IQG1_YEAST - dbPTM
IQG1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IQG1_YEAST
UniProt AC Q12280
Protein Name Ras GTPase-activating-like protein IQG1
Gene Name IQG1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1495
Subcellular Localization Bud neck . Forms a ring at the bud neck in a MLC1-dependent manner, which contracts at the end of cytokinesis.
Protein Description Required for the assembly and the contraction of the actomyosin ring at the bud neck during cytokinesis. Seems to be involved in additional tasks during cell division like axial bud-site selection and targeted secretion by recruiting the spatial landmark BUD4, the septin CDC12 and the secretion landmark SEC3 to the bud neck. May be regulated by calcium ions..
Protein Sequence MTAYSGSPSKPGNNNSYLNRYVENLGTNVTPPLRPQSSSKINSSLNIASPSHLKTKTSASNSSATILSKKVESSVSKLKPSLPNKLVGKYTVDLSNYSKIELRYYEFLCRVSEVKIWIEAVIEEALPSEIELCVGDSLRNGVFLAKLTQRINPDLTTVIFPAGDKLQFKHTQNINAFFGLVEHVGVPDSFRFELQDLYNKKNIPQVFETLHILISMINKKWPGKTPALTNVSGQISFTKEEIAACKKAWPRIRDFKSLGTNINTAPASPEEPKEKRSGLIKDFNKFERPNIPVEEILITPRKNITDANCSDFSNTPSPYNEAPKMSNLDVVVEKRKFTPIEPSLLGPTPSLEYSPIKNKSLSYYSPTISKYLTYDTEFYTRRSRAREEDLNYYQTFKYSPSHYSPMRRERMTEEQFLEKVVQLQNICRGVNTRFNLYIQKRLLNLFEQDILRFQACLRGNKFRVLSSMYLPIRRAKIDVPHVEAIQSRIKGSRIRYKYDKLKFTLSRFSCTVELLQAYCRSKLLKTTVNTKLNDIEISHYPLTKLQSYMRASYVRKKVMSLNTKLNDERESIMKFSAIIRGNVVRCSEDAILSAVHDVHKENISKLQSLIRGIFTRSCLASIIYSLGKENCNIIQLSACIRGNAVRHKVQSLFAPENNLSETVHDLQGLVRGILVRYTLDLVDDIVEYNNLALFQAFSRGALVRESLDQKSSFYKRNVRSVIMIQSWIRKSLQRSAYLELLDCPNPSLWAVKKFVHLLNGTATIEEVQNQLESCQASLDSENMKKERLLKSIRQQLNINGVLDKFGLLKDKDHELGISDSTIPKSKYQKYEKLFYMLQVDPSYWKLLYLKEPEFVAKNVYMTFGTVNQRMNDRERSYFTRFVCEMLQNAINEAPSIESFLDNRSQFWQTILQDFLRRESPEFFSIIVPVLDYLSDPVVDFESDPYKIYQEIHGFSSPQHCSPVDDASTKNKFIDNLRCLWHAIEMVAEIYTRKVHTIPVEIRYLCTKIFCYAADKNIEEIDSLRAISSILVNVFVSEYLVNREYYGYKDSNVQKNNQKIDILMKSLATVFEIKNFDGFLDPLNQYANEIKPHIKDVLYNVLVDPEYEQEGDRLIYLDMVSPSPKLELLTEKVLEISGKFEEYLNEFPEADILHDILEKNLDNSSFPRSGRVTLELDASAYRFLVSDDKMRKIYDQVKRAFVYMMQIEDVDTNLYDLSISTILPQDEPNFANFLEQNPKIRDDPMIQKLKPLKYFTLKNVTLKKIHELESTGTFCSSDNKLQNFLNDIANTIKNPNYAIDYVTQEIYITKETLTKISEMNHSLDIELSRLKKHVDHTIKDFQKAKDFSPVHKSKFGNFKNAVKKVQGRERSELQGMKFKWNTKQLYERGVLKTIRGEKLAELTVKVFGSSGPKFPDIIFKISTSDGSRFGIQMIDKRKGPDKRYSDDVDSFSFKDLIKTQVEPKIETWKLFHSNVVVNNSQLLHLIVSFFYKRNAL
