CAP_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CAP_SCHPO
• UniProt AC: P36621
• Protein Name: Adenylyl cyclase-associated protein
• Gene Name: cap1
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 551
• Protein Description: The N-terminal domain binds to adenylyl cyclase, thereby enabling adenylyl cyclase to be activated by upstream regulatory signals, such as Ras. The C-terminal domain is required for normal cellular morphology and growth control..
• Protein Sequence: MSDMINIRETGYNFTTILKRLEAATSRLEDLVESGHKPLPNMHRPSRDSNSQTHNISFNIGTPTAPTVSTGSPAVASLHDQVAAAISPRNRSLTSTSAVEAVPASISAYDEFCSKYLSKYMELSKKIGGLIAEQSEHVEKAFNLLRQVLSVALKAQKPDMDSPELLEFLKPIQSELLTITNIRDEHRTAPEFNQLSTVMSGISILGWVTVEPTPLSFMSEMKDSSQFYANRVMKEFKGKDDLQIEWVRSYLTLLTELITYVKTHFKTGLTWSTKQDAVPLKTALANLSASKTQAPSSGDSANGGLPPPPPPPPPSNDFWKDSNEPAPADNKGDMGAVFAEINKGEGITSGLRKVDKSEMTHKNPNLRKTGPTPGPKPKIKSSAPSKPAETAPVKPPRIELENTKWFVENQVDNHSIVLDSVELNHSVQIFGCSNCTIIIKGKLNTVSMSNCKRTSVVVDTLVAAFDIAKCSNFGCQVMNHVPMIVIDQCDGGSIYLSKSSLSSEVVTSKSTSLNINVPNEEGDYAERAVPEQIKHKVNEKGELVSEIVRHE

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
46	Phosphorylation	LPNMHRPSRDSNSQT CCCCCCCCCCCCCCC	48.99	29996109
62	Phosphorylation	NISFNIGTPTAPTVS EEEEEECCCCCCCCC	17.42	29996109
72	Phosphorylation	APTVSTGSPAVASLH CCCCCCCCCCHHHHH	15.13	29996109
77	Phosphorylation	TGSPAVASLHDQVAA CCCCCHHHHHHHHHH	21.46	29996109
87	Phosphorylation	DQVAAAISPRNRSLT HHHHHHHCCCCCCCC	17.06	29996109
92	Phosphorylation	AISPRNRSLTSTSAV HHCCCCCCCCCCCHH	39.28	28889911
94	Phosphorylation	SPRNRSLTSTSAVEA CCCCCCCCCCCHHHH	31.07	25720772
95	Phosphorylation	PRNRSLTSTSAVEAV CCCCCCCCCCHHHHC	26.17	25720772
96	Phosphorylation	RNRSLTSTSAVEAVP CCCCCCCCCHHHHCC	18.57	28889911
97	Phosphorylation	NRSLTSTSAVEAVPA CCCCCCCCHHHHCCC	30.04	29996109
272	Phosphorylation	FKTGLTWSTKQDAVP CCCCCCCCCCCCCCC	22.08	21712547
300	Phosphorylation	QAPSSGDSANGGLPP CCCCCCCCCCCCCCC	27.45	28889911

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CAP_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 CAP_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CYAA_SCHPO	cyr1	physical	1550959
CAP_SCHPO	cap1	physical	26542710
ACT_SCHPO	act1	physical	26542710
COFI_SCHPO	adf1	physical	26542710
RL5B_SCHPO	rpl502	physical	26542710
CSH3_SCHPO	SPBC119.05c	physical	26542710
CSH3_SCHPO	SPBC119.05c	genetic	26542710

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-92 AND THR-96, AND MASSSPECTROMETRY.
PubMed: 18257517