dbPTM

SPIN1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SPIN1_HUMAN
UniProt AC	Q9Y657
Protein Name	Spindlin-1
Gene Name	SPIN1
Organism	Homo sapiens (Human).
Sequence Length	262
Subcellular Localization	Nucleus . Nucleus, nucleolus .
Protein Description	Chromatin reader that specifically recognizes and binds histone H3 both trimethylated at 'Lys-4' and asymmetrically dimethylated at 'Arg-8' (H3K4me3 and H3R8me2a) and acts as an activator of Wnt signaling pathway downstream of PRMT2. In case of cancer, promotes cell cancer proliferation via activation of the Wnt signaling pathway. [PubMed: 24589551 Overexpression induces metaphase arrest and chromosomal instability. Localizes to active rDNA loci and promotes the expression of rRNA genes]
Protein Sequence	MKTPFGKTPGQRSRADAGHAGVSANMMKKRTSHKKHRSSVGPSKPVSQPRRNIVGCRIQHGWKEGNGPVTQWKGTVLDQVPVNPSLYLIKYDGFDCVYGLELNKDERVSALEVLPDRVATSRISDAHLADTMIGKAVEHMFETEDGSKDEWRGMVLARAPVMNTWFYITYEKDPVLYMYQLLDDYKEGDLRIMPDSNDSPPAEREPGEVVDSLVGKQVEYAKEDGSKRTGMVIHQVEAKPSVYFIKFDDDFHIYVYDLVKTS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Methylation	------MKTPFGKTP ------CCCCCCCCC	65.98	30592611
3	Phosphorylation	-----MKTPFGKTPG -----CCCCCCCCCC	23.66	21712546
7	Methylation	-MKTPFGKTPGQRSR -CCCCCCCCCCCCCC	52.50	24129315
7	Acetylation	-MKTPFGKTPGQRSR -CCCCCCCCCCCCCC	52.50	19608861
7	Sumoylation	-MKTPFGKTPGQRSR -CCCCCCCCCCCCCC	52.50	28112733
8	Phosphorylation	MKTPFGKTPGQRSRA CCCCCCCCCCCCCCC	32.79	28555341
13	Phosphorylation	GKTPGQRSRADAGHA CCCCCCCCCCCCCCC	24.75	20068231
23	Phosphorylation	DAGHAGVSANMMKKR CCCCCCCCHHHHHHC	17.01	20068231
28	Acetylation	GVSANMMKKRTSHKK CCCHHHHHHCCCCCC	28.47	25953088
28	Sumoylation	GVSANMMKKRTSHKK CCCHHHHHHCCCCCC	28.47	28112733
29	Acetylation	VSANMMKKRTSHKKH CCHHHHHHCCCCCCC	42.91	26051181
31	Phosphorylation	ANMMKKRTSHKKHRS HHHHHHCCCCCCCHH	44.02	20068231
32	Phosphorylation	NMMKKRTSHKKHRSS HHHHHCCCCCCCHHC	37.02	20068231
38	Phosphorylation	TSHKKHRSSVGPSKP CCCCCCHHCCCCCCC	29.15	23927012
39	Phosphorylation	SHKKHRSSVGPSKPV CCCCCHHCCCCCCCC	30.93	23927012
43	Phosphorylation	HRSSVGPSKPVSQPR CHHCCCCCCCCCCCC	43.60	20068231
44	Sumoylation	RSSVGPSKPVSQPRR HHCCCCCCCCCCCCC	53.20	28112733
44	Ubiquitination	RSSVGPSKPVSQPRR HHCCCCCCCCCCCCC	53.20	-
44	Acetylation	RSSVGPSKPVSQPRR HHCCCCCCCCCCCCC	53.20	23236377
47	Phosphorylation	VGPSKPVSQPRRNIV CCCCCCCCCCCCCEE	42.89	27251275
63	Ubiquitination	CRIQHGWKEGNGPVT EEECCCCCCCCCCCC	61.41	21890473
63	Ubiquitination	CRIQHGWKEGNGPVT EEECCCCCCCCCCCC	61.41	21890473
63	Ubiquitination	CRIQHGWKEGNGPVT EEECCCCCCCCCCCC	61.41	21890473
91	Phosphorylation	PSLYLIKYDGFDCVY CCEEEEEECCCCEEE	17.82	17053785
98	Phosphorylation	YDGFDCVYGLELNKD ECCCCEEEEEECCCC	23.48	17053785
104	Ubiquitination	VYGLELNKDERVSAL EEEEECCCCCCEEEE	73.85	-
109	Phosphorylation	LNKDERVSALEVLPD CCCCCCEEEEEECCC	33.10	22258766
120	Phosphorylation	VLPDRVATSRISDAH ECCCHHHHCCCCHHH	18.71	23401153
121	Phosphorylation	LPDRVATSRISDAHL CCCHHHHCCCCHHHH	20.20	20068231
124	Phosphorylation	RVATSRISDAHLADT HHHHCCCCHHHHHHH	27.86	29255136
131	Phosphorylation	SDAHLADTMIGKAVE CHHHHHHHHHHHHHH	12.70	29396449
177	Phosphorylation	YEKDPVLYMYQLLDD EECCCEEEEEEECCH	8.26	20049867
179	Phosphorylation	KDPVLYMYQLLDDYK CCCEEEEEEECCHHH	5.18	20049867
185	Phosphorylation	MYQLLDDYKEGDLRI EEEECCHHHCCCEEE	15.59	20049867
186	Ubiquitination	YQLLDDYKEGDLRIM EEECCHHHCCCEEEC	63.31	-
196	Phosphorylation	DLRIMPDSNDSPPAE CEEECCCCCCCCCCC	36.34	30266825
199	Phosphorylation	IMPDSNDSPPAEREP ECCCCCCCCCCCCCC	36.71	29255136
212	Phosphorylation	EPGEVVDSLVGKQVE CCCCHHHHHCCCEEE	17.22	30108239
216	Ubiquitination	VVDSLVGKQVEYAKE HHHHHCCCEEEEECC	43.63	-
222	Acetylation	GKQVEYAKEDGSKRT CCEEEEECCCCCCCC	56.27	155779

