PHC1_HUMAN - dbPTM
PHC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHC1_HUMAN
UniProt AC P78364
Protein Name Polyhomeotic-like protein 1
Gene Name PHC1
Organism Homo sapiens (Human).
Sequence Length 1004
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. Required for proper control of cellular levels of GMNN expression..
Protein Sequence METESEQNSNSTNGSSSSGGSSRPQIAQMSLYERQAVQALQALQRQPNAAQYFHQFMLQQQLSNAQLHSLAAVQQATIAASRQASSPNTSTTQQQTTTTQASINLATTSAAQLISRSQSVSSPSATTLTQSVLLGNTTSPPLNQSQAQMYLRPQLGNLLQVNRTLGRNVPLASQLILMPNGAVAAVQQEVPSAQSPGVHADADQVQNLAVRNQQASAQGPQMQGSTQKAIPPGASPVSSLSQASSQALAVAQASSGATNQSLNLSQAGGGSGNSIPGSMGPGGGGQAHGGLGQLPSSGMGGGSCPRKGTGVVQPLPAAQTVTVSQGSQTEAESAAAKKAEADGSGQQNVGMNLTRTATPAPSQTLISSATYTQIQPHSLIQQQQQIHLQQKQVVIQQQIAIHHQQQFQHRQSQLLHTATHLQLAQQQQQQQQQQQQQQQPQATTLTAPQPPQVPPTQQVPPSQSQQQAQTLVVQPMLQSSPLSLPPDAAPKPPIPIQSKPPVAPIKPPQLGAAKMSAAQQPPPHIPVQVVGTRQPGTAQAQALGLAQLAAAVPTSRGMPGTVQSGQAHLASSPPSSQAPGALQECPPTLAPGMTLAPVQGTAHVVKGGATTSSPVVAQVPAAFYMQSVHLPGKPQTLAVKRKADSEEERDDVSTLGSMLPAKASPVAESPKVMDEKSSLGEKAESVANVNANTPSSELVALTPAPSVPPPTLAMVSRQMGDSKPPQAIVKPQILTHIIEGFVIQEGAEPFPVGCSQLLKESEKPLQTGLPTGLTENQSGGPLGVDSPSAELDKKANLLKCEYCGKYAPAEQFRGSKRFCSMTCAKRYNVSCSHQFRLKRKKMKEFQEANYARVRRRGPRRSSSDIARAKIQGKCHRGQEDSSRGSDNSSYDEALSPTSPGPLSVRAGHGERDLGNPNTAPPTPELHGINPVFLSSNPSRWSVEEVYEFIASLQGCQEIAEEFRSQEIDGQALLLLKEEHLMSAMNIKLGPALKICAKINVLKET
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
32PhosphorylationQIAQMSLYERQAVQA
HHHHHHHHHHHHHHH		11.1918083107
63PhosphorylationFMLQQQLSNAQLHSL
HHHHHHHCHHHHHHH		26.2824043423
69PhosphorylationLSNAQLHSLAAVQQA
HCHHHHHHHHHHHHH		28.4424043423
77PhosphorylationLAAVQQATIAASRQA
HHHHHHHHHHHHHHC		13.5524043423
81PhosphorylationQQATIAASRQASSPN
HHHHHHHHHHCCCCC		18.8624043423
192PhosphorylationAVQQEVPSAQSPGVH
EHHHCCCCCCCCCCC		44.0828348404
195PhosphorylationQEVPSAQSPGVHADA
HCCCCCCCCCCCCCH		24.2828348404
309PhosphorylationGSCPRKGTGVVQPLP
CCCCCCCCCCCCCCC		29.82-
324PhosphorylationAAQTVTVSQGSQTEA
CCCEEEEECCCHHHH		21.32-
324O-linked_GlycosylationAAQTVTVSQGSQTEA
CCCEEEEECCCHHHH		21.3228657654
327PhosphorylationTVTVSQGSQTEAESA
EEEEECCCHHHHHHH		26.71-
329PhosphorylationTVSQGSQTEAESAAA
EEECCCHHHHHHHHH		38.57-
337UbiquitinationEAESAAAKKAEADGS
HHHHHHHHHHHCCCC		48.03-
338UbiquitinationAESAAAKKAEADGSG
HHHHHHHHHHCCCCC		46.89-
344PhosphorylationKKAEADGSGQQNVGM
HHHHCCCCCCCCCCC		33.69-
354PhosphorylationQNVGMNLTRTATPAP
CCCCCCCEECCCCCC		22.44-
356PhosphorylationVGMNLTRTATPAPSQ
CCCCCEECCCCCCCC		29.6424247654
554O-linked_GlycosylationQLAAAVPTSRGMPGT
HHHHHCCCCCCCCCC		25.1828657654
555O-linked_GlycosylationLAAAVPTSRGMPGTV
HHHHCCCCCCCCCCC		22.2928657654
571PhosphorylationSGQAHLASSPPSSQA
CCCCEECCCCCHHHC		50.1428348404
572PhosphorylationGQAHLASSPPSSQAP
CCCEECCCCCHHHCC		34.9128348404
575PhosphorylationHLASSPPSSQAPGAL
