MID2_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MID2_SCHPO
• UniProt AC: Q9P7Y8
• Protein Name: Septin ring organizing protein mid2
• Gene Name: mid2
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 706
• Subcellular Localization: Cytoplasm, cell cortex . Cytoplasm, cytoskeleton . Localizes to the medial ring at the cell cortex of dividing cells (PubMed:12654901). Initially forms a single ring, which subsequently splits into two distinct rings as the septum forms, and disappea
• Protein Description: Responsible for the proper stability and function of septins during cytokinesis. Required for the correct formation of the medial septin ring structure in mitosis and for the proper localization of endo-glucanases agn1 and eng1, which are needed for efficient cell separation. May act as a landmark for the localization of hydrolytic proteins to the medial region..
• Protein Sequence: MLMTASQQDQHAKMYLADIHRALRIPSPIPSTDYECSDYASTIASISRESTMRNFNRSNISSTAPSFAESEDAEDGDSFPYDQTLSNSSSFDDHQSLLPFSTEVRRTPTYSVMNETDSSSTSVEDVNKENILSLNDSCLIKLSDDEASNKSSRSSTPRNSIKSNSSNQGHGDIPIPKKNPARSVCNSKLFNEDTLPAEFEEVSISPPVKLELPTHSHNSSDTSFTNSIVSSVSDMVGLGEGINSIASFGFSEDSSSFQDIKTPPRLSFADENRENCRTDIYRSDSIHEYEEPLTSSITSLDSPHVLDENAPIPLLPKVVSLPDPRFTNVLSAFDALTRTYLLRQNSKVVHATSQKQEMQTSRRVVNSCYMPESLSRNLSSSLQQTGGSGRLFVRLMEIRNLTIPLASGMTTRFTYTISGKHIQVPWNALHSTTKIENEYTFDESISSSIVCTLRAAYDPPKVRTRSTLGKVFSTNKRKSMTTDPVSEALHGFVSEDGTFGEVTINTDSVSRTALGRCQSMVLPIMNKWTVDPAAKDVKPLPRKVGELEIHVFFLPALPVSLKELPASIESAMYDLKLAEWDRTLLCDGYLCQQGGDCPYWRRRYFQLIGSKLVAFQQFSKVRRATIDLSEATHIVDDNHYSDEEELEGYLYFESGFRIIFSNGDYIDFYAETVGEKDEWMSTLRQHLGQCSMVHKNWTKSFLSLSF

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
163	Phosphorylation	TPRNSIKSNSSNQGH CCCHHCCCCCCCCCC	40.03	24763107
165	Phosphorylation	RNSIKSNSSNQGHGD CHHCCCCCCCCCCCC	37.44	21712547
166	Phosphorylation	NSIKSNSSNQGHGDI HHCCCCCCCCCCCCC	37.11	24763107
183	Phosphorylation	PKKNPARSVCNSKLF CCCCCCHHHHCCCCC	32.88	27738172
283	Phosphorylation	CRTDIYRSDSIHEYE HCCCHHCCCCCCCCC	20.81	29996109
285	Phosphorylation	TDIYRSDSIHEYEEP CCHHCCCCCCCCCCC	27.39	29996109
367	Phosphorylation	TSRRVVNSCYMPESL HHHHHHHHHCCCHHH	8.60	29996109
373	Phosphorylation	NSCYMPESLSRNLSS HHHCCCHHHHHHHHH	26.27	29996109
375	Phosphorylation	CYMPESLSRNLSSSL HCCCHHHHHHHHHHH	28.53	29996109
379	Phosphorylation	ESLSRNLSSSLQQTG HHHHHHHHHHHHHHC	22.79	28889911
473	Phosphorylation	STLGKVFSTNKRKSM HHHCCHHCCCCCCCC	33.77	27738172

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

Oops, there are no upstream regulatory protein records of MID2_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MID2_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 MID2_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SDS23_SCHPO	sds23	genetic	22681890
ILVB_SCHPO	ilv1	genetic	22681890
YGWH_SCHPO	gmh4	genetic	22681890
MU113_SCHPO	mug113	genetic	22681890
YAOF_SCHPO	SPAC11D3.15	genetic	22681890
YEEB_SCHPO	SPAC19A8.11c	genetic	22681890
YOI9_SCHPO	SPBC1778.09	genetic	22681890
YBW4_SCHPO	SPBC651.04	genetic	22681890
SPT20_SCHPO	spt20	physical	25015293
SPN2_SCHPO	spn2	physical	25015293

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379, AND MASSSPECTROMETRY.
PubMed: 18257517