PO2F1_HUMAN - dbPTM
PO2F1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PO2F1_HUMAN
UniProt AC P14859
Protein Name POU domain, class 2, transcription factor 1
Gene Name POU2F1
Organism Homo sapiens (Human).
Sequence Length 743
Subcellular Localization Nucleus.
Protein Description Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3') and activates the promoters of the genes for some small nuclear RNAs (snRNA) and of genes such as those for histone H2B and immunoglobulins. Modulates transcription transactivation by NR3C1, AR and PGR (By similarity). In case of human herpes simplex virus (HSV) infection, POU2F1 forms a multiprotein-DNA complex with the viral transactivator protein VP16 and HCFC1 thereby enabling the transcription of the viral immediate early genes..
Protein Sequence MNNPSETSKPSMESGDGNTGTQTNGLDFQKQPVPVGGAISTAQAQAFLGHLHQVQLAGTSLQAAAQSLNVQSKSNEESGDSQQPSQPSQQPSVQAAIPQTQLMLAGGQITGLTLTPAQQQLLLQQAQAQAQLLAAAVQQHSASQQHSAAGATISASAATPMTQIPLSQPIQIAQDLQQLQQLQQQNLNLQQFVLVHPTTNLQPAQFIISQTPQGQQGLLQAQNLLTQLPQQSQANLLQSQPSITLTSQPATPTRTIAATPIQTLPQSQSTPKRIDTPSLEEPSDLEELEQFAKTFKQRRIKLGFTQGDVGLAMGKLYGNDFSQTTISRFEALNLSFKNMCKLKPLLEKWLNDAENLSSDSSLSSPSALNSPGIEGLSRRRKKRTSIETNIRVALEKSFLENQKPTSEEITMIADQLNMEKEVIRVWFCNRRQKEKRINPPSSGGTSSSPIKAIFPSPTSLVATTPSLVTSSAATTLTVSPVLPLTSAAVTNLSVTGTSDTTSNNTATVISTAPPASSAVTSPSLSPSPSASASTSEASSASETSTTQTTSTPLSSPLGTSQVMVTASGLQTAAAAALQGAAQLPANASLAAMAAAAGLNPSLMAPSQFAAGGALLSLNPGTLSGALSPALMSNSTLATIQALASGGSLPITSLDATGNLVFANAGGAPNIVTAPLFLNPQNLSLLTSNPVSLVSAAAASAGNSAPVASLHATSTSAESIQNSLFTVASASGAASTTTTASKAQ
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 2)Phosphorylation-56.4824043423
7 (in isoform 2)Phosphorylation-46.5224043423
8 (in isoform 5)Phosphorylation-38.2228355574
8 (in isoform 6)Phosphorylation-38.2228355574
9AcetylationNNPSETSKPSMESGD
CCCCCCCCCCCCCCC		48.8326051181
11 (in isoform 2)Phosphorylation-38.6324043423
12 (in isoform 5)Phosphorylation-6.8823663014
12 (in isoform 6)Phosphorylation-6.8823663014
13 (in isoform 5)Phosphorylation-56.7725849741
13 (in isoform 6)Phosphorylation-56.7725849741
21PhosphorylationSGDGNTGTQTNGLDF
CCCCCCCCCCCCCCC		30.1325690035
22 (in isoform 5)Phosphorylation-34.0226552605
22 (in isoform 6)Phosphorylation-34.0226552605
78PhosphorylationQSKSNEESGDSQQPS
CCCCCCCCCCCCCCC		41.5417213819
81PhosphorylationSNEESGDSQQPSQPS
CCCCCCCCCCCCCCC		33.9517213819
85PhosphorylationSGDSQQPSQPSQQPS
CCCCCCCCCCCCCCC		50.8417213819
88PhosphorylationSQQPSQPSQQPSVQA
CCCCCCCCCCCCHHH		33.5417213819
92PhosphorylationSQPSQQPSVQAAIPQ
CCCCCCCCHHHHCCH		23.6417213819
100PhosphorylationVQAAIPQTQLMLAGG
HHHHCCHHHHHHCCC		20.5117213819
141PhosphorylationAAAVQQHSASQQHSA
HHHHHHHCHHHHHCC		25.8517213819
143PhosphorylationAVQQHSASQQHSAAG
HHHHHCHHHHHCCCC		33.1317213819
147PhosphorylationHSASQQHSAAGATIS
