AINX_RAT - dbPTM
AINX_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AINX_RAT
UniProt AC P23565
Protein Name Alpha-internexin
Gene Name Ina
Organism Rattus norvegicus (Rat).
Sequence Length 505
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 (By similarity)..
Protein Sequence MSFGSEHYLCSASSYRKVFGDGSRLSARLSGPGASGSFRSQSLSRSNVASTAACSSASSLGLGLAYRRLPASDGLDLSQAAARTNEYKIIRTNEKEQLQGLNDRFAVFIEKVHQLETQNRALEAELAALRQRHAEPSRVGELFQRELRELRAQLEEASSARAQALLERDGLAEEVQRLRARCEEESRGREGAERALKAQQRDVDGATLARLDLEKKVESLLDELAFVRQVHDEEVAELLATLQASSQAAAEVDVAVAKPDLTSALREIRAQYESLAAKNLQSAEEWYKSKFANLNEQAARSTEAIRASREEIHEYRRQLQARTIEIEGLRGANESLERQILELEERHSAEVAGYQDSIGQLESDLRNTKSEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETRFSTSGLSISGLNPLPNPSYLLPPRILSSTTSKVSSAGLSLKKEEEEEEEEEEGASKEVTKKTSKVGESFEETLEETVVSTKKTEKSTIEEITTSSSQKM
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
17AcetylationCSASSYRKVFGDGSR
ECHHHHCHHHCCCCC
33.4122902405
66PhosphorylationSLGLGLAYRRLPASD
HCCCCHHHCCCCCCC
10.99-
72PhosphorylationAYRRLPASDGLDLSQ
HHCCCCCCCCCCHHH
30.21-
78PhosphorylationASDGLDLSQAAARTN
CCCCCCHHHHHHHCC
19.89-
87PhosphorylationAAARTNEYKIIRTNE
HHHHCCCCEEEECCH
15.01-
88AcetylationAARTNEYKIIRTNEK
HHHCCCCEEEECCHH
26.0222902405
95AcetylationKIIRTNEKEQLQGLN
EEEECCHHHHHCCCH
53.4822902405
95UbiquitinationKIIRTNEKEQLQGLN
EEEECCHHHHHCCCH
53.48-
216AcetylationARLDLEKKVESLLDE
HHHCHHHHHHHHHHH
41.6922902405
219PhosphorylationDLEKKVESLLDELAF
CHHHHHHHHHHHHHH
36.90-
278UbiquitinationQYESLAAKNLQSAEE
HHHHHHHHHCCCHHH
53.21-
288AcetylationQSAEEWYKSKFANLN
CCHHHHHHHHHCCHH
48.5222902405
290AcetylationAEEWYKSKFANLNEQ
HHHHHHHHHCCHHHH
44.3222902405
315PhosphorylationSREEIHEYRRQLQAR
HHHHHHHHHHHHHHH
9.27-
335PhosphorylationGLRGANESLERQILE
CCCCCCHHHHHHHHH
35.0225403869
354PhosphorylationHSAEVAGYQDSIGQL
HHHHHHCCHHHHHHH
10.22-
369AcetylationESDLRNTKSEMARHL
HHHHHHCHHHHHHHH
48.2222902405
379PhosphorylationMARHLREYQDLLNVK
HHHHHHHHHHHHCHH
10.82-
396PhosphorylationLDIEIAAYRKLLEGE
HHHHHHHHHHHHCCC
10.16-
398AcetylationIEIAAYRKLLEGEET
HHHHHHHHHHCCCCC
44.7672622467
408PhosphorylationEGEETRFSTSGLSIS
CCCCCEECCCCCCCC
20.5522673903
409PhosphorylationGEETRFSTSGLSISG
CCCCEECCCCCCCCC
24.8922673903
410PhosphorylationEETRFSTSGLSISGL
CCCEECCCCCCCCCC
36.2222673903
413PhosphorylationRFSTSGLSISGLNPL
EECCCCCCCCCCCCC
20.4522673903
415PhosphorylationSTSGLSISGLNPLPN
CCCCCCCCCCCCCCC
33.5722673903
425PhosphorylationNPLPNPSYLLPPRIL
CCCCCHHHCCCCHHC
17.32-
434PhosphorylationLPPRILSSTTSKVSS
CCCHHCCCCCCCCHH
32.0528432305
435PhosphorylationPPRILSSTTSKVSSA
CCHHCCCCCCCCHHC
31.5428432305
436PhosphorylationPRILSSTTSKVSSAG
CHHCCCCCCCCHHCC
28.6228432305
437PhosphorylationRILSSTTSKVSSAGL
HHCCCCCCCCHHCCC
31.0228432305
440PhosphorylationSSTTSKVSSAGLSLK
CCCCCCCHHCCCCCC
20.4328432305
441PhosphorylationSTTSKVSSAGLSLKK
CCCCCCHHCCCCCCH
29.3728432305
445PhosphorylationKVSSAGLSLKKEEEE
CCHHCCCCCCHHHHH
36.9128432305
468PhosphorylationSKEVTKKTSKVGESF
CHHHHHHHHHCCCHH
35.0228432305
469PhosphorylationKEVTKKTSKVGESFE
HHHHHHHHHCCCHHH
33.9328432305
474PhosphorylationKTSKVGESFEETLEE
HHHHCCCHHHHHHHH
31.8427097102
478PhosphorylationVGESFEETLEETVVS
CCCHHHHHHHHHHHC
32.0727097102
501PhosphorylationIEEITTSSSQKM---
HHHHHCCCCCCC---
34.3928551015
502PhosphorylationEEITTSSSQKM----
HHHHCCCCCCC----
33.3228551015

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AINX_RAT !!

Disease-associated PTM Sites based on SAP

* 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_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of AINX_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AINX_RAT

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Related Literatures of Post-Translational Modification

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