dbPTM

LIN9_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LIN9_HUMAN
UniProt AC	Q5TKA1
Protein Name	Protein lin-9 homolog
Gene Name	LIN9
Organism	Homo sapiens (Human).
Sequence Length	542
Subcellular Localization	Nucleus, nucleoplasm . Found in perinucleolar structures. Associated with chromatin.
Protein Description	Acts as a tumor suppressor. Inhibits DNA synthesis. Its ability to inhibit oncogenic transformation is mediated through its association with RB1. Plays a role in the expression of genes required for the G1/S transition..
Protein Sequence	MAELDQLPDESSSAKALVSLKEGSLSNTWNEKYSSLQKTPVWKGRNTSSAVEMPFRNSKRSRLFSDEDDRQINTRSPKRNQRVAMVPQKFTATMSTPDKKASQKIGFRLRNLLKLPKAHKWCIYEWFYSNIDKPLFEGDNDFCVCLKESFPNLKTRKLTRVEWGKIRRLMGKPRRCSSAFFEEERSALKQKRQKIRLLQQRKVADVSQFKDLPDEIPLPLVIGTKVTARLRGVHDGLFTGQIDAVDTLNATYRVTFDRTGLGTHTIPDYEVLSNEPHETMPIAAFGQKQRPSRFFMTPPRLHYTPPLQSPIIDNDPLLGQSPWRSKISGSDTETLGGFPVEFLIQVTRLSKILMIKKEHIKKLREMNTEAEKLKSYSMPISIEFQRRYATIVLELEQLNKDLNKVLHKVQQYCYELAPDQGLQPADQPTDMRRRCEEEAQEIVRHANSSTGQPCVENENLTDLISRLTAILLQIKCLAEGGDLNSFEFKSLTDSLNDIKSTIDASNISCFQNNVEIHVAHIQSGLSQMGNLHAFAANNTNRD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAELDQLPD ------CCCHHCCCC	26.51	19413330
3 (in isoform 2)	Methylation	-	52.13	-
11	Phosphorylation	LDQLPDESSSAKALV HHCCCCCCCCCHHHH	36.65	20068231
12	Phosphorylation	DQLPDESSSAKALVS HCCCCCCCCCHHHHH	32.06	20068231
13	Phosphorylation	QLPDESSSAKALVSL CCCCCCCCCHHHHHC	42.97	20068231
21	Sumoylation	AKALVSLKEGSLSNT CHHHHHCCCCCCCCC	53.15	28112733
24	Phosphorylation	LVSLKEGSLSNTWNE HHHCCCCCCCCCHHH	29.71	-
27	Phosphorylation	LKEGSLSNTWNEKYS CCCCCCCCCHHHHCC	55.17	20068231
28	Phosphorylation	KEGSLSNTWNEKYSS CCCCCCCCHHHHCCC	26.70	20068231
29	Phosphorylation	EGSLSNTWNEKYSSL CCCCCCCHHHHCCCC	18.42	20068231
32 (in isoform 3)	Ubiquitination	-	47.41	21890473
32	Ubiquitination	LSNTWNEKYSSLQKT CCCCHHHHCCCCCCC	47.41	21890473
33	Phosphorylation	SNTWNEKYSSLQKTP CCCHHHHCCCCCCCC	9.41	25884760
35	Phosphorylation	TWNEKYSSLQKTPVW CHHHHCCCCCCCCCC	31.56	-
37	Ubiquitination	NEKYSSLQKTPVWKG HHHCCCCCCCCCCCC	49.91	-
39	Phosphorylation	KYSSLQKTPVWKGRN HCCCCCCCCCCCCCC	15.32	22617229
48 (in isoform 2)	Ubiquitination	-	21.61	21890473
48	Phosphorylation	VWKGRNTSSAVEMPF CCCCCCCCCCEECCC	21.61	28555341
48	Ubiquitination	VWKGRNTSSAVEMPF CCCCCCCCCCEECCC	21.61	-
49	Phosphorylation	WKGRNTSSAVEMPFR CCCCCCCCCEECCCC	34.00	28555341
54	Ubiquitination	TSSAVEMPFRNSKRS CCCCEECCCCCCCCC	16.13	-
55	Phosphorylation	SSAVEMPFRNSKRSR CCCEECCCCCCCCCC	12.78	-
55 (in isoform 2)	Phosphorylation	-	12.78	24719451
58	Phosphorylation	VEMPFRNSKRSRLFS EECCCCCCCCCCCCC	25.78	25072903
61	Phosphorylation	PFRNSKRSRLFSDED CCCCCCCCCCCCCHH	36.75	23927012
