HCFC2_HUMAN - dbPTM
HCFC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HCFC2_HUMAN
UniProt AC Q9Y5Z7
Protein Name Host cell factor 2
Gene Name HCFC2
Organism Homo sapiens (Human).
Sequence Length 792
Subcellular Localization Cytoplasm . Nucleus .
Protein Description
Protein Sequence MAAPSLLNWRRVSSFTGPVPRARHGHRAVAIRELMIIFGGGNEGIADELHVYNTATNQWFLPAVRGDIPPGCAAHGFVCDGTRILVFGGMVEYGRYSNELYELQASRWLWKKVKPHPPPSGLPPCPRLGHSFSLYGNKCYLFGGLANESEDSNNNVPRYLNDFYELELQHGSGVVGWSIPVTKGVVPSPRESHTAVIYCKKDSGSPKMYVFGGMCGARLDDLWQLDLETMSWSKPETKGTVPLPRSLHTASVIGNKMYIFGGWVPHKGENTETSPHDCEWRCTSSFSYLNLDTTEWTTLVSDSQEDKKNSRPRPRAGHCAVAIGTRLYFWSGRDGYKKALNSQVCCKDLWYLDTEKPPAPSQVQLIKATTNSFHVKWDEVSTVEGYLLQLSTDLPYQAASSDSSAAPNMQGVRMDPHRQGSNNIVPNSINDTINSTKTEQPATKETSMKNKPDFKALTDSNAILYPSLASNASNHNSHVVDMLRKNEGPHTSANVGVLSSCLDVRTVIPETSVSSTVSSTQTMVTQQTIKTESSSTNGAVVKDETSLTTFSTKSEVDETYALPATKISRVETHATATPFSKETPSNPVATVKAGERQWCDVGIFKNNTALVSQFYLLPKGKQSISKVGNADVPDYSLLKKQDLVPGTGYRFRVAAINGCGIGPFSKISEFKTCIPGFPGAPSAVRISKNVEGIHLSWEPPTSPSGNILEYSAYLAIRTAQIQDNPSQLVFMRIYCGLKTSCIVTAGQLANAHIDYTSRPAIVFRISAKNEKGYGPATQVRWLQGNNKKAPLN
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
13PhosphorylationLLNWRRVSSFTGPVP
CCCCEEECCCCCCCC		20.2330266825
14PhosphorylationLNWRRVSSFTGPVPR
CCCEEECCCCCCCCC		24.7830266825
16PhosphorylationWRRVSSFTGPVPRAR
CEEECCCCCCCCCCC		42.3930266825
159PhosphorylationSNNNVPRYLNDFYEL
CCCCCCCHHHHHHEE		12.0917053785
207AcetylationKKDSGSPKMYVFGGM
ECCCCCCCEEEECCC		44.5619816957
209PhosphorylationDSGSPKMYVFGGMCG
CCCCCCEEEECCCCC		9.9622817900
237PhosphorylationMSWSKPETKGTVPLP
CCCCCCCCCCCCCCC		43.21-
240PhosphorylationSKPETKGTVPLPRSL
CCCCCCCCCCCCCCC		22.1020068231
246PhosphorylationGTVPLPRSLHTASVI
CCCCCCCCCEEEEEE		23.6720068231
249PhosphorylationPLPRSLHTASVIGNK
CCCCCCEEEEEECCE		26.3920068231
251PhosphorylationPRSLHTASVIGNKMY
CCCCEEEEEECCEEE		18.5420068231
338UbiquitinationSGRDGYKKALNSQVC
ECCHHHHHHHHCCEE		50.01-
338UbiquitinationSGRDGYKKALNSQVC
ECCHHHHHHHHCCEE		50.01-
347UbiquitinationLNSQVCCKDLWYLDT
HHCCEECEECEEECC		51.2129967540
347UbiquitinationLNSQVCCKDLWYLDT
HHCCEECEECEEECC		51.21-
356UbiquitinationLWYLDTEKPPAPSQV
CEEECCCCCCCCCCE		59.3929967540
444UbiquitinationKTEQPATKETSMKNK
CCCCCCCCHHCCCCC		62.19-
444AcetylationKTEQPATKETSMKNK
CCCCCCCCHHCCCCC		62.1926051181
446PhosphorylationEQPATKETSMKNKPD
CCCCCCHHCCCCCCC		35.3629449344
447PhosphorylationQPATKETSMKNKPDF
CCCCCHHCCCCCCCH		28.9329449344
465PhosphorylationTDSNAILYPSLASNA
