dbPTM

SMC1A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SMC1A_MOUSE
UniProt AC	Q9CU62
Protein Name	Structural maintenance of chromosomes protein 1A
Gene Name	Smc1a
Organism	Mus musculus (Mouse).
Sequence Length	1233
Subcellular Localization	Nucleus. Chromosome. Chromosome, centromere. Associates with chromatin. The phosphorylated form on Ser-957 and Ser-966 associates with chromatin during G1/S/G2 phases but not during M phase, suggesting that phosphorylation does not regulate cohesin f
Protein Description	Involved in chromosome cohesion during cell cycle and in DNA repair. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, and works as a downstream effector in the ATM/NBS1 branch of S-phase checkpoint (By similarity). Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms 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. The cohesin complex may also play a role in spindle pole assembly during mitosis. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint..
Protein Sequence	MGFLKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAPVGKPAANRAFVSMVYSEEGAEDRTFARVIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQPTQKKYQIAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEPPHIKKALQYACGNALVCDNVEDARRIAFGGHQRHKTVALDGTLFQKSGVISGGASDLKAKARRWDEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDEVFEEFCREIGVRNIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKLPLSKGTMDDISQEEGSSQGEESVSGSQRTSSIYAREALIEIDYGDLCEDLKDAQAEEEIKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNACFESVATNIDEIYKALSRNSSAQAFLGPENPEEPYLDGINYNCVAPGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTCNFQAIVISLKEEFYTKAESLIGVYPEQGDCVISKVLTFDLTKYPDANPNPNEQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
161	Phosphorylation	LFEEISRSGELAQEY HHHHHHHHCHHHHHH	29.81	20469934
182	Phosphorylation	MVKAEEDTQFNYHRK HHHHHHHHCCCHHHH	38.04	20469934
186	Phosphorylation	EEDTQFNYHRKKNIA HHHHCCCHHHHHCHH	12.32	-
244	Phosphorylation	KLNKELASKNKEIEK HHHHHHHHCCCHHHH	49.76	22817900
324	Acetylation	KSLQNAQKHYKKRKG HHHHHHHHHHHHHCC	46.63	23806337
358	Phosphorylation	EERMEEESQSQGRDL HHHHHHHHHHCCCCC	38.11	26643407
360	Phosphorylation	RMEEESQSQGRDLTL HHHHHHHHCCCCCCC	43.83	26824392
366	Phosphorylation	QSQGRDLTLEENQVK HHCCCCCCCCHHHHH	36.09	29550500
508	Acetylation	AEIMESIKRLYPGSV HHHHHHHHHHCCCCH	45.70	2391819
540	Ubiquitination	AVTKVLGKNMDAIIV HHHHHHCCCCCEEEE	44.96	22790023
540	Acetylation	AVTKVLGKNMDAIIV HHHHHHCCCCCEEEE	44.96	22826441
561	Ubiquitination	RDCIQYIKEQRGEPE HHHHHHHHHHCCCCC	42.75	22790023
589	Ubiquitination	DEKLRELKGAKLVID HHHHHHHCCCEEEEE	52.66	27667366
611	Phosphorylation	HIKKALQYACGNALV HHHHHHHHHHCCEEE	12.52	17242355
637	Ubiquitination	FGGHQRHKTVALDGT CCCCCCCCEEEECCC	47.05	22790023
648	Acetylation	LDGTLFQKSGVISGG ECCCEEECCCCCCCC	41.67	-
649	Phosphorylation	DGTLFQKSGVISGGA CCCEEECCCCCCCCH	27.75	21454597
653	Phosphorylation	FQKSGVISGGASDLK EECCCCCCCCHHHHH	28.86	29899451
657	Phosphorylation	GVISGGASDLKAKAR CCCCCCHHHHHHHHH	46.91	21454597
713	Acetylation	HGLQMRLKYSQSDLE HHHHHHHHCCHHHHH	32.27	22826441
723	Ubiquitination	QSDLEQTKTRHLALN HHHHHHHHHHHHHHH	43.16	27667366
805	Acetylation	KRQNEIAKKRLEFEN HHHHHHHHHHHHHHC	44.05	7615751
806	Acetylation	RQNEIAKKRLEFENQ HHHHHHHHHHHHHCH	53.87	7615761
946	Phosphorylation	KLPLSKGTMDDISQE CCCCCCCCHHHCHHH	22.59	26160508
951	Phosphorylation	KGTMDDISQEEGSSQ CCCHHHCHHHCCCCC	38.24	26239621
956	Phosphorylation	DISQEEGSSQGEESV HCHHHCCCCCCCCCC	23.83	26239621
957	Phosphorylation	ISQEEGSSQGEESVS CHHHCCCCCCCCCCC	53.73	27087446
962	Phosphorylation	GSSQGEESVSGSQRT CCCCCCCCCCCCCHH	19.79	25159016
964	Phosphorylation	SQGEESVSGSQRTSS CCCCCCCCCCCHHCC	41.84	25159016
966	Phosphorylation	GEESVSGSQRTSSIY CCCCCCCCCHHCCHH	14.69	23429704
969	Phosphorylation	SVSGSQRTSSIYARE CCCCCCHHCCHHHHH	21.13	28833060
970	Phosphorylation	VSGSQRTSSIYAREA CCCCCHHCCHHHHHH	19.54	28833060
971	Phosphorylation	SGSQRTSSIYAREAL CCCCHHCCHHHHHHH	21.00	28833060
973	Phosphorylation	SQRTSSIYAREALIE CCHHCCHHHHHHHHC	11.10	28833060
1015	Phosphorylation	QKLNEQQSVLQRIAA HHHHHHHHHHHHHHC	25.21	29514104
1037	Acetylation	KLESVRDKFQETSDE HHHHHHHHHHHCHHH	38.08	23806337
1222	Ubiquitination	VLTFDLTKYPDANPN EEEEECCCCCCCCCC	63.18	-

