dbPTM

LIN54_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LIN54_HUMAN
UniProt AC	Q6MZP7
Protein Name	Protein lin-54 homolog
Gene Name	LIN54
Organism	Homo sapiens (Human).
Sequence Length	749
Subcellular Localization	Nucleus .
Protein Description	Component of the DREAM complex, a multiprotein complex that can both act as a transcription activator or repressor depending on the context. [PubMed: 17671431]
Protein Sequence	MEVVPAEVNSLLPEEIMDTGITLVDDDSIEAVIVSSPIPMETELEEIVNINSTGDSTATPISTEPITVYSNHTNQVAVNTTITKADSNTTVKPAFPSGLQKLGAQTPVTISANQIILNKVSQTSDLKLGNQTLKPDGQKLILTTLGKSGSPIVLALPHSQLPQAQKVTTQAQSGDAKLPPQQIKVVTIGGRPEVKPVIGVSALTPGSQLINTTTQPSVLQTQQLKTVQIAKKPRTPTSGPVITKLIFAKPINSKAVTGQTTQVSPPVIAGRVLSQSTPGTPSKTITISESGVIGSTLNSTTQTPNKIAISPLKSPNKAVKSTVQTITVGGVSTSQFKTIIPLATAPNVQQIQVPGSKFHYVRLVTATSASSSTQPVSQNPSTNTQPLQQAKPVVVNTTPVRMSVPIVSAQAVKQVVPKPINPTSQIVTTSQPQQRLIMPATPLPQIQPNLTNLPPGTVLAPAPGTGNVGYAVLPAQYVTQLQQSSYVSIASNSTFTGTSGIQTQARLPFNGIIPSESASRPRKPCNCTKSLCLKLYCDCFANGEFCNNCNCTNCYNNLEHENERQKAIKACLDRNPEAFKPKIGKGKEGESDRRHSKGCNCKRSGCLKNYCECYEAKIMCSSICKCIGCKNFEESPERKTLMHLADAAEVRVQQQTAAKTKLSSQISDLLTRPTPALNSGGGKLPFTFVTKEVAEATCNCLLAQAEQADKKGKSKAAAERMILEEFGRCLMSVINSAGKAKSDPCAMNC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11 (in isoform 3)	Ubiquitination	-	8.57	-
14 (in isoform 3)	Phosphorylation	-	61.19	25159151
16 (in isoform 3)	Phosphorylation	-	2.63	25627689
23	Acetylation	IMDTGITLVDDDSIE HHHCCCEEECCCCCE	3.62	19608861
28	Acetylation	ITLVDDDSIEAVIVS CEEECCCCCEEEEEC	29.35	19608861
35	Phosphorylation	SIEAVIVSSPIPMET CCEEEEECCCCCCCC	21.19	26074081
36	Phosphorylation	IEAVIVSSPIPMETE CEEEEECCCCCCCCC	18.89	26074081
42	Phosphorylation	SSPIPMETELEEIVN CCCCCCCCCHHHHHC	39.35	26074081
92	Acetylation	ADSNTTVKPAFPSGL CCCCCCCCCCCCCHH	28.65	23954790
92	Ubiquitination	ADSNTTVKPAFPSGL CCCCCCCCCCCCCHH	28.65	-
101	Ubiquitination	AFPSGLQKLGAQTPV CCCCHHHHCCCCCCE	54.66	-
106	Phosphorylation	LQKLGAQTPVTISAN HHHCCCCCCEEEECC	21.13	25159151
106	O-linked_Glycosylation	LQKLGAQTPVTISAN HHHCCCCCCEEEECC	21.13	20068230
109	O-linked_Glycosylation	LGAQTPVTISANQII CCCCCCEEEECCHHH	15.49	20068230
109	Phosphorylation	LGAQTPVTISANQII CCCCCCEEEECCHHH	15.49	27174698
111	O-linked_Glycosylation	AQTPVTISANQIILN CCCCEEEECCHHHHH	16.29	20068230
111	Phosphorylation	AQTPVTISANQIILN CCCCEEEECCHHHHH	16.29	27174698
119	Ubiquitination	ANQIILNKVSQTSDL CCHHHHHCCCCCCCC	39.56	-
121	Phosphorylation	QIILNKVSQTSDLKL HHHHHCCCCCCCCCC	29.38	27174698
123	Phosphorylation	ILNKVSQTSDLKLGN HHHCCCCCCCCCCCC	19.39	27174698
124	Phosphorylation	LNKVSQTSDLKLGNQ HHCCCCCCCCCCCCE	33.05	27174698
127	Ubiquitination	VSQTSDLKLGNQTLK CCCCCCCCCCCEEEC	60.38	-
