dbPTM

SMC3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SMC3_MOUSE
UniProt AC	Q9CW03
Protein Name	Structural maintenance of chromosomes protein 3
Gene Name	Smc3
Organism	Mus musculus (Mouse).
Sequence Length	1217
Subcellular Localization	Nucleus . Chromosome . Chromosome, centromere . Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK, except
Protein Description	Central component of cohesin, a complex required for chromosome cohesion during the cell cycle. The cohesin complex may form a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. Cohesion is coupled to DNA replication and is involved in DNA repair. The cohesin complex plays also an important role in spindle pole assembly during mitosis and in chromosomes movement..
Protein Sequence	MYIKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTGPRVISAFVEIIFDNSDNRLPIDKEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQLLRAATGKAILNGIDSINKVLEHFRRKGINQHVQNGYHGIVMNNFECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILMEFNKMNLPGEVTFLPLNKLDVRDTAYPETNDAIPMISKLRYNPRFDKAFKHVFGKTLICRSMEVSTQLARAFTMDCITLEGDQVSHRGALTGGYYDTRKSRLELQKDVRKAEEELGELEAKLNENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRLDQVEQELNELRETEGGTVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEAFEKYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGYKSIMELMNVLELRKYEAIQLTFKQVSKNFSEVFQKLVPGGKATLVMKKGDVEGSQSQDEGEGSGESERGSGSQSSVPSVDQFTGVGIRVSFTGKQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYGVKFRNKVSHIDVITAEMAKDFVEDDTTHG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
18	Phosphorylation	FRSYRDQTIVDPFSS HHHCCCCCEECCCCC	27.53	-
69	Phosphorylation	LALLHEGTGPRVISA HHHHHCCCCHHHHHE	40.82	28066266
105	Acetylation	LRRVIGAKKDQYFLD HHHHHCCCCCCHHCC	52.23	23806337
106	Acetylation	RRVIGAKKDQYFLDK HHHHCCCCCCHHCCC	49.91	23806337
140	Acetylation	SNPYYIVKQGKINQM CCCEEEEECCCCCCC	43.72	22826441
149	Phosphorylation	GKINQMATAPDSQRL CCCCCCCCCCCHHHH	33.12	22345495
153	Phosphorylation	QMATAPDSQRLKLLR CCCCCCCHHHHHHHH	19.01	22345495
194	Ubiquitination	EKINELLKYIEERLH HHHHHHHHHHHHHHH	57.73	-
213	Phosphorylation	EKEELAQYQKWDKMR HHHHHHHHHHHHHHH	13.37	22817900
225	Phosphorylation	KMRRALEYTIYNQEL HHHHHHHHHHHHHHH	10.17	-
252	Acetylation	KRETSGEKSRQLRDA HHHCCCHHHHHHHHH	55.23	7618105
459	Ubiquitination	DRKYYEVKNKKDELQ HHHHHHHCCCHHHHH	51.62	-
461	Acetylation	KYYEVKNKKDELQSE HHHHHCCCHHHHHHH	56.75	7611975
462	Ubiquitination	YYEVKNKKDELQSER HHHHCCCHHHHHHHH	66.87	-
462	Acetylation	YYEVKNKKDELQSER HHHHCCCHHHHHHHH	66.87	7616431
560	Phosphorylation	TAGNRLFYHIVDSDE ECCCEEEEEEECCCC	8.67	17242355
665	Phosphorylation	VSHRGALTGGYYDTR CCCCCCCCCCCCHHH	28.20	29514104
668	Phosphorylation	RGALTGGYYDTRKSR CCCCCCCCCHHHHHH	10.26	29514104
671	Phosphorylation	LTGGYYDTRKSRLEL CCCCCCHHHHHHHHH	24.71	29514104
783	Phosphorylation	SLKAELGTDLLSQLS HHHHHHCHHHHHHCC	35.78	28066266
787	Phosphorylation	ELGTDLLSQLSLEDQ HHCHHHHHHCCHHHH	36.05	17525332
790	Phosphorylation	TDLLSQLSLEDQKRV HHHHHHCCHHHHHHH	23.29	28066266
886	Phosphorylation	RSEDLDNSIDKTEAG CCHHHCCCCCHHHHH	31.65	27841257
889	Acetylation	DLDNSIDKTEAGIKE HHCCCCCHHHHHHHH	46.74	23806337
968	Malonylation	SLKQLFRKLEQCNTE CHHHHHHHHHHHCHH	49.38	26320211
1013	Phosphorylation	ELDRGYKSIMELMNV HHHHHHHHHHHHHHH	20.77	25159016
1065	Phosphorylation	KKGDVEGSQSQDEGE EECCCCCCCCCCCCC	17.10	17525332
1067	Phosphorylation	GDVEGSQSQDEGEGS CCCCCCCCCCCCCCC	41.10	27087446
1074	Phosphorylation	SQDEGEGSGESERGS CCCCCCCCCCCCCCC	34.78	17525332
1077	Phosphorylation	EGEGSGESERGSGSQ CCCCCCCCCCCCCCC	35.80	28833060
1081	Phosphorylation	SGESERGSGSQSSVP CCCCCCCCCCCCCCC	41.30	23684622
1083	Phosphorylation	ESERGSGSQSSVPSV CCCCCCCCCCCCCCH	28.69	23984901
1085	Phosphorylation	ERGSGSQSSVPSVDQ CCCCCCCCCCCCHHH	34.69	25619855
1086	Phosphorylation	RGSGSQSSVPSVDQF CCCCCCCCCCCHHHC	30.34	25619855
1089	Phosphorylation	GSQSSVPSVDQFTGV CCCCCCCCHHHCCCE	35.85	25619855
1094	Phosphorylation	VPSVDQFTGVGIRVS CCCHHHCCCEEEEEE	25.89	25619855
1190	Acetylation	ADKFYGVKFRNKVSH CCHHCCCCCCCCCCE	33.95	-

