CHSS3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CHSS3_HUMAN
• UniProt AC: Q70JA7
• Protein Name: Chondroitin sulfate synthase 3
• Gene Name: CHSY3
• Organism: Homo sapiens (Human).
• Sequence Length: 882
• Subcellular Localization: Golgi apparatus, Golgi stack membrane ; Single-pass type II membrane protein .
• 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. Specific activity is much reduced compared to CHSY1..
• Protein Sequence: MAVRSRRPWMSVALGLVLGFTAASWLIAPRVAELSERKRRGSSLCSYYGRSAAGPRAGAQQPLPQPQSRPRQEQSPPPARQDLQGPPLPEAAPGITSFRSSPWQQPPPLQQRRRGREPEGATGLPGAPAAEGEPEEEDGGAAGQRRDGRPGSSHNGSGDGGAAAPSARPRDFLYVGVMTAQKYLGSRALAAQRTWARFIPGRVEFFSSQQPPNAGQPPPPLPVIALPGVDDSYPPQKKSFMMIKYMHDHYLDKYEWFMRADDDVYIKGDKLEEFLRSLNSSKPLYLGQTGLGNIEELGKLGLEPGENFCMGGPGMIFSREVLRRMVPHIGECLREMYTTHEDVEVGRCVRRFGGTQCVWSYEMQQLFHENYEHNRKGYIQDLHNSKIHAAITLHPNKRPAYQYRLHNYMLSRKISELRYRTIQLHRESALMSKLSNTEVSKEDQQLGVIPSFNHFQPRERNEVIEWEFLTGKLLYSAAENQPPRQSLSSILRTALDDTVLQVMEMINENAKSRGRLIDFKEIQYGYRRVNPMHGVEYILDLLLLYKRHKGRKLTVPVRRHAYLQQLFSKPFFRETEELDVNSLVESINSETQSFSFISNSLKILSSFQGAKEMGGHNEKKVHILVPLIGRYDIFLRFMENFENMCLIPKQNVKLVIILFSRDSGQDSSKHIELIKGYQNKYPKAEMTLIPMKGEFSRGLGLEMASAQFDNDTLLLFCDVDLIFREDFLQRCRDNTIQGQQVYYPIIFSQYDPKVTNGGNPPTDDYFIFSKKTGFWRDYGYGITCIYKSDLLGAGGFDTSIQGWGLEDVDLYNKVILSGLRPFRSQEVGVVHIFHPVHCDPNLDPKQYKMCLGSKASTFASTMQLAELWLEKHLGVRYNRTLS

