CSPG5_HUMAN - dbPTM
CSPG5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CSPG5_HUMAN
UniProt AC O95196
Protein Name Chondroitin sulfate proteoglycan 5
Gene Name CSPG5
Organism Homo sapiens (Human).
Sequence Length 566
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Endoplasmic reticulum membrane
Single-pass type I membrane protein . Golgi apparatus membrane
Single-pass type I membrane protein . Cell surface . In neurons, localizes to synaptic junctions.
Protein Description May function as a growth and differentiation factor involved in neuritogenesis. May induce ERBB3 activation..
Protein Sequence MGRAGGGGPGRGPPPLLLFLGAALVLASGAVPAREAGSAVEAEELVKGSPAWEPPANDTREEAGPPAAGEDEASWTAPGGELAGPEEVLQESAAVTGTAWLEADSPGLGGVTAEAGSGDAQALPATLQAPHEVLGQSIMPPAIPEATEASGPPSPTPGDKLSPASELPKESPLEVWLNLGGSTPDPQGPELTYPFQGTLEPQPASDIIDIDYFEGLDGEGRGADLGSFPGSPGTSENHPDTEGETPSWSLLDLYDDFTPFDESDFYPTTSFYDDLDEEEEEEEDDKDAVGGGDLEDENELLVPTGKPGLGPGTGQPTSRWHAVPPQHTLGSVPGSSIALRPRPGEPGRDLASSENGTECRSGFVRHNGSCRSVCDLFPSYCHNGGQCYLVENIGAFCRCNTQDYIWHKGMRCESIITDFQVMCVAVGSAALVLLLLFMMTVFFAKKLYLLKTENTKLRRTNKFRTPSELHNDNFSLSTIAEGSHPNVRKLCNTPRTSSPHARALAHYDNVICQDDPSAPHKIQEVLKSCLKEEESFNIQNSMSPKLEGGKGDQADLDVNCLQNNLT
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
28PhosphorylationGAALVLASGAVPARE
HHHHHHHHCCCCHHH
24.1128348404
38PhosphorylationVPAREAGSAVEAEEL
CCHHHCCCCEEHHHH
35.8728348404
57N-linked_GlycosylationPAWEPPANDTREEAG
CCCCCCCCCCCHHHC
57.89UniProtKB CARBOHYD
117O-linked_GlycosylationGVTAEAGSGDAQALP
CEEEECCCCCCCCCC
40.31-
162O-linked_GlycosylationPTPGDKLSPASELPK
CCCCCCCCCHHHCCC
24.9455824583
165O-linked_GlycosylationGDKLSPASELPKESP
CCCCCCHHHCCCCCC
42.9555824589
327 (in isoform 3)Phosphorylation-28.9126471730
328O-linked_GlycosylationHAVPPQHTLGSVPGS
EECCCCCCCCCCCCC
27.8055823879
329 (in isoform 3)Phosphorylation-4.5226471730
335O-linked_GlycosylationTLGSVPGSSIALRPR
CCCCCCCCCEEEECC
16.70OGP
352 (in isoform 3)Phosphorylation-45.54-
465PhosphorylationRRTNKFRTPSELHND
CCCCCCCCHHHHCCC
34.0129978859
465 (in isoform 2)Phosphorylation-34.0126471730
467PhosphorylationTNKFRTPSELHNDNF
CCCCCCHHHHCCCCC
52.7829978859
467 (in isoform 2)Phosphorylation-52.7826471730
475PhosphorylationELHNDNFSLSTIAEG
HHCCCCCCHHHHCCC
27.8829978859
477PhosphorylationHNDNFSLSTIAEGSH
CCCCCCHHHHCCCCC
19.3029978859
478PhosphorylationNDNFSLSTIAEGSHP
CCCCCHHHHCCCCCC
29.5129978859
483PhosphorylationLSTIAEGSHPNVRKL
HHHHCCCCCCCHHHH
27.55-
490 (in isoform 2)Phosphorylation-1.58-
507PhosphorylationHARALAHYDNVICQD
HHHHHHHCCCEECCC
12.0129978859
531UbiquitinationEVLKSCLKEEESFNI
HHHHHHHCHHHCCCC
68.36-
541PhosphorylationESFNIQNSMSPKLEG
HCCCCCCCCCCCCCC
12.3123532336
543PhosphorylationFNIQNSMSPKLEGGK
CCCCCCCCCCCCCCC
20.7823532336

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 CSPG5_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CSPG5_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 CSPG5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GOPC_HUMANGOPCphysical
12885772

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CSPG5_HUMAN

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Related Literatures of Post-Translational Modification

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