CHPF2_HUMAN - dbPTM
CHPF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHPF2_HUMAN
UniProt AC Q9P2E5
Protein Name Chondroitin sulfate glucuronyltransferase
Gene Name CHPF2
Organism Homo sapiens (Human).
Sequence Length 772
Subcellular Localization Golgi apparatus, Golgi stack membrane
Single-pass type II membrane protein .
Protein Description Transfers glucuronic acid (GlcUA) from UDP-GlcUA to N-acetylgalactosamine residues on the non-reducing end of the elongating chondroitin polymer. Has no N-acetylgalactosaminyltransferase activity..
Protein Sequence MRLSSLLALLRPALPLILGLSLGCSLSLLRVSWIQGEGEDPCVEAVGERGGPQNPDSRARLDQSDEDFKPRIVPYYRDPNKPYKKVLRTRYIQTELGSRERLLVAVLTSRATLSTLAVAVNRTVAHHFPRLLYFTGQRGARAPAGMQVVSHGDERPAWLMSETLRHLHTHFGADYDWFFIMQDDTYVQAPRLAALAGHLSINQDLYLGRAEEFIGAGEQARYCHGGFGYLLSRSLLLRLRPHLDGCRGDILSARPDEWLGRCLIDSLGVGCVSQHQGQQYRSFELAKNRDPEKEGSSAFLSAFAVHPVSEGTLMYRLHKRFSALELERAYSEIEQLQAQIRNLTVLTPEGEAGLSWPVGLPAPFTPHSRFEVLGWDYFTEQHTFSCADGAPKCPLQGASRADVGDALETALEQLNRRYQPRLRFQKQRLLNGYRRFDPARGMEYTLDLLLECVTQRGHRRALARRVSLLRPLSRVEILPMPYVTEATRVQLVLPLLVAEAAAAPAFLEAFAANVLEPREHALLTLLLVYGPREGGRGAPDPFLGVKAAAAELERRYPGTRLAWLAVRAEAPSQVRLMDVVSKKHPVDTLFFLTTVWTRPGPEVLNRCRMNAISGWQAFFPVHFQEFNPALSPQRSPPGPPGAGPDPPSPPGADPSRGAPIGGRFDRQASAEGCFYNADYLAARARLAGELAGQEEEEALEGLEVMDVFLRFSGLHLFRAVEPGLVQKFSLRDCSPRLSEELYHRCRLSNLEGLGGRAQLAMALFEQEQANST
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
57PhosphorylationGGPQNPDSRARLDQS
CCCCCCCCCCCCCCC
29.1528509920
64PhosphorylationSRARLDQSDEDFKPR
CCCCCCCCCCCCCCC
42.5128355574
69UbiquitinationDQSDEDFKPRIVPYY
CCCCCCCCCCCCCCC
45.79-
83PhosphorylationYRDPNKPYKKVLRTR
CCCCCCCHHHHHHHH
25.6724719451
89PhosphorylationPYKKVLRTRYIQTEL
CHHHHHHHHHCHHHC
24.5424719451
91PhosphorylationKKVLRTRYIQTELGS
HHHHHHHHCHHHCCC
9.2124905233
94PhosphorylationLRTRYIQTELGSRER
HHHHHCHHHCCCHHH
24.5024905233
98PhosphorylationYIQTELGSRERLLVA
HCHHHCCCHHHHHHH
43.5224905233
121N-linked_GlycosylationSTLAVAVNRTVAHHF
HHHHHHHHHHHHHHC
24.94UniProtKB CARBOHYD
229PhosphorylationYCHGGFGYLLSRSLL
HCCCCHHHHHCHHHH
11.3830576142
232PhosphorylationGGFGYLLSRSLLLRL
CCHHHHHCHHHHHHH
19.7530576142
252PhosphorylationGCRGDILSARPDEWL
CCCCCHHHCCCCHHH
23.6724719451
287UbiquitinationYRSFELAKNRDPEKE
EEEEEHHHCCCHHHC
66.20-
301PhosphorylationEGSSAFLSAFAVHPV
CCCHHHHHHEEEEEC
18.19-
315PhosphorylationVSEGTLMYRLHKRFS
CCCCCHHHHHHHHCH
17.09-
342N-linked_GlycosylationQLQAQIRNLTVLTPE
HHHHHHHCCEEECCC
41.51UniProtKB CARBOHYD
467PhosphorylationRALARRVSLLRPLSR
HHHHHHHHHHCCCCC
21.6326434776
473PhosphorylationVSLLRPLSRVEILPM
HHHHCCCCCCEEECC
36.6426434776
546UbiquitinationPDPFLGVKAAAAELE
CCCCHHHHHHHHHHH
30.43-
582UbiquitinationRLMDVVSKKHPVDTL
EHHHHHCCCCCCCEE
43.42-
631PhosphorylationQEFNPALSPQRSPPG
HHCCCCCCCCCCCCC
22.5424719451
648O-linked_GlycosylationGAGPDPPSPPGADPS
CCCCCCCCCCCCCCC
49.46OGP
727UbiquitinationVEPGLVQKFSLRDCS
CCCCCEEEEECCCCC
29.46-
729PhosphorylationPGLVQKFSLRDCSPR
CCCEEEEECCCCCHH
29.5425394399

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 CHPF2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHPF2_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 CHPF2_HUMAN !!

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

Oops, there are no PPI records of CHPF2_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CHPF2_HUMAN

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Related Literatures of Post-Translational Modification

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