CND2_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CND2_SCHPO
• UniProt AC: Q9Y7R3
• Protein Name: Condensin complex subunit 2
• Gene Name: cnd2
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 742
• Subcellular Localization: Nucleus . Cytoplasm . Chromosome . In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chro
• Protein Description: Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. The condensin complex probably also plays a role during interphase in processes such as DNA repair..
• Protein Sequence: MKRASLGGHAPVSLPSLNDDALEKKRAKENSRKQRELRRSSALHSITPRRESLNNSSPFNSSHQVPVLSNFEEWIKLATDNKINSTNTWNFALIDYFHDMSLLRDGEDINFQKASCTLDGCVKIYTSRIDSVATETGKLLSGLANDSKVLQQTEEGEDAENDDEDLQKKKERKRAQRSVKTLVKDFESIRAKKFELECSFDPLFKKMCADFDEDGAKGLLMNHLCVDQHGRIVFDSSDTVIKDLENKDVEAESQEAVVAAPIESHDTEMTNVHDNISRETLNGIYKCYFTDIDQLTICPSLQGFEFDSKGNLDVSLLKSLSDEVNMITTTSLVDNTMEKTDADAASLSSDSDGEEGHIVHALEEMAYDEENPYVDVVPKAMDESENPDFGVDTEVNMADGSTMNENYSIISTAAANGVYEYFDKSMKKNWAGPEHWRIQALRKNINNASTVFNSSNTAESSDNVSRSLSSTERKKRRELDNAIDFLQEVDVEALFTPATSSLKLPKSHWKRHNRCLLPDDYQYDSKRLLQLFLKPKMSVLPNADGEGQLQLNKALDDENDLDGIQPHGFDSDGSDNVDEGIPPYGFGDSDSPKQTPLLTPPSSSGFGDNLLLTARLAKPDMLNYAKRAKKVDVRVLKEKLWKCLDLENTIKENSINSHIEGSEMESEETNMPVKSFFSTVNQLEETYEKKELKDISTSFAFICVLHLANEHNLELTSNEDFSDVFIRPGPNLTTLEALENDV

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
5	Phosphorylation	---MKRASLGGHAPV ---CCCCCCCCCCCC	31.42	24763107
13	Phosphorylation	LGGHAPVSLPSLNDD CCCCCCCCCCCCCHH	33.24	29996109
40	Phosphorylation	KQRELRRSSALHSIT HHHHHHHHHHHHHCC	17.33	29996109
41	Phosphorylation	QRELRRSSALHSITP HHHHHHHHHHHHCCC	32.79	29996109
45	Phosphorylation	RRSSALHSITPRRES HHHHHHHHCCCCHHH	29.07	29996109
47	Phosphorylation	SSALHSITPRRESLN HHHHHHCCCCHHHCC	17.48	29996109
52	Phosphorylation	SITPRRESLNNSSPF HCCCCHHHCCCCCCC	34.29	29996109
62	Phosphorylation	NSSPFNSSHQVPVLS CCCCCCCCCCCCCCC	21.02	29996109
253	Phosphorylation	NKDVEAESQEAVVAA CCCCCHHHHHEEEEC	40.13	29996109
264	Phosphorylation	VVAAPIESHDTEMTN EEECCCCCCCCCCCC	27.64	29996109
571	Phosphorylation	IQPHGFDSDGSDNVD CCCCCCCCCCCCCCC	41.43	21712547
574	Phosphorylation	HGFDSDGSDNVDEGI CCCCCCCCCCCCCCC	30.88	21712547
589	Phosphorylation	PPYGFGDSDSPKQTP CCCCCCCCCCCCCCC	40.13	21712547

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

Oops, there are no upstream regulatory protein records of CND2_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CND2_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 CND2_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CDS1_SCHPO	cds1	genetic	12000964
SMC4_SCHPO	cut3	physical	21633354
SMC4_SCHPO	cut3	physical	26257282
SMC2_SCHPO	cut14	physical	26257282
CND1_SCHPO	cnd1	physical	26257282
CND3_SCHPO	cnd3	physical	26257282
TBP_SCHPO	tbp1	physical	26257282
SFC1_SCHPO	sfc1	physical	26257282
SFC3_SCHPO	sfc3	physical	26257282
SFC4_SCHPO	sfc4	physical	26257282
SFC6_SCHPO	sfc6	physical	26257282
SFC7_SCHPO	sfc7	physical	26257282
SFC9_SCHPO	sfc9	physical	26257282
TF3B_SCHPO	brf1	physical	26257282
SMC2_SCHPO	cut14	genetic	25764183
SMC4_SCHPO	cut3	genetic	25764183

Drug and Disease Associations

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