PHC2_HUMAN - dbPTM
PHC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHC2_HUMAN
UniProt AC Q8IXK0
Protein Name Polyhomeotic-like protein 2
Gene Name PHC2
Organism Homo sapiens (Human).
Sequence Length 858
Subcellular Localization Nucleus .
Protein Description Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility..
Protein Sequence MENELPVPHTSSSACATSSTSGASSSSGCNNSSSGGSGRPTGPQISVYSGIPDRQTVQVIQQALHRQPSTAAQYLQQMYAAQQQHLMLQTAALQQQHLSSAQLQSLAAVQQASLVSNRQGSTSGSNVSAQAPAQSSSINLAASPAAAQLLNRAQSVNSAAASGIAQQAVLLGNTSSPALTASQAQMYLRAQMLIFTPTATVATVQPELGTGSPARPPTPAQVQNLTLRTQQTPAAAASGPTPTQPVLPSLALKPTPGGSQPLPTPAQSRNTAQASPAGAKPGIADSVMEPHKKGDGNSSVPGSMEGRAGLSRTVPAVAAHPLIAPAYAQLQPHQLLPQPSSKHLQPQFVIQQQPQPQQQQPPPQQSRPVLQAEPHPQLASVSPSVALQPSSEAHAMPLGPVTPALPLQCPTANLHKPGGSQQCHPPTPDTGPQNGHPEGVPHTPQRRFQHTSAVILQLQPASPPQQCVPDDWKEVAPGEKSVPETRSGPSPHQQAIVTAMPGGLPVPTSPNIQPSPAHETGQGIVHALTDLSSPGMTSGNGNSASSIAGTAPQNGENKPPQAIVKPQILTHVIEGFVIQEGAEPFPVGRSSLLVGNLKKKYAQGFLPEKLPQQDHTTTTDSEMEEPYLQESKEEGAPLKLKCELCGRVDFAYKFKRSKRFCSMACAKRYNVGCTKRVGLFHSDRSKLQKAGAATHNRRRASKASLPPLTKDTKKQPTGTVPLSVTAALQLTHSQEDSSRCSDNSSYEEPLSPISASSSTSRRRQGQRDLELPDMHMRDLVGMGHHFLPSEPTKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLKDS
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
97 (in isoform 3)Ubiquitination-24.2821906983
97 (in isoform 2)Ubiquitination-24.2821906983
155PhosphorylationQLLNRAQSVNSAAAS
HHHHHHHHHHHHHHH		23.4522210691
158PhosphorylationNRAQSVNSAAASGIA
HHHHHHHHHHHHCHH		19.6822210691
174PhosphorylationQAVLLGNTSSPALTA
HHHHHCCCCCCCCCH		28.8720068231
180PhosphorylationNTSSPALTASQAQMY
CCCCCCCCHHHHHHH		26.7722210691
226PhosphorylationPAQVQNLTLRTQQTP
HHHHCEEEEEECCCC		23.0324719451
258 (in isoform 3)Ubiquitination-25.0621906983
258 (in isoform 2)Ubiquitination-25.0621906983
271PhosphorylationTPAQSRNTAQASPAG
CCCCCCCCCCCCCCC		21.0225002506
275PhosphorylationSRNTAQASPAGAKPG
CCCCCCCCCCCCCCC		11.8222617229
286PhosphorylationAKPGIADSVMEPHKK
CCCCCCCCCCCCCCC		17.8425002506
295 (in isoform 2)Ubiquitination-63.08-
298PhosphorylationHKKGDGNSSVPGSME
CCCCCCCCCCCCCCC		37.9430631047
303PhosphorylationGNSSVPGSMEGRAGL
CCCCCCCCCCCCCCC		13.9524425749
311PhosphorylationMEGRAGLSRTVPAVA
CCCCCCCCCCCCHHH		25.6130631047
462 (in isoform 5)Phosphorylation-43.7428188228
590PhosphorylationEPFPVGRSSLLVGNL
CCCCCCCCCEEHHHH		21.2930266825
591PhosphorylationPFPVGRSSLLVGNLK
CCCCCCCCEEHHHHH		25.1030266825
598SumoylationSLLVGNLKKKYAQGF
CEEHHHHHHHHHCCC		51.7428112733
5982-HydroxyisobutyrylationSLLVGNLKKKYAQGF
CEEHHHHHHHHHCCC		51.74-
600SumoylationLVGNLKKKYAQGFLP
EHHHHHHHHHCCCCC		44.2028112733
601PhosphorylationVGNLKKKYAQGFLPE
HHHHHHHHHCCCCCC		17.0323403867
603 (in isoform 4)Ubiquitination-39.8321906983
616PhosphorylationKLPQQDHTTTTDSEM
CCCCCCCCCCCCHHH		33.8430266825
617PhosphorylationLPQQDHTTTTDSEME
CCCCCCCCCCCHHHC		25.0330266825
618PhosphorylationPQQDHTTTTDSEMEE
CCCCCCCCCCHHHCC		29.7530266825
619PhosphorylationQQDHTTTTDSEMEEP
CCCCCCCCCHHHCCC		35.1223927012
621PhosphorylationDHTTTTDSEMEEPYL
CCCCCCCHHHCCCHH		36.4330266825
627PhosphorylationDSEMEEPYLQESKEE
CHHHCCCHHHHCHHC		25.0530266825
631PhosphorylationEEPYLQESKEEGAPL
CCCHHHHCHHCCCCC		32.1923403867
