dbPTM

GEMI_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GEMI_HUMAN
UniProt AC	O75496
Protein Name	Geminin
Gene Name	GMNN
Organism	Homo sapiens (Human).
Sequence Length	209
Subcellular Localization	Cytoplasm. Nucleus. Mainly cytoplasmic but can be relocalized to the nucleus.
Protein Description	Inhibits DNA replication by preventing the incorporation of MCM complex into pre-replication complex (pre-RC). It is degraded during the mitotic phase of the cell cycle. Its destruction at the metaphase-anaphase transition permits replication in the succeeding cell cycle.; Inhibits the transcriptional activity of a subset of Hox proteins, enrolling them in cell proliferative control..
Protein Sequence	MNPSMKQKQEEIKENIKNSSVPRRTLKMIQPSASGSLVGRENELSAGLSKRKHRNDHLTSTTSSPGVIVPESSENKNLGGVTQESFDLMIKENPSSQYWKEVAEKRRKALYEALKENEKLHKEIEQKDNEIARLKKENKELAEVAEHVQYMAELIERLNGEPLDNFESLDNQEFDSEEETVEDSLVEDSEIGTCAEGTVSSSTDAKPCI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MNPSMKQKQEE ----CCHHHHHHHHH	33.34	28122231
6	Ubiquitination	--MNPSMKQKQEEIK --CCHHHHHHHHHHH	59.69	-
6	Acetylation	--MNPSMKQKQEEIK --CCHHHHHHHHHHH	59.69	25953088
17	Ubiquitination	EEIKENIKNSSVPRR HHHHHHHHCCCCCHH	63.46	-
25	Phosphorylation	NSSVPRRTLKMIQPS CCCCCHHHHHHHCCC	31.82	-
27	Ubiquitination	SVPRRTLKMIQPSAS CCCHHHHHHHCCCCC	33.09	19608861
27	Acetylation	SVPRRTLKMIQPSAS CCCHHHHHHHCCCCC	33.09	19608861
28	Sulfoxidation	VPRRTLKMIQPSASG CCHHHHHHHCCCCCC	3.75	21406390
32	O-linked_Glycosylation	TLKMIQPSASGSLVG HHHHHCCCCCCCCCC	20.77	OGP
32	Phosphorylation	TLKMIQPSASGSLVG HHHHHCCCCCCCCCC	20.77	23403867
34	Phosphorylation	KMIQPSASGSLVGRE HHHCCCCCCCCCCCH	33.00	23403867
36	O-linked_Glycosylation	IQPSASGSLVGRENE HCCCCCCCCCCCHHH	19.86	30379171
36	Phosphorylation	IQPSASGSLVGRENE HCCCCCCCCCCCHHH	19.86	23403867
45	Phosphorylation	VGRENELSAGLSKRK CCCHHHHCHHHCCCC	17.70	23403867
49	Phosphorylation	NELSAGLSKRKHRND HHHCHHHCCCCCCCC	29.51	23401153
50	Acetylation	ELSAGLSKRKHRNDH HHCHHHCCCCCCCCC	71.19	25953088
50	Ubiquitination	ELSAGLSKRKHRNDH HHCHHHCCCCCCCCC	71.19	21906983
52	Ubiquitination	SAGLSKRKHRNDHLT CHHHCCCCCCCCCCC	51.13	-
59	Phosphorylation	KHRNDHLTSTTSSPG CCCCCCCCCCCCCCC	22.17	22167270
60	Phosphorylation	HRNDHLTSTTSSPGV CCCCCCCCCCCCCCE	35.73	22167270
61	Phosphorylation	RNDHLTSTTSSPGVI CCCCCCCCCCCCCEE	26.01	22167270
62	Phosphorylation	NDHLTSTTSSPGVIV CCCCCCCCCCCCEEC	27.29	22167270
63	Phosphorylation	DHLTSTTSSPGVIVP CCCCCCCCCCCEECC	34.32	22167270
64	Phosphorylation	HLTSTTSSPGVIVPE CCCCCCCCCCEECCC	24.47	22167270
72	Phosphorylation	PGVIVPESSENKNLG CCEECCCCCCCCCCC	36.56	20068231
73	Phosphorylation	GVIVPESSENKNLGG CEECCCCCCCCCCCC	43.45	29978859
76	Ubiquitination	VPESSENKNLGGVTQ CCCCCCCCCCCCCCH	49.88	-
82	Phosphorylation	NKNLGGVTQESFDLM CCCCCCCCHHHHHHH	29.87	23186163
85	Phosphorylation	LGGVTQESFDLMIKE CCCCCHHHHHHHCCC	17.78	22912867
91	Ubiquitination	ESFDLMIKENPSSQY HHHHHHCCCCCCHHH	37.16	-
95	Phosphorylation	LMIKENPSSQYWKEV HHCCCCCCHHHHHHH	41.47	-
96	Phosphorylation	MIKENPSSQYWKEVA HCCCCCCHHHHHHHH	28.66	-
98	Phosphorylation	KENPSSQYWKEVAEK CCCCCHHHHHHHHHH	22.01	-
100	Ubiquitination	NPSSQYWKEVAEKRR CCCHHHHHHHHHHHH	37.06	-
105	Acetylation	YWKEVAEKRRKALYE HHHHHHHHHHHHHHH	48.00	20167786
108	Ubiquitination	EVAEKRRKALYEALK HHHHHHHHHHHHHHH	46.94	-
111	Phosphorylation	EKRRKALYEALKENE HHHHHHHHHHHHHHH	12.19	27642862
115	Ubiquitination	KALYEALKENEKLHK HHHHHHHHHHHHHHH	66.59	-
122	Ubiquitination	KENEKLHKEIEQKDN HHHHHHHHHHHHHHH	71.47	-
127	Ubiquitination	LHKEIEQKDNEIARL HHHHHHHHHHHHHHH	50.13	-
139	Ubiquitination	ARLKKENKELAEVAE HHHHHHHHHHHHHHH	56.02	22053931
150	Phosphorylation	EVAEHVQYMAELIER HHHHHHHHHHHHHHH	9.37	-
184	Phosphorylation	EEETVEDSLVEDSEI CCCCHHHHCCCCCCC	22.32	14702039
200	Phosphorylation	TCAEGTVSSSTDAKP CCCCCCCCCCCCCCC	20.57	17261582
201	Phosphorylation	CAEGTVSSSTDAKPC CCCCCCCCCCCCCCC	32.68	17261582
202	Phosphorylation	AEGTVSSSTDAKPCI CCCCCCCCCCCCCCC	23.85	17261582
203	Phosphorylation	EGTVSSSTDAKPCI- CCCCCCCCCCCCCC-	41.76	17261582

