UniProt ID | AINX_HUMAN | |
---|---|---|
UniProt AC | Q16352 | |
Protein Name | Alpha-internexin | |
Gene Name | INA | |
Organism | Homo sapiens (Human). | |
Sequence Length | 499 | |
Subcellular Localization | ||
Protein Description | Class-IV neuronal intermediate filament that is able to self-assemble. It is involved in the morphogenesis of neurons. It may form an independent structural network without the involvement of other neurofilaments or it may cooperate with NF-L to form the filamentous backbone to which NF-M and NF-H attach to form the cross-bridges.. | |
Protein Sequence | MSFGSEHYLCSSSSYRKVFGDGSRLSARLSGAGGAGGFRSQSLSRSNVASSAACSSASSLGLGLAYRRPPASDGLDLSQAAARTNEYKIIRTNEKEQLQGLNDRFAVFIEKVHQLETQNRALEAELAALRQRHAEPSRVGELFQRELRDLRAQLEEASSARSQALLERDGLAEEVQRLRARCEEESRGREGAERALKAQQRDVDGATLARLDLEKKVESLLDELAFVRQVHDEEVAELLATLQASSQAAAEVDVTVAKPDLTSALREIRAQYESLAAKNLQSAEEWYKSKFANLNEQAARSTEAIRASREEIHEYRRQLQARTIEIEGLRGANESLERQILELEERHSAEVAGYQDSIGQLENDLRNTKSEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETRFSTSGLSISGLNPLPNPSYLLPPRILSATTSKVSSTGLSLKKEEEEEEASKVASKKTSQIGESFEEILEETVISTKKTEKSNIEETTISSQKI | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSFGSEHYL ------CCCCCCCEE | 38.01 | 27732954 | |
5 | Phosphorylation | ---MSFGSEHYLCSS ---CCCCCCCEECCC | 21.13 | 27732954 | |
8 | Phosphorylation | MSFGSEHYLCSSSSY CCCCCCCEECCCHHC | 12.83 | 26552605 | |
11 | Phosphorylation | GSEHYLCSSSSYRKV CCCCEECCCHHCCCH | 30.57 | 26552605 | |
12 | Phosphorylation | SEHYLCSSSSYRKVF CCCEECCCHHCCCHH | 23.47 | 26552605 | |
13 | Phosphorylation | EHYLCSSSSYRKVFG CCEECCCHHCCCHHC | 18.33 | 26552605 | |
14 | Phosphorylation | HYLCSSSSYRKVFGD CEECCCHHCCCHHCC | 30.79 | 26552605 | |
15 | Phosphorylation | YLCSSSSYRKVFGDG EECCCHHCCCHHCCC | 19.19 | 26552605 | |
23 | Phosphorylation | RKVFGDGSRLSARLS CCHHCCCCHHHHHHC | 34.48 | 28348404 | |
26 | Phosphorylation | FGDGSRLSARLSGAG HCCCCHHHHHHCCCC | 15.38 | 32142685 | |
30 | Phosphorylation | SRLSARLSGAGGAGG CHHHHHHCCCCCCCC | 22.50 | 29691806 | |
40 | Phosphorylation | GGAGGFRSQSLSRSN CCCCCCCCCCCCCCC | 23.12 | 22210691 | |
42 | Phosphorylation | AGGFRSQSLSRSNVA CCCCCCCCCCCCCCC | 29.56 | 22210691 | |
44 | Phosphorylation | GFRSQSLSRSNVASS CCCCCCCCCCCCCCH | 38.62 | 22210691 | |
46 | Phosphorylation | RSQSLSRSNVASSAA CCCCCCCCCCCCHHH | 32.07 | 29978859 | |
50 | O-linked_Glycosylation | LSRSNVASSAACSSA CCCCCCCCHHHHHHH | 19.07 | 30379171 | |
50 | Phosphorylation | LSRSNVASSAACSSA CCCCCCCCHHHHHHH | 19.07 | 29978859 | |
