UniProt ID | FMN1_MOUSE | |
---|---|---|
UniProt AC | Q05860 | |
Protein Name | Formin-1 | |
Gene Name | Fmn1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 1466 | |
Subcellular Localization |
Nucleus. Cytoplasm. Cell junction, adherens junction. Cell membrane Peripheral membrane protein Cytoplasmic side. Localization to the adherens junctions is alpha-catenin-dependent. Also localizes to F-actin bundles originating from adherens junctio |
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Protein Description | Plays a role in the formation of adherens junction and the polymerization of linear actin cables.. | |
Protein Sequence | MEGTHCTLQLHNPIAELCYISFYLPKGEVRGFSYKGTVTLDRSNNAFHNCYQVREGPDITSLSQQPNEHPGDIFFKQTPTKNILTELYKLTAEKERLLDSLLRSDNILGVSMGSQEGKLQELSVILATGDEYFQSAGNWRRELPVSSLIRRSTQENKKPRRSGRRRESPEELRQKRTRRKGRGCQESAFQMGKDQVCSSSSLSFRARPNLRLLEERGNLVPRGTLTSSLRRRESCPANILRTPDADLAFGNSGRTSEDTDLEGPLSPDSSPTEVGDADVGGQLKSSHQQEPPQPNVSESHGKHAGAERWSSRTRKSKSLERTCSKKPVSKVVAKIQEPSAPVKRIVRAHHDGKGRVAYGPETQTEFIPKADFLTLPGGETETHSSGRLEEEQPGIKSLRSSAPERASITKEPASTEAAVNKVLRKVIESEKLDEATEGKRLGFSLNTRATHTFPETRSQRKAGLPQSGHKFLLLDLPHTVGPDSPQPKCDEKKPTPQVPTALGMVFNNSSPQSSAHKRLSPVPSPLSPRCPSPQQHHRILLLPPLPSEGEVVFNEYPSRKNDVSSGFPSADTLEPSSTTKVTETKGASPTSLRASQTWLVSEEASEKGLGPEKITAPPQHQLPPGIASEGFPCDNFKEQTAKDLPNKDGGVWVPGYRAGPPCPFLLHEEKEKTSRSELYLDLNPDQSPTEQDDRTPGRLQAVWPPPKTKDTEEKVGLKYTEAEYQAAILHLKREHKEEIETLQAQFELKTFHIRGEHALVTARLEEAIENLKQQLGKRREGCEEMRDVCISTDDDCSPKAFRNVCIQTDRETFLKPCDAESKATRSSQIVPKKLTISLTQLSPSKDSKDIHAPFQTREGTSSSSQHKISPPAPPTPPPLPPPLIPPPPPLPPGLGPLPPAPPIPPVCPVSPPPPPPPPPPTPVPPSDGPPPPPPPPPPLPNVLALPNSGGPPPPPPPPPPGLAPPPPPGLSFGLSSSSSQYPRKPAIEPSCPMKPLYWTRIQINDKSQDAAPTLWDSLEEPHIRDTSEFEYLFSKDTTQQKKKPLSEAYEKKNKVKKIIKLLDGKRSQTVGILISSLHLEMKDIQQAIFTVDDSVVDLETLAALYENRAQEDELTKIRKYYETSKEEDLKLLDKPEQFLHELAQIPNFAERAQCIIFRAVFSEGITSLHRKVEIVTRASKGLLHMKSVKDILALILAFGNYMNGGNRTRGQADGYSLEILPKLKDVKSRDNGMNLVDYVVKYYLRYYDQCKHHDQEASCRGKDLFSLYFHIAVHPQRKSGLELKQEAGTDKSVFPLPEPQDFFLASQVKFEDLLKDLRKLKRQLEASEQQMKLVCKESPREYLQPFKDKLEEFFKKAKKEHKMEESHLENAQKSFETTVGYFGMKPKTGEKEVTPSYVFMVWFEFCSDFKTIWKRESKNISKERLKMAQASVSKLTSEKKVETKKINPTASLKERLRQKEASVATN | |
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 |
---|---|---|---|---|---|
37 | Phosphorylation | RGFSYKGTVTLDRSN CCEEEEEEEEEECCC | 13.23 | 24759943 | |
47 (in isoform 5) | Phosphorylation | - | 4.65 | 25338131 | |
62 (in isoform 5) | Phosphorylation | - | 3.92 | 25338131 | |
91 | Phosphorylation | LTELYKLTAEKERLL HHHHHHHHHHHHHHH | 28.72 | 22942356 | |
168 | Phosphorylation | RSGRRRESPEELRQK CCCCCCCCHHHHHHH | 35.48 | 25521595 | |
224 (in isoform 5) | Phosphorylation | - | 28.30 | 29233185 | |
228 | Phosphorylation | PRGTLTSSLRRRESC CCCCHHHHHHCHHCC | 22.21 | 23140645 | |
230 (in isoform 5) | Phosphorylation | - | 37.24 | 26824392 | |
234 | Phosphorylation | SSLRRRESCPANILR HHHHCHHCCCCCCCC | 24.48 | 29899451 | |
324 (in isoform 5) | Phosphorylation | - | 43.00 | 25168779 | |
327 (in isoform 5) | Phosphorylation | - | 39.07 | 27149854 | |
372 (in isoform 5) | Phosphorylation | - | 7.20 | 29550500 | |
373 (in isoform 5) | Phosphorylation | - | 5.04 | 29550500 | |
374 (in isoform 5) | Phosphorylation | - | 30.79 | 29550500 | |
381 (in isoform 5) | Phosphorylation | - | 39.97 | 23375375 | |
