIF11-B (Kinesin-5) (Kinesin-related motor protein Eg5-1) (XLEg5K1) (XlEg5)
[wisp CG15737] Poly(A) RNA polymerase gld-2 homolog B (EC 2.7.7.19) (Protein wispy)
[CIT CRIK KIAA0949 STK21] Citron Rho-interacting kinase (CRIK) (EC 2.7.11.1) (Serine/threonine-protein kinase 21)
[kif11-a eg5] Kinesin-like protein KIF11-A (Kinesin-5) (Kinesin-related motor protein Eg5-2) (XLEg5K2)
[MIF2 At3g28917 MLD15.10] Mini zinc finger protein 2 (AtMIF2)
[RAMAC C15orf18 FAM103A1 RAMMET] RNA guanine-N7 methyltransferase activating subunit (Protein FAM103A1) (RNA guanine-7 methyltransferase activating subunit) (RNMT-activating mRNA cap methyltransferase subunit) (RNMT-activating mini protein) (RAM)
[Mcm9 Mcmdc1] DNA helicase MCM9 (EC 3.6.4.12) (Mini-chromosome maintenance deficient domain-containing protein 1) (Minichromosome maintenance 9)
[MCM9 C6orf61 MCMDC1] DNA helicase MCM9 (hMCM9) (EC 3.6.4.12) (Mini-chromosome maintenance deficient domain-containing protein 1) (Minichromosome maintenance 9)
[Top2 CG10223] DNA topoisomerase 2 (EC 5.99.1.3) (DNA topoisomerase II)

Bibliography :
[30811267] CEP135 isoform dysregulation promotes centrosome amplification in breast cancer cells.
[28512144] TOG-tubulin binding specificity promotes microtubule dynamics and mitotic spindle formation.
[28296067] RNA-binding proteins of the NXF (nuclear export factor) family and their connection with the cytoskeleton.
[27132131] Central Spindle Self-Organization and Cytokinesis in Artificially Activated Sea Urchin Eggs.
[26953351] Arl2- and Msps-dependent microtubule growth governs asymmetric division.
[26406596] TOG Proteins Are Spatially Regulated by Rac-GSK3β to Control Interphase Microtubule Dynamics.
[25971232] Solution NMR assignment of the cryptic sixth TOG domain of mini spindles.
[25720490] Drosophila melanogaster mini spindles TOG3 utilizes unique structural elements to promote domain stability and maintain a TOG1- and TOG2-like tubulin-binding surface.
[24966168] The XMAP215 family drives microtubule polymerization using a structurally diverse TOG array.
[23336298] A new model for dura mater healing: human dural fibroblast culture.
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