dbPTM

GNS_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GNS_HUMAN
UniProt AC	P15586
Protein Name	N-acetylglucosamine-6-sulfatase
Gene Name	GNS
Organism	Homo sapiens (Human).
Sequence Length	552
Subcellular Localization	Lysosome.
Protein Description
Protein Sequence	MRLLPLAPGRLRRGSPRHLPSCSPALLLLVLGGCLGVFGVAAGTRRPNVVLLLTDDQDEVLGGMTPLKKTKALIGEMGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNNTLEGNCSSKSWQKIQEPNTFPAILRSMCGYQTFFAGKYLNEYGAPDAGGLEHVPLGWSYWYALEKNSKYYNYTLSINGKARKHGENYSVDYLTDVLANVSLDFLDYKSNFEPFFMMIATPAPHSPWTAAPQYQKAFQNVFAPRNKNFNIHGTNKHWLIRQAKTPMTNSSIQFLDNAFRKRWQTLLSVDDLVEKLVKRLEFTGELNNTYIFYTSDNGYHTGQFSLPIDKRQLYEFDIKVPLLVRGPGIKPNQTSKMLVANIDLGPTILDIAGYDLNKTQMDGMSLLPILRGASNLTWRSDVLVEYQGEGRNVTDPTCPSLSPGVSQCFPDCVCEDAYNNTYACVRTMSALWNLQYCEFDDQEVFVEVYNLTADPDQITNIAKTIDPELLGKMNYRLMMLQSCSGPTCRTPGVFDPGYRFDPRLMFSNRGSVRTRRFSKHLL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
65	Phosphorylation	DEVLGGMTPLKKTKA CHHHCCCCCCHHHHH	28.83	-
80	Phosphorylation	LIGEMGMTFSSAYVP HHHHCCCCCCCCCCC	18.03	-
91	3-oxoalanine (Cys)	AYVPSALCCPSRASI CCCCHHHCCCCCHHH	2.99	-
91	Oxidation	AYVPSALCCPSRASI CCCCHHHCCCCCHHH	2.99	-
105	Ubiquitination	ILTGKYPHNHHVVNN HHCCCCCCCCCCCCC	43.07	-
111	N-linked_Glycosylation	PHNHHVVNNTLEGNC CCCCCCCCCCCCCCC	34.38	UniProtKB CARBOHYD
117	N-linked_Glycosylation	VNNTLEGNCSSKSWQ CCCCCCCCCCCCHHH	17.08	UniProtKB CARBOHYD
125	Ubiquitination	CSSKSWQKIQEPNTF CCCCHHHHCCCCCCH	39.85	21890473
125	Ubiquitination	CSSKSWQKIQEPNTF CCCCHHHHCCCCCCH	39.85	21890473
183	N-linked_Glycosylation	EKNSKYYNYTLSING HHCCCEEEEEEEECC	21.89	12754519
198	N-linked_Glycosylation	KARKHGENYSVDYLT EEHHCCCCCCHHHHH	38.68	UniProtKB CARBOHYD
210	N-linked_Glycosylation	YLTDVLANVSLDFLD HHHHHHHHCCCHHHC	21.54	UniProtKB CARBOHYD
255	Methylation	FQNVFAPRNKNFNIH HHHCCCCCCCCEEEC	64.42	-
257	Ubiquitination	NVFAPRNKNFNIHGT HCCCCCCCCEEECCC	65.28	-
275	Phosphorylation	WLIRQAKTPMTNSSI EEEEECCCCCCCCHH	22.70	24043423
275	O-linked_Glycosylation	WLIRQAKTPMTNSSI EEEEECCCCCCCCHH	22.70	30059200
278	Phosphorylation	RQAKTPMTNSSIQFL EECCCCCCCCHHHHH	32.90	24043423
278	O-linked_Glycosylation	RQAKTPMTNSSIQFL EECCCCCCCCHHHHH	32.90	30059200
279	N-linked_Glycosylation	QAKTPMTNSSIQFLD ECCCCCCCCHHHHHH	27.75	12754519
279	N-linked_Glycosylation	QAKTPMTNSSIQFLD ECCCCCCCCHHHHHH	27.75	12754519
280	Phosphorylation	AKTPMTNSSIQFLDN CCCCCCCCHHHHHHH	21.47	24043423
317	N-linked_Glycosylation	LEFTGELNNTYIFYT CCEEEECCCEEEEEE	34.20	16399764
317	N-linked_Glycosylation	LEFTGELNNTYIFYT CCEEEECCCEEEEEE	34.20	16399764
362	N-linked_Glycosylation	RGPGIKPNQTSKMLV ECCCCCCCCCCEEEE	53.40	16399764
362	N-linked_Glycosylation	RGPGIKPNQTSKMLV ECCCCCCCCCCEEEE	53.40	UniProtKB CARBOHYD
387	N-linked_Glycosylation	DIAGYDLNKTQMDGM HHCCCCCCCCCCCHH	42.29	16399764
387	N-linked_Glycosylation	DIAGYDLNKTQMDGM HHCCCCCCCCCCCHH	42.29	16399764
404	O-linked_Glycosylation	LPILRGASNLTWRSD HHHHHCCCCCEECCC	34.89	30059200