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
109	S	Phosphorylation	Kinase	AURA	O14965	PSP
124	S	Phosphorylation	Kinase	AURA	O14965	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SPIN1_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 SPIN1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ANM6_HUMAN	PRMT6	physical	23455924
SPIN4_HUMAN	SPIN4	physical	26186194
SP16H_HUMAN	SUPT16H	physical	26186194
BCLF1_HUMAN	BCLAF1	physical	26186194
TR150_HUMAN	THRAP3	physical	26186194
CGBP1_HUMAN	CGGBP1	physical	26186194
SSRP1_HUMAN	SSRP1	physical	26186194
YRDC_HUMAN	YRDC	physical	26186194
CK084_HUMAN	C11orf84	physical	26186194
MCM2_HUMAN	MCM2	physical	26186194
ZGPAT_HUMAN	ZGPAT	physical	26186194
SF3A3_HUMAN	SF3A3	physical	26186194
SCNM1_HUMAN	SCNM1	physical	26186194
TOPRS_HUMAN	TOPORS	physical	26186194
PAX3_HUMAN	PAX3	physical	26186194
CK084_HUMAN	C11orf84	physical	28514442
CGBP1_HUMAN	CGGBP1	physical	28514442
YRDC_HUMAN	YRDC	physical	28514442
TOPRS_HUMAN	TOPORS	physical	28514442
SCNM1_HUMAN	SCNM1	physical	28514442
ZGPAT_HUMAN	ZGPAT	physical	28514442
PAX3_HUMAN	PAX3	physical	28514442
SF3A3_HUMAN	SF3A3	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.

Regulatory Network of SPIN1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-7, AND MASS SPECTROMETRY.	19608861 [Abstract]
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-124 AND SER-199, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38 AND SER-39, AND MASSSPECTROMETRY.	17287340 [Abstract]
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling."; Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.; EMBO J. 25:5058-5070(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-91 AND TYR-98, AND MASSSPECTROMETRY.	17053785 [Abstract]