EECCCCCHHHCCCHH		38.1728348404
576PhosphorylationLASSPPSSQAPGALQ
ECCCCCHHHCCCHHH		35.8128348404
610PhosphorylationHVVKGGATTSSPVVA
EEECCCCCCCCCEEE		30.4127251275
611PhosphorylationVVKGGATTSSPVVAQ
EECCCCCCCCCEEEC		27.0328985074
612PhosphorylationVKGGATTSSPVVAQV
ECCCCCCCCCEEECC		28.4328348404
613PhosphorylationKGGATTSSPVVAQVP
CCCCCCCCCEEECCC		21.4428348404
640AcetylationKPQTLAVKRKADSEE
CCCEEEEEECCCCHH		42.4425953088
645PhosphorylationAVKRKADSEEERDDV
EEEECCCCHHHCCCH		52.3323401153
653PhosphorylationEEERDDVSTLGSMLP
HHHCCCHHHHHHHCC		25.5530576142
654PhosphorylationEERDDVSTLGSMLPA
HHCCCHHHHHHHCCC		34.6821406692
657PhosphorylationDDVSTLGSMLPAKAS
CCHHHHHHHCCCCCC		21.9126074081
664PhosphorylationSMLPAKASPVAESPK
HHCCCCCCCCCCCCC		21.1419413330
669PhosphorylationKASPVAESPKVMDEK
CCCCCCCCCCCCCCC		21.9330266825
677PhosphorylationPKVMDEKSSLGEKAE
CCCCCCCCCHHHHHH		28.8426699800
678PhosphorylationKVMDEKSSLGEKAES
CCCCCCCCHHHHHHH		52.0026699800
693PhosphorylationVANVNANTPSSELVA
HHCCCCCCCHHHHEE		23.3328348404
695PhosphorylationNVNANTPSSELVALT
CCCCCCCHHHHEEEC		34.1128348404
696PhosphorylationVNANTPSSELVALTP
CCCCCCHHHHEEECC		35.8328348404
702PhosphorylationSSELVALTPAPSVPP
HHHHEEECCCCCCCC		13.9928348404
706PhosphorylationVALTPAPSVPPPTLA
EEECCCCCCCCCCHH		49.7328348404
761PhosphorylationCSQLLKESEKPLQTG
HHHHHHHCCCCCCCC		49.7025002506
763UbiquitinationQLLKESEKPLQTGLP
HHHHHCCCCCCCCCC		61.38-
763SumoylationQLLKESEKPLQTGLP
HHHHHCCCCCCCCCC		61.3828112733
767PhosphorylationESEKPLQTGLPTGLT
HCCCCCCCCCCCCCC		48.6625002506
771PhosphorylationPLQTGLPTGLTENQS
CCCCCCCCCCCCCCC		50.2826074081
774PhosphorylationTGLPTGLTENQSGGP
CCCCCCCCCCCCCCC		33.9529978859
778PhosphorylationTGLTENQSGGPLGVD
CCCCCCCCCCCCCCC		58.2529978859
786PhosphorylationGGPLGVDSPSAELDK
CCCCCCCCCCHHHHH		20.5323401153
788PhosphorylationPLGVDSPSAELDKKA
CCCCCCCCHHHHHHC		38.0230576142
793AcetylationSPSAELDKKANLLKC
CCCHHHHHHCCEEEC		67.4220167786
794AcetylationPSAELDKKANLLKCE
CCHHHHHHCCEEECC		42.0220167786
815PhosphorylationPAEQFRGSKRFCSMT
CHHHHCCCCCCCCCC		19.1925159151
832PhosphorylationKRYNVSCSHQFRLKR
HHHCCCCCCHHHCCH		16.9028555341
850PhosphorylationKEFQEANYARVRRRG
HHHHHHHHHHHHHHC		11.6627642862
861PhosphorylationRRRGPRRSSSDIARA
HHHCCCCCHHHHHHH		35.1629691806
862PhosphorylationRRGPRRSSSDIARAK
HHCCCCCHHHHHHHH		30.1625884760
863PhosphorylationRGPRRSSSDIARAKI
HCCCCCHHHHHHHHH		33.9923532336
881PhosphorylationCHRGQEDSSRGSDNS
CCCCCCCCCCCCCCC		22.6023401153
882PhosphorylationHRGQEDSSRGSDNSS
CCCCCCCCCCCCCCC		53.6421406692
885PhosphorylationQEDSSRGSDNSSYDE
CCCCCCCCCCCCCCC		32.2926074081
888PhosphorylationSSRGSDNSSYDEALS
CCCCCCCCCCCCCCC		34.9526074081
889PhosphorylationSRGSDNSSYDEALSP
CCCCCCCCCCCCCCC		42.7426074081
890PhosphorylationRGSDNSSYDEALSPT
CCCCCCCCCCCCCCC		20.0221406692
895PhosphorylationSSYDEALSPTSPGPL
CCCCCCCCCCCCCCC		32.9328985074
