dbPTM

SMC5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SMC5_HUMAN
UniProt AC	Q8IY18
Protein Name	Structural maintenance of chromosomes protein 5
Gene Name	SMC5
Organism	Homo sapiens (Human).
Sequence Length	1101
Subcellular Localization	Nucleus . Chromosome . Nucleus, PML body . Chromosome, telomere . Associates with chromatin (PubMed:25931565). Colocalizes with SMC6 on the X-Y chromosome pair within the sex vesicle during late pachytene/diplotene (By similarity). Localizes to PML n
Protein Description	Core component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). Required for recruitment of telomeres to PML nuclear bodies. Required for sister chromatid cohesion during prometaphase and mitotic progression; the function seems to be independent of SMC6. SMC5-SMC6 complex may prevent transcription of episomal DNA, such as circular viral DNA genome. [PubMed: 26983541]
Protein Sequence	MATPSKKTSTPSPQPSKRALPRDPSSEVPSKRKNSAPQLPLLQSSGPFVEGSIVRISMENFLTYDICEVSPGPHLNMIVGANGTGKSSIVCAICLGLAGKPAFMGRADKVGFFVKRGCSRGMVEIELFRASGNLVITREIDVAKNQSFWFINKKSTTQKIVEEKVAALNIQVGNLCQFLPQDKVGEFAKLSKIELLEATEKSIGPPEMHKYHCELKNLREKEKQLETSCKEKTEYLQKMVQRNERYKQDVERFYERKRHLDLIEMLEAKRPWVEYENVRQEYEEVKLVRDRVKEEVRKLKEGQIPVTCRIEEMENERHNLEARIKEKATDIKEASQKCKQKQDVIERKDKHIEELQQALIVKQNEELDRQRRIGNTRKMIEDLQNELKTTENCENLQPQIDAITNDLRRIQDEKALCEGEIIDKRRERETLEKEKKSVDDHIVRFDNLMNQKEDKLRQRFRDTYDAVLWLRNNRDKFKQRVCEPIMLTINMKDNKNAKYIENHIPSNDLRAFVFESQEDMEVFLKEVRDNKKLRVNAVIAPKSSYADKAPSRSLNELKQYGFFSYLRELFDAPDPVMSYLCCQYHIHEVPVGTEKTRERIERVIQETRLKQIYTAEEKYVVKTSFYSNKVISSNTSLKVAQFLTVTVDLEQRRHLEEQLKEIHRKLQAVDSGLIALRETSKHLEHKDNELRQKKKELLERKTKKRQLEQKISSKLGSLKLMEQDTCNLEEEERKASTKIKEINVQKAKLVTELTNLIKICTSLHIQKVDLILQNTTVISEKNKLESDYMAASSQLRLTEQHFIELDENRQRLLQKCKELMKRARQVCNLGAEQTLPQEYQTQVPTIPNGHNSSLPMVFQDLPNTLDEIDALLTEERSRASCFTGLNPTIVQEYTKREEEIEQLTEELKGKKVELDQYRENISQVKERWLNPLKELVEKINEKFSNFFSSMQCAGEVDLHTENEEDYDKYGIRIRVKFRSSTQLHELTPHHQSGGERSVSTMLYLMALQELNRCPFRVVDEINQGMDPINERRVFEMVVNTACKENTSQYFFITPKLLQNLPYSEKMTVLFVYNGPHMLEPNTWNLKAFQRRRRRITFTQPS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MATPSKKTSTPSPQP CCCCCCCCCCCCCCC	41.38	27794612
9	Phosphorylation	ATPSKKTSTPSPQPS CCCCCCCCCCCCCCC	47.39	27794612
10	Phosphorylation	TPSKKTSTPSPQPSK CCCCCCCCCCCCCCC	32.77	26055452
12	Phosphorylation	SKKTSTPSPQPSKRA CCCCCCCCCCCCCCC	35.93	23401153
16	Phosphorylation	STPSPQPSKRALPRD CCCCCCCCCCCCCCC	29.53	27794612
17	Acetylation	TPSPQPSKRALPRDP CCCCCCCCCCCCCCC	48.66	25953088
25	Phosphorylation	RALPRDPSSEVPSKR CCCCCCCCCCCCCCC	43.34	25159151
26	Phosphorylation	ALPRDPSSEVPSKRK CCCCCCCCCCCCCCC	48.26	21815630