65	Phosphorylation	SKRSRLFSDEDDRQI CCCCCCCCCHHCCCC	44.69	23401153
74	Phosphorylation	EDDRQINTRSPKRNQ HHCCCCCCCCCCCCC	33.87	30576142
76	Phosphorylation	DRQINTRSPKRNQRV CCCCCCCCCCCCCEE	32.50	25884760
81 (in isoform 2)	Phosphorylation	-	45.30	24719451
81	Phosphorylation	TRSPKRNQRVAMVPQ CCCCCCCCEEEECCC	45.30	20068231
89	Acetylation	RVAMVPQKFTATMST EEEECCCEEEEECCC	38.32	25953088
90 (in isoform 2)	Phosphorylation	-	4.78	24719451
91	Phosphorylation	AMVPQKFTATMSTPD EECCCEEEEECCCCC	28.40	29396449
92	Phosphorylation	MVPQKFTATMSTPDK ECCCEEEEECCCCCH	12.39	-
92 (in isoform 2)	Phosphorylation	-	12.39	27251275
93	Phosphorylation	VPQKFTATMSTPDKK CCCEEEEECCCCCHH	14.48	29255136
95	Phosphorylation	QKFTATMSTPDKKAS CEEEEECCCCCHHHH	32.22	29255136
96	Phosphorylation	KFTATMSTPDKKASQ EEEEECCCCCHHHHH	25.37	29255136
111	Phosphorylation	KIGFRLRNLLKLPKA HHCHHHHHHHCCCHH	55.08	18691976
111 (in isoform 2)	Phosphorylation	-	55.08	27251275
112 (in isoform 2)	Phosphorylation	-	3.45	24719451
112	Phosphorylation	IGFRLRNLLKLPKAH HCHHHHHHHCCCHHH	3.45	19413330
170	Ubiquitination	WGKIRRLMGKPRRCS HHHHHHHHCCCCCCH	6.51	-
177	Phosphorylation	MGKPRRCSSAFFEEE HCCCCCCHHHHHHHH	23.92	28450419
178	Phosphorylation	GKPRRCSSAFFEEER CCCCCCHHHHHHHHH	32.49	19664994
182 (in isoform 1)	Ubiquitination	-	53.12	21890473
194 (in isoform 2)	Phosphorylation	-	33.55	27251275
194	Phosphorylation	ALKQKRQKIRLLQQR HHHHHHHHHHHHHHH	33.55	19664994
207	Phosphorylation	QRKVADVSQFKDLPD HHCCCCHHHCCCCCC	30.37	25159151
218	Ubiquitination	DLPDEIPLPLVIGTK CCCCCCCCCEEEECE	6.69	-
223	Phosphorylation	IPLPLVIGTKVTARL CCCCEEEECEEEEEC	16.41	-
226	Ubiquitination	PLVIGTKVTARLRGV CEEEECEEEEECCCC	5.20	-
297	Phosphorylation	RPSRFFMTPPRLHYT CCCCCCCCCCCCCCC	25.61	21130716
303	Phosphorylation	MTPPRLHYTPPLQSP CCCCCCCCCCCCCCC	26.07	21712546
304	Phosphorylation	TPPRLHYTPPLQSPI CCCCCCCCCCCCCCC	14.00	25159151
309	Phosphorylation	HYTPPLQSPIIDNDP CCCCCCCCCCCCCCC	26.25	25159151
313	Phosphorylation	PLQSPIIDNDPLLGQ CCCCCCCCCCCCCCC	54.95	20068231
313 (in isoform 2)	Phosphorylation	-	54.95	24719451
319	Phosphorylation	IDNDPLLGQSPWRSK CCCCCCCCCCCCCCC	33.33	20068231
320 (in isoform 2)	Phosphorylation	-	46.41	27251275
320	Phosphorylation	DNDPLLGQSPWRSKI CCCCCCCCCCCCCCC	46.41	20068231
321	Phosphorylation	NDPLLGQSPWRSKIS CCCCCCCCCCCCCCC	25.32	25159151
325 (in isoform 2)	Phosphorylation	-	30.39	24719451
325	Phosphorylation	LGQSPWRSKISGSDT CCCCCCCCCCCCCCC	30.39	18691976
337 (in isoform 2)	Phosphorylation	-	27.14	24719451
337	Phosphorylation	SDTETLGGFPVEFLI CCCCCCCCCCHHHHH	27.14	18220336
347	Phosphorylation	VEFLIQVTRLSKILM HHHHHHHHHHHHHHH	14.98	25278378
350	Phosphorylation	LIQVTRLSKILMIKK HHHHHHHHHHHHHCH	17.85	-
