dbPTM

SGT1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SGT1_HUMAN
UniProt AC	Q9Y2Z0
Protein Name	Protein SGT1 homolog {ECO:0000250\|UniProtKB:Q08446}
Gene Name	SUGT1 {ECO:0000312\|HGNC:HGNC:16987}
Organism	Homo sapiens (Human).
Sequence Length	365
Subcellular Localization	Cytoplasm . Nucleus . Translocates to the nucleus upon heat shock, requiring S100A6.
Protein Description	May play a role in ubiquitination and subsequent proteasomal degradation of target proteins..
Protein Sequence	MAAAAAGTATSQRFFQSFSDALIDEDPQAALEELTKALEQKPDDAQYYCQRAYCHILLGNYCVAVADAKKSLELNPNNSTAMLRKGICEYHEKNYAAALETFTEGQKLDIETGFHRVGQAGLQLLTSSDPPALDSQSAGITGADANFSVWIKRCQEAQNGSESEVWTHQSKIKYDWYQTESQVVITLMIKNVQKNDVNVEFSEKELSALVKLPSGEDYNLKLELLHPIIPEQSTFKVLSTKIEIKLKKPEAVRWEKLEGQGDVPTPKQFVADVKNLYPSSSPYTRNWDKLVGEIKEEEKNEKLEGDAALNRLFQQIYSDGSDEVKRAMNKSFMESGGTVLSTNWSDVGKRKVEINPPDDMEWKKY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAAAAGTA ------CCCCCCCCH	63.27	20068231
8	Phosphorylation	MAAAAAGTATSQRFF CCCCCCCCHHHHHHH	10.20	30108239
10	Phosphorylation	AAAAGTATSQRFFQS CCCCCCHHHHHHHHH	3.50	29255136
11	Phosphorylation	AAAGTATSQRFFQSF CCCCCHHHHHHHHHH	46.29	29255136
17	Phosphorylation	TSQRFFQSFSDALID HHHHHHHHHHHHHCC	1.05	-
19	Phosphorylation	QRFFQSFSDALIDED HHHHHHHHHHHCCCC	5.33	-
41	Ubiquitination	LTKALEQKPDDAQYY HHHHHHCCCCCHHHH	18.95	-
41	Acetylation	LTKALEQKPDDAQYY HHHHHHCCCCCHHHH	18.95	26051181
47	Phosphorylation	QKPDDAQYYCQRAYC CCCCCHHHHHHHHHH	5.82	28152594
48	Phosphorylation	KPDDAQYYCQRAYCH CCCCHHHHHHHHHHH	17.58	28152594
61	Phosphorylation	CHILLGNYCVAVADA HHHHHCCEEEEEECH	42.16	27642862
70	Ubiquitination	VAVADAKKSLELNPN EEEECHHHHHCCCCC	26.22	-
71	Phosphorylation	AVADAKKSLELNPNN EEECHHHHHCCCCCC	5.29	20860994
79	Phosphorylation	LELNPNNSTAMLRKG HCCCCCCCHHHHHHC	22.49	20860994
80	Phosphorylation	ELNPNNSTAMLRKGI CCCCCCCHHHHHHCH	44.97	22210691
82	Sulfoxidation	NPNNSTAMLRKGICE CCCCCHHHHHHCHHH	28.72	21406390
85	Ubiquitination	NSTAMLRKGICEYHE CCHHHHHHCHHHHHH	9.32	-
88	S-nitrosocysteine	AMLRKGICEYHEKNY HHHHHCHHHHHHHHH	31.34	-
93	Ubiquitination	GICEYHEKNYAAALE CHHHHHHHHHHHHHH	7.52	-
93	2-Hydroxyisobutyrylation	GICEYHEKNYAAALE CHHHHHHHHHHHHHH	7.52	-
95	Phosphorylation	CEYHEKNYAAALETF HHHHHHHHHHHHHHC	1.17	20068231
101	Phosphorylation	NYAAALETFTEGQKL HHHHHHHHCCCCCCE	58.76	20068231
103	Phosphorylation	AAALETFTEGQKLDI HHHHHHCCCCCCEEC	34.79	20068231
161	Phosphorylation	CQEAQNGSESEVWTH HHHHHCCCCCCCEEE	28.15	23898821
171	Acetylation	EVWTHQSKIKYDWYQ CCEEECCCCCCCCCC	3.89	26051181
171	Ubiquitination	EVWTHQSKIKYDWYQ CCEEECCCCCCCCCC	3.89	-
174	Phosphorylation	THQSKIKYDWYQTES EECCCCCCCCCCCCC	2.44	27732954
177	Phosphorylation	SKIKYDWYQTESQVV CCCCCCCCCCCCCEE	28.04	27732954
179	Phosphorylation	IKYDWYQTESQVVIT CCCCCCCCCCCEEEE	33.96	27732954
181	Phosphorylation	YDWYQTESQVVITLM CCCCCCCCCEEEEEE	3.22	27732954
186	Phosphorylation	TESQVVITLMIKNVQ CCCCEEEEEEEECCC	18.19	27732954
