HYCCI_HUMAN - dbPTM
HYCCI_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HYCCI_HUMAN
UniProt AC Q9BYI3
Protein Name Hyccin {ECO:0000303|PubMed:16951682}
Gene Name FAM126A
Organism Homo sapiens (Human).
Sequence Length 521
Subcellular Localization Cytoplasm, cytosol . Cell membrane . Localizes to the cytosol and is recruited to the plasma membrane following interaction with other components of the phosphatidylinositol 4-kinase (PI4K) complex.
Protein Description Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. [PubMed: 26571211 The complex acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis]
Protein Sequence MFTSEKGVVEEWLSEFKTLPETSLPNYATNLKDKSSLVSSLYKVIQEPQSELLEPVCHQLFEFYRSGEEQLLQFTLQFLPELIWCYLAVSASRNVHSSGCIEALLLGVYNLEIVDKQGHTKVLSFTIPSLSKPSVYHEPSSIGSMALTESALSQHGLSKVVYSGPHPQREMLTAQNRFEVLTFLLLCYNAALTYMPSVSLQSLCQICSRICVCGYPRQHVRKYKGISSRIPVSSGFMVQMLTGIYFAFYNGEWDLAQKALDDIIYRAQLELYPEPLLVANAIKASLPHGPMKSNKEGTRCIQVEITPTSSRISRNAVTSMSIRGHRWKRHGNTELTGQEELMEISEVDEGFYSRAASSTSQSGLSNSSHNCSNKPSIGKNHRRSGGSKTGGKEKETTGESCKDHFARKQTQRAQSENLELLSLKRLTLTTSQSLPKPSSHGLAKTAATVFSKSFEQVSGVTVPHNPSSAVGCGAGTDANRFSACSLQEEKLIYVSERTELPMKHQSGQQRPPSISITLSTD
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
3Phosphorylation-----MFTSEKGVVE
-----CCCCCCCHHH		34.38-
4Phosphorylation----MFTSEKGVVEE
----CCCCCCCHHHH		26.50-
14PhosphorylationGVVEEWLSEFKTLPE
CHHHHHHHHHCCCCC		41.9029759185
17UbiquitinationEEWLSEFKTLPETSL
HHHHHHHCCCCCCCC		45.1329967540
18PhosphorylationEWLSEFKTLPETSLP
HHHHHHCCCCCCCCC		53.5226657352
22PhosphorylationEFKTLPETSLPNYAT
HHCCCCCCCCCCCCC		33.3626657352
23PhosphorylationFKTLPETSLPNYATN
HCCCCCCCCCCCCCC		39.9225159151
29PhosphorylationTSLPNYATNLKDKSS
CCCCCCCCCCCCHHH		30.6226657352
32UbiquitinationPNYATNLKDKSSLVS
CCCCCCCCCHHHHHH		66.2427667366
34UbiquitinationYATNLKDKSSLVSSL
CCCCCCCHHHHHHHH		40.1229967540
188PhosphorylationLTFLLLCYNAALTYM
HHHHHHHHHHHHHCC		14.0619690332
193PhosphorylationLCYNAALTYMPSVSL
HHHHHHHHCCCCCCH		17.0419690332
208PhosphorylationQSLCQICSRICVCGY
HHHHHHHHHHHHCCC		26.7219690332
283UbiquitinationLLVANAIKASLPHGP
HHHHHHHHHHCCCCC		29.52-
292MethylationSLPHGPMKSNKEGTR
HCCCCCCCCCCCCCE		54.75-
306PhosphorylationRCIQVEITPTSSRIS
EEEEEEEECCCCCCC		13.6521712546
308PhosphorylationIQVEITPTSSRISRN
EEEEEECCCCCCCCC		30.5921815630
309PhosphorylationQVEITPTSSRISRNA
EEEEECCCCCCCCCE		20.8723403867
310PhosphorylationVEITPTSSRISRNAV
EEEECCCCCCCCCEE		35.7923403867
313PhosphorylationTPTSSRISRNAVTSM
ECCCCCCCCCEEEEE		20.55-
318PhosphorylationRISRNAVTSMSIRGH
CCCCCEEEEEEECCC		19.1221712546
319 (in isoform 3)Phosphorylation-12.1625159151
319PhosphorylationISRNAVTSMSIRGHR
CCCCEEEEEEECCCC		12.1629255136
319PhosphorylationISRNAVTSMSIRGHR
CCCCEEEEEEECCCC		12.1625627689
321 (in isoform 3)Phosphorylation-14.6525159151
321PhosphorylationRNAVTSMSIRGHRWK
CCEEEEEEECCCCHH		14.6525627689
321PhosphorylationRNAVTSMSIRGHRWK
CCEEEEEEECCCCHH		14.6523401153
323MethylationAVTSMSIRGHRWKRH
EEEEEEECCCCHHCC		27.79-
352PhosphorylationSEVDEGFYSRAASST
HHCCCCHHHHCCCCC		14.2227642862
357PhosphorylationGFYSRAASSTSQSGL
CHHHHCCCCCCCCCC		32.9128111955
358PhosphorylationFYSRAASSTSQSGLS
HHHHCCCCCCCCCCC		27.6128111955
359PhosphorylationYSRAASSTSQSGLSN
HHHCCCCCCCCCCCC		28.4328111955
360PhosphorylationSRAASSTSQSGLSNS
HHCCCCCCCCCCCCC		25.0528111955
362PhosphorylationAASSTSQSGLSNSSH
CCCCCCCCCCCCCCC		41.2828111955
365PhosphorylationSTSQSGLSNSSHNCS
CCCCCCCCCCCCCCC		37.8925159151
367PhosphorylationSQSGLSNSSHNCSNK
CCCCCCCCCCCCCCC		29.6025159151
