SMC1_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SMC1_SCHPO
• UniProt AC: O94383
• Protein Name: Structural maintenance of chromosomes protein 1
• Gene Name: psm1
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 1228
• Subcellular Localization: Nucleus . Chromosome . Associates with chromatin. Before prophase it is scattered along chromosome arms. At anaphase, the rad21 subunit of the cohesin complex is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosom
• Protein Description: Involved in chromosome cohesion during cell cycle and in DNA repair. 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..
• Protein Sequence: MGRLLRLEVENFKSYRGHQIIGPFEDFTSIIGPNGAGKSNLMDAISFVLGVKSSHLRSTNVKELIYRGKILQRDNTDFTDSSNPTTAYVKLMYELDNGEQREYKRAITPSGATEYKIDEEIVTFSEYCGSLQKENILVRARNFLVFQGDVETIASQSPLELSKLVEQISGSLEYKSEYDKSKDEQDKAVNLSAHSFNKKRGINAELRQYQEQKTEAERYQSQKEKRDSAQLVYLLWKLFHLEKSISSNMAEVTRLKADSIQLIERRDENTKEIEKLKEKEGSIRRNLLAFDRKVRKQEKLIASKRPELISIAEKALESKSNLRKIQRKAAEIEKDYSDQASTLQVLENQLTSLSAAEKEFLKDMQEKEQLKGLRLLPEDKEEYEGLRSEADKLNSNLLFKLQTLNRNIKVTSQSKDSLTSIVGDLESKIKSLHESVSSLDTERADLLAKINEKIESLELEKHDQQKKRLTYSELFHKTQELNEELQSCLQKILEASADRNESKQDAKKREALYALKRIYPEVKGRIIDLCTPTQKKYESAIAAALGKNFDAIVVETQAVAKECIDYIKEQRIGIMTFFPMDTIAASPVNQKFRGTHKGARLAIDVLNFESEYERVMISAVGNTLICDSMTVARDLSYNKRLNAKTVTLEGTVIHKTGLITGGSSNNRSAKHWDDHDFDLLTQTKDRLMHQIGEIEYQKSSCVITESDTVKLHSLESEISLLKDKYTVVSRSVEDKKKEIGHYESLIKEKQPHLSELEMELRNFVKSRDELQIQVEKVEEKIFSGFCKRIGISDIHTYDEIHRTFTQSFTQKQLEFTKQKSLLENRISFEKQRVSDTRLRLERMHKFIEKDQESIDNYEQNREALESEVATAEAELELLKEDFASENSKTEKILLAASEKKLVGKRLVSELTKLSGNITLLESEIDRYVSEWHAILRKCKLEDIDVPLREGSLTSIPIDDVSNSGDITMGEEPSEPVINFEKFGVEVDYDELDEELRNDGSESMASVLQEKLREYSEELDQMSPNLRAIERLETVETRLAKLDEEFAAARKAAKNAKERFNAVKQKRLQKFQAAFSHISEQIDPIYKELTKSPAFPLGGTAYLTLDDLDEPYLGGIKFHAMPPMKRFRDMDQLSGGEKTMAALALLFAIHSYQPSPFFVLDEIDAALDQTNVTKIANYIRQHASSGFQFVVISLKNQLFSKSEALVGIYRDQQENSSRTLSINLEGYVE

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
76	Phosphorylation	KILQRDNTDFTDSSN CCEECCCCCCCCCCC	36.46	25720772
79	Phosphorylation	QRDNTDFTDSSNPTT ECCCCCCCCCCCCCC	37.47	25720772
85	Phosphorylation	FTDSSNPTTAYVKLM CCCCCCCCCEEEEEE	28.45	25720772
1022	Phosphorylation	SEELDQMSPNLRAIE HHHHHHCCCCHHHHH	12.66	29996109

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

Oops, there are no upstream regulatory protein records of SMC1_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SMC1_SCHPO !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of SMC1_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CUT1_SCHPO	cut1	genetic	15507118
ALP14_SCHPO	alp14	genetic	15507118
SMC3_SCHPO	psm3	physical	12773391
RAD21_SCHPO	rad21	genetic	15507118

Drug and Disease Associations

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