30	Phosphorylation	DPSSEVPSKRKNSAP CCCCCCCCCCCCCCC	50.71	21815630
31	Acetylation	PSSEVPSKRKNSAPQ CCCCCCCCCCCCCCC	62.41	25953088
31	Ubiquitination	PSSEVPSKRKNSAPQ CCCCCCCCCCCCCCC	62.41	-
35	Phosphorylation	VPSKRKNSAPQLPLL CCCCCCCCCCCCCCC	44.34	25159151
44	Phosphorylation	PQLPLLQSSGPFVEG CCCCCCCCCCCCCCC	36.91	23927012
45	Phosphorylation	QLPLLQSSGPFVEGS CCCCCCCCCCCCCCC	37.21	23927012
52	Phosphorylation	SGPFVEGSIVRISME CCCCCCCCEEEEECC	12.38	23898821
100	Ubiquitination	ICLGLAGKPAFMGRA HHHHHCCCCHHCCCC	27.80	-
109	Acetylation	AFMGRADKVGFFVKR HHCCCCHHHEEEEEC	43.18	30592491
109	Ubiquitination	AFMGRADKVGFFVKR HHCCCCHHHEEEEEC	43.18	-
115	Acetylation	DKVGFFVKRGCSRGM HHHEEEEECCCCCCC	37.61	30592497
115	Ubiquitination	DKVGFFVKRGCSRGM HHHEEEEECCCCCCC	37.61	-
120	Ubiquitination	FVKRGCSRGMVEIEL EEECCCCCCCEEEEE	41.10	22505724
142	Ubiquitination	VITREIDVAKNQSFW EEEEEEEECCCCCEE	11.39	23000965
157	Phosphorylation	FINKKSTTQKIVEEK EEECCCCCHHHHHHH	34.65	-
159	Ubiquitination	NKKSTTQKIVEEKVA ECCCCCHHHHHHHHH	46.78	-
180	Ubiquitination	GNLCQFLPQDKVGEF CCHHHHCCCCCHHHH	41.43	23000965
183	Ubiquitination	CQFLPQDKVGEFAKL HHHCCCCCHHHHHHH	47.06	23000965
189	Ubiquitination	DKVGEFAKLSKIELL CCHHHHHHHHHHHHH	59.62	23000965
192	Ubiquitination	GEFAKLSKIELLEAT HHHHHHHHHHHHHHH	51.11	23000965
199	Phosphorylation	KIELLEATEKSIGPP HHHHHHHHHHHCCCH	34.27	20068231
210	Ubiquitination	IGPPEMHKYHCELKN CCCHHHHHHHHHHHH	35.07	29967540
216	Acetylation	HKYHCELKNLREKEK HHHHHHHHHHHHHHH	31.48	26051181
216	Ubiquitination	HKYHCELKNLREKEK HHHHHHHHHHHHHHH	31.48	29967540
227	Phosphorylation	EKEKQLETSCKEKTE HHHHHHHHHHHHHHH	48.28	29083192
228	Phosphorylation	KEKQLETSCKEKTEY HHHHHHHHHHHHHHH	17.51	29083192
232	Ubiquitination	LETSCKEKTEYLQKM HHHHHHHHHHHHHHH	31.95	-
233	Phosphorylation	ETSCKEKTEYLQKMV HHHHHHHHHHHHHHH	30.84	29083192
235	Phosphorylation	SCKEKTEYLQKMVQR HHHHHHHHHHHHHHH	21.47	29083192
238	Ubiquitination	EKTEYLQKMVQRNER HHHHHHHHHHHHCHH	38.14	21906983
254	Phosphorylation	KQDVERFYERKRHLD HHHHHHHHHHHHHHH	22.50	26657352
269	Ubiquitination	LIEMLEAKRPWVEYE HHHHHHHCCCCCCEE	50.01	29967540
275	Phosphorylation	AKRPWVEYENVRQEY HCCCCCCEEHHHHHH	11.81	-
282	Phosphorylation	YENVRQEYEEVKLVR EEHHHHHHHHHHHHH	14.73	-
286	Acetylation	RQEYEEVKLVRDRVK HHHHHHHHHHHHHHH	44.54	25953088
286	Ubiquitination	RQEYEEVKLVRDRVK HHHHHHHHHHHHHHH	44.54	33845483
300	Ubiquitination	KEEVRKLKEGQIPVT HHHHHHHHCCCCCCE	63.93	29967540
329	Phosphorylation	ARIKEKATDIKEASQ HHHHHHCHHHHHHHH	49.69	29396449
350	Ubiquitination	DVIERKDKHIEELQQ HHHHHHHHHHHHHHH	49.90	29967540
362	Acetylation	LQQALIVKQNEELDR HHHHHHHHCHHHHHH	40.17	25953088