194	Ubiquitination	LMIKNVQKNDVNVEF EEEECCCCCCCCCCC	20.11	-
202	Phosphorylation	NDVNVEFSEKELSAL CCCCCCCCHHHHHHH	3.84	29978859
204	Ubiquitination	VNVEFSEKELSALVK CCCCCCHHHHHHHEE	19.96	-
211	Ubiquitination	KELSALVKLPSGEDY HHHHHHEECCCCCCC	3.51	-
221	Ubiquitination	SGEDYNLKLELLHPI CCCCCCEEEEECCCC	2.56	-
224 (in isoform 2)	Ubiquitination	-	19.40	21890473
235 (in isoform 2)	Ubiquitination	-	3.10	21890473
242 (in isoform 2)	Ubiquitination	-	35.17	21890473
256 (in isoform 1)	Ubiquitination	-	24.45	21890473
256	Ubiquitination	PEAVRWEKLEGQGDV CCCCCHHHCCCCCCC	24.45	21890473
265	Phosphorylation	EGQGDVPTPKQFVAD CCCCCCCCCHHHHHH	16.10	19664994
267	Ubiquitination	QGDVPTPKQFVADVK CCCCCCCHHHHHHHH	2.97	21890473
267 (in isoform 1)	Ubiquitination	-	2.97	21890473
270 (in isoform 2)	Ubiquitination	-	5.36	21890473
274	Ubiquitination	KQFVADVKNLYPSSS HHHHHHHHHHCCCCC	37.01	21890473
274	Acetylation	KQFVADVKNLYPSSS HHHHHHHHHHCCCCC	37.01	25953088
274 (in isoform 1)	Ubiquitination	-	37.01	21890473
277	Phosphorylation	VADVKNLYPSSSPYT HHHHHHHCCCCCCCC	8.98	23927012
279	Phosphorylation	DVKNLYPSSSPYTRN HHHHHCCCCCCCCCC	27.03	22167270
280	Phosphorylation	VKNLYPSSSPYTRNW HHHHCCCCCCCCCCH	54.01	22167270
281	Phosphorylation	KNLYPSSSPYTRNWD HHHCCCCCCCCCCHH	28.70	22167270
283	Phosphorylation	LYPSSSPYTRNWDKL HCCCCCCCCCCHHHH	40.86	25159151
284	Phosphorylation	YPSSSPYTRNWDKLV CCCCCCCCCCHHHHH	15.12	23927012
289	Ubiquitination	PYTRNWDKLVGEIKE CCCCCHHHHHHHHCH	45.69	-
293 (in isoform 2)	Ubiquitination	-	37.12	21890473
295	Sumoylation	DKLVGEIKEEEKNEK HHHHHHHCHHHHHHH	18.37	-
295	Sumoylation	DKLVGEIKEEEKNEK HHHHHHHCHHHHHHH	18.37	25114211
299	Ubiquitination	GEIKEEEKNEKLEGD HHHCHHHHHHHCCHH	46.14	-
302	Ubiquitination	KEEEKNEKLEGDAAL CHHHHHHHCCHHHHH	5.13	21906983
302 (in isoform 1)	Ubiquitination	-	5.13	21890473
317	Phosphorylation	NRLFQQIYSDGSDEV HHHHHHHHCCCCHHH	41.85	27273156
318	Phosphorylation	RLFQQIYSDGSDEVK HHHHHHHCCCCHHHH	20.67	25159151
321	Phosphorylation	QQIYSDGSDEVKRAM HHHHCCCCHHHHHHH	47.51	25159151
325 (in isoform 1)	Ubiquitination	-	17.36	21890473
325	Ubiquitination	SDGSDEVKRAMNKSF CCCCHHHHHHHHHHH	17.36	2190698
330	Ubiquitination	EVKRAMNKSFMESGG HHHHHHHHHHHHCCC	15.91	-
331	Phosphorylation	VKRAMNKSFMESGGT HHHHHHHHHHHCCCE	29.47	25159151
335	Phosphorylation	MNKSFMESGGTVLST HHHHHHHCCCEEEEC	20.84	28857561
338	Phosphorylation	SFMESGGTVLSTNWS HHHHCCCEEEECCHH	52.60	21406692
341	Phosphorylation	ESGGTVLSTNWSDVG HCCCEEEECCHHHCC	59.83	21406692
342	Phosphorylation	SGGTVLSTNWSDVGK CCCEEEECCHHHCCC	61.41	21406692
345	Phosphorylation	TVLSTNWSDVGKRKV EEEECCHHHCCCCCC	19.31	21406692
349	Ubiquitination	TNWSDVGKRKVEINP CCHHHCCCCCCCCCC	3.12	-
349	Acetylation	TNWSDVGKRKVEINP CCHHHCCCCCCCCCC	3.12	25953088
351	Ubiquitination	WSDVGKRKVEINPPD HHHCCCCCCCCCCCC	52.73	-
365	Phosphorylation	DDMEWKKY------- CCCCCCCC-------	33.12	-