405	N-linked_Glycosylation	PILRGASNLTWRSDV HHHHCCCCCEECCCE	40.74	16399764
405	N-linked_Glycosylation	PILRGASNLTWRSDV HHHHCCCCCEECCCE	40.74	UniProtKB CARBOHYD
416	Phosphorylation	RSDVLVEYQGEGRNV CCCEEEEECCCCCCC	17.84	-
422	N-linked_Glycosylation	EYQGEGRNVTDPTCP EECCCCCCCCCCCCC	52.47	1463457
449	N-linked_Glycosylation	CVCEDAYNNTYACVR CEEEHHCCCHHHHHH	35.77	16399764
449	N-linked_Glycosylation	CVCEDAYNNTYACVR CEEEHHCCCHHHHHH	35.77	UniProtKB CARBOHYD
480	N-linked_Glycosylation	EVFVEVYNLTADPDQ EEEEEEEECCCCHHH	35.77	16399764
480	N-linked_Glycosylation	EVFVEVYNLTADPDQ EEEEEEEECCCCHHH	35.77	UniProtKB CARBOHYD
482	Ubiquitination	FVEVYNLTADPDQIT EEEEEECCCCHHHHH	25.94	-
502	Ubiquitination	IDPELLGKMNYRLMM CCHHHHHHHHHHHCC	24.76	21890473
502	Ubiquitination	IDPELLGKMNYRLMM CCHHHHHHHHHHHCC	24.76	21890473
505	Phosphorylation	ELLGKMNYRLMMLQS HHHHHHHHHHCCCCC	11.13	-
537	Phosphorylation	FDPRLMFSNRGSVRT CCCCCCCCCCCCHHH	16.20	23186163
541	Phosphorylation	LMFSNRGSVRTRRFS CCCCCCCCHHHHHCH	12.75	1463457

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 GNS_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GNS_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 GNS_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BCCIP_HUMAN	BCCIP	physical	22863883
CAN1_HUMAN	CAPN1	physical	22863883
CASP7_HUMAN	CASP7	physical	22863883
CNDP2_HUMAN	CNDP2	physical	22863883
IF5A1_HUMAN	EIF5A	physical	22863883
G6PD_HUMAN	G6PD	physical	22863883
GBP2_HUMAN	GBP2	physical	22863883
GUAD_HUMAN	GDA	physical	22863883
AGAL_HUMAN	GLA	physical	22863883
GLSK_HUMAN	GLS	physical	22863883
KYNU_HUMAN	KYNU	physical	22863883
LDH6B_HUMAN	LDHAL6B	physical	22863883
MVD1_HUMAN	MVD	physical	22863883
KS6A1_HUMAN	RPS6KA1	physical	22863883
SCLY_HUMAN	SCLY	physical	22863883
SMAP_HUMAN	C11orf58	physical	22863883
UBFD1_HUMAN	UBFD1	physical	22863883
ENASE_HUMAN	ENGASE	physical	28514442
SUMF1_HUMAN	SUMF1	physical	28514442
FKB14_HUMAN	FKBP14	physical	28514442
SULF2_HUMAN	SULF2	physical	28514442
CLPX_HUMAN	CLPX	physical	28514442
CAN2_HUMAN	CAPN2	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
252940	Mucopolysaccharidosis 3D (MPS3D)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of GNS_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-183; ASN-317; ASN-387 ANDASN-422, AND MASS SPECTROMETRY.	19159218 [Abstract]
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry."; Zhang H., Li X.-J., Martin D.B., Aebersold R.; Nat. Biotechnol. 21:660-666(2003). Cited for: GLYCOSYLATION AT ASN-183 AND ASN-279.	12754519 [Abstract]
"A cDNA clone for human glucosamine-6-sulphatase reveals differencesbetween arylsulphatases and non-arylsulphatases."; Robertson D.A., Freeman C., Morris C.P., Hopwood J.J.; Biochem. J. 288:539-544(1992). Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, ANDGLYCOSYLATION AT ASN-422.	1463457 [Abstract]