CDC12_SCHPO - dbPTM
CDC12_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CDC12_SCHPO
UniProt AC Q10059
Protein Name Cell division control protein 12
Gene Name cdc12
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 1841
Subcellular Localization Nucleus . Nuclear, and septum.
Protein Description Plays a role in the cell cycle. Involved in cytokinesis. Component of the cell division ring. In the absence of profilin, caps the barbed end of actin filaments, thus preventing subunit addition and dissociation. In the presence of profilin, nucleates actin filaments that grow rapidly from their barbed ends..
Protein Sequence MRNSSKGQDPNFSYDSILSTPTPSARRTIGPRAPKSKTTYHKPPSSIESVSTLIQPNKSQSVTSPYVKQFTFSSKEYNSHNKHALQNSQLPLPKTPEKSTVHRPKANKVEVTDLPSSSSVEHLHTSKHLKGPRLPKNIIKSSEDVQIAPVTPPVHSRSFDPLPKPPVPSVPVSKTKRRTKHKLAPVVEVPEITNEVSPKFTSTNDEQVYRLRSIRAGSPNSVCSFQFEIPSTRPPSLDQLIHLFNDFLRHPVFDFDENAIEMLQSCTPDEKWCFIRSNFAGFDDPSFQIPELAAVHRPVSWFVIQLWNKTISNLQLITLSSLLSTQSDRWISLFLELQGLRALHNLLTYFNSSAVVQPQQAEVPRCMLTLLKKKPTLVTSNSYIFQAITVTLISPNLLPRKVAADLLTWVLSLKEPLVVSILETGFKEINAEYEKEVPLFFGWIKSFKDIILEKELARTPPSSPARNSASSSPSNIAFLEYCTSTMEFINQLIVACEELEQGFDLDILDSLRESGIHEVIQLLRNFPDQQLEKQLNIYESEEERRTISQTTHEDVDSFMSNESSILSSFNEFASNEVGRLLESTIQNILLAKGTEKQKVKLIKVFNSLLQRILLNSKVSNESFEDSLQASLNMLTERFYSDDTARNALKEAKASRAMAEKMVIERDAMAAQVNLGAEDLIAKLNKEVEDQKDVILSQKRTNETLKTEIDALQKSHVTQIQRSEVELRELYLLINSDSFQGSTNSKERIIEYLLDKLDLRKKEIAAESTLWSNDGIDDKLRDLREQMSRQSSQPSTVSTILQIPDKKFHRPFPRHLHRYVGRSASESLTSEKDESIKSMKGIDDFANLEIPGKGIESNVVIKDISNQTHEINSVENKAETVSNNSKITNFDIPNDATSLPTIITHPTPPPPPPLPVKTSLNTFSHPDSVNIVANDTSVAGVMPAFPPPPPPPPPLVSAAGGKFVSPAVSNNISKDDLHKTTGLTRRPTRRLKQMHWEKLNSGLEFTFWTGPSDEANKILETLHTSGVLDELDESFAMKEAKTLVKKTCARTDYMSSELQKLFGIHFHKLSHKNPNEIIRMILHCDDSMNECVEFLSSDKVLNQPKLKADLEPYRIDWANGGDLVNSEKDASELSRWDYLYVRLIVDLGGYWNQRMNALKVKNIIETNYENLVRQTKLIGRAALELRDSKVFKGLLYLILYLGNYMNDYVRQAKGFAIGSLQRLPLIKNANNTKSLLHILDITIRKHFPQFDNFSPELSTVTEAAKLNIEAIEQECSELIRGCQNLQIDCDSGALSDPTVFHPDDKILSVILPWLMEGTKKMDFLKEHLRTMNTTLNNAMRYFGEQPNDPNSKNLFFKRVDSFIIDYSKARSDNLKSEEEEASQHRRLNLVNNHKEHVLERAMSENNKMDNEAMDGFLDKLRNVKLESHHKPRNRSAITMGKEHLIEAPNTSTKSSPAKNELFVPKRSSVKSDLAKVRPRYPKGSESTDGLSDALNITPTKKGEVSSKAKKGYNYEKRRSGRQVSDSYVLNKNSKNKSNKGRSASYTFSDPSSLEDSNRQKPFNGEKFRRFSSKSRRGSQNRDSKKTGKARKDKGINNNQTSPQNKPSKESLKSDTISNEKKVFPQKASKVNLLTPTISNGTRASKHANEKENTFPRGVENNLVAPMIPNNTELNEDTSAVSRNLENATNDLKETFPTTTTISTARAKPGNNDINTILRRNNSRGRRRMLQQMSPLKSNKFSGTNDLNFQQATKPDGSNKSSYMERLEKLKQNSERHLQSVGGKKVYSSEETPVNKILVSPSVSILDHNRILSQSTPIKSPQRAQEMLAGLLSGKLAPKENEK
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 Orthologous
Protein Cluster
59PhosphorylationTLIQPNKSQSVTSPY
HHCCCCCCCCCCCCC		34.0425720772
61PhosphorylationIQPNKSQSVTSPYVK
CCCCCCCCCCCCCEE		34.1625720772
63PhosphorylationPNKSQSVTSPYVKQF
CCCCCCCCCCCEEEE		29.2725720772
95PhosphorylationSQLPLPKTPEKSTVH
CCCCCCCCCCCCCCC		34.4421712547
197PhosphorylationPEITNEVSPKFTSTN