CCCCCCCCHHHCCCC		5.6727642862
514O-linked_GlycosylationVIPETSVSSTVSSTQ
CCCCCCCCCCCCCCC		21.7631492838
553SumoylationSLTTFSTKSEVDETY
CCEEEECCCCCCCCE		43.3428112733
554PhosphorylationLTTFSTKSEVDETYA
CEEEECCCCCCCCEE		42.8321945579
559PhosphorylationTKSEVDETYALPATK
CCCCCCCCEECCCCE		15.0521945579
560PhosphorylationKSEVDETYALPATKI
CCCCCCCEECCCCEE		12.2321945579
565PhosphorylationETYALPATKISRVET
CCEECCCCEEEEEEE		27.2821945579
581AcetylationATATPFSKETPSNPV
CCCCCCCCCCCCCCE		67.0226051181
623PhosphorylationLLPKGKQSISKVGNA
EECCCCCCCHHCCCC		32.1128258704
625PhosphorylationPKGKQSISKVGNADV
CCCCCCCHHCCCCCC		26.9128258704
635PhosphorylationGNADVPDYSLLKKQD
CCCCCCCHHHCCCCC		8.6424719451
636PhosphorylationNADVPDYSLLKKQDL
CCCCCCHHHCCCCCC		34.3124719451
639AcetylationVPDYSLLKKQDLVPG
CCCHHHCCCCCCCCC		54.4026051181
647PhosphorylationKQDLVPGTGYRFRVA
CCCCCCCCCCCEEEE		25.6028634298
649PhosphorylationDLVPGTGYRFRVAAI
CCCCCCCCCEEEEEE		13.3528634298
771AcetylationRISAKNEKGYGPATQ
EEECCCCCCCCCHHH		67.82-
771UbiquitinationRISAKNEKGYGPATQ
EEECCCCCCCCCHHH		67.82-
788AcetylationWLQGNNKKAPLN---
EECCCCCCCCCC---		58.3120167786
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 HCFC2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HCFC2_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 HCFC2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MEN1_HUMANMEN1physical
15199122
KMT2A_HUMANKMT2Aphysical
15199122
RBBP5_HUMANRBBP5physical
15199122
WDR5_HUMANWDR5physical
15199122
KMT2B_HUMANKMT2Bphysical
28514442
KMT2A_HUMANKMT2Aphysical
28514442
CXXC1_HUMANCXXC1physical
28514442
SET1A_HUMANSETD1Aphysical
28514442
DIDO1_HUMANDIDO1physical
28514442
BD1L1_HUMANBOD1L1physical
28514442
ASH2L_HUMANASH2Lphysical
28514442
TCPB_HUMANCCT2physical
28514442
TCPW_HUMANCCT6Bphysical
28514442
RBBP5_HUMANRBBP5physical
28514442
TCPH_HUMANCCT7physical
28514442
HCFC1_HUMANHCFC1physical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
TCPZ_HUMANCCT6Aphysical
28514442
TCPA_HUMANTCP1physical
28514442
TCPE_HUMANCCT5physical
28514442
HSP7C_HUMANHSPA8physical
28514442
NUDC3_HUMANNUDCD3physical
28514442
TCPD_HUMANCCT4physical
28514442
TCPG_HUMANCCT3physical
28514442
TBB8_HUMANTUBB8physical
28514442
OGT1_HUMANOGTphysical
28514442
K0232_HUMANKIAA0232physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HCFC2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-159, AND MASSSPECTROMETRY.

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