134	Ubiquitination	KLGNQTLKPDGQKLI CCCCEEECCCCCEEE	44.44	-
134	Acetylation	KLGNQTLKPDGQKLI CCCCEEECCCCCEEE	44.44	26051181
136	Acetylation	GNQTLKPDGQKLILT CCEEECCCCCEEEEE	71.25	19608861
136	Ubiquitination	GNQTLKPDGQKLILT CCEEECCCCCEEEEE	71.25	19608861
139	Ubiquitination	TLKPDGQKLILTTLG EECCCCCEEEEEECC	42.92	-
139	Sumoylation	TLKPDGQKLILTTLG EECCCCCEEEEEECC	42.92	28112733
143	Phosphorylation	DGQKLILTTLGKSGS CCCEEEEEECCCCCC	17.00	25954137
144	Phosphorylation	GQKLILTTLGKSGSP CCEEEEEECCCCCCC	30.02	25954137
147	Ubiquitination	LILTTLGKSGSPIVL EEEEECCCCCCCEEE	55.55	-
147	Acetylation	LILTTLGKSGSPIVL EEEEECCCCCCCEEE	55.55	25953088
148	Phosphorylation	ILTTLGKSGSPIVLA EEEECCCCCCCEEEE	42.58	24732914
150	Phosphorylation	TTLGKSGSPIVLALP EECCCCCCCEEEEEC	20.67	25159151
159	Phosphorylation	IVLALPHSQLPQAQK EEEEECHHHCCCCCC	31.32	25954137
166	Ubiquitination	SQLPQAQKVTTQAQS HHCCCCCCCCCCCCC	44.56	-
168	O-linked_Glycosylation	LPQAQKVTTQAQSGD CCCCCCCCCCCCCCC	21.89	20068230
195	Ubiquitination	IGGRPEVKPVIGVSA ECCCCCCCCEEEEEE	31.72	-
195	Acetylation	IGGRPEVKPVIGVSA ECCCCCCCCEEEEEE	31.72	26051181
235	Phosphorylation	QIAKKPRTPTSGPVI EECCCCCCCCCCCCE	39.17	26657352
235	O-linked_Glycosylation	QIAKKPRTPTSGPVI EECCCCCCCCCCCCE	39.17	20068230
237	Phosphorylation	AKKPRTPTSGPVITK CCCCCCCCCCCCEEE	45.78	28450419
237	O-linked_Glycosylation	AKKPRTPTSGPVITK CCCCCCCCCCCCEEE	45.78	20068230
238	O-linked_Glycosylation	KKPRTPTSGPVITKL CCCCCCCCCCCEEEE	42.16	32574038
238	Phosphorylation	KKPRTPTSGPVITKL CCCCCCCCCCCEEEE	42.16	28450419
238	O-linked_Glycosylation	KKPRTPTSGPVITKL CCCCCCCCCCCEEEE	42.16	20068230
243	Phosphorylation	PTSGPVITKLIFAKP CCCCCCEEEEEEEEE	21.74	28450419
243	O-linked_Glycosylation	PTSGPVITKLIFAKP CCCCCCEEEEEEEEE	21.74	20068230
244	Acetylation	TSGPVITKLIFAKPI CCCCCEEEEEEEEEC	28.58	19608861
249	Acetylation	ITKLIFAKPINSKAV EEEEEEEEECCCCCC	35.36	19608861
249	Ubiquitination	ITKLIFAKPINSKAV EEEEEEEEECCCCCC	35.36	19608861
253	O-linked_Glycosylation	IFAKPINSKAVTGQT EEEEECCCCCCCCCC	23.78	20068230
254	Ubiquitination	FAKPINSKAVTGQTT EEEECCCCCCCCCCC	42.25	-
257	Phosphorylation	PINSKAVTGQTTQVS ECCCCCCCCCCCCCC	28.56	24732914
260	Phosphorylation	SKAVTGQTTQVSPPV CCCCCCCCCCCCCCE	22.12	24732914
261	Phosphorylation	KAVTGQTTQVSPPVI CCCCCCCCCCCCCEE	21.05	30266825
264	Phosphorylation	TGQTTQVSPPVIAGR CCCCCCCCCCEEECE	17.42	23401153
268	Acetylation	TQVSPPVIAGRVLSQ CCCCCCEEECEEECC	4.08	19608861
268	Ubiquitination	TQVSPPVIAGRVLSQ CCCCCCEEECEEECC	4.08	19608861
274	Phosphorylation	VIAGRVLSQSTPGTP EEECEEECCCCCCCC	21.16	30266825
276	Phosphorylation	AGRVLSQSTPGTPSK ECEEECCCCCCCCCC	32.94	30266825
276	O-linked_Glycosylation	AGRVLSQSTPGTPSK ECEEECCCCCCCCCC	32.94	20068230