396 (in isoform 5) | Phosphorylation | - | 49.72 | 29514104 | |
399 (in isoform 5) | Phosphorylation | - | 35.34 | 27149854 | |
446 (in isoform 5) | Phosphorylation | - | 26.73 | 26824392 | |
451 (in isoform 5) | Phosphorylation | - | 25.24 | 30635358 | |
453 (in isoform 5) | Phosphorylation | - | 3.90 | 30635358 | |
457 (in isoform 5) | Phosphorylation | - | 29.18 | 30635358 | |
461 (in isoform 5) | Phosphorylation | - | 38.89 | 25195567 | |
463 (in isoform 5) | Phosphorylation | - | 40.71 | 30635358 | |
469 (in isoform 5) | Phosphorylation | - | 23.96 | 25159016 | |
500 | Phosphorylation | KPTPQVPTALGMVFN CCCCCCCCHHHHHCC | 35.34 | 28059163 | |
509 | Phosphorylation | LGMVFNNSSPQSSAH HHHHCCCCCCCCCCC | 44.49 | 28059163 | |
520 | Phosphorylation | SSAHKRLSPVPSPLS CCCCCCCCCCCCCCC | 28.08 | 25293948 | |
524 | Phosphorylation | KRLSPVPSPLSPRCP CCCCCCCCCCCCCCC | 38.41 | 20139300 | |
527 | Phosphorylation | SPVPSPLSPRCPSPQ CCCCCCCCCCCCCCC | 17.43 | 20139300 | |
532 | Phosphorylation | PLSPRCPSPQQHHRI CCCCCCCCCCCCCEE | 38.68 | 29899451 | |
582 | Phosphorylation | PSSTTKVTETKGASP CCCCCEEEECCCCCC | 39.22 | 25168779 | |
584 | Phosphorylation | STTKVTETKGASPTS CCCEEEECCCCCCCC | 25.97 | 25168779 | |
588 | Phosphorylation | VTETKGASPTSLRAS EEECCCCCCCCCCHH | 37.06 | 25168779 | |
590 | Phosphorylation | ETKGASPTSLRASQT ECCCCCCCCCCHHEE | 37.59 | 25168779 | |
591 | Phosphorylation | TKGASPTSLRASQTW CCCCCCCCCCHHEEE | 21.17 | 25168779 | |
605 | Phosphorylation | WLVSEEASEKGLGPE EEECHHHHHCCCCCC | 43.02 | 20531401 | |
673 | Phosphorylation | LHEEKEKTSRSELYL CCCHHCCCCCCEEEE | 30.39 | 22802335 | |
674 | Phosphorylation | HEEKEKTSRSELYLD CCHHCCCCCCEEEEE | 44.89 | 22802335 | |
689 | Phosphorylation | LNPDQSPTEQDDRTP CCCCCCCCCCCCCCC | 52.07 | 22802335 | |
792 | Phosphorylation | MRDVCISTDDDCSPK HHHHEEECCCCCCHH | 24.44 | 29233185 | |
797 | Phosphorylation | ISTDDDCSPKAFRNV EECCCCCCHHHHHHH | 36.11 | 25521595 | |
799 | Acetylation | TDDDCSPKAFRNVCI CCCCCCHHHHHHHEE | 43.81 | - | |
835 | Phosphorylation | QIVPKKLTISLTQLS CCCCCEEEEEEEECC | 19.87 | 23984901 | |
837 | Phosphorylation | VPKKLTISLTQLSPS CCCEEEEEEEECCCC | 21.82 | 25619855 | |
839 | Phosphorylation | KKLTISLTQLSPSKD CEEEEEEEECCCCCC | 22.22 | 25619855 | |
842 | Phosphorylation | TISLTQLSPSKDSKD EEEEEECCCCCCCCC | 19.81 | 25521595 | |
844 | Phosphorylation | SLTQLSPSKDSKDIH EEEECCCCCCCCCCC | 45.80 | 25619855 | |
991 | Glutathionylation | KPAIEPSCPMKPLYW CCCCCCCCCCCCCEE | 5.81 | 24333276 | |
1347 | Acetylation | REYLQPFKDKLEEFF HHHHHHHHHHHHHHH | 61.71 | 22902405 | |
1431 | Phosphorylation | RLKMAQASVSKLTSE HHHHHHHHHHHHHCC | 18.16 | 25619855 | |
1433 | Phosphorylation | KMAQASVSKLTSEKK HHHHHHHHHHHCCHH | 21.32 | 25619855 | |
1451 | Phosphorylation | KKINPTASLKERLRQ CCCCCCHHHHHHHHH | 42.31 | 26824392 |
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 FMN1_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FMN1_MOUSE !! |
* 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 FMN1_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
ABL1_MOUSE | Abl1 | physical | 8605874 | |
FYN_MOUSE | Fyn | physical | 8605874 | |
PR40A_MOUSE | Prpf40a | physical | 8605874 | |
TCRG1_MOUSE | Tcerg1 | physical | 8605874 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234, AND MASSSPECTROMETRY. |