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
5Phosphorylation---MTAYSGSPSKPG
---CCCCCCCCCCCC		30.2627717283
7Phosphorylation-MTAYSGSPSKPGNN
-CCCCCCCCCCCCCC		21.7628889911
9PhosphorylationTAYSGSPSKPGNNNS
CCCCCCCCCCCCCHH		53.8628889911
16PhosphorylationSKPGNNNSYLNRYVE
CCCCCCHHHHHHHHH		32.8730377154
30PhosphorylationENLGTNVTPPLRPQS
HHCCCCCCCCCCCCC		22.6623749301
40UbiquitinationLRPQSSSKINSSLNI
CCCCCCCHHCCCCCC		48.1017644757
43PhosphorylationQSSSKINSSLNIASP
CCCCHHCCCCCCCCH		39.4127017623
44PhosphorylationSSSKINSSLNIASPS
CCCHHCCCCCCCCHH		22.4329688323
49PhosphorylationNSSLNIASPSHLKTK
CCCCCCCCHHHHCCC		24.1225752575
51PhosphorylationSLNIASPSHLKTKTS
CCCCCCHHHHCCCCC		38.6721440633
54UbiquitinationIASPSHLKTKTSASN
CCCHHHHCCCCCCCC		42.4217644757
58PhosphorylationSHLKTKTSASNSSAT
HHHCCCCCCCCCCCH		31.1223749301
62PhosphorylationTKTSASNSSATILSK
CCCCCCCCCCHHHHH		20.8927017623
63PhosphorylationKTSASNSSATILSKK
CCCCCCCCCHHHHHH		33.4127017623
229PhosphorylationPGKTPALTNVSGQIS
CCCCCCCCCCCCCEE		35.3627017623
232PhosphorylationTPALTNVSGQISFTK
CCCCCCCCCCEECCH		27.3527017623
236PhosphorylationTNVSGQISFTKEEIA
CCCCCCEECCHHHHH		20.9827017623
257PhosphorylationPRIRDFKSLGTNINT
HHHHCHHHHCCCCCC		31.8319779198
260PhosphorylationRDFKSLGTNINTAPA
HCHHHHCCCCCCCCC		37.9128889911
264PhosphorylationSLGTNINTAPASPEE
HHCCCCCCCCCCCCC		30.1621440633
268PhosphorylationNINTAPASPEEPKEK
CCCCCCCCCCCCHHH		31.6121551504
281UbiquitinationEKRSGLIKDFNKFER
HHCCCCCCCCCCCCC		62.4017644757
285UbiquitinationGLIKDFNKFERPNIP
CCCCCCCCCCCCCCC		48.9017644757
299PhosphorylationPVEEILITPRKNITD
CHHHEEECCCCCCCC		17.3721440633
302UbiquitinationEILITPRKNITDANC
HEEECCCCCCCCCCC		54.6417644757
310PhosphorylationNITDANCSDFSNTPS
CCCCCCCHHCCCCCC		41.3123749301