375	Phosphorylation	TEAEKLKSYSMPISI HHHHHHHHCCCCEEH	32.64	28152594
376	Phosphorylation	EAEKLKSYSMPISIE HHHHHHHCCCCEEHH	13.85	28152594
377	Phosphorylation	AEKLKSYSMPISIEF HHHHHHCCCCEEHHH	25.77	28442448
388	Ubiquitination	SIEFQRRYATIVLEL EHHHHHHHHHHHHHH	15.41	-
392	Phosphorylation	QRRYATIVLELEQLN HHHHHHHHHHHHHHC	2.70	-
420	Ubiquitination	CYELAPDQGLQPADQ HHHHCCCCCCCCCCC	54.13	-
448	Phosphorylation	EIVRHANSSTGQPCV HHHHHHHCCCCCCCC	30.02	21712546
449	Phosphorylation	IVRHANSSTGQPCVE HHHHHHCCCCCCCCC	36.04	21712546
450	Phosphorylation	VRHANSSTGQPCVEN HHHHHCCCCCCCCCC	39.39	21712546
505	Ubiquitination	IKSTIDASNISCFQN HHHHHCHHHCCHHHC	30.83	-

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
96	T	Phosphorylation	Kinase	CDK3	Q00526	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LIN9_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 LIN9_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RB_HUMAN	RB1	physical	15538385
LIN37_HUMAN	LIN37	physical	17531812
LIN52_HUMAN	LIN52	physical	17531812
LIN54_HUMAN	LIN54	physical	17531812
MYBB_HUMAN	MYBL2	physical	17531812
E2F4_HUMAN	E2F4	physical	17531812
RBL2_HUMAN	RBL2	physical	17531812
TFDP1_HUMAN	TFDP1	physical	17531812
TFDP2_HUMAN	TFDP2	physical	17531812
LIN9_HUMAN	LIN9	physical	17531812
MYBA_HUMAN	MYBL1	physical	17531812
LIN54_HUMAN	LIN54	physical	17671431
LIN37_HUMAN	LIN37	physical	17671431
MYBB_HUMAN	MYBL2	physical	17671431
RBBP4_HUMAN	RBBP4	physical	17671431
RBL2_HUMAN	RBL2	physical	17671431
RBL1_HUMAN	RBL1	physical	17671431
E2F4_HUMAN	E2F4	physical	17671431
RBL2_HUMAN	RBL2	physical	17159899
E2F4_HUMAN	E2F4	physical	17159899
MYBB_HUMAN	MYBL2	physical	17159899
MYBB_HUMAN	MYBL2	physical	25368258
MYBB_HUMAN	MYBL2	physical	28514442
LIN54_HUMAN	LIN54	physical	28514442
LIN52_HUMAN	LIN52	physical	28514442
DI3L1_HUMAN	DIS3L	physical	28514442
SLMAP_HUMAN	SLMAP	physical	28514442
RBBP4_HUMAN	RBBP4	physical	28514442
CO1A1_HUMAN	COL1A1	physical	28514442
HBS1L_HUMAN	HBS1L	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 LIN9_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-96, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309 AND SER-321, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"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-65; THR-297; THR-304;SER-309 AND SER-321, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; THR-297; SER-309 ANDSER-321, AND MASS SPECTROMETRY.	18691976 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309 AND SER-321, ANDMASS SPECTROMETRY.	18220336 [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-309, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-96, AND MASS SPECTROMETRY.	19413330 [Abstract]