277	Phosphorylation	GRVLSQSTPGTPSKT CEEECCCCCCCCCCE	20.35	30266825
280	Phosphorylation	LSQSTPGTPSKTITI ECCCCCCCCCCEEEE	26.12	30266825
282	Phosphorylation	QSTPGTPSKTITISE CCCCCCCCCEEEEEC	42.12	30266825
282	O-linked_Glycosylation	QSTPGTPSKTITISE CCCCCCCCCEEEEEC	42.12	20068230
283	Acetylation	STPGTPSKTITISES CCCCCCCCEEEEECC	45.19	26051181
288	O-linked_Glycosylation	PSKTITISESGVIGS CCCEEEEECCCCCCC	19.63	20068230
290	O-linked_Glycosylation	KTITISESGVIGSTL CEEEEECCCCCCCCC	31.41	20068230
295	Phosphorylation	SESGVIGSTLNSTTQ ECCCCCCCCCCCCCC	20.71	27080861
296	O-linked_Glycosylation	ESGVIGSTLNSTTQT CCCCCCCCCCCCCCC	25.42	20068230
296	Phosphorylation	ESGVIGSTLNSTTQT CCCCCCCCCCCCCCC	25.42	27080861
299	Phosphorylation	VIGSTLNSTTQTPNK CCCCCCCCCCCCCCE	35.62	27251275
300	Phosphorylation	IGSTLNSTTQTPNKI CCCCCCCCCCCCCEE	23.11	27080861
301	Phosphorylation	GSTLNSTTQTPNKIA CCCCCCCCCCCCEEE	30.21	27080861
303	Phosphorylation	TLNSTTQTPNKIAIS CCCCCCCCCCEEEEC	27.08	27080861
310	Phosphorylation	TPNKIAISPLKSPNK CCCEEEECCCCCCCH	18.37	29255136
313	Ubiquitination	KIAISPLKSPNKAVK EEEECCCCCCCHHHH	68.22	-
314	Phosphorylation	IAISPLKSPNKAVKS EEECCCCCCCHHHHC	41.19	29255136
321	O-linked_Glycosylation	SPNKAVKSTVQTITV CCCHHHHCCCEEEEE	27.49	20068230
321	Phosphorylation	SPNKAVKSTVQTITV CCCHHHHCCCEEEEE	27.49	25332170
332	O-linked_Glycosylation	TITVGGVSTSQFKTI EEEECCCCHHHCEEE	26.14	20068230
333	O-linked_Glycosylation	ITVGGVSTSQFKTII EEECCCCHHHCEEEE	24.92	20068230
333	Phosphorylation	ITVGGVSTSQFKTII EEECCCCHHHCEEEE	24.92	25332170
344	O-linked_Glycosylation	KTIIPLATAPNVQQI EEEEEECCCCCEEEE	50.78	20068230
344	Phosphorylation	KTIIPLATAPNVQQI EEEEEECCCCCEEEE	50.78	25332170
357	Acetylation	QIQVPGSKFHYVRLV EEECCCCCEEEEEEE	41.92	19608861
357	Ubiquitination	QIQVPGSKFHYVRLV EEECCCCCEEEEEEE	41.92	19608861
357	Sumoylation	QIQVPGSKFHYVRLV EEECCCCCEEEEEEE	41.92	28112733
371	Phosphorylation	VTATSASSSTQPVSQ EEEECCCCCCCCCCC	36.80	-
397	Phosphorylation	AKPVVVNTTPVRMSV CCCEEEECCCCCCCC	22.37	27732954
398	Phosphorylation	KPVVVNTTPVRMSVP CCEEEECCCCCCCCC	18.00	25159151
413	Ubiquitination	IVSAQAVKQVVPKPI EEEHHHHHCCCCCCC	40.15	-
418	Ubiquitination	AVKQVVPKPINPTSQ HHHCCCCCCCCCCCC	47.09	-
418	Acetylation	AVKQVVPKPINPTSQ HHHCCCCCCCCCCCC	47.09	26051181
429	O-linked_Glycosylation	PTSQIVTTSQPQQRL CCCCEEECCCCCCEE	17.92	20068230
430	O-linked_Glycosylation	TSQIVTTSQPQQRLI CCCEEECCCCCCEEE	30.42	20068230
430	Phosphorylation	TSQIVTTSQPQQRLI CCCEEECCCCCCEEE	30.42	26714015
435	Methylation	TTSQPQQRLIMPATP ECCCCCCEEECCCCC	22.42	-
515	Phosphorylation	PFNGIIPSESASRPR CCCCCCCCCCCCCCC	33.50	28555341
529	Ubiquitination	RKPCNCTKSLCLKLY CCCCCCCHHHHHHHH	43.56	-
569	Ubiquitination	NERQKAIKACLDRNP HHHHHHHHHHHHCCH	37.60	-