313PhosphorylationDANCSDFSNTPSPYN
CCCCHHCCCCCCCCC		44.8023749301
315PhosphorylationNCSDFSNTPSPYNEA
CCHHCCCCCCCCCCC		24.7621440633
317PhosphorylationSDFSNTPSPYNEAPK
HHCCCCCCCCCCCCC		37.6721440633
319PhosphorylationFSNTPSPYNEAPKMS
CCCCCCCCCCCCCCC		29.9419779198
336UbiquitinationDVVVEKRKFTPIEPS
CEEEEECCCCCCCHH		65.7317644757
338PhosphorylationVVEKRKFTPIEPSLL
EEEECCCCCCCHHHC		26.7921440633
343PhosphorylationKFTPIEPSLLGPTPS
CCCCCCHHHCCCCCC		24.3624961812
348PhosphorylationEPSLLGPTPSLEYSP
CHHHCCCCCCCCCCC		24.5827017623
350PhosphorylationSLLGPTPSLEYSPIK
HHCCCCCCCCCCCCC		35.9924603354
353PhosphorylationGPTPSLEYSPIKNKS
CCCCCCCCCCCCCCC		25.6621440633
354PhosphorylationPTPSLEYSPIKNKSL
CCCCCCCCCCCCCCC		15.6921551504
357UbiquitinationSLEYSPIKNKSLSYY
CCCCCCCCCCCCCEE		62.8017644757
364PhosphorylationKNKSLSYYSPTISKY
CCCCCCEECCCHHHH		12.5629734811
365PhosphorylationNKSLSYYSPTISKYL
CCCCCEECCCHHHHC		13.8221551504
367PhosphorylationSLSYYSPTISKYLTY
CCCEECCCHHHHCCC		31.7621440633
371PhosphorylationYSPTISKYLTYDTEF
ECCCHHHHCCCCCHH		9.4828132839
373PhosphorylationPTISKYLTYDTEFYT
CCHHHHCCCCCHHHC		19.0921551504
374PhosphorylationTISKYLTYDTEFYTR
CHHHHCCCCCHHHCC		20.4828132839
379PhosphorylationLTYDTEFYTRRSRAR
CCCCCHHHCCCHHHH		7.9728132839
398PhosphorylationNYYQTFKYSPSHYSP
CHHHHCCCCHHHCCC		22.9429688323
399PhosphorylationYYQTFKYSPSHYSPM
HHHHCCCCHHHCCCC		22.1019779198
401PhosphorylationQTFKYSPSHYSPMRR
HHCCCCHHHCCCCHH		29.1728889911
403PhosphorylationFKYSPSHYSPMRRER
CCCCHHHCCCCHHHC		20.8619779198
404PhosphorylationKYSPSHYSPMRRERM
CCCHHHCCCCHHHCC		13.5428889911
955PhosphorylationYQEIHGFSSPQHCSP
HHHHHCCCCCCCCCC		45.7821440633
1347PhosphorylationFQKAKDFSPVHKSKF
HHHCCCCCCCCHHHC		35.8328889911
1408PhosphorylationLTVKVFGSSGPKFPD
EEEEECCCCCCCCCC		22.2121440633
1409PhosphorylationTVKVFGSSGPKFPDI
EEEECCCCCCCCCCE		60.5421440633
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
-KUbiquitinationE3 ubiquitin ligaseCDH1P53197
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IQG1_YEAST !!
