EFCB7_HUMAN - dbPTM
EFCB7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EFCB7_HUMAN
UniProt AC A8K855
Protein Name EF-hand calcium-binding domain-containing protein 7
Gene Name EFCAB7
Organism Homo sapiens (Human).
Sequence Length 629
Subcellular Localization Cell projection, cilium membrane
Peripheral membrane protein
Cytoplasmic side . The EvC complex localizes at the base of cilia in the EvC zone of primary cilia in a EFCAB7-dependent manner.
Protein Description Component of the EvC complex that positively regulates ciliary Hedgehog (Hh) signaling. Required for the localization of the EVC2:EVC subcomplex at the base of primary cilia..
Protein Sequence MAISPRSDATFSSQKSTPSESPRTKKFPLTEEEIFYMNCRAAYLTVFKSSLENIISKDQLYLALQHAGRNPSQKTINKYWTPQTAKLNFDDFCIILRKEKPTSKAELLKSFKQLDVNDDGCILHTDLYKFLTKRGEKMTREEVNAIINLADVNADGKFDYIKFCKLYMTTNEQCLKTTLEKLEVDSKLMRHQFGNHIEGSPERDPSPVPKPSPKITRKTDPETFLNKGDTRSSLLSATRKFKTSVSFTVTMGANGNRNSKLMEPNLIKDWQHMQSKGCFFLEEDGEIISHQYRMQIAQRSMVYLTIKPLNLSQVEGKPSPWLSVDTALYILKENESQANLQLVCFTELRNREVFGWTGELGPGIYWLIPSTTGCRLRKKIKPVTDEAQLVYRDETGELFLTKEFKSTLSDIFEVIDLDGNGLLSLEEYNFFELRTSGEKCDEDAWAVCRENFDTKRNELTRQGFMDLNLMEANDREGDPCDLWVTLHSMGYNKALELTEACPFVIDIYAEKCKPKIKAVHMEACSGQLEKAICKSVLSNGDAKVMDGYENIIVHTYSCDTWITSVIENKSDEKVIIHISNELSKNCINNRGLNIFAVEVGPKSTMVCQHVMPLNERQEWIYYCIYSLIS
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
4Phosphorylation----MAISPRSDATF
----CCCCCCCCCCC
12.5326074081
7Phosphorylation-MAISPRSDATFSSQ
-CCCCCCCCCCCCCC
34.6726074081
10PhosphorylationISPRSDATFSSQKST
CCCCCCCCCCCCCCC
29.1026074081
12PhosphorylationPRSDATFSSQKSTPS
CCCCCCCCCCCCCCC
27.7526074081
13PhosphorylationRSDATFSSQKSTPSE
CCCCCCCCCCCCCCC
37.1226074081
15UbiquitinationDATFSSQKSTPSESP
CCCCCCCCCCCCCCC
59.2429967540
16PhosphorylationATFSSQKSTPSESPR
CCCCCCCCCCCCCCC
37.6021712546
17PhosphorylationTFSSQKSTPSESPRT
CCCCCCCCCCCCCCC
37.5621712546
19PhosphorylationSSQKSTPSESPRTKK
CCCCCCCCCCCCCCC
51.2828102081
21PhosphorylationQKSTPSESPRTKKFP
CCCCCCCCCCCCCCC
24.8228985074
24PhosphorylationTPSESPRTKKFPLTE
CCCCCCCCCCCCCCH
41.8028985074
49PhosphorylationAYLTVFKSSLENIIS
HHHHHHHHHHHHHCC
28.7928348404
50PhosphorylationYLTVFKSSLENIISK
HHHHHHHHHHHHCCH
40.0528348404
57UbiquitinationSLENIISKDQLYLAL
HHHHHCCHHHHHHHH
38.8029967540
74UbiquitinationAGRNPSQKTINKYWT
CCCCCCCCCHHHCCC
56.5627667366
75PhosphorylationGRNPSQKTINKYWTP
CCCCCCCCHHHCCCC
23.3427050516
78UbiquitinationPSQKTINKYWTPQTA
CCCCCHHHCCCCCCE
38.0129967540
87UbiquitinationWTPQTAKLNFDDFCI