897PhosphorylationYDEALSPTSPGPLSV
CCCCCCCCCCCCCEE		44.1526074081
898PhosphorylationDEALSPTSPGPLSVR
CCCCCCCCCCCCEEE		31.1022115753
903PhosphorylationPTSPGPLSVRAGHGE
CCCCCCCEEECCCCC		16.8226074081
918PhosphorylationRDLGNPNTAPPTPEL
CCCCCCCCCCCCCCC		41.6230266825
922PhosphorylationNPNTAPPTPELHGIN
CCCCCCCCCCCCCCC		28.4730266825
934PhosphorylationGINPVFLSSNPSRWS
CCCCEEECCCCCCCC		19.3226074081
935PhosphorylationINPVFLSSNPSRWSV
CCCEEECCCCCCCCH		55.7126074081
938PhosphorylationVFLSSNPSRWSVEEV
EEECCCCCCCCHHHH		51.1126074081
997UbiquitinationPALKICAKINVLKET
HHHHHHHHCCCCCCC		30.33-
997AcetylationPALKICAKINVLKET
HHHHHHHHCCCCCCC		30.3325953088
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 PHC1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHC1_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 PHC1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMBT1_HUMANSFMBT1physical
16189514
UBC9_HUMANUBE2Iphysical
16189514
PHC2_HUMANPHC2physical
16189514
CBX4_HUMANCBX4physical
9199346
BMI1_HUMANBMI1physical
9199346
PHC2_HUMANPHC2physical
9121482
BMI1_HUMANBMI1physical
9121482
RING2_HUMANRNF2physical
22325352
PCGF2_HUMANPCGF2physical
22325352
BMI1_HUMANBMI1physical
22325352
RING1_HUMANRING1physical
22325352
PHC2_HUMANPHC2physical
22325352
PHC3_HUMANPHC3physical
22325352
CBX2_HUMANCBX2physical
22325352
CBX4_HUMANCBX4physical
22325352
CBX6_HUMANCBX6physical
22325352
CBX8_HUMANCBX8physical
22325352
SCMH1_HUMANSCMH1physical
22325352
SCML1_HUMANSCML1physical
22325352
HDAC2_HUMANHDAC2physical
22325352
BMI1_HUMANBMI1physical
15563468
PHC2_HUMANPHC2physical
15563468
PHC1_HUMANPHC1physical
25416956
SIAH1_HUMANSIAH1physical
25416956
SP100_HUMANSP100physical
25416956
SUMO1_HUMANSUMO1physical
25416956
PIAS2_HUMANPIAS2physical
25416956
ZCHC7_HUMANZCCHC7physical
25416956
SCMH1_HUMANSCMH1physical
28514442
CBX8_HUMANCBX8physical
28514442
CBX2_HUMANCBX2physical
28514442
PHC3_HUMANPHC3physical
28514442
NPTXR_HUMANNPTXRphysical
28514442
CBX4_HUMANCBX4physical
28514442
PHC2_HUMANPHC2physical
28514442
BMI1_HUMANBMI1physical
28514442
CBX7_HUMANCBX7physical
28514442
SMBT2_HUMANSFMBT2physical
28514442
CBX6_HUMANCBX6physical
28514442
RING2_HUMANRNF2physical
28514442
SCML1_HUMANSCML1physical
28514442
RING1_HUMANRING1physical
28514442
CSK21_HUMANCSNK2A1physical
28514442
TRPM3_HUMANTRPM3physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615414Microcephaly 11, primary, autosomal recessive (MCPH11)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PHC1_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-898; THR-918 ANDTHR-922, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664; SER-669 ANDSER-786, AND MASS SPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-32, AND MASSSPECTROMETRY.

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