51 | Phosphorylation | SRSNVASSAACSSAS CCCCCCCHHHHHHHH | 15.33 | 29978859 | |
55 | O-linked_Glycosylation | VASSAACSSASSLGL CCCHHHHHHHHHHCC | 24.98 | 30379171 | |
55 | Phosphorylation | VASSAACSSASSLGL CCCHHHHHHHHHHCC | 24.98 | 24076635 | |
56 | Phosphorylation | ASSAACSSASSLGLG CCHHHHHHHHHHCCC | 31.86 | 24076635 | |
58 | Phosphorylation | SAACSSASSLGLGLA HHHHHHHHHHCCCCC | 28.22 | 29978859 | |
59 | Phosphorylation | AACSSASSLGLGLAY HHHHHHHHHCCCCCC | 26.60 | 24076635 | |
66 | Phosphorylation | SLGLGLAYRRPPASD HHCCCCCCCCCCCCC | 16.52 | 29978859 | |
72 | Phosphorylation | AYRRPPASDGLDLSQ CCCCCCCCCCCCHHH | 37.68 | 27732954 | |
72 | O-linked_Glycosylation | AYRRPPASDGLDLSQ CCCCCCCCCCCCHHH | 37.68 | 30379171 | |
78 | Phosphorylation | ASDGLDLSQAAARTN CCCCCCHHHHHHHCC | 19.89 | 27732954 | |
95 | Ubiquitination | KIIRTNEKEQLQGLN EEEECCHHHHHCCCH | 53.48 | 29967540 | |
95 | 2-Hydroxyisobutyrylation | KIIRTNEKEQLQGLN EEEECCHHHHHCCCH | 53.48 | - | |
104 | Methylation | QLQGLNDRFAVFIEK HHCCCHHHHHHHHHH | 21.98 | 115480323 | |
111 | 2-Hydroxyisobutyrylation | RFAVFIEKVHQLETQ HHHHHHHHHHHHHHH | 39.95 | - | |
215 | Ubiquitination | LARLDLEKKVESLLD HHHHCHHHHHHHHHH | 70.21 | 33845483 | |
216 | 2-Hydroxyisobutyrylation | ARLDLEKKVESLLDE HHHCHHHHHHHHHHH | 41.69 | - | |
216 | Ubiquitination | ARLDLEKKVESLLDE HHHCHHHHHHHHHHH | 41.69 | 33845483 | |
219 | Phosphorylation | DLEKKVESLLDELAF CHHHHHHHHHHHHHH | 36.90 | - | |
272 | Phosphorylation | LREIRAQYESLAAKN HHHHHHHHHHHHHHH | 13.39 | - | |
287 | Phosphorylation | LQSAEEWYKSKFANL CCCHHHHHHHHHCCH | 14.52 | - | |
288 | Ubiquitination | QSAEEWYKSKFANLN CCHHHHHHHHHCCHH | 48.52 | 32142685 | |
290 | Acetylation | AEEWYKSKFANLNEQ HHHHHHHHHCCHHHH | 44.32 | 19608861 | |
290 | Ubiquitination | AEEWYKSKFANLNEQ HHHHHHHHHCCHHHH | 44.32 | 19608861 | |
302 | Phosphorylation | NEQAARSTEAIRASR HHHHHHHHHHHHHHH | 24.71 | 26425664 | |
308 | Phosphorylation | STEAIRASREEIHEY HHHHHHHHHHHHHHH | 30.31 | 26425664 | |
323 | Phosphorylation | RRQLQARTIEIEGLR HHHHHHHEEEEECCC | 26.44 | 30576142 | |
335 | Phosphorylation | GLRGANESLERQILE CCCCCCHHHHHHHHH | 35.02 | 22617229 | |
369 | 2-Hydroxyisobutyrylation | ENDLRNTKSEMARHL HHHHHHCHHHHHHHH | 48.22 | - | |
377 | Methylation | SEMARHLREYQDLLN HHHHHHHHHHHHHHC | 34.16 | - | |
379 | Phosphorylation | MARHLREYQDLLNVK HHHHHHHHHHHHCHH | 10.82 | 21253578 | |
396 | Phosphorylation | LDIEIAAYRKLLEGE HHHHHHHHHHHHCCC | 10.16 | - | |
405 | Phosphorylation | KLLEGEETRFSTSGL HHHCCCCCEECCCCC | 32.48 | 21815630 | |
