ABRA_HUMAN - dbPTM
ABRA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ABRA_HUMAN
UniProt AC Q8N0Z2
Protein Name Actin-binding Rho-activating protein
Gene Name ABRA {ECO:0000312|EMBL:AAI05106.1}
Organism Homo sapiens (Human).
Sequence Length 381
Subcellular Localization Cytoplasm, myofibril, sarcomere. Cytoplasm, cytoskeleton. Localized to the I-band of the sarcomere and to a lesser extent to the sarcomeric structure between Z-lines..
Protein Description Acts as an activator of serum response factor (SRF)-dependent transcription possibly by inducing nuclear translocation of MKL1 or MKL2 and through a mechanism requiring Rho-actin signaling..
Protein Sequence MAPGEKESGEGPAKSALRKIRTATLVISLARGWQQWANENSIRQAQEPTGWLPGGTQDSPQAPKPITPPTSHQKAQSAPKSPPRLPEGHGDGQSSEKAPEVSHIKKKEVSKTVVSKTYERGGDVSHLSHRYERDAGVLEPGQPENDIDRILHSHGSPTRRRKCANLVSELTKGWRVMEQEEPTWRSDSVDTEDSGYGGEAEERPEQDGVQVAVVRIKRPLPSQVNRFTEKLNCKAQQKYSPVGNLKGRWQQWADEHIQSQKLNPFSEEFDYELAMSTRLHKGDEGYGRPKEGTKTAERAKRAEEHIYREMMDMCFIICTMARHRRDGKIQVTFGDLFDRYVRISDKVVGILMRARKHGLVDFEGEMLWQGRDDHVVITLLK
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
8PhosphorylationMAPGEKESGEGPAKS
CCCCCCCCCCCCHHH
53.8923898821
24PhosphorylationLRKIRTATLVISLAR
HHHHHHHHHHHHHHH
22.4246157307
28PhosphorylationRTATLVISLARGWQQ
HHHHHHHHHHHHHHH
14.4346157295
81PhosphorylationKAQSAPKSPPRLPEG
HHHCCCCCCCCCCCC
38.7922210691
94PhosphorylationEGHGDGQSSEKAPEV
CCCCCCCCCCCCCCC
46.0922210691
95PhosphorylationGHGDGQSSEKAPEVS
CCCCCCCCCCCCCCC
34.9222210691
110PhosphorylationHIKKKEVSKTVVSKT
CCCHHHCCCEEEEEC
24.5723403867
112PhosphorylationKKKEVSKTVVSKTYE
CHHHCCCEEEEECEE
20.7323403867
115PhosphorylationEVSKTVVSKTYERGG
HCCCEEEEECEECCC
18.2323403867
117PhosphorylationSKTVVSKTYERGGDV
CCEEEEECEECCCCH
24.1023403867
118PhosphorylationKTVVSKTYERGGDVS
CEEEEECEECCCCHH
13.8323403867
156PhosphorylationRILHSHGSPTRRRKC
HHHHHCCCHHHHHHH
20.0626437602
188PhosphorylationEPTWRSDSVDTEDSG
CCCCCCCCCCCCCCC
24.12-
259PhosphorylationWADEHIQSQKLNPFS
HHHHHHHHCCCCCCC
28.7830576142
266PhosphorylationSQKLNPFSEEFDYEL
HCCCCCCCHHHCHHH
37.1630576142
271PhosphorylationPFSEEFDYELAMSTR
CCCHHHCHHHHHHCC
20.4030576142
286PhosphorylationLHKGDEGYGRPKEGT
CCCCCCCCCCCCCCC
14.121948195
332PhosphorylationRDGKIQVTFGDLFDR
CCCCEEEEEHHHHHH
12.91100646207
344PhosphorylationFDRYVRISDKVVGIL
HHHHEEHHHHHHHHH
22.3346157301
356UbiquitinationGILMRARKHGLVDFE
HHHHHHHHHCCEECC
40.83-

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 ABRA_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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 ABRA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACTS_HUMANACTA1physical
17194709
ABLM2_HUMANABLIM2physical
17194709
ABLM3_HUMANABLIM3physical
17194709

Drug and Disease Associations
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.
Regulatory Network of ABRA_HUMAN

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Related Literatures of Post-Translational Modification

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