362	Ubiquitination	LQQALIVKQNEELDR HHHHHHHHCHHHHHH	40.17	29967540
378	Ubiquitination	RRIGNTRKMIEDLQN HHHCHHHHHHHHHHH	42.04	29967540
405	Ubiquitination	PQIDAITNDLRRIQD HHHHHHHHHHHHHHH	39.96	24816145
414	Acetylation	LRRIQDEKALCEGEI HHHHHHHHHHHCCCC	55.75	26051181
414	Ubiquitination	LRRIQDEKALCEGEI HHHHHHHHHHHCCCC	55.75	29967540
424	Ubiquitination	CEGEIIDKRRERETL HCCCCCCHHHHHHHH	42.84	29967540
436	Ubiquitination	ETLEKEKKSVDDHIV HHHHHHHHCHHHHHH	57.72	29967540
443	Ubiquitination	KSVDDHIVRFDNLMN HCHHHHHHHHHHHHC	4.47	24816145
452	Ubiquitination	FDNLMNQKEDKLRQR HHHHHCHHHHHHHHH	63.98	32015554
455	Acetylation	LMNQKEDKLRQRFRD HHCHHHHHHHHHHHH	46.81	26051181
455	Ubiquitination	LMNQKEDKLRQRFRD HHCHHHHHHHHHHHH	46.81	29967540
474	Ubiquitination	VLWLRNNRDKFKQRV HHHHHCCHHHHHHHH	52.63	22505724
492	Ubiquitination	IMLTINMKDNKNAKY EEEEEECCCCCCCCH	54.37	-
495	Ubiquitination	TINMKDNKNAKYIEN EEECCCCCCCCHHHH	69.30	-
498	Ubiquitination	MKDNKNAKYIENHIP CCCCCCCCHHHHCCC	57.04	22505724
506	Phosphorylation	YIENHIPSNDLRAFV HHHHCCCCCHHHHHE	42.23	25159151
520	Ubiquitination	VFESQEDMEVFLKEV EECCHHHHHHHHHHH	4.68	23000965
534	Ubiquitination	VRDNKKLRVNAVIAP HHCCCCEEEEEEECC	28.64	23000965
542	Ubiquitination	VNAVIAPKSSYADKA EEEEECCCCHHCCCC	42.91	33845483
548	Acetylation	PKSSYADKAPSRSLN CCCHHCCCCCCCCHH	54.76	19608861
548	Ubiquitination	PKSSYADKAPSRSLN CCCHHCCCCCCCCHH	54.76	19608861
558	Ubiquitination	SRSLNELKQYGFFSY CCCHHHHHHCCHHHH	34.98	23000965
560	Phosphorylation	SLNELKQYGFFSYLR CHHHHHHCCHHHHHH	17.82	21406692
564	Phosphorylation	LKQYGFFSYLRELFD HHHCCHHHHHHHHHC	22.46	21406692
565	Phosphorylation	KQYGFFSYLRELFDA HHCCHHHHHHHHHCC	12.48	21406692
595	Ubiquitination	EVPVGTEKTRERIER ECCCCCHHHHHHHHH	53.36	-
610	Malonylation	VIQETRLKQIYTAEE HHHHHHHHHHCCCCC	31.21	26320211
610	Ubiquitination	VIQETRLKQIYTAEE HHHHHHHHHHCCCCC	31.21	33845483
614	Phosphorylation	TRLKQIYTAEEKYVV HHHHHHCCCCCEEEE	29.26	30242111
618	Acetylation	QIYTAEEKYVVKTSF HHCCCCCEEEEEEEE	34.55	26051181
618	Ubiquitination	QIYTAEEKYVVKTSF HHCCCCCEEEEEEEE	34.55	29967540
619	Phosphorylation	IYTAEEKYVVKTSFY HCCCCCEEEEEEEEC	17.47	-
626	Phosphorylation	YVVKTSFYSNKVISS EEEEEEECCCCEECC	15.88	25884760
629	Ubiquitination	KTSFYSNKVISSNTS EEEECCCCEECCCCC	34.70	29967540
665	Ubiquitination	QLKEIHRKLQAVDSG HHHHHHHHHHHHHHH	30.68	29967540
671	Phosphorylation	RKLQAVDSGLIALRE HHHHHHHHHHHHHHH	28.97	22210691
686	Acetylation	TSKHLEHKDNELRQK HHHHHCCHHHHHHHH	53.53	25953088
714	Acetylation	LEQKISSKLGSLKLM HHHHHHHHHHHHHHH	50.50	25953088
714	Ubiquitination	LEQKISSKLGSLKLM HHHHHHHHHHHHHHH	50.50	29967540
719	Ubiquitination	SSKLGSLKLMEQDTC HHHHHHHHHHHCCCC	47.70	32015554