368PhosphorylationQSGLSNSSHNCSNKP
CCCCCCCCCCCCCCC		23.9925159151
372PhosphorylationSNSSHNCSNKPSIGK
CCCCCCCCCCCCCCC		53.8823401153
374UbiquitinationSSHNCSNKPSIGKNH
CCCCCCCCCCCCCCC		24.6929967540
376PhosphorylationHNCSNKPSIGKNHRR
CCCCCCCCCCCCCCC		45.6523401153
384PhosphorylationIGKNHRRSGGSKTGG
CCCCCCCCCCCCCCC		47.68-
387PhosphorylationNHRRSGGSKTGGKEK
CCCCCCCCCCCCCCC		30.48-
396PhosphorylationTGGKEKETTGESCKD
CCCCCCCCCCCHHHH		51.6925002506
397PhosphorylationGGKEKETTGESCKDH
CCCCCCCCCCHHHHH		39.7925002506
400PhosphorylationEKETTGESCKDHFAR
CCCCCCCHHHHHHHH		28.0125002506
402UbiquitinationETTGESCKDHFARKQ
CCCCCHHHHHHHHHH		64.61-
410PhosphorylationDHFARKQTQRAQSEN
HHHHHHHHHHHHHHC		24.0626074081
413 (in isoform 3)Phosphorylation-13.8725850435
413PhosphorylationARKQTQRAQSENLEL
HHHHHHHHHHHCCHH		13.8725627689
413PhosphorylationARKQTQRAQSENLEL
HHHHHHHHHHHCCHH		13.8725627689
415PhosphorylationKQTQRAQSENLELLS
HHHHHHHHHCCHHHE		27.7129255136
422PhosphorylationSENLELLSLKRLTLT
HHCCHHHEEEEEECC		44.4628348404
424UbiquitinationNLELLSLKRLTLTTS
CCHHHEEEEEECCCC		41.8229967540
424MethylationNLELLSLKRLTLTTS
CCHHHEEEEEECCCC		41.82-
427PhosphorylationLLSLKRLTLTTSQSL
HHEEEEEECCCCCCC		26.5423090842
429PhosphorylationSLKRLTLTTSQSLPK
EEEEEECCCCCCCCC		21.1130108239
430PhosphorylationLKRLTLTTSQSLPKP
EEEEECCCCCCCCCC		28.0728152594
431PhosphorylationKRLTLTTSQSLPKPS
EEEECCCCCCCCCCC		16.7323401153
433PhosphorylationLTLTTSQSLPKPSSH
EECCCCCCCCCCCCC		46.5425159151
438PhosphorylationSQSLPKPSSHGLAKT
CCCCCCCCCCCCHHH		40.8828152594
439PhosphorylationQSLPKPSSHGLAKTA
CCCCCCCCCCCHHHH		30.0628152594
445PhosphorylationSSHGLAKTAATVFSK
CCCCCHHHHHHHHHH		18.8724719451
448PhosphorylationGLAKTAATVFSKSFE
CCHHHHHHHHHHCHH		21.4423401153
451PhosphorylationKTAATVFSKSFEQVS
HHHHHHHHHCHHHCC		24.0523401153
452UbiquitinationTAATVFSKSFEQVSG
HHHHHHHHCHHHCCC		47.9329967540
453PhosphorylationAATVFSKSFEQVSGV
HHHHHHHCHHHCCCC		32.5823401153
458PhosphorylationSKSFEQVSGVTVPHN
HHCHHHCCCCCCCCC		27.5229255136
461PhosphorylationFEQVSGVTVPHNPSS
HHHCCCCCCCCCCCC		31.6729255136
467PhosphorylationVTVPHNPSSAVGCGA
CCCCCCCCCCCCCCC		35.9323927012
468PhosphorylationTVPHNPSSAVGCGAG
CCCCCCCCCCCCCCC		28.3823927012
476PhosphorylationAVGCGAGTDANRFSA
CCCCCCCCCCCCCCC		31.2523312004
482PhosphorylationGTDANRFSACSLQEE
CCCCCCCCCCCCCCC		25.7329449344
485PhosphorylationANRFSACSLQEEKLI
CCCCCCCCCCCCEEE		32.5723401153
490UbiquitinationACSLQEEKLIYVSER
CCCCCCCEEEEEEEC		39.1629967540
493PhosphorylationLQEEKLIYVSERTEL
CCCCEEEEEEECCCC		14.3626356563
503UbiquitinationERTELPMKHQSGQQR
ECCCCCCCCCCCCCC		36.23-
506PhosphorylationELPMKHQSGQQRPPS
CCCCCCCCCCCCCCC		37.9828555341
513PhosphorylationSGQQRPPSISITLST
CCCCCCCCEEEEEEC		31.4825627689
515PhosphorylationQQRPPSISITLSTD-
CCCCCCEEEEEECC-		17.5425056879
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 HYCCI_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HYCCI_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 HYCCI_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VTDB_HUMANGCphysical
28514442
RPGR_HUMANRPGRphysical
28514442
SHPK_HUMANSHPKphysical
28514442
COT2_HUMANNR2F2physical
28514442
Drug and Disease Associations
Kegg Disease
H00679 Hypomyelinating leukodystrophy (HLD); Pelizaeus-Merzbacher disease (PMD)
OMIM Disease
610532Leukodystrophy, hypomyelinating, 5 (HLD5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HYCCI_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-306, AND MASSSPECTROMETRY.

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