SMC1B_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SMC1B_MOUSE
• UniProt AC: Q920F6
• Protein Name: Structural maintenance of chromosomes protein 1B
• Gene Name: Smc1b
• Organism: Mus musculus (Mouse).
• Sequence Length: 1248
• Subcellular Localization: Nucleus . Chromosome . Chromosome, centromere . Associates with chromatin. In prophase I stage of meiosis, localizes along the AE of synaptonemal complexes. In late-pachytene-diplotene, the bulk of protein dissociates from the chromosome arms probabl
• Protein Description: Meiosis-specific component of cohesin complex. Required for the maintenance of meiotic cohesion, but not, or only to a minor extent, for its establishment. Contributes to axial element (AE) formation and the organization of chromatin loops along the AE. Plays a key role in synapsis, recombination and chromosome movements. 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 meiosis-specific cohesin complex probably replaces mitosis specific cohesin complex when it dissociates from chromatin during prophase I..
• Protein Sequence: MGHLELLLVENFKSWRGRQVIGPFKRFTCIIGPNGSGKSNVMDALSFVMGEKTTNLRVKNIQELIHGAHTGKPVSSSASVTIIYIEDSGEEKTFTRIIRGGCSEYHFGDKPVSRSVYVAQLENIGIIVKAQNCLVFQGTVESISMKKPKERTQFFEEISTSGEFIGEYEAKKKKLQKAEEDAQFHFNVKKNVAAERKHAKIEKEEAEHYQNLLEELKINKIQLMLFQLYYNEEKINVLNTELEQMDGNLSVVKDTLSHHENIFKAKKKDYGMLTRQLQQTAKELKSVEAILNQKRPQYIKAKENTSHHLKKLDLSKKLITDNEKQCSKQEDGIRALVAELADLDRAWKSFEKQMEEKILQKGRDIELENSQLDRYKLLKEQVRRKVGIMTQQLEKLQWEQKAEKERLAFEKRRHGDTQGNLKQIKEQIEEHKKRIEKLEEYTKTCMDCLEDKKQQEEALKKEIENTKSRMSEVNEELSLIRNELQNAGIDNHEGKRQQKRAEVLEHLKRLYPDSVFGRLLDLCHPIHKKYQLAVTKLFGRYMVAIVVASEKIAKDCIRFLKAERAEPETFLALDYLDIKPINERLREIKGCKMMIDVIKTQFPQLKKVIQFVCGNGLVCETVEEARHIAFGGPERRKAVALDGTLFLKSGVISGGSSDLKHKALCWDEKELHNLRDKRSQLVQELKELMKTLRKETDLKQIQTLVQGTNTRLKYSQNELEMIKKKHLATFYREQSQLQSELLNIDSQCTMLSEGINKQQQKIEEFQDKIDEVEDDIFQDFCEEIGVENIREFENKHVKQQQENDQKRLEFEKQKTRLNIQLEYSRNQLKKKLNNIDTLKTTIQKGKEDIDNLKKTEEECLKIVEELMVKQEQIKEVLATQSSNIEKIHIQIEEERKKVLAVDREVGKLQKEVVIIQGSLEQKLLEKHNLLLDCKVQDIDISLVLGSLEDIIEMELTETESTQATADIYEKEASIQIDYSPLREDLKALQSDKEVEAHLTLLLQQVASQENTLLKTTAPNLRAQENLKTVRDKFQESADVFEASRKEARICRQEFEQVKRRRYDAFSQCFEHISVSIDQIYKKLCRNNSAQAFLSPENPEEPYLDGISYNCVAPGKRFMPMDNLSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVSSYIKEQSQEQFQMIIISLKEEFYSKADALIGVYPEHNECMFSHVLTLDLSKYPDTEDQEGSRSHRKPRVPRVSMSPKSPQSR

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
286	Phosphorylation	QTAKELKSVEAILNQ HHHHHHHHHHHHHHC	37.50	22942356
315	Phosphorylation	HLKKLDLSKKLITDN HHHHCHHHHHHCCCC	27.66	-
384	Dimethylation	LLKEQVRRKVGIMTQ HHHHHHHHHHCHHHH	38.87	-
384	Methylation	LLKEQVRRKVGIMTQ HHHHHHHHHHCHHHH	38.87	18961039
453	Malonylation	MDCLEDKKQQEEALK HHHHHHHHHHHHHHH	70.32	26320211
460	Malonylation	KQQEEALKKEIENTK HHHHHHHHHHHHHHH	56.24	26320211
648	Acetylation	LDGTLFLKSGVISGG ECCEEEEECCCCCCC	37.52	-
656	Phosphorylation	SGVISGGSSDLKHKA CCCCCCCCCHHHHCC	24.97	24453211
713	Acetylation	QGTNTRLKYSQNELE HCCCHHCEECHHHHH	39.29	-
731	Phosphorylation	KKHLATFYREQSQLQ HHHHHHHHHHHHHHH	14.64	-
812	Ubiquitination	QKRLEFEKQKTRLNI HHHHHHHHHHHHHHH	63.52	-
830	Acetylation	YSRNQLKKKLNNIDT HCHHHHHHHHCCHHH	71.70	7611925
831	Acetylation	SRNQLKKKLNNIDTL CHHHHHHHHCCHHHH	55.66	7611935
1032	Acetylation	NLKTVRDKFQESADV HHHHHHHHHHHHHHH	38.08	-
1036	Phosphorylation	VRDKFQESADVFEAS HHHHHHHHHHHHHHH	20.98	26643407
1045	Acetylation	DVFEASRKEARICRQ HHHHHHHHHHHHHHH	53.91	7923653
1241	Phosphorylation	RVPRVSMSPKSPQSR CCCCCCCCCCCCCCC	22.97	22817900
1244	Phosphorylation	RVSMSPKSPQSR--- CCCCCCCCCCCC---	31.40	19060867
1247	Phosphorylation	MSPKSPQSR------ CCCCCCCCC------	43.26	21183079

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of SMC1B_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SMC1B_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SMC1B_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of SMC1B_MOUSE !!

Drug and Disease Associations

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