632UbiquitinationEPYLQESKEEGAPLK
CCHHHHCHHCCCCCE		60.0621906983
632SumoylationEPYLQESKEEGAPLK
CCHHHHCHHCCCCCE		60.0628112733
633 (in isoform 1)Ubiquitination-71.5821906983
641SumoylationEGAPLKLKCELCGRV
CCCCCEEEEEECCCC		24.87-
641SumoylationEGAPLKLKCELCGRV
CCCCCEEEEEECCCC		24.87-
653AcetylationGRVDFAYKFKRSKRF
CCCEEEECCCCHHCC		40.7723236377
655UbiquitinationVDFAYKFKRSKRFCS
CEEEECCCCHHCCCH		52.16-
662PhosphorylationKRSKRFCSMACAKRY
CCHHCCCHHHHHHHH		13.5028857561
667AcetylationFCSMACAKRYNVGCT
CCHHHHHHHHCCCCC		56.1325953088
667UbiquitinationFCSMACAKRYNVGCT
CCHHHHHHHHCCCCC		56.13-
669PhosphorylationSMACAKRYNVGCTKR
HHHHHHHHCCCCCCC		17.3129759185
6752-HydroxyisobutyrylationRYNVGCTKRVGLFHS
HHCCCCCCCEECCCC		49.52-
675AcetylationRYNVGCTKRVGLFHS
HHCCCCCCCEECCCC		49.5230591265
682PhosphorylationKRVGLFHSDRSKLQK
CCEECCCCCHHHHHH		27.6425159151
685PhosphorylationGLFHSDRSKLQKAGA
ECCCCCHHHHHHHCH		42.5828555341
701PhosphorylationTHNRRRASKASLPPL
HHHHHHHHHCCCCCC		27.2626055452
702SumoylationHNRRRASKASLPPLT
HHHHHHHHCCCCCCC		40.8028112733
704PhosphorylationRRRASKASLPPLTKD
HHHHHHCCCCCCCCC		45.1825159151
709PhosphorylationKASLPPLTKDTKKQP
HCCCCCCCCCCCCCC		32.4220873877
710UbiquitinationASLPPLTKDTKKQPT
CCCCCCCCCCCCCCC		71.70-
712PhosphorylationLPPLTKDTKKQPTGT
CCCCCCCCCCCCCCC		41.5220068231
717PhosphorylationKDTKKQPTGTVPLSV
CCCCCCCCCCCCEEH		42.8829978859
719PhosphorylationTKKQPTGTVPLSVTA
CCCCCCCCCCEEHHE		22.7929978859
723PhosphorylationPTGTVPLSVTAALQL
CCCCCCEEHHEHHHH		16.0226657352
725PhosphorylationGTVPLSVTAALQLTH
CCCCEEHHEHHHHHC		11.6629978859
731PhosphorylationVTAALQLTHSQEDSS
HHEHHHHHCCCCCHH		13.4028450419
733PhosphorylationAALQLTHSQEDSSRC
EHHHHHCCCCCHHCC		29.9917525332
737PhosphorylationLTHSQEDSSRCSDNS
HHCCCCCHHCCCCCC		20.9428450419
738PhosphorylationTHSQEDSSRCSDNSS
HCCCCCHHCCCCCCC		50.0228450419
741PhosphorylationQEDSSRCSDNSSYEE
CCCHHCCCCCCCCCC		38.4229396449
744PhosphorylationSSRCSDNSSYEEPLS
HHCCCCCCCCCCCCC		39.0129396449
745PhosphorylationSRCSDNSSYEEPLSP
HCCCCCCCCCCCCCC		42.7028102081
746PhosphorylationRCSDNSSYEEPLSPI
CCCCCCCCCCCCCCC		24.9230108239
751PhosphorylationSSYEEPLSPISASSS
CCCCCCCCCCCCCHH		30.7928102081
754PhosphorylationEEPLSPISASSSTSR
CCCCCCCCCCHHHHH		26.0330108239
756PhosphorylationPLSPISASSSTSRRR
CCCCCCCCHHHHHHH		20.3130108239
757PhosphorylationLSPISASSSTSRRRQ
CCCCCCCHHHHHHHH		37.0330108239
758PhosphorylationSPISASSSTSRRRQG
CCCCCCHHHHHHHHC		28.1030108239
759PhosphorylationPISASSSTSRRRQGQ
CCCCCHHHHHHHHCC		28.3529978859
760PhosphorylationISASSSTSRRRQGQR
CCCCHHHHHHHHCCC		26.2420068231
764 (in isoform 4)Ubiquitination-51.0321906983
793UbiquitinationFLPSEPTKWNVEDVY
CCCCCCCCCCHHHHH		47.702190698
794 (in isoform 1)Ubiquitination-19.3121906983
801 (in isoform 5)Phosphorylation-34.1527642862
841SumoylationLMSAMNIKLGPALKI
HHHHHCCCHHHHHHH		42.24-
841SumoylationLMSAMNIKLGPALKI
HHHHHCCCHHHHHHH		42.24-
847SumoylationIKLGPALKIYARISM
CCHHHHHHHHHHHHH		35.4628112733
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 PHC2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHC2_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 PHC2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FHL3_HUMANFHL3physical