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
25	T	Phosphorylation	Kinase	AURKA	O14965	GPS
150	Y	Phosphorylation	Kinase	ABL	P00519	PSP
184	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
184	S	Phosphorylation	Kinase	CK2	-	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	FZR1	Q9UM11	PMID:21700221
-	K	Ubiquitination	E3 ubiquitin ligase	ANAPC11	Q9NYG5	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	BMI1	P35226	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	RNF2	Q99496	PMID:20697353

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
184	S	Phosphorylation		22615398
Phosphorylation at Ser-184 by CK2 results in enhanced binding to Hox proteins and more potent inhibitory effect on Hox transcriptional activity.

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 GEMI_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
REPI1_HUMAN	REPIN1	physical	16924111
CDT1_HUMAN	CDT1	physical	15257290
CDT1_HUMAN	CDT1	physical	15138268
SMCA4_HUMAN	SMARCA4	physical	16024661
CDT1_HUMAN	CDT1	physical	17261582
CDN2A_HUMAN	CDKN2A	physical	15232106
ARF_HUMAN	CDKN2A	physical	15232106
MCM6_HUMAN	MCM6	physical	15232106
CDN1A_HUMAN	CDKN1A	physical	15232106
CDC20_HUMAN	CDC20	physical	23695679
CADH1_HUMAN	CDH1	physical	23695679
AURKA_HUMAN	AURKA	physical	23695679
IMDH1_HUMAN	IMPDH1	physical	21988832
CC146_HUMAN	CCDC146	physical	25416956
ZN439_HUMAN	ZNF439	physical	25416956
CDT1_HUMAN	CDT1	physical	14578910
ZMYM4_HUMAN	ZMYM4	physical	26344197
ATM_HUMAN	ATM	physical	26496610
CASP8_HUMAN	CASP8	physical	26496610
CLCB_HUMAN	CLTB	physical	26496610
SPT6H_HUMAN	SUPT6H	physical	26496610
HERC4_HUMAN	HERC4	physical	26496610
EHMT1_HUMAN	EHMT1	physical	26496610
CDT1_HUMAN	CDT1	physical	26496610
FZR1_HUMAN	FZR1	physical	21700221
CCNA2_HUMAN	CCNA2	physical	28514442
CDT1_HUMAN	CDT1	physical	28514442
NPHP3_HUMAN	NPHP3	physical	28514442
TRIM1_HUMAN	MID2	physical	28514442
E2F5_HUMAN	E2F5	physical	28514442
MSL1_HUMAN	MSL1	physical	28514442
CDK2_HUMAN	CDK2	physical	28514442
STN1_HUMAN	OBFC1	physical	28514442
MTMR1_HUMAN	MTMR1	physical	28514442
CTC1_HUMAN	CTC1	physical	28514442
TFDP1_HUMAN	TFDP1	physical	28514442
E2F4_HUMAN	E2F4	physical	28514442
HMMR_HUMAN	HMMR	physical	28514442
CERK1_HUMAN	CERK	physical	28514442
TRI18_HUMAN	MID1	physical	28514442
TYK2_HUMAN	TYK2	physical	28514442
HSP7C_HUMAN	HSPA8	physical	28514442
FA83D_HUMAN	FAM83D	physical	28514442
MYO5C_HUMAN	MYO5C	physical	28514442
HPBP1_HUMAN	HSPBP1	physical	28514442
SKP2_HUMAN	SKP2	physical	28514442
MCIN_HUMAN	MCIDAS	physical	28514442
BAG4_HUMAN	BAG4	physical	28514442
KLH22_HUMAN	KLHL22	physical	28514442
CDK1_HUMAN	CDK1	physical	28514442
TARB1_HUMAN	TARBP1	physical	28514442
HECD1_HUMAN	HECTD1	physical	28514442
ZZEF1_HUMAN	ZZEF1	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 GEMI_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-27, 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-63 AND SER-64, AND MASSSPECTROMETRY.	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-64, AND MASSSPECTROMETRY.	17287340 [Abstract]

show