CCCCCCCCCCCCCCC		19.0524763107
822PhosphorylationLHRYVGRSASESLTS
HHHHHCCCHHHCCCC		30.1625720772
824PhosphorylationRYVGRSASESLTSEK
HHHCCCHHHCCCCCC		29.0325720772
1449PhosphorylationHLIEAPNTSTKSSPA
HHEECCCCCCCCCCC		36.3924763107
1450PhosphorylationLIEAPNTSTKSSPAK
HEECCCCCCCCCCCC		40.2421712547
1451PhosphorylationIEAPNTSTKSSPAKN
EECCCCCCCCCCCCC		32.6721712547
1453PhosphorylationAPNTSTKSSPAKNEL
CCCCCCCCCCCCCCC		41.4624763107
1490PhosphorylationSESTDGLSDALNITP
CCCCCCCCCCCCCCC		26.7729996109
1496PhosphorylationLSDALNITPTKKGEV
CCCCCCCCCCCCCCC		24.6725720772
1498PhosphorylationDALNITPTKKGEVSS
CCCCCCCCCCCCCCC		36.4229996109
1523PhosphorylationRRSGRQVSDSYVLNK
CCCCCCCCCHHCCCC		16.7029996109
1541PhosphorylationNKSNKGRSASYTFSD
CCCCCCCCCEEECCC		30.1828889911
1543PhosphorylationSNKGRSASYTFSDPS
CCCCCCCEEECCCCC		26.4225720772
1544PhosphorylationNKGRSASYTFSDPSS
CCCCCCEEECCCCCC		16.1228889911
1547PhosphorylationRSASYTFSDPSSLED
CCCEEECCCCCCCCC		40.5921712547
1599PhosphorylationKGINNNQTSPQNKPS
CCCCCCCCCCCCCCC		44.4924763107
1600PhosphorylationGINNNQTSPQNKPSK
CCCCCCCCCCCCCCH		18.0921712547
1606PhosphorylationTSPQNKPSKESLKSD
CCCCCCCCHHHHCCC		51.1421712547
1732PhosphorylationRRMLQQMSPLKSNKF
HHHHHHCCCCCCCCC		23.8125720772
1798PhosphorylationPVNKILVSPSVSILD
CCCEEEECCCEEHHC		14.1721712547
1811PhosphorylationLDHNRILSQSTPIKS
HCCCCHHCCCCCCCC		21.5129996109
1813PhosphorylationHNRILSQSTPIKSPQ
CCCHHCCCCCCCCHH		32.5421712547
1814PhosphorylationNRILSQSTPIKSPQR
CCHHCCCCCCCCHHH		22.7729996109
1818PhosphorylationSQSTPIKSPQRAQEM
CCCCCCCCHHHHHHH		27.3021712547
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of CDC12_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CDC12_SCHPO !!
Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CDC12_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CAPZB_SCHPOacp2genetic
15743909
PROF_SCHPOcdc3genetic
9105045
ACT_SCHPOact1genetic
10371213
CDC15_SCHPOcdc15physical
12939254
TPM_SCHPOcdc8physical
9105045
PROF_SCHPOcdc3physical
9105045
CDC15_SCHPOcdc15physical
9105045
MLR4_SCHPOcdc4physical
9105045
CDC15_SCHPOcdc15physical
20603077
FOR3_SCHPOfor3genetic
23185032
ACT_SCHPOact1genetic
24115772
MLR1_SCHPOrlc1genetic
24115772
MYO2_SCHPOmyo2genetic
24115772
MID1_SCHPOmid1genetic
24115772
CDC15_SCHPOcdc15genetic
24115772
FLP1_SCHPOclp1genetic
24115772
BGS1_SCHPObgs1genetic
24115772
CDC12_SCHPOcdc12physical
24115772
FIMB_SCHPOfim1genetic
24115772
ACT_SCHPOact1physical
24115772
FOR3_SCHPOfor3genetic
24127216
CDC15_SCHPOcdc15genetic
24127216
MID1_SCHPOmid1genetic
24127216
RNG2_SCHPOrng2genetic
24127216
MLR4_SCHPOcdc4genetic
24127216
MYO2_SCHPOmyo2genetic
24127216
MLR1_SCHPOrlc1genetic
24127216
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CDC12_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-1541 AND TYR-1544, ANDMASS SPECTROMETRY.

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