16189514
PHC2_HUMANPHC2physical
16189514
LMO3_HUMANLMO3physical
16189514
MCRS1_HUMANMCRS1physical
16189514
SMBT1_HUMANSFMBT1physical
16189514
MAPK2_HUMANMAPKAPK2physical
15094067
BMI1_HUMANBMI1physical
9121482
PHC1_HUMANPHC1physical
9121482
AFG32_HUMANAFG3L2physical
16169070
BSDC1_HUMANBSDC1physical
16169070
RL7_HUMANRPL7physical
16169070
MCM2_HUMANMCM2physical
16169070
SCMH1_HUMANSCMH1physical
16169070
BMI1_HUMANBMI1physical
16751658
RING2_HUMANRNF2physical
22325352
PCGF2_HUMANPCGF2physical
22325352
BMI1_HUMANBMI1physical
22325352
RING1_HUMANRING1physical
22325352
PHC1_HUMANPHC1physical
22325352
PHC3_HUMANPHC3physical
22325352
CBX2_HUMANCBX2physical
22325352
CBX4_HUMANCBX4physical
22325352
CBX6_HUMANCBX6physical
22325352
CBX8_HUMANCBX8physical
22325352
SCMH1_HUMANSCMH1physical
22325352
SCML1_HUMANSCML1physical
22325352
SCML2_HUMANSCML2physical
22325352
HDAC2_HUMANHDAC2physical
22325352
PLK1_HUMANPLK1physical
21988832
SIAH1_HUMANSIAH1physical
21988832
KDM1A_HUMANKDM1Aphysical
23455924
PHC2_HUMANPHC2physical
25416956
KIFC3_HUMANKIFC3physical
25416956
RBTN1_HUMANLMO1physical
25416956
RBTN2_HUMANLMO2physical
25416956
SMAD3_HUMANSMAD3physical
25416956
MFAP1_HUMANMFAP1physical
25416956
DRG1_HUMANDRG1physical
25416956
RPAB5_HUMANPOLR2Lphysical
25416956
AAPK1_HUMANPRKAA1physical
25416956
SDCB1_HUMANSDCBPphysical
25416956
SIAH1_HUMANSIAH1physical
25416956
PCGF2_HUMANPCGF2physical
25416956
AP1M1_HUMANAP1M1physical
25416956
RBM39_HUMANRBM39physical
25416956
MO4L2_HUMANMORF4L2physical
25416956
ZBT24_HUMANZBTB24physical
25416956
RWD2B_HUMANRWDD2Bphysical
25416956
PCGF3_HUMANPCGF3physical
25416956
KAT5_HUMANKAT5physical
25416956
PP16B_HUMANPPP1R16Bphysical
25416956
PRP31_HUMANPRPF31physical
25416956
SMBT1_HUMANSFMBT1physical
25416956
CA109_HUMANC1orf109physical
25416956
CBX8_HUMANCBX8physical
25416956
CARD9_HUMANCARD9physical
25416956
AEN_HUMANAENphysical
25416956
THAP7_HUMANTHAP7physical
25416956
SYT16_HUMANSYT16physical
25416956
KBTB7_HUMANKBTBD7physical
25416956
ENKD1_HUMANENKD1physical
25416956
F161A_HUMANFAM161Aphysical
25416956
SPC1L_HUMANSPATC1Lphysical
25416956
PCGF5_HUMANPCGF5physical
25416956
LMBL3_HUMANL3MBTL3physical
25416956
ZGPAT_HUMANZGPATphysical
25416956
TRI41_HUMANTRIM41physical
25416956
ADIP_HUMANSSX2IPphysical
25416956
MB213_HUMANMAB21L3physical
25416956
ZN417_HUMANZNF417physical
25416956
ZMAT2_HUMANZMAT2physical
25416956
MAGB6_HUMANMAGEB6physical
25416956
F124A_HUMANFAM124Aphysical
25416956
FA13C_HUMANFAM13Cphysical
25416956
RBTN1_HUMANLMO1physical
21516116
RBTN2_HUMANLMO2physical
21516116
DRG1_HUMANDRG1physical
21516116
SIAH1_HUMANSIAH1physical
21516116
BYST_HUMANBYSLphysical
21516116
KBTB7_HUMANKBTBD7physical
21516116
ENKD1_HUMANENKD1physical
21516116
LMBL3_HUMANL3MBTL3physical
21516116
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 PHC2_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-621, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-733, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-701 AND SER-704, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-745, AND MASSSPECTROMETRY.

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