BIR1_SCHPO - dbPTM
BIR1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BIR1_SCHPO
UniProt AC O14064
Protein Name Protein bir1
Gene Name bir1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 997
Subcellular Localization Nucleus. Cytoplasm, cytoskeleton, spindle. Chromosome, centromere. Interacts with the outer centromeric regions of the chromosomes during interphase. After chromatid separation moves to the middle of the spindle.
Protein Description Seems to act in the pleiotropic control of cell division. Has a role in chromosome segregation by recruiting condensin and ark1 kinase to appropriate sites as the cell progresses through mitosis. Ark1 activity depends upon bir1 function and phosphorylation. Ark1 with bir1 function is required for full-scale association with kinetochores and formation of a complex with mad3..
Protein Sequence MKPITSSSKRRWNRFRREMCNYSKRLDTFQKKKWPRAKPTPETLATVGFYYNPISESNSEERLDNVTCYMCTKSFYDWEDDDDPLKEHITHSPSCPWAYILSSKNNPNQNPQAAALTKCREQTFVDKVWPYTNRPDYHCEPSVMAASGFVYNPTADAKDAAHCLYCDINLHDWEPDDDPYTEHKRRRADCVFFTWKDPNSLSPTKLSFLSTSNIDPEDLTEDNSILPVSPTRDSTKSHKTLNFSPSRKNNLNARPLTMSLYTNTSEEKDSQPTRAPQSPTKPVLLTAPRRKNKSPKKSKPAVFKPVKPIFSDEDEDDDDLTASQPFSKGICNDSMQVAKKNFTEEIPLKEDEKDNELEHLVSPATSVHTTVSDITGHQSVTDESDEQNNCMSTPPKIEIESKIEEEISVVSKSKEISSSVSSVGKEQNHTEKQVAIETPEQQKVEKEDEHLNLQGSFIEESTKQPISSKPSTSSPDMTDAATGGRVSSSSFRDKILQTNFSPRSTIDSFSNISKKRNSEEANDENDETNLKIPIPEKKRKFQEVLQSKNILVSSTEDSHEPVKVTEDSQTAIHVSKFEDLENKSMESEQSLQLLSESENDDKPLIDLIPLLAIKRKDNLVSGVLEKGKSTSTSKTKFDTSIVDFIEKPKTEISEVLPEEKRKAICDESQTVRVSIDRGVTKTRDVSSPVSDEKSENVNHEEANSGHTVMNVHSSLDPQPIVQPNELESGSYLKDLPDRNVGNSEKVTFQEDDINSPKLQSKNNQTVEAVNTETSDKLQEKEANHELENIEKIEEKLTEVDKVSLSDAFPDQEIKNSRTSVQNGTRSVSKNTPEKETKVDKIDNVSKKDVETSPGSCETSSAFAKTYAEKEVTSINLPSVRKPLDESYYDHSISPFDPLCQSSFLAPQTPVKSKHALPLVEANAPPWEPIDFSSLLESPVPNPVEPNKLSEKELDMTVEQWIKFMYAKCAKEFEEACEEKIEWLLEEGKRAEEYIQNL
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
202PhosphorylationWKDPNSLSPTKLSFL
ECCCCCCCCCEEEEE
30.2827738172
220PhosphorylationNIDPEDLTEDNSILP
CCCHHHCCCCCCEEE
54.3221712547
224PhosphorylationEDLTEDNSILPVSPT
HHCCCCCCEEECCCC
37.5129996109
229PhosphorylationDNSILPVSPTRDSTK
CCCEEECCCCCCCCC
20.7221712547
231PhosphorylationSILPVSPTRDSTKSH
CEEECCCCCCCCCCC
39.3329996109
244PhosphorylationSHKTLNFSPSRKNNL
CCCCCCCCCCCCCCC
22.3824763107
270PhosphorylationNTSEEKDSQPTRAPQ
CCCCCCCCCCCCCCC
49.4821712547
278PhosphorylationQPTRAPQSPTKPVLL
CCCCCCCCCCCCEEE
33.2124763107
280PhosphorylationTRAPQSPTKPVLLTA
CCCCCCCCCCEEEEC
53.9121712547
311PhosphorylationKPVKPIFSDEDEDDD
CCCCCCCCCCCCCCC
40.5924763107
384PhosphorylationHQSVTDESDEQNNCM
CCCCCCCCCCCCCCC
49.6227738172
438PhosphorylationEKQVAIETPEQQKVE
CEEEEECCHHHHHCH
26.4729996109
456PhosphorylationEHLNLQGSFIEESTK
HHCCCCHHHHHCCCC
15.3024763107
467PhosphorylationESTKQPISSKPSTSS
CCCCCCCCCCCCCCC
38.7121712547
473PhosphorylationISSKPSTSSPDMTDA
CCCCCCCCCCCCCCC
