PO2F2_HUMAN - dbPTM
PO2F2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PO2F2_HUMAN
UniProt AC P09086
Protein Name POU domain, class 2, transcription factor 2
Gene Name POU2F2
Organism Homo sapiens (Human).
Sequence Length 479
Subcellular Localization Cytoplasm. Nucleus.
Protein Description Transcription factor that specifically binds to the octamer motif (5'-ATTTGCAT-3'). Regulates transcription in a number of tissues in addition to activating immunoglobulin gene expression. Modulates transcription transactivation by NR3C1, AR and PGR. Isoform 5 activates the U2 small nuclear RNA (snRNA) promoter..
Protein Sequence MVHSSMGAPEIRMSKPLEAEKQGLDSPSEHTDTERNGPDTNHQNPQNKTSPFSVSPTGPSTKIKAEDPSGDSAPAAPLPPQPAQPHLPQAQLMLTGSQLAGDIQQLLQLQQLVLVPGHHLQPPAQFLLPQAQQSQPGLLPTPNLFQLPQQTQGALLTSQPRAGLPTQAVTRPTLPDPHLSHPQPPKCLEPPSHPEEPSDLEELEQFARTFKQRRIKLGFTQGDVGLAMGKLYGNDFSQTTISRFEALNLSFKNMCKLKPLLEKWLNDAETMSVDSSLPSPNQLSSPSLGFDGLPGRRRKKRTSIETNVRFALEKSFLANQKPTSEEILLIAEQLHMEKEVIRVWFCNRRQKEKRINPCSAAPMLPSPGKPASYSPHMVTPQGGAGTLPLSQASSSLSTTVTTLSSAVGTLHPSRTAGGGGGGGGAAPPLNSIPSVTPPPPATTNSTNPSPQGSHSAIGLSGLNPSTGPGLWWNPAPYQP
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
4Phosphorylation----MVHSSMGAPEI
----CCCCCCCCCCC		15.6020068231
5Phosphorylation---MVHSSMGAPEIR
---CCCCCCCCCCCC		13.3220068231
14PhosphorylationGAPEIRMSKPLEAEK
CCCCCCCCCCCHHHH		22.6724719451
26PhosphorylationAEKQGLDSPSEHTDT
HHHCCCCCCCCCCCC		35.0526657352
28PhosphorylationKQGLDSPSEHTDTER
HCCCCCCCCCCCCCC		46.0628450419
31PhosphorylationLDSPSEHTDTERNGP
CCCCCCCCCCCCCCC		40.3328450419
33PhosphorylationSPSEHTDTERNGPDT
CCCCCCCCCCCCCCC		37.6926714015
49PhosphorylationHQNPQNKTSPFSVSP
CCCCCCCCCCCCCCC		49.5430108239
50PhosphorylationQNPQNKTSPFSVSPT
CCCCCCCCCCCCCCC		26.0930108239
53PhosphorylationQNKTSPFSVSPTGPS
CCCCCCCCCCCCCCC		25.6830108239
55PhosphorylationKTSPFSVSPTGPSTK
CCCCCCCCCCCCCCC		18.6220164059
57PhosphorylationSPFSVSPTGPSTKIK
CCCCCCCCCCCCCEE		54.9730108239
60PhosphorylationSVSPTGPSTKIKAED
CCCCCCCCCCEEECC		43.6130108239
61PhosphorylationVSPTGPSTKIKAEDP
CCCCCCCCCEEECCC		39.6630108239
141PhosphorylationSQPGLLPTPNLFQLP
CCCCCCCCCCHHCCC		25.4426853621
192PhosphorylationPKCLEPPSHPEEPSD
CCCCCCCCCCCCCCC		63.4926714015
192O-linked_GlycosylationPKCLEPPSHPEEPSD
CCCCCCCCCCCCCCC		63.4913547601
214 (in isoform 4)Ubiquitination-28.0921906983
216UbiquitinationTFKQRRIKLGFTQGD
HHHHHHHHCCCCCHH		40.52-
223 (in isoform 3)Ubiquitination-22.8421906983
230 (in isoform 1)Ubiquitination-26.0021906983
230 (in isoform 2)Ubiquitination-26.0021906983
230 (in isoform 5)Ubiquitination-26.0021906983
230UbiquitinationDVGLAMGKLYGNDFS
HHHHHHHHHHCCCCC		26.00-
234 (in isoform 1)Phosphorylation-33.33-
237PhosphorylationKLYGNDFSQTTISRF
HHHCCCCCHHHHHHH		29.4928555341
250PhosphorylationRFEALNLSFKNMCKL
HHHHHCCHHHHHHHH		32.8525159151
272O-linked_GlycosylationLNDAETMSVDSSLPS
HHCCHHCCCCCCCCC		30.1413547603
275O-linked_GlycosylationAETMSVDSSLPSPNQ
CHHCCCCCCCCCCCC		31.4513547605
279PhosphorylationSVDSSLPSPNQLSSP
CCCCCCCCCCCCCCC		41.6028348404
287PhosphorylationPNQLSSPSLGFDGLP
CCCCCCCCCCCCCCC		42.9726714015
302O-linked_GlycosylationGRRRKKRTSIETNVR
CCCCCCCCCCHHHHH		42.8313547599
302PhosphorylationGRRRKKRTSIETNVR
CCCCCCCCCCHHHHH		42.8330108239
303PhosphorylationRRRKKRTSIETNVRF
CCCCCCCCCHHHHHH		23.5928674151
306PhosphorylationKKRTSIETNVRFALE
CCCCCCHHHHHHHHH		37.0330108239
309MethylationTSIETNVRFALEKSF
CCCHHHHHHHHHHHH		17.12115367733
324O-linked_GlycosylationLANQKPTSEEILLIA
HHCCCCCHHHHHHHH		41.5813547607
372O-linked_GlycosylationPSPGKPASYSPHMVT
CCCCCCCCCCCCEEC		34.3713547623
390O-linked_GlycosylationGAGTLPLSQASSSLS
CCCCCCHHHHCCCCC		23.0413547621
395O-linked_GlycosylationPLSQASSSLSTTVTT
CHHHHCCCCCCCHHH		24.6813547619
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 PO2F2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PO2F2_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 PO2F2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
G3P_HUMANGAPDHphysical
12887926
ESR1_HUMANESR1physical
10480874
GCR_HUMANNR3C1physical
10480874
ANDR_HUMANARphysical
10480874
PRGR_HUMANPGRphysical
10480874
MAT1_HUMANMNAT1physical
9368058
HMGB2_HUMANHMGB2physical
7720710
PO2F2_HUMANPOU2F2physical
10383413
RXRA_HUMANRXRAphysical
10383413
TRXR1_HUMANTXNRD1physical
10383413
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
DB08930Dolutegravir
Regulatory Network of PO2F2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-250, AND MASSSPECTROMETRY.

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