AHSA1_MOUSE - dbPTM
AHSA1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AHSA1_MOUSE
UniProt AC Q8BK64
Protein Name Activator of 90 kDa heat shock protein ATPase homolog 1
Gene Name Ahsa1
Organism Mus musculus (Mouse).
Sequence Length 338
Subcellular Localization Cytoplasm, cytosol . Endoplasmic reticulum . May transiently interact with the endoplasmic reticulum.
Protein Description Acts as a co-chaperone of HSP90AA1. [PubMed: 29127155 Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity]
Protein Sequence MAKWGEGDPRWIVEERADATNVNNWHWTERDASNWSTEKLKTLFLAVRVENEEGKCEVTEVNKLDGEASINNRKGKLIFFYEWTIKLNWTGTSKSGVQYKGHVEIPNLSDENSVDEVEISVSLAKDEPDTNLVALMKEDGVKLLREAVGIYISTLKTEFTQGMILPTVNGESVDPVGQPALKTETCKAKSAPSKSQAKPVGVKIPTCKITLKETFLTSPEELYRVFTTQELVQAFTHAPAALEADRGGKFHMVDGNVTGEFTDLVPEKHIAMKWRFKSWPEGHFATITLTFIDKNGETELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFGYGARLF
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
3Acetylation-----MAKWGEGDPR
-----CCCCCCCCCC
55.2023806337
56S-nitrosocysteineVENEEGKCEVTEVNK
EECCCCCEEEEEEEE
8.16-
56S-nitrosylationVENEEGKCEVTEVNK
EECCCCCEEEEEEEE
8.1621278135
69PhosphorylationNKLDGEASINNRKGK
EECCCEEEECCCCCE
22.8825159016
193PhosphorylationCKAKSAPSKSQAKPV
CCCCCCCCHHHCCCC
44.66-
194AcetylationKAKSAPSKSQAKPVG
CCCCCCCHHHCCCCC
45.5923806337
195PhosphorylationAKSAPSKSQAKPVGV
CCCCCCHHHCCCCCC
39.4481018081
198MalonylationAPSKSQAKPVGVKIP
CCCHHHCCCCCCCCC
32.3826320211
203MalonylationQAKPVGVKIPTCKIT
HCCCCCCCCCCCEEE
36.7226320211
208MalonylationGVKIPTCKITLKETF
CCCCCCCEEEEEEEC
41.0026320211
212AcetylationPTCKITLKETFLTSP
CCCEEEEEEECCCCH
46.1623236377
217PhosphorylationTLKETFLTSPEELYR
EEEEECCCCHHHHHH
37.7429899451
218PhosphorylationLKETFLTSPEELYRV
EEEECCCCHHHHHHH
32.2525338131
223PhosphorylationLTSPEELYRVFTTQE
CCCHHHHHHHCCHHH
14.17-
249AcetylationLEADRGGKFHMVDGN
EECCCCCCEEEECCC
34.6123806337

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
223YPhosphorylationKinaseABLP00520
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AHSA1_MOUSE !!

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 AHSA1_MOUSE !!

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

Oops, there are no PPI records of AHSA1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AHSA1_MOUSE

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Related Literatures of Post-Translational Modification

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