CHSS2_HUMAN - dbPTM
CHSS2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHSS2_HUMAN
UniProt AC Q8IZ52
Protein Name Chondroitin sulfate synthase 2
Gene Name CHPF
Organism Homo sapiens (Human).
Sequence Length 775
Subcellular Localization Isoform 1: Golgi apparatus, Golgi stack membrane
Single-pass type II membrane protein . Cytoplasm, cytosol .
Isoform 3: Cytoplasm, cytosol . Mitochondrion .
Isoform 2: Mitochondrion matrix .
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. Isoform 2 may facilitate PRKN transport into the mitochondria. In collaboration with PRKN, isoform 2 may enhance cell viability and protect cells from oxidative stress..
Protein Sequence MRASLLLSVLRPAGPVAVGISLGFTLSLLSVTWVEEPCGPGPPQPGDSELPPRGNTNAARRPNSVQPGAEREKPGAGEGAGENWEPRVLPYHPAQPGQAAKKAVRTRYISTELGIRQRLLVAVLTSQTTLPTLGVAVNRTLGHRLERVVFLTGARGRRAPPGMAVVTLGEERPIGHLHLALRHLLEQHGDDFDWFFLVPDTTYTEAHGLARLTGHLSLASAAHLYLGRPQDFIGGEPTPGRYCHGGFGVLLSRMLLQQLRPHLEGCRNDIVSARPDEWLGRCILDATGVGCTGDHEGVHYSHLELSPGEPVQEGDPHFRSALTAHPVRDPVHMYQLHKAFARAELERTYQEIQELQWEIQNTSHLAVDGDQAAAWPVGIPAPSRPASRFEVLRWDYFTEQHAFSCADGSPRCPLRGADRADVADVLGTALEELNRRYHPALRLQKQQLVNGYRRFDPARGMEYTLDLQLEALTPQGGRRPLTRRVQLLRPLSRVEILPVPYVTEASRLTVLLPLAAAERDLAPGFLEAFATAALEPGDAAAALTLLLLYEPRQAQRVAHADVFAPVKAHVAELERRFPGARVPWLSVQTAAPSPLRLMDLLSKKHPLDTLFLLAGPDTVLTPDFLNRCRMHAISGWQAFFPMHFQAFHPAVAPPQGPGPPELGRDTGRFDRQAASEACFYNSDYVAARGRLAAASEQEEELLESLDVYELFLHFSSLHVLRAVEPALLQRYRAQTCSARLSEDLYHRCLQSVLEGLGSRTQLAMLLFEQEQGNST
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
8PhosphorylationMRASLLLSVLRPAGP
CCHHHHHHHHCCCCC		21.0524719451
47UbiquitinationPGPPQPGDSELPPRG
CCCCCCCCCCCCCCC		45.6922817900
56PhosphorylationELPPRGNTNAARRPN
CCCCCCCCCCCCCCC		29.1122210691
64PhosphorylationNAARRPNSVQPGAER
CCCCCCCCCCCCCCC		25.4722210691
73UbiquitinationQPGAEREKPGAGEGA
CCCCCCCCCCCCCCC		55.7821906983
91PhosphorylationWEPRVLPYHPAQPGQ
CCCCCCCCCCCCCCH		19.10-
101UbiquitinationAQPGQAAKKAVRTRY
CCCCHHHHHHHHHHH		44.2621906983
102UbiquitinationQPGQAAKKAVRTRYI
CCCHHHHHHHHHHHH		47.6022817900
110PhosphorylationAVRTRYISTELGIRQ
HHHHHHHHHHHHHHH		13.5923186163
111PhosphorylationVRTRYISTELGIRQR
HHHHHHHHHHHHHHH		26.1823186163
126PhosphorylationLLVAVLTSQTTLPTL
HHHHHHHCCCCCCCH		22.7417525332
129PhosphorylationAVLTSQTTLPTLGVA
HHHHCCCCCCCHHHH		24.0917525332
138N-linked_GlycosylationPTLGVAVNRTLGHRL
CCHHHHHHHHHHHHC		22.83UniProtKB CARBOHYD
154UbiquitinationRVVFLTGARGRRAPP
EEEEEECCCCCCCCC		12.9121963094
176UbiquitinationGEERPIGHLHLALRH
CCCCCHHHHHHHHHH		15.7022817900
276UbiquitinationDIVSARPDEWLGRCI
CHHHCCCCHHHHCHH		54.9021963094
283UbiquitinationDEWLGRCILDATGVG
CHHHHCHHHHCCCCC		3.6221963094
312UbiquitinationLSPGEPVQEGDPHFR
ECCCCCCCCCCCCHH		60.7222817900
313UbiquitinationSPGEPVQEGDPHFRS
CCCCCCCCCCCCHHH		66.8422817900
323PhosphorylationPHFRSALTAHPVRDP
CCHHHHHHCCCCCCC		23.72-
338UbiquitinationVHMYQLHKAFARAEL
CHHHHHHHHHHHHHH		54.5121906983
361N-linked_GlycosylationELQWEIQNTSHLAVD
HHHHHHHCCCCEEEC		49.57UniProtKB CARBOHYD
405UbiquitinationTEQHAFSCADGSPRC
CCCCEEECCCCCCCC		3.0221963094
441UbiquitinationNRRYHPALRLQKQQL
HHHHCHHHHHHHHHH		7.0922817900
442UbiquitinationRRYHPALRLQKQQLV
HHHCHHHHHHHHHHH		36.8622817900
445UbiquitinationHPALRLQKQQLVNGY
CHHHHHHHHHHHCCC		44.6021906983
452PhosphorylationKQQLVNGYRRFDPAR
HHHHHCCCCCCCCCC		8.07-
492PhosphorylationVQLLRPLSRVEILPV
HHHCCCCCCCEEECC		36.6426434776
567UbiquitinationADVFAPVKAHVAELE
CCCHHHHHHHHHHHH		31.5421906983
603UbiquitinationRLMDLLSKKHPLDTL
HHHHHHCCCCCCCEE		55.8821906983
604UbiquitinationLMDLLSKKHPLDTLF
HHHHHCCCCCCCEEE		47.2622817900
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 CHSS2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHSS2_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 CHSS2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRKN_HUMANPARK2physical
22082830
TRIPB_HUMANTRIP11physical
27173435
MED4_HUMANMED4physical
27173435
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 CHSS2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126 AND THR-129, ANDMASS SPECTROMETRY.

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