408 | Phosphorylation | EGEETRFSTSGLSIS CCCCCEECCCCCCCC | 20.55 | 24076635 | |
415 | O-linked_Glycosylation | STSGLSISGLNPLPN CCCCCCCCCCCCCCC | 33.57 | 30379171 | |
415 | Phosphorylation | STSGLSISGLNPLPN CCCCCCCCCCCCCCC | 33.57 | 26657352 | |
424 | Phosphorylation | LNPLPNPSYLLPPRI CCCCCCHHHCCCHHH | 34.74 | 26657352 | |
425 | Phosphorylation | NPLPNPSYLLPPRIL CCCCCHHHCCCHHHH | 17.32 | 26657352 | |
433 | Phosphorylation | LLPPRILSATTSKVS CCCHHHHHHCCCCHH | 22.62 | 32142685 | |
435 | Phosphorylation | PPRILSATTSKVSST CHHHHHHCCCCHHHC | 28.38 | 24076635 | |
436 | Phosphorylation | PRILSATTSKVSSTG HHHHHHCCCCHHHCC | 26.68 | 24076635 | |
437 | Phosphorylation | RILSATTSKVSSTGL HHHHHCCCCHHHCCC | 27.06 | 24076635 | |
438 | Ubiquitination | ILSATTSKVSSTGLS HHHHCCCCHHHCCCC | 44.00 | 32142685 | |
440 | O-linked_Glycosylation | SATTSKVSSTGLSLK HHCCCCHHHCCCCCC | 26.39 | 30379171 | |
440 | Phosphorylation | SATTSKVSSTGLSLK HHCCCCHHHCCCCCC | 26.39 | 26657352 | |
441 | Phosphorylation | ATTSKVSSTGLSLKK HCCCCHHHCCCCCCH | 29.49 | 26657352 | |
442 | Phosphorylation | TTSKVSSTGLSLKKE CCCCHHHCCCCCCHH | 34.34 | 26657352 | |
445 | Phosphorylation | KVSSTGLSLKKEEEE CHHHCCCCCCHHHHH | 39.21 | 24719451 | |
447 | 2-Hydroxyisobutyrylation | SSTGLSLKKEEEEEE HHCCCCCCHHHHHHH | 55.55 | - | |
447 | Ubiquitination | SSTGLSLKKEEEEEE HHCCCCCCHHHHHHH | 55.55 | 32142685 | |
463 | Phosphorylation | SKVASKKTSQIGESF HHHHHHHHHHHCHHH | 29.60 | 27732954 | |
464 | Phosphorylation | KVASKKTSQIGESFE HHHHHHHHHHCHHHH | 28.78 | 27732954 | |
469 | Phosphorylation | KTSQIGESFEEILEE HHHHHCHHHHHHHHH | 32.51 | 29691806 | |
483 | Acetylation | ETVISTKKTEKSNIE HHHHCCCCCCCCCCC | 63.10 | 19811059 | |
486 | Ubiquitination | ISTKKTEKSNIEETT HCCCCCCCCCCCCCC | 54.77 | 32142685 | |
487 | Phosphorylation | STKKTEKSNIEETTI CCCCCCCCCCCCCCC | 36.49 | 27732954 | |
493 | O-linked_Glycosylation | KSNIEETTISSQKI- CCCCCCCCCCCCCC- | 23.34 | 30379171 | |
496 | Phosphorylation | IEETTISSQKI---- CCCCCCCCCCC---- | 31.48 | 17525332 | |
498 | Acetylation | ETTISSQKI------ CCCCCCCCC------ | 52.94 | 30586113 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of AINX_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AINX_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of AINX_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of AINX_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-290, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496, AND MASSSPECTROMETRY. |