Q4FZC9
PR
Gene name |
Syne3 |
Protein name |
Nesprin-3 |
Names |
KASH domain-containing protein 3, KASH3, Nuclear envelope spectrin repeat protein 3 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:212073 |
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 Q4FZC9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q4FZC9-F1 | Predicted | AlphaFoldDB |
77 variants for Q4FZC9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs225764808 | 42 | A>E | No | EVA | |
| rs33184070 | 58 | M>I | No | EVA | |
| rs250096773 | 58 | M>K | No | EVA | |
| rs48707589 | 58 | M>L | No | EVA | |
| rs3403595860 | 69 | E>V | No | EVA | |
| rs3403691795 | 83 | I>T | No | EVA | |
| rs3389260728 | 122 | Q>* | No | EVA | |
| rs3389266333 | 133 | V>G | No | EVA | |
| rs387448629 | 135 | A>T | No | EVA | |
| rs3389260735 | 137 | E>D | No | EVA | |
| rs3389260712 | 177 | A>G | No | EVA | |
| rs3389254427 | 208 | A>S | No | EVA | |
| rs246077403 | 228 | D>N | No | EVA | |
| rs223536254 | 242 | K>N | No | EVA | |
| rs3413085481 | 245 | S>C | No | EVA | |
| rs251260722 | 257 | L>R | No | EVA | |
| rs233561606 | 258 | R>C | No | EVA | |
| rs3389254436 | 264 | D>V | No | EVA | |
| rs3389251389 | 272 | G>D | No | EVA | |
| rs3389266348 | 278 | R>K | No | EVA | |
| rs3389267735 | 282 | Q>* | No | EVA | |
| rs3389251421 | 282 | Q>L | No | EVA | |
| rs220932439 | 288 | Q>R | No | EVA | |
| rs3389216862 | 300 | G>W | No | EVA | |
| rs235355486 | 324 | R>Q | No | EVA | |
| rs3389257821 | 330 | R>K | No | EVA | |
| rs226829764 | 346 | D>E | No | EVA | |
| rs3389243368 | 346 | D>G | No | EVA | |
| rs255224272 | 348 | K>R | No | EVA | |
| rs236831668 | 350 | S>N | No | EVA | |
| rs213268339 | 359 | L>M | No | EVA | |
| rs3389226158 | 373 | A>V | No | EVA | |
| rs3389226160 | 410 | S>P | No | EVA | |
| rs3389260707 | 452 | Q>L | No | EVA | |
| rs3389251344 | 460 | R>M | No | EVA | |
| rs3389251352 | 465 | T>M | No | EVA | |
| rs3389190248 | 470 | D>Y | No | EVA | |
| rs3389267726 | 475 | H>Q | No | EVA | |
| rs3389260736 | 498 | L>M | No | EVA | |
| rs3389231498 | 499 | Q>L | No | EVA | |
| rs3389231526 | 503 | D>N | No | EVA | |
| rs3389260730 | 506 | G>V | No | EVA | |
| rs3389231508 | 539 | K>M | No | EVA | |
| rs3389190293 | 550 | K>T | No | EVA | |
| rs257505079 | 577 | P>L | No | EVA | |
| rs3389216859 | 578 | R>G | No | EVA | |
| rs3403783272 | 584 | Q>* | No | EVA | |
| rs3389190282 | 618 | Q>H | No | EVA | |
| rs3389231547 | 619 | Q>H | No | EVA | |
| rs3389260692 | 621 | V>E | No | EVA | |
| rs3389267683 | 623 | Q>* | No | EVA | |
| rs3389255656 | 629 | Q>L | No | EVA | |
| rs3389257445 | 637 | D>N | No | EVA | |
| rs230605088 | 646 | V>I | No | EVA | |
| rs33182674 | 657 | S>L | No | EVA | |
| rs3389258803 | 676 | D>V | No | EVA | |
| rs228985749 | 678 | R>C | No | EVA | |
| rs33180831 | 691 | T>M | No | EVA | |
| rs29167927 | 697 | P>L | No | EVA | |
| rs29163734 | 723 | T>A | No | EVA | |
| rs3389216812 | 727 | E>D | No | EVA | |
| rs3389274278 | 745 | N>T | No | EVA | |
| rs3389226082 | 761 | D>S | No | EVA | |
| rs3389266329 | 774 | K>E | No | EVA | |
| rs29216358 | 789 | Q>P | No | EVA | |
| rs29216358 | 789 | Q>R | No | EVA | |
| rs3389251404 | 800 | L>P | No | EVA | |
| rs245938121 | 802 | E>G | No | EVA | |
| rs3389257808 | 805 | P>H | No | EVA | |
| rs33184598 | 823 | R>H | No | EVA | |
| rs3403747309 | 834 | K>T | No | EVA | |
| rs241144287 | 837 | R>K | No | EVA | |
| rs241144287 | 837 | R>M | No | EVA | |
| rs3389251397 | 843 | L>P | No | EVA | |
| rs3389258836 | 885 | S>F | No | EVA | |
| rs3389225999 | 896 | E>V | No | EVA | |
| rs3389243391 | 897 | S>DG* | No | EVA |
No associated diseases with Q4FZC9
6 regional properties for Q4FZC9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| repeat | Spectrin repeat | 221 - 324 | IPR002017-1 |
| repeat | Spectrin repeat | 651 - 743 | IPR002017-2 |
| domain | KASH domain | 917 - 975 | IPR012315 |
| repeat | Spectrin/alpha-actinin | 7 - 109 | IPR018159-1 |
| repeat | Spectrin/alpha-actinin | 223 - 324 | IPR018159-2 |
| repeat | Spectrin/alpha-actinin | 650 - 751 | IPR018159-3 |