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
957	S	Phosphorylation	Kinase	ATM	Q62388	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
957	S	Phosphorylation	-
Phosphorylation of Ser-957 and Ser-966 activates it and is required for S-phase checkpoint activation (By similarity).
966	S	Phosphorylation	-
Phosphorylation of Ser-957 and Ser-966 activates it and is required for S-phase checkpoint activation (By similarity).

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 SMC1A_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MECP2_MOUSE	Mecp2	physical	20159591
ATRX_MOUSE	Atrx	physical	20159591
SMC3_MOUSE	Smc3	physical	21139566
SMC3_MOUSE	Smc3	physical	21699228
RAD21_MOUSE	Rad21	physical	21699228
PDS5B_MOUSE	Pds5b	physical	21699228
WAPL_MOUSE	Wapal	physical	21699228
STAG2_MOUSE	Stag2	physical	21699228
CDCA5_MOUSE	Cdca5	physical	21699228
SMC1B_MOUSE	Smc1b	physical	11564881
GNAS3_HUMAN	GNAS	physical	26496610
GNAS2_HUMAN	GNAS	physical	26496610
ALEX_HUMAN	GNAS	physical	26496610
GNAS1_HUMAN	GNAS	physical	26496610
HELLS_HUMAN	HELLS	physical	26496610
NCBP1_HUMAN	NCBP1	physical	26496610
NDUV3_HUMAN	NDUFV3	physical	26496610
RAD21_HUMAN	RAD21	physical	26496610
S10A4_HUMAN	S100A4	physical	26496610
UBP13_HUMAN	USP13	physical	26496610
SMC3_HUMAN	SMC3	physical	26496610
ABCF2_HUMAN	ABCF2	physical	26496610
TRI38_HUMAN	TRIM38	physical	26496610
STAG2_HUMAN	STAG2	physical	26496610
KLD10_HUMAN	KLHDC10	physical	26496610
PDS5B_HUMAN	PDS5B	physical	26496610
WAPL_HUMAN	WAPAL	physical	26496610
KIF1B_HUMAN	KIF1B	physical	26496610
RT27_HUMAN	MRPS27	physical	26496610
PDS5A_HUMAN	PDS5A	physical	26496610
PATZ1_HUMAN	PATZ1	physical	26496610
RM27_HUMAN	MRPL27	physical	26496610
MRRP1_HUMAN	TRMT10C	physical	26496610
DEFM_HUMAN	PDF	physical	26496610
NBEL1_HUMAN	NBEAL1	physical	26496610
CDCA5_HUMAN	CDCA5	physical	26496610
PGAM5_HUMAN	PGAM5	physical	26496610
K2C73_HUMAN	KRT73	physical	26496610
STAG1_HUMAN	STAG1	physical	26496610

Drug and Disease Associations

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

Regulatory Network of SMC1A_MOUSE

Related Literatures of Post-Translational Modification

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