VIP1_SCHPO - dbPTM
VIP1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VIP1_SCHPO
UniProt AC O74429
Protein Name Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase
Gene Name asp1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 920
Subcellular Localization Cytoplasm . Nucleus . Cytoplasm, cytoskeleton .
Protein Description Bifunctional inositol kinase that acts in concert with the IP6K kinases to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. Phosphorylates inositol hexakisphosphate (InsP6) at positions 1 or 3 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively, phosphorylates at position 1 or 3 PP-InsP5, produced by IP6Ks from InsP6, to produce (PP)2-InsP4 (By similarity). Required for maintaining cellular integrity, normal growth and interactions with the ARP complex. [PubMed: 10388810 Acts as a regulator of the PHO80-PHO85 cyclin/cyclin-dependent kinase (CDK) complex, thereby regulating signaling of phosphate availability (By similarity Required for the function of the cortical actin cytoskeleton, possibly by participating in correct F-actin localization and ensuring polarized growth]
Protein Sequence MIQNASHLTSIDTESSTRTASPVSSIVTPTKRNVVGICAMDAKARSKPCRNILNRIIAEGEFEAIVFGDNMILDEAVENWPACDYLICFYSSGFPLKKAEKYVELRKPFCVNDVVFQELLWDRRLVLNILDAIRVSTPQRLICSRDGGPKINKVLEEKLRRKFGIEITEVPTPEVKMLDEDTLSVDGKIIKKPYVEKPVYGEDHNIYIYFPKSVGGGGRKLFRKVANKSSDYDPDLCAPRTEGSFIYEEFMNVDNAEDVKVYTVGPHYSHAETRKSPVVDGIVRRNPHGKEIRFITNLSEEEKNMASKISIAFEQPVCGFDLLRVSGQSYVIDVNGWSFVKDNNDYYDNAARILKQMFHVAERHRRNRVPSVQEVLNPPPRESEAWRLKSLVGVLRHADRTPKQKFKFSFTSDPFVKLLQGHTEEVILRNEQLNSVLAATNLATELKCEDINKLKQLRLALETKKDLPGTKVQLKPAYSPEGKLLKLQLIIKWGGEFTHSARYQSKDLGEQFHKDLYIMNRDCLKDVEIYTSSERRVSASAEIFAMAFLEQETIPSDLLKVRKDLLDDSNAAKDTMDKVKKHLKSLLRVGDTARKEFTWPENMPKPCEVMQQVVQLMKYHRAVMRENFIILGPEVEQVQSRWCCNENPALFRERWEKLFSEFCDSEKADPSKVSELYDTLKYDALHNRQFLERIFTPYQYLKLPQSPSLIAKEPPQRTDSNGNLVGMTGANTNHTERPLEKLYELYDLAKVLFDFVSPQEYGIEPKEKLEIGLLTSVPLLRQIIHDIKEARDSDHASTRMYFTKESHIYTLLNCILESGLPMKLPRNQIPELDYLTQICFELFERTNPSGNKEFSVRITLSPGCYAQCPLDMNLDAKHCISVSPRRSLTRHLDLQQFITKTEDLCNSVHLPKRFIPVNIN
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
9PhosphorylationIQNASHLTSIDTESS
CCCCCCCCCCCCCCC		20.4321712547
13PhosphorylationSHLTSIDTESSTRTA
CCCCCCCCCCCCCCC		35.7821712547
15PhosphorylationLTSIDTESSTRTASP
CCCCCCCCCCCCCCC		38.8229996109
16PhosphorylationTSIDTESSTRTASPV
CCCCCCCCCCCCCCC		18.7121712547
17PhosphorylationSIDTESSTRTASPVS
CCCCCCCCCCCCCCH		41.1221712547
19PhosphorylationDTESSTRTASPVSSI
CCCCCCCCCCCCHHC		31.4128889911
21PhosphorylationESSTRTASPVSSIVT
CCCCCCCCCCHHCCC		25.8128889911
24PhosphorylationTRTASPVSSIVTPTK
CCCCCCCHHCCCCCC		20.1025720772
25PhosphorylationRTASPVSSIVTPTKR
CCCCCCHHCCCCCCC		22.7025720772
371PhosphorylationHRRNRVPSVQEVLNP
HHHCCCCCHHHHHCC		33.3125720772
674PhosphorylationKADPSKVSELYDTLK
CCCHHHHHHHHHHHH		26.1421712547
679PhosphorylationKVSELYDTLKYDALH
HHHHHHHHHHHHHHH		16.1621712547
706PhosphorylationQYLKLPQSPSLIAKE
HHCCCCCCCHHHCCC		17.9528889911
708PhosphorylationLKLPQSPSLIAKEPP
CCCCCCCHHHCCCCC		37.3429996109
718PhosphorylationAKEPPQRTDSNGNLV
CCCCCCCCCCCCCEE		38.2321712547
720PhosphorylationEPPQRTDSNGNLVGM
CCCCCCCCCCCEEEC		46.1328889911
728PhosphorylationNGNLVGMTGANTNHT
CCCEEECCCCCCCCC		27.4929996109
735PhosphorylationTGANTNHTERPLEKL
CCCCCCCCCCHHHHH		35.4421712547
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 VIP1_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VIP1_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 VIP1_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
H2AZ_SCHPOpht1genetic
19547744
UBP3_SCHPOubp3genetic
19547744
MAL3_SCHPOmal3genetic
20624911
TEA2_SCHPOtea2genetic
20624911
TEA1_SCHPOtea1genetic
20624911
ARP3_SCHPOarp3genetic
20624911
STU1_SCHPOpeg1genetic
20624911
SPM1_SCHPOpmk1genetic
20624911
HOG1_SCHPOsty1genetic
20624911
INN1_SCHPOfic1genetic
23093943
SPN1_SCHPOspn1genetic
23093943
VPS24_SCHPOvps24genetic
23093943
MPH1L_SCHPOmph1genetic
27697865
MAD2_SCHPOmad2genetic
27697865
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VIP1_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 THR-19; SER-21; SER-706 ANDSER-720, AND MASS SPECTROMETRY.

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