HCHHHHHCCCCCEEE		18.5717213819
162PhosphorylationASAATPMTQIPLSQP
CCCCCCCCCCCCCCH		25.2617213819
167PhosphorylationPMTQIPLSQPIQIAQ
CCCCCCCCCHHHHHH		28.6717213819
226O-linked_GlycosylationLQAQNLLTQLPQQSQ
HHHHHHHHHCCHHHH		31.0930059200
226PhosphorylationLQAQNLLTQLPQQSQ
HHHHHHHHHCCHHHH		31.0917213819
232O-linked_GlycosylationLTQLPQQSQANLLQS
HHHCCHHHHHHHHHC		26.4730059200
232PhosphorylationLTQLPQQSQANLLQS
HHHCCHHHHHHHHHC		26.4717213819
242O-linked_GlycosylationNLLQSQPSITLTSQP
HHHHCCCCEEEECCC		22.1430059200
251PhosphorylationTLTSQPATPTRTIAA
EEECCCCCCCCEEEE		31.6926657352
253PhosphorylationTSQPATPTRTIAATP
ECCCCCCCCEEEEEE		35.7728102081
255O-linked_GlycosylationQPATPTRTIAATPIQ
CCCCCCCEEEEEECC		19.9030059200
255PhosphorylationQPATPTRTIAATPIQ
CCCCCCCEEEEEECC		19.9023403867
259O-linked_GlycosylationPTRTIAATPIQTLPQ
CCCEEEEEECCCCCC		16.3530059200
259PhosphorylationPTRTIAATPIQTLPQ
CCCEEEEEECCCCCC		16.3528176443
263PhosphorylationIAATPIQTLPQSQST
EEEEECCCCCCCCCC		40.9222167270
267PhosphorylationPIQTLPQSQSTPKRI
ECCCCCCCCCCCCCC		24.9422167270
269PhosphorylationQTLPQSQSTPKRIDT
CCCCCCCCCCCCCCC		52.5023401153
270PhosphorylationTLPQSQSTPKRIDTP
CCCCCCCCCCCCCCC		25.7822167270
272AcetylationPQSQSTPKRIDTPSL
CCCCCCCCCCCCCCC		63.1725953088
276PhosphorylationSTPKRIDTPSLEEPS
CCCCCCCCCCCCCCC		16.6530266825
278PhosphorylationPKRIDTPSLEEPSDL
CCCCCCCCCCCCCCH		50.9730266825
282 (in isoform 6)Phosphorylation-24.6227251275
283PhosphorylationTPSLEEPSDLEELEQ
CCCCCCCCCHHHHHH		59.0930266825
284 (in isoform 2)Ubiquitination-69.67-
290PhosphorylationSDLEELEQFAKTFKQ
CCHHHHHHHHHHHHH		57.1118691976
290 (in isoform 2)Phosphorylation-57.1121406692
290 (in isoform 6)Phosphorylation-57.1124719451
292PhosphorylationLEELEQFAKTFKQRR
HHHHHHHHHHHHHHH		15.0718669648
293PhosphorylationEELEQFAKTFKQRRI
HHHHHHHHHHHHHHH		56.6419664995
299PhosphorylationAKTFKQRRIKLGFTQ
HHHHHHHHHHCCCCC		28.0920068231
299 (in isoform 6)Phosphorylation-28.0924719451
301PhosphorylationTFKQRRIKLGFTQGD
HHHHHHHHCCCCCCH		40.5218669648
306PhosphorylationRIKLGFTQGDVGLAM
HHHCCCCCCHHHHHH		43.7718669648
313 (in isoform 2)Ubiquitination-6.14-
313 (in isoform 3)Ubiquitination-6.1421906983
315UbiquitinationDVGLAMGKLYGNDFS
HHHHHHHHHHCCCCC		26.00-
315 (in isoform 1)Ubiquitination-26.0021906983
315 (in isoform 4)Ubiquitination-26.0021906983
322PhosphorylationKLYGNDFSQTTISRF
HHHCCCCCHHHHHHH		29.4928555341
327 (in isoform 2)Ubiquitination-28.9121906983
335PhosphorylationRFEALNLSFKNMCKL
HHHHHCCHHHHHHHC		32.8525159151
357PhosphorylationLNDAENLSSDSSLSS
HHHHHHCCCCCCCCC		43.6229978859
358PhosphorylationNDAENLSSDSSLSSP
HHHHHCCCCCCCCCH		44.6818691976
358 (in isoform 6)Phosphorylation-44.6824719451
360PhosphorylationAENLSSDSSLSSPSA
HHHCCCCCCCCCHHH		34.8229978859
361PhosphorylationENLSSDSSLSSPSAL
HHCCCCCCCCCHHHH		36.9429978859