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
331	S	Phosphorylation	Kinase	PLK1	P53350	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
281	S	Phosphorylation	21864708
Phosphorylated at Ser-281 and Ser-331, dephosphorylation promotes nuclear translocation, most likely due to disruption of the SUGT1-HSP90 complex.
331	S	Phosphorylation	20068231
Phosphorylated at Ser-281 and Ser-331, dephosphorylation promotes nuclear translocation, most likely due to disruption of the SUGT1-HSP90 complex.

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 SGT1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
S10A6_HUMAN	S100A6	physical	12746458
SKP1_HUMAN	SKP1	physical	12746458
SKP1_HUMAN	SKP1	physical	18818696
HS90A_HUMAN	HSP90AA1	physical	14761955
NLRP3_HUMAN	NLRP3	physical	17435760
HS90A_HUMAN	HSP90AA1	physical	17435760
NSL1_HUMAN	NSL1	physical	20404110
PMF1_HUMAN	PMF1	physical	20404110
MIS12_HUMAN	MIS12	physical	20404110
DSN1_HUMAN	DSN1	physical	20404110
HSP74_HUMAN	HSPA4	physical	17466273
HS90A_HUMAN	HSP90AA1	physical	17466273
WDR12_HUMAN	WDR12	physical	22939629
HS90A_HUMAN	HSP90AA1	physical	16501598
HS90B_HUMAN	HSP90AB1	physical	16501598
HSP7C_HUMAN	HSPA8	physical	16501598
SKP1_HUMAN	SKP1	physical	16501598
PHLP1_HUMAN	PHLPP1	physical	23440515
PLK1_HUMAN	PLK1	physical	22869522
DSN1_HUMAN	DSN1	physical	22869522
CENPH_HUMAN	CENPH	physical	22869522
NSL1_HUMAN	NSL1	physical	22869522
MIS12_HUMAN	MIS12	physical	22869522
CHRD1_MOUSE	Chordc1	physical	23184943
NOD1_HUMAN	NOD1	physical	17420470
NOD2_HUMAN	NOD2	physical	17420470
NALP2_HUMAN	NLRP2	physical	17420470
NALP4_HUMAN	NLRP4	physical	17420470
HS90A_HUMAN	HSP90AA1	physical	22869522
PMF1_HUMAN	PMF1	physical	22869522
DX39A_HUMAN	DDX39A	physical	22863883
LRC40_HUMAN	LRRC40	physical	25036637
AIP_HUMAN	AIP	physical	25036637
CYBP_HUMAN	CACYBP	physical	25036637
RNF41_HUMAN	RNF41	physical	25036637
FKBP5_HUMAN	FKBP5	physical	25036637
FKBP4_HUMAN	FKBP4	physical	25036637
RSU1_HUMAN	RSU1	physical	25036637
SKP2_HUMAN	SKP2	physical	25036637
CEP97_HUMAN	CEP97	physical	25036637
CLIC4_HUMAN	CLIC4	physical	26344197
EF1A1_HUMAN	EEF1A1	physical	26545799

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 SGT1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503; SER-505 ANDSER-518, AND MASS SPECTROMETRY.	18669648 [Abstract]
"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-503; SER-505 ANDSER-518, AND MASS SPECTROMETRY.	17081983 [Abstract]

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