44.1829996109
474PhosphorylationSSKPSTSSPDMTDAA
CCCCCCCCCCCCCCC
25.6329996109
482PhosphorylationPDMTDAATGGRVSSS
CCCCCCCCCCCCCCH
41.7221712547
487PhosphorylationAATGGRVSSSSFRDK
CCCCCCCCCHHHHHH
24.1224763107
488PhosphorylationATGGRVSSSSFRDKI
CCCCCCCCHHHHHHH
27.4324763107
489PhosphorylationTGGRVSSSSFRDKIL
CCCCCCCHHHHHHHH
26.4521712547
490PhosphorylationGGRVSSSSFRDKILQ
CCCCCCHHHHHHHHC
26.6721712547
498PhosphorylationFRDKILQTNFSPRST
HHHHHHCCCCCCCHH
34.4829996109
501PhosphorylationKILQTNFSPRSTIDS
HHHCCCCCCCHHHHH
22.8228889911
504PhosphorylationQTNFSPRSTIDSFSN
CCCCCCCHHHHHCCC
32.8521712547
505PhosphorylationTNFSPRSTIDSFSNI
CCCCCCHHHHHCCCH
30.0421712547
508PhosphorylationSPRSTIDSFSNISKK
CCCHHHHHCCCHHHH
27.0721712547
518PhosphorylationNISKKRNSEEANDEN
CHHHHCCCHHCCCCC
40.6324763107
565PhosphorylationSHEPVKVTEDSQTAI
CCCCEEECCCCCEEE
28.4929996109
568PhosphorylationPVKVTEDSQTAIHVS
CEEECCCCCEEEEHH
24.1724763107
570PhosphorylationKVTEDSQTAIHVSKF
EECCCCCEEEEHHHH
31.3729996109
590PhosphorylationKSMESEQSLQLLSES
CCCCCHHHHHHHHHC
17.6529996109
595PhosphorylationEQSLQLLSESENDDK
HHHHHHHHHCCCCCC
47.9024763107
682PhosphorylationIDRGVTKTRDVSSPV
EECCCCCCCCCCCCC
23.8029996109
686PhosphorylationVTKTRDVSSPVSDEK
CCCCCCCCCCCCCCC
32.9621712547
687PhosphorylationTKTRDVSSPVSDEKS
CCCCCCCCCCCCCCC
29.2124763107
690PhosphorylationRDVSSPVSDEKSENV
CCCCCCCCCCCCCCC
43.3621712547
755PhosphorylationFQEDDINSPKLQSKN
ECCCCCCCHHHHCCC
24.6028889911
760PhosphorylationINSPKLQSKNNQTVE
CCCHHHHCCCCCEEE
48.0329996109
771PhosphorylationQTVEAVNTETSDKLQ
CEEEEECHHHHHHHH
33.7621712547
803PhosphorylationLTEVDKVSLSDAFPD
HHHCCCCCHHHHCCC
28.0924763107
805PhosphorylationEVDKVSLSDAFPDQE
HCCCCCHHHHCCCHH
21.2729996109
818PhosphorylationQEIKNSRTSVQNGTR
HHHHCCCHHHHCCCC
32.8224763107
831PhosphorylationTRSVSKNTPEKETKV
CCCCCCCCCCCCCCC
36.2427738172
851PhosphorylationVSKKDVETSPGSCET
CCHHHCCCCCCCCHH
39.8229996109
852PhosphorylationSKKDVETSPGSCETS
CHHHCCCCCCCCHHH
17.4828889911
908PhosphorylationSSFLAPQTPVKSKHA
CCCCCCCCCCCCCCC
29.0529996109
932PhosphorylationPWEPIDFSSLLESPV
CCCCCCHHHHHCCCC
19.1429996109
933PhosphorylationWEPIDFSSLLESPVP
CCCCCHHHHHCCCCC
36.6529996109
937PhosphorylationDFSSLLESPVPNPVE
CHHHHHCCCCCCCCC
31.0329996109

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 BIR1_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BIR1_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 BIR1_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PIC1_SCHPOpic1genetic
16199877
PSF2_SCHPOpsf2genetic
16199877
PSF2_SCHPOpsf2physical
16199877
SGO2_SCHPOsgo2physical
17301288
ARK1_SCHPOark1physical
17301288
ARK1_SCHPOark1physical
17322402
SGO2_SCHPOsgo2physical
17322402
SGO2_SCHPOsgo2physical
20739936
ARK1_SCHPOark1genetic
11950927

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BIR1_SCHPO

loading...

Related Literatures of Post-Translational Modification

TOP