740	Ubiquitination	RKASTKIKEINVQKA HHHHHHHHHHHHHHH	54.84	-
746	Ubiquitination	IKEINVQKAKLVTEL HHHHHHHHHHHHHHH	43.11	-
748	Acetylation	EINVQKAKLVTELTN HHHHHHHHHHHHHHH	50.99	25953088
748	Ubiquitination	EINVQKAKLVTELTN HHHHHHHHHHHHHHH	50.99	-
751	Phosphorylation	VQKAKLVTELTNLIK HHHHHHHHHHHHHHH	35.40	22817900
754	Phosphorylation	AKLVTELTNLIKICT HHHHHHHHHHHHHHH	23.03	22817900
779	Phosphorylation	LQNTTVISEKNKLES EECCEECCCCCCCCH	37.88	18491316
783	Ubiquitination	TVISEKNKLESDYMA EECCCCCCCCHHHHH	65.78	24816145
786	Phosphorylation	SEKNKLESDYMAASS CCCCCCCHHHHHHHH	44.47	30576142
788	Phosphorylation	KNKLESDYMAASSQL CCCCCHHHHHHHHHH	9.64	20873877
792	Phosphorylation	ESDYMAASSQLRLTE CHHHHHHHHHHHHHH	14.74	25159151
793	Phosphorylation	SDYMAASSQLRLTEQ HHHHHHHHHHHHHHH	28.62	25159151
797	Ubiquitination	AASSQLRLTEQHFIE HHHHHHHHHHHHHHH	9.33	24816145
821	Ubiquitination	QKCKELMKRARQVCN HHHHHHHHHHHHHHH	56.37	24816145
895	Ubiquitination	TIVQEYTKREEEIEQ HHHHHHHHCHHHHHH	57.84	-
908	Ubiquitination	EQLTEELKGKKVELD HHHHHHHCCCCCCHH	72.47	32015554
911	Ubiquitination	TEELKGKKVELDQYR HHHHCCCCCCHHHHH	50.00	29967540
925	Ubiquitination	RENISQVKERWLNPL HHHHHHHHHHHHHHH	33.65	29967540
933	Ubiquitination	ERWLNPLKELVEKIN HHHHHHHHHHHHHHH	50.70	29967540
979	Phosphorylation	RIRVKFRSSTQLHEL EEEEEECCCCCCEEC	40.65	20873877
980	Phosphorylation	IRVKFRSSTQLHELT EEEEECCCCCCEECC	18.86	28555341
981	Phosphorylation	RVKFRSSTQLHELTP EEEECCCCCCEECCC	36.07	28555341
987	Phosphorylation	STQLHELTPHHQSGG CCCCEECCCCCCCCC	20.00	22067460
1025	Sulfoxidation	VDEINQGMDPINERR HCHHHCCCCCCCHHH	3.89	21406390
1046	Phosphorylation	NTACKENTSQYFFIT CHHHHCCCCCEEEEC	20.49	-
1047	Phosphorylation	TACKENTSQYFFITP HHHHCCCCCEEEECH	34.17	-
1062	Phosphorylation	KLLQNLPYSEKMTVL HHHCCCCCCCCEEEE	32.40	-
1096	Phosphorylation	QRRRRRITFTQPS-- HHHHHCCEEECCC--	20.86	23312004

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
-	K	Ubiquitination	E3 ubiquitin ligase	X	P03165	PMID:31167910

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SMC5_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 SMC5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMC6_HUMAN	SMC6	physical	11408570
NSE2_HUMAN	NSMCE2	physical	16055714
NSE1_HUMAN	NSMCE1	physical	16055714

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 SMC5_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-548, AND MASS SPECTROMETRY.	19608861 [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-35, AND MASSSPECTROMETRY.	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-35, AND MASSSPECTROMETRY.	18669648 [Abstract]