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 SMC3_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
105	K	Acetylation	23806337
Acetylation at Lys-105 and Lys-106 by ESCO1 is important for genome stability and S phase sister chromatid cohesion.
106	K	Acetylation	23806337
Acetylation at Lys-105 and Lys-106 by ESCO1 is important for genome stability and S phase sister chromatid cohesion.
1083	S	Phosphorylation	22346761
Phosphorylated at Ser-1083 in a SPO11-dependent manner.

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 SMC3_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MECP2_MOUSE	Mecp2	physical	20159591
SYCP2_MOUSE	Sycp2	physical	22346761
HORM1_MOUSE	Hormad1	physical	22346761
SMC1B_MOUSE	Smc1b	physical	22346761
STAG3_MOUSE	Stag3	physical	22346761
REC8_MOUSE	Rec8	physical	22346761
SMC1A_MOUSE	Smc1a	physical	11564881
SMC1B_MOUSE	Smc1b	physical	11564881
ECT2_HUMAN	ECT2	physical	26496610
IF5A1_HUMAN	EIF5A	physical	26496610
KIF22_HUMAN	KIF22	physical	26496610
MVD1_HUMAN	MVD	physical	26496610
NCBP1_HUMAN	NCBP1	physical	26496610
RAD21_HUMAN	RAD21	physical	26496610
TAF1_HUMAN	TAF1	physical	26496610
TAF5_HUMAN	TAF5	physical	26496610
TAF12_HUMAN	TAF12	physical	26496610
THIO_HUMAN	TXN	physical	26496610
SMC1A_HUMAN	SMC1A	physical	26496610
IQGA1_HUMAN	IQGAP1	physical	26496610
UBP13_HUMAN	USP13	physical	26496610
RUSC2_HUMAN	RUSC2	physical	26496610
STAG1_HUMAN	STAG1	physical	26496610
TRI38_HUMAN	TRIM38	physical	26496610
SMC2_HUMAN	SMC2	physical	26496610
STAG2_HUMAN	STAG2	physical	26496610
PDS5B_HUMAN	PDS5B	physical	26496610
WAPL_HUMAN	WAPAL	physical	26496610
PDS5A_HUMAN	PDS5A	physical	26496610
ZFY26_HUMAN	ZFYVE26	physical	26496610
SK2L2_HUMAN	SKIV2L2	physical	26496610
GPKOW_HUMAN	GPKOW	physical	26496610
COA3_HUMAN	COA3	physical	26496610
T11L1_HUMAN	TCP11L1	physical	26496610
DEFM_HUMAN	PDF	physical	26496610
OBSCN_HUMAN	OBSCN	physical	26496610
ARI5B_HUMAN	ARID5B	physical	26496610
UIF_HUMAN	FYTTD1	physical	26496610
CDCA5_HUMAN	CDCA5	physical	26496610
CN080_HUMAN	C14orf80	physical	26496610
K2C6C_HUMAN	KRT6C	physical	26496610

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SMC3_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1067, AND MASSSPECTROMETRY.	19367708 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-787; SER-1065; SER-1067AND SER-1074, AND MASS SPECTROMETRY.	17525332 [Abstract]
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1067, AND MASSSPECTROMETRY.	17203969 [Abstract]
"Phosphoproteome analysis of mouse liver using immobilized metalaffinity purification and linear ion trap mass spectrometry."; Jin W.-H., Dai J., Zhou H., Xia Q.-C., Zou H.-F., Zeng R.; Rapid Commun. Mass Spectrom. 18:2169-2176(2004). Cited for: PHOSPHORYLATION AT SER-1013.	15378723 [Abstract]

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