CCCCCEECCCCCEEE
7.7727667366
100UbiquitinationCIILRKEKPTSKAEL
EEEEECCCCCCHHHH
57.5429967540
104UbiquitinationRKEKPTSKAELLKSF
ECCCCCCHHHHHHHH
48.64-
109UbiquitinationTSKAELLKSFKQLDV
CCHHHHHHHHHHCCC
67.48-
110PhosphorylationSKAELLKSFKQLDVN
CHHHHHHHHHHCCCC
37.3324719451
112UbiquitinationAELLKSFKQLDVNDD
HHHHHHHHHCCCCCC
57.9829967540
128PhosphorylationCILHTDLYKFLTKRG
EEEEHHHHHHHHHHC
11.5125147952
129UbiquitinationILHTDLYKFLTKRGE
EEEHHHHHHHHHHCC
40.9929967540
157UbiquitinationADVNADGKFDYIKFC
HHCCCCCCCCEEEEE
35.2929967540
165UbiquitinationFDYIKFCKLYMTTNE
CCEEEEEEEEECCCH
45.87-
181UbiquitinationCLKTTLEKLEVDSKL
HHHHHHHHHHHCHHH
53.7329967540
187UbiquitinationEKLEVDSKLMRHQFG
HHHHHCHHHHHHHCC
41.6729967540
200PhosphorylationFGNHIEGSPERDPSP
CCCCCCCCCCCCCCC
15.7026055452
206PhosphorylationGSPERDPSPVPKPSP
CCCCCCCCCCCCCCC
42.7026055452
210UbiquitinationRDPSPVPKPSPKITR
CCCCCCCCCCCCCCC
59.36-
212PhosphorylationPSPVPKPSPKITRKT
CCCCCCCCCCCCCCC
44.9726055452
227AcetylationDPETFLNKGDTRSSL
CHHHHHCCCCCHHHH
61.387712211
227UbiquitinationDPETFLNKGDTRSSL
CHHHHHCCCCCHHHH
61.3829967540
232PhosphorylationLNKGDTRSSLLSATR
HCCCCCHHHHHHHHC
27.6828555341
233PhosphorylationNKGDTRSSLLSATRK
CCCCCHHHHHHHHCC
30.0028555341
243PhosphorylationSATRKFKTSVSFTVT
HHHCCCCCEEEEEEE
37.1822210691
244PhosphorylationATRKFKTSVSFTVTM
HHCCCCCEEEEEEEE
19.1622210691
246PhosphorylationRKFKTSVSFTVTMGA
CCCCCEEEEEEEECC
18.2422210691
250PhosphorylationTSVSFTVTMGANGNR
CEEEEEEEECCCCCC
13.5622210691
260UbiquitinationANGNRNSKLMEPNLI
CCCCCCCCCCCCCHH
56.2425015289
273UbiquitinationLIKDWQHMQSKGCFF
HHHCHHHHHHCCCEE
2.6325015289
381UbiquitinationCRLRKKIKPVTDEAQ
CCCCCCCCCCCCCCE
42.1729967540
395PhosphorylationQLVYRDETGELFLTK
EEEEECCCCCEEEEH
40.0028348404
402UbiquitinationTGELFLTKEFKSTLS
CCCEEEEHHHHHHHH
64.4029967540
439UbiquitinationELRTSGEKCDEDAWA
EEECCCCCCCHHHHH
50.97-
525PhosphorylationAVHMEACSGQLEKAI
EEHHHHCCHHHHHHH
36.3023403867
535PhosphorylationLEKAICKSVLSNGDA
HHHHHHHHHHHCCCC
24.7129978859
538PhosphorylationAICKSVLSNGDAKVM
HHHHHHHHCCCCEEE
36.2929978859

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 EFCB7_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EFCB7_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 EFCB7_HUMAN !!

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

Oops, there are no PPI records of EFCB7_HUMAN !!

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 EFCB7_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP