IQCE_HUMAN - dbPTM
IQCE_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IQCE_HUMAN
UniProt AC Q6IPM2
Protein Name IQ domain-containing protein E
Gene Name IQCE
Organism Homo sapiens (Human).
Sequence Length 695
Subcellular Localization Cell projection, cilium membrane
Peripheral membrane protein
Cytoplasmic side . The EvC complex localizes at the base of cilia in the EvC zone of primary cilia in a EFCAB7-dependent manner.
Protein Description Component of the EvC complex that positively regulates ciliary Hedgehog (Hh) signaling..
Protein Sequence MFLGTGEPALDTGDDSLSAVTFDSDVETKAKRKAFHKPPPTSPKSPYLSKPRKVASWRSLRTAGSMPLGGRASLTPQKLWLGTAKPGSLTQALNSPLTWEHAWTGVPGGTPDCLTDTFRVKRPHLRRSASNGHVPGTPVYREKEDMYDEIIELKKSLHVQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPSRGTDFVRTLAEKRPDASWVINGLKQRILKLEQQCKEKDGTISKLQTDMKTTNLEEMRIAMETYYEEVHRLQTLLASSETTGKKPLGEKKTGAKRQKKMGSALLSLSRSVQELTEENQSLKEDLDRVLSTSPTISKTQGYVEWSKPRLLRRIVELEKKLSVMESSKSHAAEPVRSHPPACLASSSALHRQPRGDRNKDHERLRGAVRDLKEERTALQEQLLQRDLEVKQLLQAKADLEKELECAREGEEERREREEVLREEIQTLTSKLQELQEMKKEEKEDCPEVPHKAQELPAPTPSSRHCEQDWPPDSSEEGLPRPRSPCSDGRRDAAARVLQAQWKVYKHKKKKAVLDEAAVVLQAAFRGHLTRTKLLASKAHGSEPPSVPGLPDQSSPVPRVPSPIAQATGSPVQEEAIVIIQSALRAHLARARHSATGKRTTTAASTRRRSASATHGDASSPPFLAALPDPSPSGPQALAPLPGDDVNSDDSDDIVIAPSLPTKNFPV
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
5 (in isoform 4)Phosphorylation-40.2825850435
41PhosphorylationAFHKPPPTSPKSPYL
HHCCCCCCCCCCCCC		64.5328348404
42PhosphorylationFHKPPPTSPKSPYLS
HCCCCCCCCCCCCCC		35.7825159151
65PhosphorylationRSLRTAGSMPLGGRA
HHHHCCCCCCCCCCC		18.11-
75PhosphorylationLGGRASLTPQKLWLG
CCCCCCCCCCEEECC		22.6024719451
83PhosphorylationPQKLWLGTAKPGSLT
CCEEECCCCCCCCHH		29.3624719451
117PhosphorylationTPDCLTDTFRVKRPH
CCCCHHHCCCCCCHH		14.2227251275
128PhosphorylationKRPHLRRSASNGHVP
CCHHHHHCCCCCCCC		29.6128450419
130PhosphorylationPHLRRSASNGHVPGT
HHHHHCCCCCCCCCC		44.5926055452
137PhosphorylationSNGHVPGTPVYREKE
CCCCCCCCCCCCCCC		11.9626055452
140PhosphorylationHVPGTPVYREKEDMY
CCCCCCCCCCCCHHH		17.7927080861
143AcetylationGTPVYREKEDMYDEI
CCCCCCCCCHHHHHH		50.4419822219
147PhosphorylationYREKEDMYDEIIELK
CCCCCHHHHHHHHHH		23.81-
155AcetylationDEIIELKKSLHVQKS
HHHHHHHHHHCCCHH		71.5219822227
162PhosphorylationKSLHVQKSDVDLMRT
HHHCCCHHHHHHHHH		26.2720068231
169PhosphorylationSDVDLMRTKLRRLEE
HHHHHHHHHHHHHHH		22.0620068231
179PhosphorylationRRLEEENSRKDRQIE
HHHHHHHHHHHHHHH		43.9426307563
256PhosphorylationRIAMETYYEEVHRLQ
HHHHHHHHHHHHHHH		17.0327642862
264PhosphorylationEEVHRLQTLLASSET
HHHHHHHHHHHCCCC		28.4725850435
268PhosphorylationRLQTLLASSETTGKK
HHHHHHHCCCCCCCC		28.7725850435
269PhosphorylationLQTLLASSETTGKKP
HHHHHHCCCCCCCCC		33.1025850435
271PhosphorylationTLLASSETTGKKPLG
HHHHCCCCCCCCCCC		42.6825850435
272PhosphorylationLLASSETTGKKPLGE
HHHCCCCCCCCCCCC		42.8428302921
292PhosphorylationKRQKKMGSALLSLSR
HHHHHHHHHHHHHHH		16.55-
296PhosphorylationKMGSALLSLSRSVQE
HHHHHHHHHHHHHHH		25.7524719451
298PhosphorylationGSALLSLSRSVQELT
HHHHHHHHHHHHHHH		21.0917081983
300PhosphorylationALLSLSRSVQELTEE
HHHHHHHHHHHHHHH		25.4425850435
312UbiquitinationTEENQSLKEDLDRVL
HHHHHHHHHHHHHHH		55.20-
320PhosphorylationEDLDRVLSTSPTISK
HHHHHHHHCCCCCCC		24.7930266825
321PhosphorylationDLDRVLSTSPTISKT
HHHHHHHCCCCCCCC		34.2730266825
322PhosphorylationLDRVLSTSPTISKTQ
HHHHHHCCCCCCCCC		19.3730266825
324PhosphorylationRVLSTSPTISKTQGY
HHHHCCCCCCCCCCC		37.3430266825
326PhosphorylationLSTSPTISKTQGYVE
HHCCCCCCCCCCCCC		31.9329514088
328PhosphorylationTSPTISKTQGYVEWS
CCCCCCCCCCCCCCC		22.04-
356PhosphorylationKLSVMESSKSHAAEP
HHHHHHHCCCCCCCC		25.5223836654
405PhosphorylationRDLKEERTALQEQLL
HHHHHHHHHHHHHHH		34.6927174698
570PhosphorylationLASKAHGSEPPSVPG
HHHHHCCCCCCCCCC		36.7421712546
574PhosphorylationAHGSEPPSVPGLPDQ
HCCCCCCCCCCCCCC		52.2221712546
582PhosphorylationVPGLPDQSSPVPRVP
CCCCCCCCCCCCCCC		43.9525850435
583PhosphorylationPGLPDQSSPVPRVPS
CCCCCCCCCCCCCCC		25.0425850435
590PhosphorylationSPVPRVPSPIAQATG
CCCCCCCCCHHHHCC		26.5330278072
596PhosphorylationPSPIAQATGSPVQEE
CCCHHHHCCCCCHHH		26.5528450419
598PhosphorylationPIAQATGSPVQEEAI
CHHHHCCCCCHHHHH		19.9728450419
676PhosphorylationLPGDDVNSDDSDDIV
CCCCCCCCCCCCCEE		42.5225921289
679PhosphorylationDDVNSDDSDDIVIAP
CCCCCCCCCCEEECC		42.0225921289
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 IQCE_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IQCE_HUMAN !!
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 IQCE_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CARD9_HUMANCARD9physical
24722188
CEP70_HUMANCEP70physical
24722188
GOGA2_HUMANGOLGA2physical
24722188
HOOK2_HUMANHOOK2physical
24722188
LZTS2_HUMANLZTS2physical
24722188
MTUS2_HUMANMTUS2physical
24722188
RPGR1_HUMANRPGRIP1physical
24722188
SPAG5_HUMANSPAG5physical
24722188
TRI23_HUMANTRIM23physical
24722188
TRI27_HUMANTRIM27physical
24722188
TT23L_HUMANTTC23Lphysical
24722188
PSA3_HUMANPSMA3physical
24722188
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IQCE_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND MASSSPECTROMETRY.

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