580	Ubiquitination	DRNPEAFKPKIGKGK HCCHHHHCCCCCCCC	53.07	-
580	Acetylation	DRNPEAFKPKIGKGK HCCHHHHCCCCCCCC	53.07	26051181
582	Ubiquitination	NPEAFKPKIGKGKEG CHHHHCCCCCCCCCC	65.76	-
608	Ubiquitination	CKRSGCLKNYCECYE CCCCCCCHHHHHHHH	50.36	-
635	Phosphorylation	GCKNFEESPERKTLM CCCCCCCCCCHHHHH	25.51	23401153
639	Sumoylation	FEESPERKTLMHLAD CCCCCCHHHHHHHHH	44.33	-
639	Sumoylation	FEESPERKTLMHLAD CCCCCCHHHHHHHHH	44.33	28112733
639	Ubiquitination	FEESPERKTLMHLAD CCCCCCHHHHHHHHH	44.33	-
640	Phosphorylation	EESPERKTLMHLADA CCCCCHHHHHHHHHH	35.22	24719451
659	Sumoylation	VQQQTAAKTKLSSQI HHHHHHHHHHHHHHH	43.67	28112733
661	Sumoylation	QQTAAKTKLSSQISD HHHHHHHHHHHHHHH	45.74	-
661	Sumoylation	QQTAAKTKLSSQISD HHHHHHHHHHHHHHH	45.74	28112733
661	Ubiquitination	QQTAAKTKLSSQISD HHHHHHHHHHHHHHH	45.74	-
661	Acetylation	QQTAAKTKLSSQISD HHHHHHHHHHHHHHH	45.74	25953088
663	Phosphorylation	TAAKTKLSSQISDLL HHHHHHHHHHHHHHH	23.04	26714015
664	Phosphorylation	AAKTKLSSQISDLLT HHHHHHHHHHHHHHH	41.80	26714015
667	Phosphorylation	TKLSSQISDLLTRPT HHHHHHHHHHHHCCC	17.99	28555341
671	Phosphorylation	SQISDLLTRPTPALN HHHHHHHHCCCCCCC	41.73	26714015
683	Ubiquitination	ALNSGGGKLPFTFVT CCCCCCCCCCEEEEC	57.15	-
683	Acetylation	ALNSGGGKLPFTFVT CCCCCCCCCCEEEEC	57.15	26051181
710	Ubiquitination	AQAEQADKKGKSKAA HHHHHHCCCCCCHHH	67.45	-
711	Ubiquitination	QAEQADKKGKSKAAA HHHHHCCCCCCHHHH	72.60	-
715	Acetylation	ADKKGKSKAAAERMI HCCCCCCHHHHHHHH	45.60	7365103
741	Sumoylation	INSAGKAKSDPCAMN HHHCCCCCCCCCCCC	59.90	-
741	Sumoylation	INSAGKAKSDPCAMN HHHCCCCCCCCCCCC	59.90	-
741	Ubiquitination	INSAGKAKSDPCAMN HHHCCCCCCCCCCCC	59.90	-

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 LIN54_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LIN54_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 LIN54_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LIN9_HUMAN	LIN9	physical	17531812
LIN37_HUMAN	LIN37	physical	17531812
LIN52_HUMAN	LIN52	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
RBBP4_HUMAN	RBBP4	physical	17531812
MYBA_HUMAN	MYBL1	physical	17531812
LIN9_HUMAN	LIN9	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	19725879
MYBB_HUMAN	MYBL2	physical	19725879
MYBB_HUMAN	MYBL2	physical	25368258

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 LIN54_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-244; LYS-249 AND LYS-357,AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, AND MASSSPECTROMETRY.	19413330 [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-310 AND SER-314, ANDMASS SPECTROMETRY.	18669648 [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-310 AND SER-314, ANDMASS SPECTROMETRY.	18220336 [Abstract]