363PhosphorylationLSSDSSLSSPSALNS
CCCCCCCCCHHHHCC		41.9929978859
364PhosphorylationSSDSSLSSPSALNSP
CCCCCCCCHHHHCCC		28.3229978859
366PhosphorylationDSSLSSPSALNSPGI
CCCCCCHHHHCCCCH		47.5429978859
370PhosphorylationSSPSALNSPGIEGLS
CCHHHHCCCCHHHHH		25.9229978859
377PhosphorylationSPGIEGLSRRRKKRT
CCCHHHHHHHHHCCC		34.3020639409
384PhosphorylationSRRRKKRTSIETNIR
HHHHHCCCCHHHHHH		42.8325159151
385PhosphorylationRRRKKRTSIETNIRV
HHHHCCCCHHHHHHH		23.5925159151
386 (in isoform 6)Phosphorylation-8.1724719451
388PhosphorylationKKRTSIETNIRVALE
HCCCCHHHHHHHHHH		33.9929978859
389 (in isoform 6)Phosphorylation-13.7924719451
393 (in isoform 6)Phosphorylation-10.5224719451
408PhosphorylationNQKPTSEEITMIADQ
CCCCCHHHHHHHHHH		43.4520068231
408 (in isoform 6)Phosphorylation-43.4524719451
441PhosphorylationEKRINPPSSGGTSSS
CCCCCCCCCCCCCCC		42.7623927012
442PhosphorylationKRINPPSSGGTSSSP
CCCCCCCCCCCCCCC		47.1925159151
445PhosphorylationNPPSSGGTSSSPIKA
CCCCCCCCCCCCCEE		29.0325159151
446PhosphorylationPPSSGGTSSSPIKAI
CCCCCCCCCCCCEEE		31.9029255136
447PhosphorylationPSSGGTSSSPIKAIF
CCCCCCCCCCCEEEC		39.7229255136
448PhosphorylationSSGGTSSSPIKAIFP
CCCCCCCCCCEEECC		30.3429255136
453 (in isoform 2)Phosphorylation-4.4221406692
454 (in isoform 2)Phosphorylation-6.1521406692
457 (in isoform 2)Phosphorylation-26.6721406692
458 (in isoform 2)Phosphorylation-38.7421406692
459 (in isoform 2)Phosphorylation-25.0021406692
460 (in isoform 2)Phosphorylation-3.1521406692
464PhosphorylationPTSLVATTPSLVTSS
CCCEEEECCCHHCCC		10.9218691976
468PhosphorylationVATTPSLVTSSAATT
EEECCCHHCCCCCCE		5.9819664995
469PhosphorylationATTPSLVTSSAATTL
EECCCHHCCCCCCEE		23.4319664995
470PhosphorylationTTPSLVTSSAATTLT
ECCCHHCCCCCCEEE		15.5319413330
470 (in isoform 6)Phosphorylation-15.5324719451
471PhosphorylationTPSLVTSSAATTLTV
CCCHHCCCCCCEEEE		16.7419664995
471 (in isoform 6)Phosphorylation-16.7427251275
535O-linked_GlycosylationPSASASTSEASSASE
CCCCCCCCCCCCCCC		28.7730059200
725O-linked_GlycosylationSIQNSLFTVASASGA
HHHHHHHHHHCCCCC		22.0630059200
728O-linked_GlycosylationNSLFTVASASGAAST
HHHHHHHCCCCCCCC		20.7330059200
730O-linked_GlycosylationLFTVASASGAASTTT
HHHHHCCCCCCCCCC		26.8630059200
734O-linked_GlycosylationASASGAASTTTTASK
HCCCCCCCCCCCCCC		26.2530059200
735O-linked_GlycosylationSASGAASTTTTASKA
CCCCCCCCCCCCCCC		24.3630059200
736O-linked_GlycosylationASGAASTTTTASKAQ
CCCCCCCCCCCCCCC		21.4730059200
737O-linked_GlycosylationSGAASTTTTASKAQ-
CCCCCCCCCCCCCC-		22.0630059200
738O-linked_GlycosylationGAASTTTTASKAQ--
CCCCCCCCCCCCC--		27.1730059200
740O-linked_GlycosylationASTTTTASKAQ----
CCCCCCCCCCC----		26.8230059200
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
78SPhosphorylationKinasePRKDCP78527
GPS
81SPhosphorylationKinasePRKDCP78527
GPS
85SPhosphorylationKinasePRKDCP78527
GPS
88SPhosphorylationKinasePRKDCP78527