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 IQG1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BUD4_YEASTBUD4physical
12446742
AFR1_YEASTAFR1physical
9679143
AKR1_YEASTAKR1physical
9679143
CDC42_YEASTCDC42physical
9679143
MLC1_YEASTMLC1physical
15210731
CYK3_YEASTCYK3genetic
10959846
MLC1_YEASTMLC1genetic
11082046
SEC3_YEASTSEC3genetic
12446742
MLC1_YEASTMLC1genetic
10873803
CDC15_YEASTCDC15genetic
17005296
DBF2_YEASTDBF2genetic
17005296
DBF20_YEASTDBF20genetic
17005296
BSP1_YEASTBSP1genetic
18430924
BSP1_YEASTBSP1physical
18430924
CALM_YEASTCMD1physical
18675924
MLC1_YEASTMLC1physical
18675924
CDC42_YEASTCDC42physical
18675924
TEM1_YEASTTEM1genetic
17005296
TCO89_YEASTTCO89physical
22328503
KOG1_YEASTKOG1physical
22328503
CYK2_YEASTHOF1genetic
10959846
DMA1_YEASTDMA1genetic
23966170
DMA2_YEASTDMA2genetic
23966170
MLC1_YEASTMLC1physical
24895401
CYK2_YEASTHOF1physical
24895401
CYK3_YEASTCYK3genetic
24895401
MYO1_YEASTMYO1genetic
24895401
CYK3_YEASTCYK3genetic
23878277
RHO1_YEASTRHO1genetic
23878277
RHO2_YEASTRHO2genetic
23878277
RGD2_YEASTRGD2genetic
23878277
CDC24_YEASTCDC24genetic
23878277
KDX1_YEASTKDX1genetic
23878277
NAB6_YEASTNAB6genetic
23878277
TUS1_YEASTTUS1genetic
23878277
RGD1_YEASTRGD1genetic
23878277
CYK2_YEASTHOF1physical
24413167
MLC1_YEASTMLC1physical
24413167
CDC14_YEASTCDC14physical
26085509
SMD1_YEASTSMD1genetic
27708008
SHE1_YEASTSHE1genetic
27708008
DLDH_YEASTLPD1genetic
27708008
OSH6_YEASTOSH6genetic
27708008
RL22A_YEASTRPL22Agenetic
27708008
INO4_YEASTINO4genetic
27708008
DPOA2_YEASTPOL12genetic
27708008
PSB6_YEASTPRE7genetic
27708008
CALM_YEASTCMD1genetic
27708008
TAF5_YEASTTAF5genetic
27708008
DBF4_YEASTDBF4genetic
27708008
ERF3_YEASTSUP35genetic
27708008
GPI19_YEASTGPI19genetic
27708008
RSP5_YEASTRSP5genetic
27708008
COG3_YEASTCOG3genetic
27708008
MOB2_YEASTMOB2genetic
27708008
ACT_YEASTACT1genetic
27708008
MOB1_YEASTMOB1genetic
27708008
NU192_YEASTNUP192genetic
27708008
KTHY_YEASTCDC8genetic
27708008
CDC11_YEASTCDC11genetic
27708008
PRI2_YEASTPRI2genetic
27708008
SEC22_YEASTSEC22genetic
27708008
TAD3_YEASTTAD3genetic
27708008
ROT1_YEASTROT1genetic
27708008
CAP_YEASTSRV2genetic
27708008
PROF_YEASTPFY1genetic
27708008
GPI2_YEASTGPI2genetic
27708008
URA7_YEASTURA7genetic
27708008
RMD9L_YEASTYBR238Cgenetic
27708008
MGR1_YEASTMGR1genetic
27708008
RV161_YEASTRVS161genetic
27708008
RS29B_YEASTRPS29Bgenetic
27708008
CYK3_YEASTCYK3genetic
27708008
GCST_YEASTGCV1genetic
27708008
RV167_YEASTRVS167genetic
27708008
3HAO_YEASTBNA1genetic
27708008
BUD6_YEASTBUD6genetic
27708008
RM39_YEASTMRPL39genetic
27708008
NDI1_YEASTNDI1genetic
27708008
MSC1_YEASTMSC1genetic
27708008
MGR3_YEASTMGR3genetic
27708008
ATG16_YEASTATG16genetic
27708008
MAS5_YEASTYDJ1genetic
27708008
TPM1_YEASTTPM1genetic
27708008
SIN3_YEASTSIN3genetic
27708008
YP066_YEASTRGL1genetic
27708008
YME1_YEASTYME1genetic
27708008
BSP1_YEASTBSP1genetic
27708008
INN1_YEASTINN1physical
26891268
CHS2_YEASTCHS2physical
26891268
CYK3_YEASTCYK3physical
26891268
SWI6_YEASTSWI6genetic
27453043
ACE2_YEASTACE2genetic
27453043
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IQG1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354 AND SER-365, ANDMASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND MASSSPECTROMETRY.

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