CHSS1_HUMAN - dbPTM
CHSS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHSS1_HUMAN
UniProt AC Q86X52
Protein Name Chondroitin sulfate synthase 1
Gene Name CHSY1
Organism Homo sapiens (Human).
Sequence Length 802
Subcellular Localization Golgi apparatus, Golgi stack membrane
Single-pass type II membrane protein . Secreted .
Protein Description Has both beta-1,3-glucuronic acid and beta-1,4-N-acetylgalactosamine transferase activity. Transfers glucuronic acid (GlcUA) from UDP-GlcUA and N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of the elongating chondroitin polymer. Involved in the negative control of osteogenesis likely through the modulation of NOTCH signaling..
Protein Sequence MAARGRRAWLSVLLGLVLGFVLASRLVLPRASELKRAGPRRRASPEGCRSGQAAASQAGGARGDARGAQLWPPGSDPDGGPRDRNFLFVGVMTAQKYLQTRAVAAYRTWSKTIPGKVQFFSSEGSDTSVPIPVVPLRGVDDSYPPQKKSFMMLKYMHDHYLDKYEWFMRADDDVYIKGDRLENFLRSLNSSEPLFLGQTGLGTTEEMGKLALEPGENFCMGGPGVIMSREVLRRMVPHIGKCLREMYTTHEDVEVGRCVRRFAGVQCVWSYEMQQLFYENYEQNKKGYIRDLHNSKIHQAITLHPNKNPPYQYRLHSYMLSRKISELRHRTIQLHREIVLMSKYSNTEIHKEDLQLGIPPSFMRFQPRQREEILEWEFLTGKYLYSAVDGQPPRRGMDSAQREALDDIVMQVMEMINANAKTRGRIIDFKEIQYGYRRVNPMYGAEYILDLLLLYKKHKGKKMTVPVRRHAYLQQTFSKIQFVEHEELDAQELAKRINQESGSLSFLSNSLKKLVPFQLPGSKSEHKEPKDKKINILIPLSGRFDMFVRFMGNFEKTCLIPNQNVKLVVLLFNSDSNPDKAKQVELMRDYRIKYPKADMQILPVSGEFSRALALEVGSSQFNNESLLFFCDVDLVFTTEFLQRCRANTVLGQQIYFPIIFSQYDPKIVYSGKVPSDNHFAFTQKTGFWRNYGFGITCIYKGDLVRVGGFDVSIQGWGLEDVDLFNKVVQAGLKTFRSQEVGVVHVHHPVFCDPNLDPKQYKMCLGSKASTYGSTQQLAEMWLEKNDPSYSKSSNNNGSVRTA
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
93PhosphorylationFLFVGVMTAQKYLQT
CEEEEEEHHHHHHHH
24.4327794612
142PhosphorylationPLRGVDDSYPPQKKS
ECCCCCCCCCCCHHC
34.77-
143PhosphorylationLRGVDDSYPPQKKSF
CCCCCCCCCCCHHCH
26.40-
189N-linked_GlycosylationENFLRSLNSSEPLFL
HHHHHHCCCCCCEEC
44.74UniProtKB CARBOHYD
325PhosphorylationYMLSRKISELRHRTI
HHHHHHHHHHHHHHH
33.3524719451
344PhosphorylationEIVLMSKYSNTEIHK
HHHHHHCCCCCEECH
10.3925884760
422PhosphorylationMINANAKTRGRIIDF
HHHCCCCCCCCCCCH
35.63-
436PhosphorylationFKEIQYGYRRVNPMY
HHHHHHCCCCCCCCC
7.13-
541PhosphorylationINILIPLSGRFDMFV
EEEEEECCCCCHHHH
23.67-
623N-linked_GlycosylationVGSSQFNNESLLFFC
CCCCCCCCCCEEEEE
41.33UniProtKB CARBOHYD
669PhosphorylationQYDPKIVYSGKVPSD
CCCCEEEEECCCCCC
18.38-
691PhosphorylationKTGFWRNYGFGITCI
CCCCHHHCCEEEEEE
12.78-
699PhosphorylationGFGITCIYKGDLVRV
CEEEEEEEECCEEEE
15.86-
769O-linked_GlycosylationMCLGSKASTYGSTQQ
HHHCCHHHCCCCHHH
26.3755832869
770O-linked_GlycosylationCLGSKASTYGSTQQL
HHCCHHHCCCCHHHH
36.4455832875
796N-linked_GlycosylationYSKSSNNNGSVRTA-
CCCCCCCCCCCCCC-
48.65UniProtKB CARBOHYD
798PhosphorylationKSSNNNGSVRTA---
CCCCCCCCCCCC---
15.56-

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 CHSS1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHSS1_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 CHSS1_HUMAN !!

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

Oops, there are no PPI records of CHSS1_HUMAN !!

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
605282Temtamy preaxial brachydactyly syndrome (TPBS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CHSS1_HUMAN

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Related Literatures of Post-Translational Modification

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