GPS
92SPhosphorylationKinasePRKDCP78527
GPS
100TPhosphorylationKinasePRKDCP78527
GPS
141SPhosphorylationKinasePRKDCP78527
GPS
143SPhosphorylationKinasePRKDCP78527
GPS
147SPhosphorylationKinasePRKDCP78527
GPS
162TPhosphorylationKinasePRKDCP78527
GPS
167SPhosphorylationKinasePRKDCP78527
GPS
226TPhosphorylationKinasePRKDCP78527
GPS
232SPhosphorylationKinasePRKDCP78527
GPS
335SPhosphorylationKinasePRKAA1Q13131
GPS
335SPhosphorylationKinaseAMPKB1Q9Y478
PSP
385SPhosphorylationKinasePRKACAP00517
GPS
385SPhosphorylationKinaseCDK7P50613
PhosphoELM
385SPhosphorylationKinasePKA-FAMILY-GPS
385SPhosphorylationKinasePKA_GROUP-PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PO2F1_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 PO2F1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
G3P_HUMANGAPDHphysical
12887926
NPAT_HUMANNPATphysical
12887926
STIP1_HUMANSTIP1physical
12887926
NCOR2_HUMANNCOR2physical
11134019
ESR1_HUMANESR1physical
10480874
RXRA_HUMANRXRAphysical
10480874
RARA_HUMANRARAphysical
10480874
THA_HUMANTHRAphysical
10480874
ANDR_HUMANARphysical
10480874
PRGR_HUMANPGRphysical
10480874
GCR_HUMANNR3C1physical
10480874
MAT1_HUMANMNAT1physical
9368058
XRCC6_HUMANXRCC6physical
11279128
XRCC5_HUMANXRCC5physical
11279128
SNPC4_HUMANSNAPC4physical
11856838
PO2F1_HUMANPOU2F1physical
11583619
HCFC1_HUMANHCFC1physical
9889203
RXRA_HUMANRXRAphysical
10383413
TRXR1_HUMANTXNRD1physical
10383413
VDR_HUMANVDRphysical
10383413
TF65_HUMANRELAphysical
12019209
BRD7_HUMANBRD7physical
20215511
HDAC1_HUMANHDAC1physical
19617623
NCOR2_HUMANNCOR2physical
19617623
IRF9_HUMANIRF9physical
20211142
HXB13_HUMANHOXB13physical
20211142
CREB1_HUMANCREB1physical
12391146
STA5B_HUMANSTAT5Bphysical
16025120
PBX1_MOUSEPbx1physical
15138251
PBX1_HUMANPBX1physical
15138251
PKNX1_HUMANPKNOX1physical
15138251
BRCA1_HUMANBRCA1physical
18000219
CD11B_HUMANCDK11Bphysical
21897860
HXC4_HUMANHOXC4physical
12672812
XRCC6_HUMANXRCC6physical
12672812
XRCC5_HUMANXRCC5physical
12672812
A4_HUMANAPPphysical
21832049
SPTB2_HUMANSPTBN1physical
22939629
LMNB1_HUMANLMNB1physical
23580612
PO2F1_HUMANPOU2F1physical
25416956
SP4_HUMANSP4physical
25416956
POGZ_HUMANPOGZphysical
25416956
BRCA1_HUMANBRCA1physical
20215511
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 PO2F1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-270; SER-447 ANDSER-448, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-270; SER-283 ANDSER-448, AND MASS SPECTROMETRY.
"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 SER-335 AND SER-385, ANDMASS SPECTROMETRY.
"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-448, AND MASSSPECTROMETRY.
"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-448, AND MASSSPECTROMETRY.

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