7 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| meiotic nuclear membrane microtubule tethering complex | A nuclear membrane protein complex which connects the nuclear outer and inner membranes together, and links links the nuclear lumen to cytoplasmic microtubules during meiosis. |
| nuclear envelope | The double lipid bilayer enclosing the nucleus and separating its contents from the rest of the cytoplasm; includes the intermembrane space, a gap of width 20-40 nm (also called the perinuclear space). |
| nuclear membrane | Either of the lipid bilayers that surround the nucleus and form the nuclear envelope; excludes the intermembrane space. |
| nuclear outer membrane | The outer, i.e. cytoplasm-facing, lipid bilayer of the nuclear envelope; continuous with the endoplasmic reticulum of the cell and sometimes studded with ribosomes. |
| rough endoplasmic reticulum | The rough (or granular) endoplasmic reticulum (ER) has ribosomes adhering to the outer surface; the ribosomes are the site of translation of the mRNA for those proteins which are either to be retained within the cisternae (ER-resident proteins), the proteins of the lysosomes, or the proteins destined for export from the cell. Glycoproteins undergo their initial glycosylation within the cisternae. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| actin filament binding | Binding to an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits. |
| cytoskeleton-nuclear membrane anchor activity | The binding activity of a molecule that brings together a cytoskeletal protein or protein complex and a nuclear membrane lipid or membrane-associated protein, in order to maintain the localization of the cytoskeleton at a specific location of the nuclear membrane. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| 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. |
| establishment of protein localization to membrane | The directed movement of a protein to a specific location in a membrane. |
| nuclear migration | The directed movement of the nucleus to a specific location within a cell. |
| regulation of cell shape | Any process that modulates the surface configuration of a cell. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTQQPQEDFE | RSVEDAQAWM | KVIQEQLQVN | DNTKGPRAAL | EARLRETEKI | CQLESEGMVK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VELVLRAAEA | LLATCQEGQK | PEILARLRDI | KSQWEETVTY | MTHCHSRIEW | VWLHWSEYLL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AQDEFYRWFQ | KMVVALEPPV | ELQLGLKEKQ | WQLSHAQVLL | HNVDNQAVLL | DRLLEEAGSL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FSRIGDPSVD | EDAQKRMKAE | YDAVKARAQR | RVDLLAQVAQ | DHEQYREDVN | EFQLWLKAVV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EKVHSCLGRN | CKLATELRLS | TLQDIAKDFP | RGEESLKRLE | EQAVGVIQNT | SPLGAEKISG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ELEEMRGVLE | KLRVLWKEEE | GRLRGLLQSR | GDCEQQIQQL | EAELGDFKKS | LQRLAQEGLE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PTVKTATEDE | LVAQWRLFSG | TRAALASEEP | RVDRLQTQLK | KLVTFPDLQS | LSDSVVATIQ |
| 430 | 440 | 450 | 460 | 470 | 480 |
| EYQSMKGKNT | RLHNATRAEL | WQRFQRPLND | LQLWKALAQR | LLDITASLPD | LASIHTFLPQ |
| 490 | 500 | 510 | 520 | 530 | 540 |
| IEAALTESSR | LKEQLAMLQL | KTDLLGSIFG | QERAATLLEQ | VTSSVRDRDL | LHNSLLQRKS |
| 550 | 560 | 570 | 580 | 590 | 600 |
| KLQSLLVQHK | DFGVAFDPLN | RKLLDLQARI | QAEKGLPRDL | PGKQVQLLRL | QGLQEEGLDL |
| 610 | 620 | 630 | 640 | 650 | 660 |
| GTQIEAVRPL | AHGNSKHQQK | VDQISCDQQA | LQRSLEDLVD | RCQQNVREHC | TFSHRLSELQ |
| 670 | 680 | 690 | 700 | 710 | 720 |
| LWITMATQTL | ESHQGDVRLW | DAESQEAGLE | TLLSEIPEKE | VQVSLLQALG | QLVMKKSSPE |
| 730 | 740 | 750 | 760 | 770 | 780 |
| GATMVQEELR | KLMESWQALR | LLEENMLSLM | RNQQLQRTEV | DTGKKQVFTN | NIPKAGFLIN |
| 790 | 800 | 810 | 820 | 830 | 840 |
| PQDPIPRRQH | GANPLEGHDL | PEDHPQLLRD | FEQWLQAENS | KLRRIITMRV | ATAKDLRTRE |
| 850 | 860 | 870 | 880 | 890 | 900 |
| VKLQELEARI | PEGQHLFENL | LRLRPARDPS | NELEDLRYRW | MLYKSKLKDS | GHLLTESSPG |
| 910 | 920 | 930 | 940 | 950 | 960 |
| ELTAFQKSRR | QKRWSPCSLL | QKACRVALPL | QLLLLLFLLL | LFLLPAGEEE | RSCALANNFA |
| 970 | |||||
| RSFALMLRYN | GPPPT |