P50275
PR
Gene name |
ASE1 (YOR058C, YOR29-09) |
Protein name |
Anaphase spindle elongation protein |
Names |
|
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YOR058C |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P50275
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P50275-F1 | Predicted | AlphaFoldDB |
18 variants for P50275
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s15-436175 | 58 | R>L | No | SGRP | |
| s15-435947 | 134 | S>F | No | SGRP | |
| s15-435632 | 239 | H>L | No | SGRP | |
| s15-435570 | 260 | A>T | No | SGRP | |
| s15-435530 | 273 | L>S | No | SGRP | |
| s15-435371 | 326 | R>K | No | SGRP | |
| s15-435288 | 354 | G>S | No | SGRP | |
| s15-435181 | 389 | D>E | No | SGRP | |
| s15-435183 | 389 | D>N | No | SGRP | |
| s15-435179 | 390 | I>T | No | SGRP | |
| s15-435064 | 428 | K>N | No | SGRP | |
| s15-435057 | 431 | M>V | No | SGRP | |
| s15-434572 | 592 | E>D | No | SGRP | |
| s15-434397 | 651 | F>V | No | SGRP | |
| s15-434366 | 661 | P>L | No | SGRP | |
| s15-434342 | 669 | A>V | No | SGRP | |
| s15-434279 | 690 | S>F | No | SGRP | |
| s15-433995 | 785 | A>T | No | SGRP |
No associated diseases with P50275
No regional properties for P50275
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for P50275 | |||
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| microtubule | Any of the long, generally straight, hollow tubes of internal diameter 12-15 nm and external diameter 24 nm found in a wide variety of eukaryotic cells; each consists (usually) of 13 protofilaments of polymeric tubulin, staggered in such a manner that the tubulin monomers are arranged in a helical pattern on the microtubular surface, and with the alpha/beta axes of the tubulin subunits parallel to the long axis of the tubule; exist in equilibrium with pool of tubulin monomers and can be rapidly assembled or disassembled in response to physiological stimuli; concerned with force generation, e.g. in the spindle. |
| mitotic spindle midzone | The area in the center of the anaphase spindle consisting of microtubules, microtubule bundling factors and kinesin motors where the spindle microtubules from opposite poles overlap in an antiparallel manner. |
| nuclear microtubule | Any microtubule in the nucleus of a cell. |
| spindle | The array of microtubules and associated molecules that forms between opposite poles of a eukaryotic cell during mitosis or meiosis and serves to move the duplicated chromosomes apart. |
| spindle midzone | The area in the center of the spindle where the spindle microtubules from opposite poles overlap. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| microtubule binding | Binding to a microtubule, a filament composed of tubulin monomers. |
8 GO annotations of biological process
| Name | Definition |
|---|---|
| initial mitotic spindle pole body separation | The release of duplicated mitotic spindle pole bodies (SPBs) that begins with the nucleation of microtubules from each SPB within the nucleus, leading to V-shaped spindle microtubules. Interpolar microtubules that elongate from each pole are interconnected, forming overlapping microtubules. Capturing and antiparallel sliding apart of microtubules promotes the initial separation of the SPB. |
| microtubule bundle formation | A process that results in a parallel arrangement of microtubules. |
| microtubule cytoskeleton organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising microtubules and their associated proteins. |
| mitotic spindle elongation | The cell cycle process in which the distance is lengthened between poles of the mitotic spindle. Mitotic spindle elongation begins during mitotic prophase and ends during mitotic anaphase B. |
| mitotic spindle midzone assembly | The cell cycle process in which the aggregation, arrangement and bonding together of a set of components forms the spindle midzone. |
| mitotic spindle organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the microtubule spindle during a mitotic cell cycle. |
| septum digestion after cytokinesis | The process of physically separating the septal cell wall material by enzymatic digestion, that occurs after daughter cells are separated by cytokinesis. |
| spindle midzone assembly | The cell cycle process in which aggregation, arrangement and bonding together of a set of components to form the spindle midzone. The spindle midzone is the area in the center of the spindle where the spindle microtubules from opposite poles overlap. |
3 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| O43663 | PRC1 | Protein regulator of cytokinesis 1 | Homo sapiens (Human) | PR |
| Q9ZVJ3 | MAP65-5 | 65-kDa microtubule-associated protein 5 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q9FLP0 | MAP65-1 | 65-kDa microtubule-associated protein 1 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| METATSSPLP | IKSRRNSENS | GSTTVIPHMN | PSLATPLTVS | TMVNQSNSKE | FMKLTPVRIR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DFGSPLKNVS | TNYHFLDSEN | GKGNTMDNMY | RENFILISKD | LEKLLENLNV | IYQNIGYSNT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EIITKEKIIF | TTISNSIKQF | FEQADEELKR | LSAENGIEQD | ILNNILERIN | DPSGIKTIPD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LYIRNAILLQ | ESKTVPQSPK | KPLSLLSKKA | ALDTAKKFVL | GSFLPRLRDY | LKSLITLKHL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IQSVKENLPG | LTEADNEAIA | EFPELSTLTA | YLLQIENGKG | DIGLSMKFII | DNRKDILKGS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AFKTINEESV | KHMNEVIKIY | EEEYERRFKS | VLTKKVSISS | ICEQLGTPLA | TLIGEDFEQD |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LRSYGEEENS | TSEIPNFHPV | DRERMSKIDI | TLEKLQAIHK | ERADKKRLLM | EQCQKLWTRL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KISQEYIKTF | MRNNSSLSTE | SLGRISKEVM | RLEAMKKKLI | KKLISDSWDK | IQELWRTLQY |
| 490 | 500 | 510 | 520 | 530 | 540 |
| SEESRSKFII | VFEELRNSAT | TLQEDELLLE | TCENELKRLE | EKLTLYKPIL | KLISDFESLQ |
| 550 | 560 | 570 | 580 | 590 | 600 |
| EDQEFLERSS | KDSSRLLSRN | SHKILLTEEK | MRKRITRHFP | RVINDLRIKL | EEADGLFDQP |
| 610 | 620 | 630 | 640 | 650 | 660 |
| FLFKGKPLSE | AIDIQQQEIE | AKYPRCRVRM | QRSKKGKCGA | NKENKVIKNT | FKATESSIRV |
| 670 | 680 | 690 | 700 | 710 | 720 |
| PIGLNLNDAN | ITYKTPSKKT | IQGLTKNDLS | QENSLARHMQ | GTTKLSSPNR | RATRLLAPTV |
| 730 | 740 | 750 | 760 | 770 | 780 |
| ISRNSKGNIE | RPTLNRNRSS | DLSSSPRINH | THGEHAVKPR | QLFPIPLNKV | DTKGSHIPQL |
| 790 | 800 | 810 | 820 | 830 | 840 |
| TKEKALELLK | RSTGTTGKEN | VRSPERKSSL | EDYAQKLSSP | YKEPEHSIYK | LSMSPEGKFQ |
| 850 | 860 | 870 | 880 | ||
| LNIQQKDIES | GFDDTSMMED | ENDKDFITWK | NEQVSKLNGF | SFTDI |