PCP1_SCHPO - dbPTM
PCP1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCP1_SCHPO
UniProt AC Q92351
Protein Name Spindle pole body protein pcp1
Gene Name pcp1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 1208
Subcellular Localization Nucleus . Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body .
Protein Description Spindle pole body component that binds calmodulin. Overexpression of pcp1 causes the formation of supernumerary SPB-like structures and disrupts both mitotic spindle assembly and chromosome segregation..
Protein Sequence MSERDFNTQSPKFKDENANSVISQSDFLGKSLKNNNDDYSDFRGSYLNDKSSFQTPLRNGSYQPKGSLEFTPLLQSSNKNSDKYNGSLGDKGSFDPNSYGLSAISKQATQEALSISQGNDSYDVSKLTDLSKNSEIDHTDGELPANAALTLREQEKVLEKVSRENFGLRIKIVCLEKRLESMAPEQIKEAVKDNVELHAERANLQLQLKRTESLLQKSEDKNFKLEEKVDYLSKVNDVEQSQNVKVFTERIRFLENALEKVQREKDSLSTEMEEDKSNKEVDYEYEIRQLQNRLDELSEELDVAQDLLTEKEDEIATLKRQIEEKENSSSAFENEENSSYVHLQEDYAILQAKCDEFADRIQVLTADLEKEKENQIMHESEASIGLTDSMQVHTLQEQLHKANEEIEFLHDQISRMNEEGKNFEDIMLQFRSLEEERDVLESKLQTLEDDNNSLRLMTSSLGNQIESLRTQNREIDEEKNHLRLLASKNSDKALAETNIRLQEVTKELETLRMKNSNDLNEIHDLREENEGLTLKIDSITKEKDRLINELEQRIKSYEVNVSELNGTIDEYRNKLKDKEETYNEVMNAFQYKDNDLRRFHESINKLQDREKELTSNLEKKNLVISSLRETVAMLEKERESIKKYLSGNAKDLDNTNLMEILNDKISVLQRQLTDVKDELDVSEEEREEAIVAGQKLSASFELMSNEKQALELKYSSLKNELINAQNLLDRREEELSELSKKLFEERKIRSGSNDDIEKNKEINVLNSELADKLAQIRHLESDKMELDKLVHHLNRGIEEANIEENAVKKRLCLLMGCDYSSVSILQIVSQIEHFVNQQIQTIRSLKQELRHDFVQFSGKKEQELSRSFEKFGLGTETKHDILAQRNRNVSEKMNDLENAAQKFFSSPDRKNGYLYPSEHTSKIEYLEKTIEDLKLALQDELKNRNLLMDDISSYNKQTTKLQEKIKWLERERSILIDELESYRSNQFNYQNNLVQDKNELEERLKEIQKELEVYNNHFMKQAELMTSNVTDESQLMLKTLREALQSKTNNIDHLSTILERNRKEYKSLLDDYNQLRARYKNLQSNTPQSTQSGQYESEIKGLSKLTKYLQSKCRREHSLRLDLAFSKKFILMQLTGYETCNKINLRMLQKIGISPDPDLSKKHIKLKSLIIVVCSIERMKRMKNEWLKQAQLKQSLQRAAAKAKTANY
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
2Phosphorylation------MSERDFNTQ
------CCCCCCCCC		53.2821712547
10PhosphorylationERDFNTQSPKFKDEN
CCCCCCCCCCCCCCC		28.1924763107
20PhosphorylationFKDENANSVISQSDF
CCCCCCCHHCCHHHH		20.5824763107
23PhosphorylationENANSVISQSDFLGK
CCCCHHCCHHHHHCH		22.8324763107
25PhosphorylationANSVISQSDFLGKSL
CCHHCCHHHHHCHHC		24.4421712547
39PhosphorylationLKNNNDDYSDFRGSY
CCCCCCCHHHCCCHH		17.0121712547
40PhosphorylationKNNNDDYSDFRGSYL
CCCCCCHHHCCCHHC		36.9524763107
67PhosphorylationGSYQPKGSLEFTPLL
CCCCCCCCEECHHCC		30.7424763107
71PhosphorylationPKGSLEFTPLLQSSN
CCCCEECHHCCCCCC		12.0324763107
76PhosphorylationEFTPLLQSSNKNSDK
ECHHCCCCCCCCCCC		35.5324763107
93PhosphorylationGSLGDKGSFDPNSYG
CCCCCCCCCCCCCCC		32.0121712547
105PhosphorylationSYGLSAISKQATQEA
CCCCHHHHHHHHHHH		20.5921712547
131PhosphorylationVSKLTDLSKNSEIDH
HHHHCCCCCCCCCCC		32.3824763107
134PhosphorylationLTDLSKNSEIDHTDG
HCCCCCCCCCCCCCC		39.4024763107
139PhosphorylationKNSEIDHTDGELPAN
CCCCCCCCCCCCCCH		41.7824763107
211PhosphorylationLQLQLKRTESLLQKS
HHHHHHHHHHHHHHC		28.4824763107
414PhosphorylationEFLHDQISRMNEEGK
HHHHHHHHHHCCCCC		21.6125720772
453PhosphorylationTLEDDNNSLRLMTSS
HHHCCCCHHHHHHHH		22.5625720772
682PhosphorylationVKDELDVSEEEREEA
CCCCCCCCHHHHHHH		38.6721712547
750PhosphorylationFEERKIRSGSNDDIE
HHHHCCCCCCCCHHH		50.4721712547
752PhosphorylationERKIRSGSNDDIEKN
HHCCCCCCCCHHHHC		38.0321712547
865PhosphorylationGKKEQELSRSFEKFG
CCHHHHHHHHHHHHC		25.7324763107
867PhosphorylationKEQELSRSFEKFGLG
HHHHHHHHHHHHCCC		34.0924763107
905PhosphorylationNAAQKFFSSPDRKNG
HHHHHHHCCCCCCCC		44.0624763107
906PhosphorylationAAQKFFSSPDRKNGY
HHHHHHCCCCCCCCC		26.1828889911
1135PhosphorylationKFILMQLTGYETCNK
CCHHHHHHCHHHHHH		22.3321712547
1139PhosphorylationMQLTGYETCNKINLR
HHHHCHHHHHHHCHH		16.9421712547
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 PCP1_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCP1_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 PCP1_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CCQ1_SCHPOccq1genetic
15546621
PPC89_SCHPOppc89physical
16775007
CALM_SCHPOcam1physical
15004232
CCQ1_SCHPOccq1physical
15546621
CUT12_SCHPOcut12genetic
19942852
WEE1_SCHPOwee1genetic
19942852
WEE1_SCHPOwee1genetic
21233285
CUT12_SCHPOcut12physical
22438582
ALP7_SCHPOalp7physical
24937146
KMS1_SCHPOkms1genetic
24963130
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PCP1_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-906, AND MASSSPECTROMETRY.

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