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
11	Phosphorylation	RSRRPWMSVALGLVL CCCCHHHHHHHHHHH	10.60	24719451
96	Phosphorylation	PEAAPGITSFRSSPW CCCCCCCCCCCCCCC	27.94	-
97	Phosphorylation	EAAPGITSFRSSPWQ CCCCCCCCCCCCCCC	19.42	-
100	O-linked_Glycosylation	PGITSFRSSPWQQPP CCCCCCCCCCCCCCC	38.45	55827927
100	Phosphorylation	PGITSFRSSPWQQPP CCCCCCCCCCCCCCC	38.45	-
101	O-linked_Glycosylation	GITSFRSSPWQQPPP CCCCCCCCCCCCCCC	26.38	55827933
101	Phosphorylation	GITSFRSSPWQQPPP CCCCCCCCCCCCCCC	26.38	-
122	O-linked_Glycosylation	GREPEGATGLPGAPA CCCCCCCCCCCCCCC	50.54	OGP
152	Phosphorylation	RRDGRPGSSHNGSGD CCCCCCCCCCCCCCC	30.98	18785766
153	Phosphorylation	RDGRPGSSHNGSGDG CCCCCCCCCCCCCCC	27.21	18785766
155	N-linked_Glycosylation	GRPGSSHNGSGDGGA CCCCCCCCCCCCCCC	48.55	UniProtKB CARBOHYD
157	Phosphorylation	PGSSHNGSGDGGAAA CCCCCCCCCCCCCCC	38.74	25332170
166	Phosphorylation	DGGAAAPSARPRDFL CCCCCCCCCCCCCEE	31.98	18785766
179	Phosphorylation	FLYVGVMTAQKYLGS EEEEEHHHHHHHHHH	24.43	27251275
183	Phosphorylation	GVMTAQKYLGSRALA EHHHHHHHHHHHHHH	12.29	27251275
186	Phosphorylation	TAQKYLGSRALAAQR HHHHHHHHHHHHHHH	16.28	27251275
279	N-linked_Glycosylation	EEFLRSLNSSKPLYL HHHHHHCCCCCCEEC	45.54	UniProtKB CARBOHYD
281	Phosphorylation	FLRSLNSSKPLYLGQ HHHHCCCCCCEECCC	36.90	24719451
385	Phosphorylation	YIQDLHNSKIHAAIT CCCHHHHCCEEEEEE	23.41	32142685
401	Phosphorylation	HPNKRPAYQYRLHNY CCCCCCCHHHHHHHH	14.57	29978859
403	Phosphorylation	NKRPAYQYRLHNYML CCCCCHHHHHHHHHH	11.49	29978859
408	Phosphorylation	YQYRLHNYMLSRKIS HHHHHHHHHHHHHHH	6.67	29978859
411	Phosphorylation	RLHNYMLSRKISELR HHHHHHHHHHHHHHH	18.26	29978859
415	Phosphorylation	YMLSRKISELRYRTI HHHHHHHHHHHHHHH	33.35	24719451
486	Phosphorylation	ENQPPRQSLSSILRT HCCCCCCCHHHHHHH	31.34	23403867
488	Phosphorylation	QPPRQSLSSILRTAL CCCCCCHHHHHHHHC	22.15	23403867
489	Phosphorylation	PPRQSLSSILRTALD CCCCCHHHHHHHHCH	30.82	24719451
526	Phosphorylation	FKEIQYGYRRVNPMH HHHHHCCCCCCCCCC	7.13	-
568	Phosphorylation	AYLQQLFSKPFFRET HHHHHHHCCCCCCCC	48.27	24719451
593	O-linked_Glycosylation	SINSETQSFSFISNS HHCCCCCCEEHHHHH	30.22	OGP
663	Phosphorylation	IILFSRDSGQDSSKH EEEEECCCCCCHHHH	36.92	25002506
667	Phosphorylation	SRDSGQDSSKHIELI ECCCCCCHHHHHHHH	33.14	25002506
668	Phosphorylation	RDSGQDSSKHIELIK CCCCCCHHHHHHHHH	36.22	25002506
687	Phosphorylation	KYPKAEMTLIPMKGE CCCCCEEEEEECCCC	17.03	-
710	N-linked_Glycosylation	MASAQFDNDTLLLFC CEECCCCCCEEEEEE	45.51	UniProtKB CARBOHYD
755	Phosphorylation	SQYDPKVTNGGNPPT EECCCCCCCCCCCCC	33.98	23663014
762	Phosphorylation	TNGGNPPTDDYFIFS CCCCCCCCCCCEEEE	42.64	23663014
765	Phosphorylation	GNPPTDDYFIFSKKT CCCCCCCCEEEECCC	11.03	23663014
769	Phosphorylation	TDDYFIFSKKTGFWR CCCCEEEECCCCCCC	28.55	23663014
817	Phosphorylation	LYNKVILSGLRPFRS HCCCHHHHCCCCCCC	25.34	24719451
860	Phosphorylation	SKASTFASTMQLAEL CHHHHHHHHHHHHHH	21.88	-
878	N-linked_Glycosylation	KHLGVRYNRTLS--- HHHCCCCCCCCC---	21.64	UniProtKB CARBOHYD

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of CHSS3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CHSS3_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CHSS3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CHSS1_HUMAN	CHSY1	physical	28514442
GOLP3_HUMAN	GOLPH3	physical	28514442
RMND1_HUMAN	RMND1	physical	28514442
CCPG1_HUMAN	CCPG1	physical	28514442
SC65_HUMAN	P3H4	physical	28514442
ST17B_HUMAN	STK17B	physical	28514442

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411, AND MASSSPECTROMETRY.
PubMed: 17081983