PCDBG_HUMAN - dbPTM
PCDBG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCDBG_HUMAN
UniProt AC Q9NRJ7
Protein Name Protocadherin beta-16
Gene Name PCDHB16
Organism Homo sapiens (Human).
Sequence Length 776
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain..
Protein Sequence MEIGWMHNRRQRQVLVFFVLLSLSGAGAELGSYSVVEETERGSFVANLGKDLGLGLTEMSTRKARIISQGNKQHLQLKAQTGDLLINEKLDREELCGPTEPCILHFQVLMENPLEIFQAELRVIDINDHSPMFTEKEMILKIPENSPLGTEFPLNHALDLDVGSNNVQNYKISPSSHFRVLIHEFRDGRKYPELVLDKELDREEEPQLRLTLTALDGGSPPRSGTAQVRIEVVDINDNAPEFEQPIYKVQIPENSPLGSLVATVSARDLDGGANGKISYTLFQPSEDISKTLEVNPMTGEVRLRKQVDFEMVTSYEVRIKATDGGGLSGKCTLLLQVVDVNDNPPQVTMSALTSPIPENSPEIVVAVFSVSDPDSGNNGKTISSIQEDLPFLLKPSVKNFYTLVTERALDREARAEYNITLTVTDMGTPRLKTEHNITVQISDVNDNAPTFTQTSYTLFVRENNSPALHIGSVSATDRDSGTNAQVTYSLLPPQDPHLPLASLVSINADNGHLFALRSLDYEALREFEFRVSATDRGSPALSSEALVRVLVLDANDNSPFVLYPLQNGSAPCTELVPRAAEPGYLVTKVVAVDGDSGQNAWLSYQLLKATEPGLFGVWAHNGEVRTARLLSERDAAKQRLVVLVKDNGEPPRSATATLHVLLVDGFSQPFLPLPEAAPGQTQANSLTVYLVVALASVSSLFLFSVLLFVAVRLCRRSRAASVGRCSMPEGPFPGRLVDVSGTGTLSQSYQYEVCLTGGSETSEFKFLKPIIPNFSP
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
57PhosphorylationKDLGLGLTEMSTRKA
CCCCCCCHHHCHHHE
28.0423403867
60PhosphorylationGLGLTEMSTRKARII
CCCCHHHCHHHEEEH
20.8723403867
61PhosphorylationLGLTEMSTRKARIIS
CCCHHHCHHHEEEHH
34.5723403867
191PhosphorylationEFRDGRKYPELVLDK
ECCCCCCCCCCEECC
10.6922817900
298PhosphorylationTLEVNPMTGEVRLRK
CEEECCCCCEEEEEE
31.29-
313PhosphorylationQVDFEMVTSYEVRIK
ECCEEEECEEEEEEE
25.0428509920
314PhosphorylationVDFEMVTSYEVRIKA
CCEEEECEEEEEEEE
14.1128509920
315PhosphorylationDFEMVTSYEVRIKAT
CEEEECEEEEEEEEC
14.7428509920
401PhosphorylationKPSVKNFYTLVTERA
CHHHHHHHHHHHHHH
14.4622617229
402O-linked_GlycosylationPSVKNFYTLVTERAL
HHHHHHHHHHHHHHC
15.6030620550
402PhosphorylationPSVKNFYTLVTERAL
HHHHHHHHHHHHHHC
15.6022617229
417PhosphorylationDREARAEYNITLTVT
CHHHHHHEEEEEEEE
15.7522210691
418N-linked_GlycosylationREARAEYNITLTVTD
HHHHHHEEEEEEEEE
16.57UniProtKB CARBOHYD
424PhosphorylationYNITLTVTDMGTPRL
EEEEEEEEECCCCCC
18.2922210691
436N-linked_GlycosylationPRLKTEHNITVQISD
CCCEEECEEEEEEEE
25.95UniProtKB CARBOHYD
567N-linked_GlycosylationFVLYPLQNGSAPCTE
EEEEECCCCCCCCCC
54.81UniProtKB CARBOHYD
768UbiquitinationTSEFKFLKPIIPNFS
CCCEEECCCCCCCCC
36.9832142685
775PhosphorylationKPIIPNFSP------
CCCCCCCCC------
36.0222199227

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 PCDBG_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCDBG_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 PCDBG_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PCDBA_HUMANPCDHB10physical
28514442
PCDB7_HUMANPCDHB7physical
28514442
PCDB6_HUMANPCDHB6physical
28514442
GAST_HUMANGASTphysical
28514442
KCJ11_HUMANKCNJ11physical
28514442
PDZD8_HUMANPDZD8physical
28514442
TAOK2_HUMANTAOK2physical
28514442
DEF5_HUMANDEFA5physical
28514442
KCNT2_HUMANKCNT2physical
28514442
PTPRD_HUMANPTPRDphysical
28514442
C2C2L_HUMANC2CD2Lphysical
28514442
CBX6_HUMANCBX6physical
28514442
NSMA_HUMANSMPD2physical
28514442
GAS6_HUMANGAS6physical
28514442
BT2A2_HUMANBTN2A2physical
28514442
RL23_HUMANRPL23physical
28514442
ST7_HUMANST7physical
28514442
AT2A3_HUMANATP2A3physical
28514442
RETST_HUMANRETSATphysical
28514442
P121A_HUMANPOM121physical
28514442
PLPL6_HUMANPNPLA6physical
28514442
S12A4_HUMANSLC12A4physical
28514442
OSBP1_HUMANOSBPphysical
28514442
MTHR_HUMANMTHFRphysical
28514442
SEMG1_HUMANSEMG1physical
28514442
PTPRF_HUMANPTPRFphysical
28514442
UPK3L_HUMANUPK3BLphysical
28514442
POMT2_HUMANPOMT2physical
28514442
GRM1A_HUMANGRAMD1Aphysical
28514442
S39AB_HUMANSLC39A11physical
28514442
ITA6_HUMANITGA6physical
28514442
EHD4_HUMANEHD4physical
28514442
ABCA3_HUMANABCA3physical
28514442
ATF6A_HUMANATF6physical
28514442

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

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Related Literatures of Post-Translational Modification

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